NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|157419150|ref|NP_002836|]
View 

receptor-type tyrosine-protein phosphatase mu isoform 2 precursor [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
884-1156 0e+00

catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


:

Pssm-ID: 350481 [Multi-domain]  Cd Length: 273  Bit Score: 583.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  884 DLLQHITQMKCAEGYGFKEEYESFFEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQTIEGDTNSDYINGNYIDGYH 963
Cdd:cd14633     1 DLLQHITQMKCAEGYGFKEEYESFFEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  964 RPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEIYKDIKVTLIETELLAEYVIRTFAVE 1043
Cdd:cd14633    81 RPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEIYKDIKVTLIETELLAEYVIRTFAVE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1044 KRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDI 1123
Cdd:cd14633   161 KRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDI 240
                         250       260       270
                  ....*....|....*....|....*....|...
gi 157419150 1124 YNCVRELRSRRVNMVQTEEQYVFIHDAILEACL 1156
Cdd:cd14633   241 YNCVRELRSRRVNMVQTEEQYVFIHDAILEACL 273
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
1242-1447 5.24e-148

PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


:

Pssm-ID: 350483 [Multi-domain]  Cd Length: 206  Bit Score: 448.37  E-value: 5.24e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1242 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDPAQLCPQYWPENGVHRHGPIQVEFVSADLEE 1321
Cdd:cd14635     1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPAQLCPQYWPENGVHRHGPIQVEFVSADLEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1322 DIISRIFRIYNAARPQDGYRMVQQFQFLGWPMYRDTPVSKRSFLKLIRQVDKWQEEYNGGEGRTVVHCLNGGGRSGTFCA 1401
Cdd:cd14635    81 DIISRIFRIYNAARPQDGYRMVQQFQFLGWPMYRDTPVSKRSFLKLIRQVDKWQEEYNGGEGRTVVHCLNGGGRSGTFCA 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 157419150 1402 ISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 1447
Cdd:cd14635   161 ISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
22-182 4.62e-59

Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions.


:

Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 200.26  E-value: 4.62e-59
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150     22 TFSGGCLFDEPySTCGYSQSEGDDFNWEQVNTLTK---PTSDPWMPSGSFMLVNASGRPEGQRAHLLLPQLKEN-DTHCI 97
Cdd:smart00137    1 TSPGNCDFEEG-STCGWHQDSNDDGHWERVSSATGipgPNRDHTTGNGHFMFFETSSGAEGQTARLLSPPLYENrSTHCL 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150     98 DFHYFvssKSNSPPGLLNVYVKVNNGPLGNPIWNISGDPTRTWNRAELAISTfWPNFYQVIFEVITS-GHQGYLAIDEVK 176
Cdd:smart00137   80 TFWYY---MYGSGSGTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGkGHSGYIALDDIL 155

                    ....*.
gi 157419150    177 VLGHPC 182
Cdd:smart00137  156 LSNGPC 161
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
192-274 3.93e-13

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


:

Pssm-ID: 395002  Cd Length: 86  Bit Score: 66.45  E-value: 3.93e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150   192 QNVEVNAGQFATFQCSAIGRTVAGDRLWLQGIDVRDAPLKeIKVTSSRRFIASFNVVNTTKRDAGKYRCMIRTEGGVGIS 271
Cdd:pfam00047    4 PTVTVLEGDSATLTCSASTGSPGPDVTWSKEGGTLIESLK-VKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGSATL 82

                   ...
gi 157419150   272 NYA 274
Cdd:pfam00047   83 STS 85
fn3 pfam00041
Fibronectin type III domain;
499-574 2.76e-11

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 60.89  E-value: 2.76e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157419150   499 IFLQWREPTQTYGVITLYEITYKAVSSFDPEIDLSNqsgrvskLGNETHFLFFGLYPGTTYSFTIRASTAKGFGPP 574
Cdd:pfam00041   16 LTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITV-------PGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGPP 84
FN3 super family cl27307
Fibronectin type 3 domain [General function prediction only];
155-638 4.82e-11

Fibronectin type 3 domain [General function prediction only];


The actual alignment was detected with superfamily member COG3401:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 67.33  E-value: 4.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  155 YQVIFEVITSGHQGYLAIDEVKVLGHPCTRTPHFLRIQNVEVNAGQFATFqcSAIGRTVAGDRLWlqGIDVRDAPLKEIK 234
Cdd:COG3401    21 TAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTG--GRAGTTSGVAAVA--VAAAPPTATGLTT 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  235 VTSSRRFIASFNVVNTTKRDAGKYRCMIRTEGGVGISNYAELVVKEPPVPIAPPQLASVGATYlwiqlnANSINGDGPIV 314
Cdd:COG3401    97 LTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTT------ASSVAGAGVVV 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  315 AREVEYCTASGSWNDRQPVDSTSYKIGHLDPDTEYEISVLLTrpGEGGTGSPGPALRTRTKCADPMRgPRKLEVVEVKSR 394
Cdd:COG3401   171 SPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAAT--DTGGESAPSNEVSVTTPTTPPSA-PTGLTATADTPG 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  395 QITIRWEP-FGYNVTrchSYNLtvhycYQVGGQEQVREEVSWDTENSHpqhTITNLSPYTNVSVKLILMNPEGRK--ESQ 471
Cdd:COG3401   248 SVTLSWDPvTESDAT---GYRV-----YRSNSGDGPFTKVATVTTTSY---TDTGLTNGTTYYYRVTAVDAAGNEsaPSN 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  472 ELIVQTDEDLPGAvPTESIQGSTFEEKIFLQWREPTQTYgvITLYEITYKAVSSFDPEidlsnqsgRVSKLGNETHFLFF 551
Cdd:COG3401   317 VVSVTTDLTPPAA-PSGLTATAVGSSSITLSWTASSDAD--VTGYNVYRSTSGGGTYT--------KIAETVTTTSYTDT 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  552 GLYPGTTYSFTIRASTAKGFGPPATNQFT-TKISAPSMPAYELETPLNQTDNTVTVMLKPAHSRGAPVSVYQIVVEEERP 630
Cdd:COG3401   386 GLTPGTTYYYKVTAVDAAGNESAPSEEVSaTTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTG 465

                  ....*...
gi 157419150  631 RRTKKTTE 638
Cdd:COG3401   466 NAVPFTTT 473
 
Name Accession Description Interval E-value
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
884-1156 0e+00

catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350481 [Multi-domain]  Cd Length: 273  Bit Score: 583.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  884 DLLQHITQMKCAEGYGFKEEYESFFEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQTIEGDTNSDYINGNYIDGYH 963
Cdd:cd14633     1 DLLQHITQMKCAEGYGFKEEYESFFEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  964 RPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEIYKDIKVTLIETELLAEYVIRTFAVE 1043
Cdd:cd14633    81 RPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEIYKDIKVTLIETELLAEYVIRTFAVE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1044 KRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDI 1123
Cdd:cd14633   161 KRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDI 240
                         250       260       270
                  ....*....|....*....|....*....|...
gi 157419150 1124 YNCVRELRSRRVNMVQTEEQYVFIHDAILEACL 1156
Cdd:cd14633   241 YNCVRELRSRRVNMVQTEEQYVFIHDAILEACL 273
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
1242-1447 5.24e-148

PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350483 [Multi-domain]  Cd Length: 206  Bit Score: 448.37  E-value: 5.24e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1242 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDPAQLCPQYWPENGVHRHGPIQVEFVSADLEE 1321
Cdd:cd14635     1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPAQLCPQYWPENGVHRHGPIQVEFVSADLEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1322 DIISRIFRIYNAARPQDGYRMVQQFQFLGWPMYRDTPVSKRSFLKLIRQVDKWQEEYNGGEGRTVVHCLNGGGRSGTFCA 1401
Cdd:cd14635    81 DIISRIFRIYNAARPQDGYRMVQQFQFLGWPMYRDTPVSKRSFLKLIRQVDKWQEEYNGGEGRTVVHCLNGGGRSGTFCA 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 157419150 1402 ISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 1447
Cdd:cd14635   161 ISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
899-1153 7.43e-120

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 375.07  E-value: 7.43e-120
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150    899 GFKEEYESFFEGQSA--PWDSAKKDENRMKNRYGNIIAYDHSRVRLQTIEGDtNSDYINGNYIDGYHRPNHYIATQGPMQ 976
Cdd:smart00194    1 GLEEEFEKLDRLKPDdeSCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGE-GSDYINASYIDGPNGPKAYIATQGPLP 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150    977 ETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDD---TEIYKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREI 1053
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEegePLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTV 159
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150   1054 RQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSR 1133
Cdd:smart00194  160 THYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQ 239
                           250       260
                    ....*....|....*....|
gi 157419150   1134 RVNMVQTEEQYVFIHDAILE 1153
Cdd:smart00194  240 RPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
923-1153 1.81e-113

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 356.55  E-value: 1.81e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150   923 NRMKNRYGNIIAYDHSRVRLQTIEGDtnSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVE 1002
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGP--SDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  1003 VGRVKCCKYWP---DDTEIYKDIKVTLI-ETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVR 1078
Cdd:pfam00102   79 KGREKCAQYWPeeeGESLEYGDFTVTLKkEKEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157419150  1079 QV-KSKSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 1153
Cdd:pfam00102  159 KVrKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1185-1447 5.59e-87

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 284.17  E-value: 5.59e-87
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150   1185 QIKEEFRTLNMVTPTlrVEDCSIALLPRNHEKNRCMDILPPDRCLPFLITIDGESSNYINAALMDSYKQPSAFIVTQHPL 1264
Cdd:smart00194    1 GLEEEFEKLDRLKPD--DESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPL 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150   1265 PNTVKDFWRLVLDYHCTSVVMLNDVDPAQL--CPQYWPENGVH--RHGPIQVEFVSADLEEDIISRIFRIYNAARPQDgy 1340
Cdd:smart00194   79 PSTVEDFWRMVWEQKVTVIVMLTELVEKGRekCAQYWPDEEGEplTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSET-- 156
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150   1341 RMVQQFQFLGWPmYRDTPVSKRSFLKLIRQVDKWQEEYNggeGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHA 1420
Cdd:smart00194  157 RTVTHYHYTNWP-DHGVPESPESILDLIRAVRKSQSTST---GPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEI 232
                           250       260
                    ....*....|....*....|....*..
gi 157419150   1421 VKTLRNNKPNMVDLLDQYKFCYEVALE 1447
Cdd:smart00194  233 VKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1213-1447 9.52e-86

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 279.51  E-value: 9.52e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  1213 NHEKNRCMDILPPDRCLPFLiTIDGESSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDPA 1292
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKL-TGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  1293 --QLCPQYWPE--NGVHRHGPIQVEFVSA-DLEEDIISRIFRIYNAARPQdgYRMVQQFQFLGWPmYRDTPVSKRSFLKL 1367
Cdd:pfam00102   80 grEKCAQYWPEeeGESLEYGDFTVTLKKEkEDEKDYTVRTLEVSNGGSEE--TRTVKHFHYTGWP-DHGVPESPNSLLDL 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  1368 IRQVDKWQEeyNGGEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 1447
Cdd:pfam00102  157 LRKVRKSSL--DGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
22-182 4.62e-59

Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions.


Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 200.26  E-value: 4.62e-59
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150     22 TFSGGCLFDEPySTCGYSQSEGDDFNWEQVNTLTK---PTSDPWMPSGSFMLVNASGRPEGQRAHLLLPQLKEN-DTHCI 97
Cdd:smart00137    1 TSPGNCDFEEG-STCGWHQDSNDDGHWERVSSATGipgPNRDHTTGNGHFMFFETSSGAEGQTARLLSPPLYENrSTHCL 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150     98 DFHYFvssKSNSPPGLLNVYVKVNNGPLGNPIWNISGDPTRTWNRAELAISTfWPNFYQVIFEVITS-GHQGYLAIDEVK 176
Cdd:smart00137   80 TFWYY---MYGSGSGTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGkGHSGYIALDDIL 155

                    ....*.
gi 157419150    177 VLGHPC 182
Cdd:smart00137  156 LSNGPC 161
PHA02738 PHA02738
hypothetical protein; Provisional
923-1151 2.09e-49

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 178.58  E-value: 2.09e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  923 NRMKNRYGNIIAYDHSRVRLQTIEgdTNSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVE 1002
Cdd:PHA02738   49 NRKLNRYLDAVCFDHSRVILPAER--NRGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKE 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1003 VGRVKCCKYWPD---DTEIYKDIKVTLIETELLAEYVIRTFAVEKrGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQ 1079
Cdd:PHA02738  127 NGREKCFPYWSDveqGSIRFGKFKITTTQVETHPHYVKSTLLLTD-GTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVLE 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1080 VKS----------------KSPPsagPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQ 1143
Cdd:PHA02738  206 VRQcqkelaqeslqighnrLQPP---PIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQ 282

                  ....*...
gi 157419150 1144 YVFIHDAI 1151
Cdd:PHA02738  283 YFFCYRAV 290
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
27-182 7.30e-48

Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region.


Pssm-ID: 99706  Cd Length: 157  Bit Score: 167.94  E-value: 7.30e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150   27 CLFDEPysTCGYSQSEGDDFNWEQVNTLTKPTSDP-----WMPSGSFMLVNASGRPEGQRAHLLLPQLKEN-DTHCIDFH 100
Cdd:cd06263     1 CDFEDG--LCGWTQDSTDDFDWTRVSGSTPSPGTPpdhthGTGSGHYLYVESSSGREGQKARLLSPLLPPPrSSHCLSFW 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  101 YFVSSksnSPPGLLNVYVKVNNGPLGNPIWNISGDPTRTWNRAELAISTFWpNFYQVIFEVIT-SGHQGYLAIDEVKVLG 179
Cdd:cd06263    79 YHMYG---SGVGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSASS-KPFQVVFEGVRgSGSRGDIALDDISLSP 154

                  ...
gi 157419150  180 HPC 182
Cdd:cd06263   155 GPC 157
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
922-1147 4.99e-46

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 167.58  E-value: 4.99e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  922 ENRMKNRYGNIIAYDHSRVRlqtiegdTNSDYINGNYIDGYhRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLV 1001
Cdd:COG5599    41 NGSPLNRFRDIQPYKETALR-------ANLGYLNANYIQVI-GNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDD 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1002 EVG--RVKCCKYWPDDTEIYK-DIKVTLIETELLAEYV-IRTFAVEKRGV-HEIREIRQFHFTGWPDHGVP----YHAtg 1072
Cdd:COG5599   113 EISkpKVKMPVYFRQDGEYGKyEVSSELTESIQLRDGIeARTYVLTIKGTgQKKIEIPVLHVKNWPDHGAIsaeaLKN-- 190
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157419150 1073 LLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDM--AEREGVVDIYNCVRELR-SRRVNMVQTEEQYVFI 1147
Cdd:COG5599   191 LADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSinALVQITLSVEEIVIDMRtSRNGGMVQTSEQLDVL 268
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
27-182 1.65e-45

MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 161.38  E-value: 1.65e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150    27 CLFDEPySTCGYSQSEGDDFNWEQVNTL---TKPTSDPWM--PSGSFMLVNASGRPEGQRAHLLLPQLKENDT-HCIDFH 100
Cdd:pfam00629    1 CDFEDG-NLCGWTQDSSDDFDWERVSGPsvkTGPSSDHTQgtGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSpQCLRFW 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150   101 YFVSSksnSPPGLLNVYVKVNNGPLGNPIWNISGDPTRTWNRAELAISTFwPNFYQVIFEVI-TSGHQGYLAIDEVKVLG 179
Cdd:pfam00629   80 YHMSG---SGVGTLRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSS-TQPFQVVFEGIrGGGSRGGIALDDISLSS 155

                   ...
gi 157419150   180 HPC 182
Cdd:pfam00629  156 GPC 158
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
1211-1449 3.42e-32

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 128.58  E-value: 3.42e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1211 PRNHEKNRCMDILPPDRCLPFLITIDGESSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLN--- 1287
Cdd:PHA02747   49 PENQPKNRYWDIPCWDHNRVILDSGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTptk 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1288 DVDPAQLCPQYW--PENGVHRHGPIQVEFVSADLEEDIISRIFRIYNaaRPQDGYRMVQQFQFLGWPMYrDTPVSKRSFL 1365
Cdd:PHA02747  129 GTNGEEKCYQYWclNEDGNIDMEDFRIETLKTSVRAKYILTLIEITD--KILKDSRKISHFQCSEWFED-ETPSDHPDFI 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1366 KLIRQVD----KWQEEYNGGEG---RTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQY 1438
Cdd:PHA02747  206 KFIKIIDinrkKSGKLFNPKDAllcPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDY 285
                         250
                  ....*....|....
gi 157419150 1439 KF---CYEVALEYL 1449
Cdd:PHA02747  286 LFiqpGYEVLHYFL 299
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
192-274 3.93e-13

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 66.45  E-value: 3.93e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150   192 QNVEVNAGQFATFQCSAIGRTVAGDRLWLQGIDVRDAPLKeIKVTSSRRFIASFNVVNTTKRDAGKYRCMIRTEGGVGIS 271
Cdd:pfam00047    4 PTVTVLEGDSATLTCSASTGSPGPDVTWSKEGGTLIESLK-VKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGSATL 82

                   ...
gi 157419150   272 NYA 274
Cdd:pfam00047   83 STS 85
fn3 pfam00041
Fibronectin type III domain;
499-574 2.76e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 60.89  E-value: 2.76e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157419150   499 IFLQWREPTQTYGVITLYEITYKAVSSFDPEIDLSNqsgrvskLGNETHFLFFGLYPGTTYSFTIRASTAKGFGPP 574
Cdd:pfam00041   16 LTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITV-------PGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGPP 84
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
155-638 4.82e-11

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 67.33  E-value: 4.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  155 YQVIFEVITSGHQGYLAIDEVKVLGHPCTRTPHFLRIQNVEVNAGQFATFqcSAIGRTVAGDRLWlqGIDVRDAPLKEIK 234
Cdd:COG3401    21 TAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTG--GRAGTTSGVAAVA--VAAAPPTATGLTT 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  235 VTSSRRFIASFNVVNTTKRDAGKYRCMIRTEGGVGISNYAELVVKEPPVPIAPPQLASVGATYlwiqlnANSINGDGPIV 314
Cdd:COG3401    97 LTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTT------ASSVAGAGVVV 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  315 AREVEYCTASGSWNDRQPVDSTSYKIGHLDPDTEYEISVLLTrpGEGGTGSPGPALRTRTKCADPMRgPRKLEVVEVKSR 394
Cdd:COG3401   171 SPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAAT--DTGGESAPSNEVSVTTPTTPPSA-PTGLTATADTPG 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  395 QITIRWEP-FGYNVTrchSYNLtvhycYQVGGQEQVREEVSWDTENSHpqhTITNLSPYTNVSVKLILMNPEGRK--ESQ 471
Cdd:COG3401   248 SVTLSWDPvTESDAT---GYRV-----YRSNSGDGPFTKVATVTTTSY---TDTGLTNGTTYYYRVTAVDAAGNEsaPSN 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  472 ELIVQTDEDLPGAvPTESIQGSTFEEKIFLQWREPTQTYgvITLYEITYKAVSSFDPEidlsnqsgRVSKLGNETHFLFF 551
Cdd:COG3401   317 VVSVTTDLTPPAA-PSGLTATAVGSSSITLSWTASSDAD--VTGYNVYRSTSGGGTYT--------KIAETVTTTSYTDT 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  552 GLYPGTTYSFTIRASTAKGFGPPATNQFT-TKISAPSMPAYELETPLNQTDNTVTVMLKPAHSRGAPVSVYQIVVEEERP 630
Cdd:COG3401   386 GLTPGTTYYYKVTAVDAAGNESAPSEEVSaTTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTG 465

                  ....*...
gi 157419150  631 RRTKKTTE 638
Cdd:COG3401   466 NAVPFTTT 473
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
499-581 1.44e-10

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 59.05  E-value: 1.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  499 IFLQWREPTQTYGVITLYEITYKAVSSfdpeidlsNQSGRVSK-LGNETHFLFFGLYPGTTYSFTIRASTAKGFGPPATN 577
Cdd:cd00063    17 VTLSWTPPEDDGGPITGYVVEYREKGS--------GDWKEVEVtPGSETSYTLTGLKPGTEYEFRVRAVNGGGESPPSES 88

                  ....*
gi 157419150  578 -QFTT 581
Cdd:cd00063    89 vTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
383-477 5.32e-07

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 49.03  E-value: 5.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  383 PRKLEVVEVKSRQITIRWEPFGYNVTRCHSYNLtvhYCYQVGGQEQVREEVSWDTENShpqHTITNLSPYTNVSVKLILM 462
Cdd:cd00063     4 PTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVV---EYREKGSGDWKEVEVTPGSETS---YTLTGLKPGTEYEFRVRAV 77
                          90
                  ....*....|....*.
gi 157419150  463 NPEGR-KESQELIVQT 477
Cdd:cd00063    78 NGGGEsPPSESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
383-467 5.58e-07

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 48.76  E-value: 5.58e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150    383 PRKLEVVEVKSRQITIRWEPFGYNVTRchSYNLTvhycYQVGGQEQVREEVSWDTENSHPQHTITNLSPYTNVSVKLILM 462
Cdd:smart00060    4 PSNLRVTDVTSTSVTLSWEPPPDDGIT--GYIVG----YRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77

                    ....*
gi 157419150    463 NPEGR 467
Cdd:smart00060   78 NGAGE 82
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
482-572 1.40e-06

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 47.61  E-value: 1.40e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150    482 PGAVPTESIQGSTfEEKIFLQWREPTqtYGVITLYEITYKAVSSfdpeiDLSNQSGRVSKLGNETHFLFFGLYPGTTYSF 561
Cdd:smart00060    1 PSPPSNLRVTDVT-STSVTLSWEPPP--DDGITGYIVGYRVEYR-----EEGSEWKEVNVTPSSTSYTLTGLKPGTEYEF 72
                            90
                    ....*....|.
gi 157419150    562 TIRASTAKGFG 572
Cdd:smart00060   73 RVRAVNGAGEG 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
192-278 1.83e-05

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 44.42  E-value: 1.83e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150    192 QNVEVNAGQFATFQCSAIGRTVAgDRLWLQGIDVRDAPLKEIKVTSSRrFIASFNVVNTTKRDAGKYRCMIRTEGGVGIS 271
Cdd:smart00410    2 PSVTVKEGESVTLSCEASGSPPP-EVTWYKQGGKLLAESGRFSVSRSG-STSTLTISNVTPEDSGTYTCAATNSSGSASS 79

                    ....*..
gi 157419150    272 NyAELVV 278
Cdd:smart00410   80 G-TTLTV 85
fn3 pfam00041
Fibronectin type III domain;
284-361 1.15e-03

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 39.32  E-value: 1.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150   284 PIAPPQLASVGATYLWIQLNANSiNGDGPIVAREVEYCTASGSWNDRQ---PVDSTSYKIGHLDPDTEYEISVlLTRPGE 360
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEPWNEitvPGTTTSVTLTGLKPGTEYEVRV-QAVNGG 79

                   .
gi 157419150   361 G 361
Cdd:pfam00041   80 G 80
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1346-1440 1.89e-03

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 39.95  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1346 FQFLGWPMYRDTPVSKRSFLKLIRQVDKWQEEynggEGRTVVHCLNGGGRSGTFCAisivCEMLRHQRTVDvfHAVKTLR 1425
Cdd:COG2453    48 LEYLHLPIPDFGAPDDEQLQEAVDFIDEALRE----GKKVLVHCRGGIGRTGTVAA----AYLVLLGLSAE--EALARVR 117
                          90
                  ....*....|....*
gi 157419150 1426 NNKPNMVDLLDQYKF 1440
Cdd:COG2453   118 AARPGAVETPAQRAF 132
 
Name Accession Description Interval E-value
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
884-1156 0e+00

catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350481 [Multi-domain]  Cd Length: 273  Bit Score: 583.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  884 DLLQHITQMKCAEGYGFKEEYESFFEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQTIEGDTNSDYINGNYIDGYH 963
Cdd:cd14633     1 DLLQHITQMKCAEGYGFKEEYESFFEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  964 RPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEIYKDIKVTLIETELLAEYVIRTFAVE 1043
Cdd:cd14633    81 RPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEIYKDIKVTLIETELLAEYVIRTFAVE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1044 KRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDI 1123
Cdd:cd14633   161 KRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDI 240
                         250       260       270
                  ....*....|....*....|....*....|...
gi 157419150 1124 YNCVRELRSRRVNMVQTEEQYVFIHDAILEACL 1156
Cdd:cd14633   241 YNCVRELRSRRVNMVQTEEQYVFIHDAILEACL 273
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
953-1156 1.91e-150

catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The type II (or R2B) subfamily of receptor protein tyrosine phosphatases (RPTPs) include the prototypical member PTPmu (or PTPRM), PCP-2 (or PTPRU), PTPrho (or PTPRT), and PTPkappa (or PTPRK). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Type IIb RPTPs mediate cell-cell adhesion though homophilic interactions; their ligand is an identical molecule on an adjacent cell. No heterophilic interactions between the subfamily members have been observed. They also commonly function as tumor suppressors. They contain an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350403 [Multi-domain]  Cd Length: 204  Bit Score: 454.76  E-value: 1.91e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  953 YINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEIYKDIKVTLIETELL 1032
Cdd:cd14555     1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTEVYGDIKVTLVETEPL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1033 AEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCFIVIDIML 1112
Cdd:cd14555    81 AEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTGCYIVIDIML 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 157419150 1113 DMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEACL 1156
Cdd:cd14555   161 DMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILEACL 204
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
921-1157 6.51e-150

catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350478 [Multi-domain]  Cd Length: 237  Bit Score: 454.87  E-value: 6.51e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  921 DENRMKNRYGNIIAYDHSRVRLQTIEGDTNSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNL 1000
Cdd:cd14630     1 DENRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1001 VEVGRVKCCKYWPDDTEIYKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQV 1080
Cdd:cd14630    81 VEVGRVKCVRYWPDDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGFVRQV 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157419150 1081 KSKSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEACLC 1157
Cdd:cd14630   161 KFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILEACLC 237
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
1242-1447 5.24e-148

PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350483 [Multi-domain]  Cd Length: 206  Bit Score: 448.37  E-value: 5.24e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1242 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDPAQLCPQYWPENGVHRHGPIQVEFVSADLEE 1321
Cdd:cd14635     1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPAQLCPQYWPENGVHRHGPIQVEFVSADLEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1322 DIISRIFRIYNAARPQDGYRMVQQFQFLGWPMYRDTPVSKRSFLKLIRQVDKWQEEYNGGEGRTVVHCLNGGGRSGTFCA 1401
Cdd:cd14635    81 DIISRIFRIYNAARPQDGYRMVQQFQFLGWPMYRDTPVSKRSFLKLIRQVDKWQEEYNGGEGRTVVHCLNGGGRSGTFCA 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 157419150 1402 ISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 1447
Cdd:cd14635   161 ISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
939-1156 7.55e-132

catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350479 [Multi-domain]  Cd Length: 218  Bit Score: 405.56  E-value: 7.55e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  939 RVRLQTIEGDTNSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEI 1018
Cdd:cd14631     1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1019 YKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPSAGPLVVHCSAG 1098
Cdd:cd14631    81 YGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCSAG 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 157419150 1099 AGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEACL 1156
Cdd:cd14631   161 AGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACL 218
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
953-1157 7.30e-129

catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type tyrosine-protein phosphatase U (PTPRU), also known as pancreatic carcinoma phosphatase 2 (PCP-2), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRU/PCP-2 is the most distant member of the type IIb subfamily and may have a distinct biological function other than cell-cell aggregation. It localizes to the adherens junctions and directly binds and dephosphorylates beta-catenin, and regulates the balance between signaling and adhesive beta-catenin. It plays an important role in the maintenance of epithelial integrity. PTPRU contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350480 [Multi-domain]  Cd Length: 205  Bit Score: 397.11  E-value: 7.30e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  953 YINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEIYKDIKVTLIETELL 1032
Cdd:cd14632     1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSDTYGDIKITLLKTETL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1033 AEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCFIVIDIML 1112
Cdd:cd14632    81 AEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYIVLDVML 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 157419150 1113 DMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEACLC 1157
Cdd:cd14632   161 DMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEACLC 205
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
1242-1447 3.34e-127

PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350482 [Multi-domain]  Cd Length: 206  Bit Score: 392.85  E-value: 3.34e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1242 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDPAQLCPQYWPENGVHRHGPIQVEFVSADLEE 1321
Cdd:cd14634     1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDAAQLCMQYWPEKTSCCYGPIQVEFVSADIDE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1322 DIISRIFRIYNAARPQDGYRMVQQFQFLGWPMYRDTPVSKRSFLKLIRQVDKWQEEYNGGEGRTVVHCLNGGGRSGTFCA 1401
Cdd:cd14634    81 DIISRIFRICNMARPQDGYRIVQHLQYIGWPAYRDTPPSKRSILKVVRRLEKWQEQYDGREGRTVVHCLNGGGRSGTFCA 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 157419150 1402 ISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 1447
Cdd:cd14634   161 ICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
1242-1443 9.75e-127

PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The type IIb (or R2B) subfamily of receptor protein tyrosine phosphatases (RPTPs) include the prototypical member PTPmu (or PTPRM), PCP-2 (or PTPRU), PTPrho (or PTPRT), and PTPkappa (or PTPRK). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Type IIb RPTPs mediate cell-cell adhesion though homophilic interactions; their ligand is an identical molecule on an adjacent cell. No heterophilic interactions between the subfamily members have been observed. They also commonly function as tumor suppressors. They contain an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350404 [Multi-domain]  Cd Length: 201  Bit Score: 391.39  E-value: 9.75e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1242 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDP-AQLCPQYWPENGVHRHGPIQVEFVSADLE 1320
Cdd:cd14556     1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPkDQSCPQYWPDEGSGTYGPIQVEFVSTTID 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1321 EDIISRIFRIYNAARPQDGYRMVQQFQFLGWPMYRDTPVSKRSFLKLIRQVDKWQEEYngGEGRTVVHCLNGGGRSGTFC 1400
Cdd:cd14556    81 EDVISRIFRLQNTTRPQEGYRMVQQFQFLGWPRDRDTPPSKRALLKLLSEVEKWQEQS--GEGPIVVHCLNGVGRSGVFC 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 157419150 1401 AISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYE 1443
Cdd:cd14556   159 AISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
923-1157 1.63e-125

catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs) include three vertebrate members: LAR (or PTPRF), R-PTP-delta (or PTPRD), and R-PTP-sigma (or PTPRS). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules; they bind to distinct synaptic membrane proteins and are physiologically responsible for mediating presynaptic development by shaping various synaptic adhesion pathways. They play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. LAR-RPTPs contain an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350401 [Multi-domain]  Cd Length: 238  Bit Score: 389.45  E-value: 1.63e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  923 NRMKNRYGNIIAYDHSRVRLQTIEGDTNSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVE 1002
Cdd:cd14553     3 NKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1003 VGRVKCCKYWP-DDTEIYKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVK 1081
Cdd:cd14553    83 RSRVKCDQYWPtRGTETYGLIQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVK 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157419150 1082 SKSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEACLC 1157
Cdd:cd14553   163 ACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLEAVTC 238
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
899-1153 7.43e-120

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 375.07  E-value: 7.43e-120
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150    899 GFKEEYESFFEGQSA--PWDSAKKDENRMKNRYGNIIAYDHSRVRLQTIEGDtNSDYINGNYIDGYHRPNHYIATQGPMQ 976
Cdd:smart00194    1 GLEEEFEKLDRLKPDdeSCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGE-GSDYINASYIDGPNGPKAYIATQGPLP 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150    977 ETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDD---TEIYKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREI 1053
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEegePLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTV 159
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150   1054 RQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSR 1133
Cdd:smart00194  160 THYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQ 239
                           250       260
                    ....*....|....*....|
gi 157419150   1134 RVNMVQTEEQYVFIHDAILE 1153
Cdd:smart00194  240 RPGMVQTEEQYIFLYRAILE 259
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
1242-1447 7.00e-116

PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350484 [Multi-domain]  Cd Length: 206  Bit Score: 362.04  E-value: 7.00e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1242 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDPAQLCPQYWPENGVHRHGPIQVEFVSADLEE 1321
Cdd:cd14636     1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLAQGCPQYWPEEGMLRYGPIQVECMSCSMDC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1322 DIISRIFRIYNAARPQDGYRMVQQFQFLGWPMYRDTPVSKRSFLKLIRQVDKWQEEYNGGEGRTVVHCLNGGGRSGTFCA 1401
Cdd:cd14636    81 DVISRIFRICNLTRPQEGYLMVQQFQYLGWASHREVPGSKRSFLKLILQVEKWQEECDEGEGRTIIHCLNGGGRSGMFCA 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 157419150 1402 ISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 1447
Cdd:cd14636   161 ISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
923-1153 1.81e-113

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 356.55  E-value: 1.81e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150   923 NRMKNRYGNIIAYDHSRVRLQTIEGDtnSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVE 1002
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGP--SDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  1003 VGRVKCCKYWP---DDTEIYKDIKVTLI-ETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVR 1078
Cdd:pfam00102   79 KGREKCAQYWPeeeGESLEYGDFTVTLKkEKEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157419150  1079 QV-KSKSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 1153
Cdd:pfam00102  159 KVrKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
883-1157 1.79e-112

catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type tyrosine-protein phosphatase F (PTPRF), also known as leukocyte common antigen related (LAR), is the prototypical member of the LAR family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRF/LAR plays a role for LAR in cadherin complexes where it associates with and dephosphorylates beta-catenin, a pathway which may be critical for cadherin complex stability and cell-cell association. It also regulates focal adhesions through cyclin-dependent kinase-1 and is involved in axon guidance in the developing nervous system. It also functions in regulating insulin signaling. PTPRF contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350474 [Multi-domain]  Cd Length: 276  Bit Score: 355.50  E-value: 1.79e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  883 ADLLQHITQMKCAEGYGFKEEYESFFEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQTIEGDTNSDYINGNYIDGY 962
Cdd:cd14626     1 SDLADNIERLKANDGLKFSQEYESIDPGQQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  963 HRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWP-DDTEIYKDIKVTLIETELLAEYVIRTFA 1041
Cdd:cd14626    81 RKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPiRGTETYGMIQVTLLDTVELATYSVRTFA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1042 VEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVV 1121
Cdd:cd14626   161 LYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTV 240
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 157419150 1122 DIYNCVRELRSRRVNMVQTEEQYVFIHDAILEACLC 1157
Cdd:cd14626   241 DIYGHVTCMRSQRNYMVQTEDQYIFIHEALLEAATC 276
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
877-1159 3.48e-107

catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type tyrosine-protein phosphatase D (PTPRD), also known as receptor-type tyrosine-protein phosphatase delta (R-PTP-delta), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules that play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. PTPRD is involved in pre-synaptic differentiation through interaction with SLITRK2. It contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350472 [Multi-domain]  Cd Length: 284  Bit Score: 341.33  E-value: 3.48e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  877 HPAIRVADLLQHITQMKCAEGYGFKEEYESFFEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQTIEGDTNSDYING 956
Cdd:cd14624     1 HPPIPILELADHIERLKANDNLKFSQEYESIDPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  957 NYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPD-DTEIYKDIKVTLIETELLAEY 1035
Cdd:cd14624    81 NYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSrGTETYGLIQVTLLDTVELATY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1036 VIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMA 1115
Cdd:cd14624   161 CVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERI 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 157419150 1116 EREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEACLCGD 1159
Cdd:cd14624   241 KHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAVTCGN 284
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
877-1157 9.89e-107

catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type tyrosine-protein phosphatase S (PTPRS), also known as receptor-type tyrosine-protein phosphatase sigma (R-PTP-sigma), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRS is a receptor for glycosaminoglycans, including heparan sulfate proteoglycan and neural chondroitin sulfate proteoglycans (CSPGs), which present a barrier to axon regeneration. It also plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2. PTPRS contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350473 [Multi-domain]  Cd Length: 282  Bit Score: 340.15  E-value: 9.89e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  877 HPAIRVADLLQHITQMKCAEGYGFKEEYESFFEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQTIEGDTNSDYING 956
Cdd:cd14625     1 HPPIPISELAEHTERLKANDNLKLSQEYESIDPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  957 NYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPD-DTEIYKDIKVTLIETELLAEY 1035
Cdd:cd14625    81 NYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSrGTETYGMIQVTLLDTIELATF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1036 VIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMA 1115
Cdd:cd14625   161 CVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVIDAMLERI 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 157419150 1116 EREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEACLC 1157
Cdd:cd14625   241 KHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAVAC 282
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
1242-1447 7.35e-101

PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type tyrosine-protein phosphatase U (PTPRU), also known as pancreatic carcinoma phosphatase 2 (PCP-2), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRU/PCP-2 is the most distant member of the type IIb subfamily and may have a distinct biological function other than cell-cell aggregation. It localizes to the adherens junctions and directly binds and dephosphorylates beta-catenin, and regulates the balance between signaling and adhesive beta-catenin. It plays an important role in the maintenance of epithelial integrity. PTPRU contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350485 [Multi-domain]  Cd Length: 207  Bit Score: 320.70  E-value: 7.35e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1242 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVD---PAQLCPQYWPENGVHRHGPIQVEFVSAD 1318
Cdd:cd14637     1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNqsnSAWPCLQYWPEPGLQQYGPMEVEFVSGS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1319 LEEDIISRIFRIYNAARPQDGYRMVQQFQFLGWPMYRDTPVSKRSFLKLIRQVDKWQEEynGGEGRTVVHCLNGGGRSGT 1398
Cdd:cd14637    81 ADEDIVTRLFRVQNITRLQEGHLMVRHFQFLRWSAYRDTPDSKKAFLHLLASVEKWQRE--SGEGRTVVHCLNGGGRSGT 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 157419150 1399 FCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 1447
Cdd:cd14637   159 YCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
953-1149 1.14e-96

catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr (pTyr) residues, instead of pSer or pThr. This family has a distinctive active site signature motif, HCSAGxGRxG, and are characterized as either transmembrane, receptor-like or non-transmembrane (soluble) PTPs. Receptor-like PTP domains tend to occur in two copies in the cytoplasmic region of the transmembrane proteins, only one copy may be active.


Pssm-ID: 350343 [Multi-domain]  Cd Length: 200  Bit Score: 308.83  E-value: 1.14e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  953 YINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTE---IYKDIKVTLIET 1029
Cdd:cd00047     1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGkplEYGDITVTLVSE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1030 ELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCFIVID 1109
Cdd:cd00047    81 EELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTGTFIAID 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 157419150 1110 IMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHD 1149
Cdd:cd00047   161 ILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
953-1149 4.78e-95

catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 subfamily of receptor-type phosphotyrosine phosphatases (RPTP) is composed of receptor-type tyrosine-protein phosphatase Z (PTPRZ) and G (PTPRG). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. They are type 1 integral membrane proteins consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350397 [Multi-domain]  Cd Length: 204  Bit Score: 304.27  E-value: 4.78e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  953 YINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDD-TEIYKDIKVTLIETEL 1031
Cdd:cd14549     1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEgTETYGNIQVTLLSTEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1032 LAEYVIRTFAV------EKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCF 1105
Cdd:cd14549    81 LATYTVRTFSLknlklkKVKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVGRTGTY 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 157419150 1106 IVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHD 1149
Cdd:cd14549   161 IVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
928-1148 5.85e-93

catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar proteins; R3 subfamily receptor-type phosphotyrosine phosphatases (RPTP) are characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. Vertebrate members include receptor-type tyrosine-protein phosphatase-like O (PTPRO), J (PTPRJ), Q (PTPRQ), B (PTPRB), V (PTPRV) and H (PTPRH). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Most members are PTPs, except for PTPRQ, which dephosphorylates phosphatidylinositide substrates. PTPRV is characterized only in rodents; its function has been lost in humans. Both vertebrate and invertebrate R3 subfamily RPTPs are involved in the control of a variety of cellular processes, including cell growth, differentiation, mitotic cycle and oncogenic transformation.


Pssm-ID: 350396 [Multi-domain]  Cd Length: 222  Bit Score: 299.27  E-value: 5.85e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  928 RYGNIIAYDHSRVRLQTIEGDTNSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVK 1007
Cdd:cd14548     1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1008 CCKYWPDDTE--IYKDIKVTLIETELLAEYVIRTFAVEKRGvhEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSP 1085
Cdd:cd14548    81 CDHYWPFDQDpvYYGDITVTMLSESVLPDWTIREFKLERGD--EVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDYIK 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157419150 1086 PSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIH 1148
Cdd:cd14548   159 QEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLH 221
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1185-1447 5.59e-87

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 284.17  E-value: 5.59e-87
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150   1185 QIKEEFRTLNMVTPTlrVEDCSIALLPRNHEKNRCMDILPPDRCLPFLITIDGESSNYINAALMDSYKQPSAFIVTQHPL 1264
Cdd:smart00194    1 GLEEEFEKLDRLKPD--DESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPL 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150   1265 PNTVKDFWRLVLDYHCTSVVMLNDVDPAQL--CPQYWPENGVH--RHGPIQVEFVSADLEEDIISRIFRIYNAARPQDgy 1340
Cdd:smart00194   79 PSTVEDFWRMVWEQKVTVIVMLTELVEKGRekCAQYWPDEEGEplTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSET-- 156
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150   1341 RMVQQFQFLGWPmYRDTPVSKRSFLKLIRQVDKWQEEYNggeGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHA 1420
Cdd:smart00194  157 RTVTHYHYTNWP-DHGVPESPESILDLIRAVRKSQSTST---GPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEI 232
                           250       260
                    ....*....|....*....|....*..
gi 157419150   1421 VKTLRNNKPNMVDLLDQYKFCYEVALE 1447
Cdd:smart00194  233 VKELRSQRPGMVQTEEQYIFLYRAILE 259
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
873-1162 1.28e-86

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type tyrosine-protein phosphatase A (PTPRA), also known as receptor-type tyrosine-protein phosphatase alpha (R-PTP-alpha), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA is a positive regulator of Src and Src family kinases via dephosphorylation of the Src-inhibitory tyrosine 527. Thus, it affects transformation and tumorigenesis, inhibition of proliferation, cell cycle arrest, integrin signaling, neuronal differentiation and outgrowth, and ion channel activity. It is also involved in interleukin-1 signaling in fibroblasts through its interaction with the focal adhesion targeting domain of focal adhesion kinase. PTPRA comprises a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the first catalytic PTP domain (repeat 1).


Pssm-ID: 350469 [Multi-domain]  Cd Length: 296  Bit Score: 284.61  E-value: 1.28e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  873 TGQLHPAIRVADLLQHITQMKCAEGYGFKEEYESFFEGQ-SAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQTIEGDTNS 951
Cdd:cd14621     1 TNRKYPPLPVDKLEEEINRRMADDNKLFREEFNALPACPiQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  952 DYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDD-TEIYKDIKVTLIETE 1030
Cdd:cd14621    81 DYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQgCWTYGNIRVSVEDVT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1031 LLAEYVIRTFAVEKRG----VHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCFI 1106
Cdd:cd14621   161 VLVDYTVRKFCIQQVGdvtnKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFI 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 157419150 1107 VIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEACLCGDTSV 1162
Cdd:cd14621   241 VIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHYLYGDTEL 296
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
922-1156 7.36e-86

catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type tyrosine-protein phosphatase G (PTPRG), also called protein-tyrosine phosphatase gamma (R-PTP-gamma), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRG is an important tumor suppressor gene in multiple human cancers such as lung, ovarian, and breast cancers. It is widely expressed in many tissues, including the central nervous system, where it plays a role during neuroinflammation processes. It can dephosphorylate platelet-derived growth factor receptor beta (PDGFRB) and may play a role in PDGFRB-related infantile myofibromatosis. PTPRG has four splicing isoforms: three transmembrane isoforms, PTPRG-A, B, and C, and one secretory isoform, PTPRG-S, which are expressed in many tissues including the brain. PTPRG is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350505 [Multi-domain]  Cd Length: 274  Bit Score: 281.54  E-value: 7.36e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  922 ENRMKNRYGNIIAYDHSRVRLQTIEG--DTNSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTN 999
Cdd:cd17667    26 DNKHKNRYINILAYDHSRVKLRPLPGkdSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITN 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1000 LVEVGRVKCCKYWP-DDTEIYKDIKVTLIETELLAEYVIRTFAVEK-----------RGVHEIREIRQFHFTGWPDHGVP 1067
Cdd:cd17667   106 LVEKGRRKCDQYWPtENSEEYGNIIVTLKSTKIHACYTVRRFSIRNtkvkkgqkgnpKGRQNERTVIQYHYTQWPDMGVP 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1068 YHATGLLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFI 1147
Cdd:cd17667   186 EYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFI 265

                  ....*....
gi 157419150 1148 HDAILEACL 1156
Cdd:cd17667   266 HDALLEAIL 274
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1213-1447 9.52e-86

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 279.51  E-value: 9.52e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  1213 NHEKNRCMDILPPDRCLPFLiTIDGESSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDPA 1292
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKL-TGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  1293 --QLCPQYWPE--NGVHRHGPIQVEFVSA-DLEEDIISRIFRIYNAARPQdgYRMVQQFQFLGWPmYRDTPVSKRSFLKL 1367
Cdd:pfam00102   80 grEKCAQYWPEeeGESLEYGDFTVTLKKEkEDEKDYTVRTLEVSNGGSEE--TRTVKHFHYTGWP-DHGVPESPNSLLDL 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  1368 IRQVDKWQEeyNGGEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 1447
Cdd:pfam00102  157 LRKVRKSSL--DGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
899-1148 1.95e-83

catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein phosphatase non-receptor type 9 (PTPN9), also called protein-tyrosine phosphatase MEG2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN9 plays an important role in promoting intracellular secretary vesicle fusion in hematopoietic cells and promotes the dephosphorylation of ErbB2 and EGFR in breast cancer cells, leading to impaired activation of STAT5 and STAT3. It also directly dephosphorylates STAT3 at the Tyr705 residue, resulting in its inactivation. PTPN9 has been found to be dysregulated in various human cancers, including breast, colorectal, and gastric cancer.


Pssm-ID: 350391 [Multi-domain]  Cd Length: 271  Bit Score: 274.63  E-value: 1.95e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  899 GFKEEYESF-FEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQTIEGDTNSDYINGNYIDGYHRPNHYIATQGPMQE 977
Cdd:cd14543     4 GIYEEYEDIrREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGPLPK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  978 TIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDD---TEIYKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIR 1054
Cdd:cd14543    84 TYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEegsSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDESRQVT 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1055 QFHFTGWPDHGVPYHATGLLGF---VRQ-----VKSKSPPSAG-----PLVVHCSAGAGRTGCFIVIDIMLDMAEREGVV 1121
Cdd:cd14543   164 HFQFTSWPDFGVPSSAAALLDFlgeVRQqqalaVKAMGDRWKGhppgpPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTL 243
                         250       260
                  ....*....|....*....|....*..
gi 157419150 1122 DIYNCVRELRSRRVNMVQTEEQYVFIH 1148
Cdd:cd14543   244 NVMQTVRRMRTQRAFSIQTPDQYYFCY 270
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
927-1153 1.73e-82

catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type tyrosine-protein phosphatase J (PTPRJ or R-PTP-J), also known as receptor-type tyrosine-protein phosphatase eta (R-PTP-eta) or density-enhanced phosphatase 1 (DEP-1) OR CD148, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRJ is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats (eight in PTPRJ) and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed in various cell types including epithelial, hematopoietic, and endothelial cells. It plays a role in cell adhesion, migration, proliferation and differentiation. It dephosphorylates or contributes to the dephosphorylation of various substrates including protein kinases such as FLT3, PDGFRB, MET, RET (variant MEN2A), VEGFR-2, LYN, SRC, MAPK1, MAPK3, and EGFR, as well as PIK3R1 and PIK3R2.


Pssm-ID: 350463 [Multi-domain]  Cd Length: 229  Bit Score: 270.15  E-value: 1.73e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  927 NRYGNIIAYDHSRVRLqTIEGDTNSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRV 1006
Cdd:cd14615     1 NRYNNVLPYDISRVKL-SVQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1007 KCCKYWPDD-TEIYKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGF---VRQVKS 1082
Cdd:cd14615    80 KCEEYWPSKqKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFrhlVREYMK 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157419150 1083 KSPPSaGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 1153
Cdd:cd14615   160 QNPPN-SPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCALD 229
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
923-1151 1.57e-78

catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) and type 6 (PTPN6) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 and PTPN6, are also called SH2 domain-containing tyrosine phosphatase 2 (SHP2) and 1 (SHP1), respectively. They contain two tandem SH2 domains: a catalytic PTP domain, and a C-terminal tail with regulatory properties. Although structurally similar, they have different localization and different roles in signal transduction. PTPN11/SHP2 is expressed ubiquitously and plays a positive role in cell signaling, leading to cell activation, while PTPN6/SHP1 expression is restricted mainly to hematopoietic and epithelial cells and functions as a negative regulator of signaling events.


Pssm-ID: 350392 [Multi-domain]  Cd Length: 251  Bit Score: 259.70  E-value: 1.57e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  923 NRMKNRYGNIIAYDHSRVRLQTIEGD-TNSDYINGNYI-----DGYHRPNH--YIATQGPMQETIYDFWRMVWHENTASI 994
Cdd:cd14544     1 NKGKNRYKNILPFDHTRVILKDRDPNvPGSDYINANYIrneneGPTTDENAktYIATQGCLENTVSDFWSMVWQENSRVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  995 IMVTNLVEVGRVKCCKYWPDD--TEIYKDIKVTLIETELLAEYVIRTFAVEKRG-VHEIREIRQFHFTGWPDHGVPYHAT 1071
Cdd:cd14544    81 VMTTKEVERGKNKCVRYWPDEgmQKQYGPYRVQNVSEHDTTDYTLRELQVSKLDqGDPIREIWHYQYLSWPDHGVPSDPG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1072 GLLGFVRQV--KSKSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGV---VDIYNCVRELRSRRVNMVQTEEQYVF 1146
Cdd:cd14544   161 GVLNFLEDVnqRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLdcdIDIQKTIQMVRSQRSGMVQTEAQYKF 240

                  ....*
gi 157419150 1147 IHDAI 1151
Cdd:cd14544   241 IYVAV 245
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
929-1153 1.66e-78

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type tyrosine-protein phosphatase E (PTPRE), also known as receptor-type tyrosine-protein phosphatase epsilon (R-PTP-epsilon), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. The PTPRE gene contains two distinct promoters that generate the two major isoforms: transmembrane (receptor type RPTPe or PTPeM) and cytoplasmic (cyt-PTPe or PTPeC). Receptor type RPTPe plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells, and may also play a role in osteoclast formation and function. It also negatively regulates PDGFRbeta-mediated signaling pathways that are crucial for the pathogenesis of atherosclerosis. cyt-PTPe acts as a negative regulator of insulin receptor signaling in skeletal muscle. It regulates insulin-induced phosphorylation of proteins downstream of the insulin receptor. Receptor type RPTPe contains a small extracellular region, a single transmembrane segment, and an intracellular region two tandem catalytic PTP domains. This model represents the first PTP domain (repeat 1).


Pssm-ID: 350468 [Multi-domain]  Cd Length: 229  Bit Score: 258.72  E-value: 1.66e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  929 YGNIIAYDHSRVRLQTIEGDTNSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKC 1008
Cdd:cd14620     1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1009 CKYWPDD-TEIYKDIKVTLIETELLAEYVIRTFAVEKR---GVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKS 1084
Cdd:cd14620    81 YQYWPDQgCWTYGNIRVAVEDCVVLVDYTIRKFCIQPQlpdGCKAPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVKSVN 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157419150 1085 PPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 1153
Cdd:cd14620   161 PVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
927-1153 5.04e-77

catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type tyrosine-protein phosphatase H (PTPRH or R-PTP-H), also known as stomach cancer-associated protein tyrosine phosphatase 1 (SAP-1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRH is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is localized specifically at microvilli of the brush border in gastrointestinal epithelial cells. It plays a role in intestinal immunity by regulating CEACAM20 through tyrosine dephosphorylation. It is also a negative regulator of integrin-mediated signaling and may contribute to contact inhibition of cell growth and motility.


Pssm-ID: 350467 [Multi-domain]  Cd Length: 233  Bit Score: 254.81  E-value: 5.04e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  927 NRYGNIIAYDHSRVRLQTIEGDTNSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRV 1006
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1007 KCCKYWPDDTE--IYKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKS-- 1082
Cdd:cd14619    81 KCEHYWPLDYTpcTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRQwl 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157419150 1083 KSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 1153
Cdd:cd14619   161 DQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILD 231
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
927-1148 5.87e-77

catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type tyrosine-protein phosphatase B (PTPRB), also known as receptor-type tyrosine-protein phosphatase beta (R-PTP-beta) or vascular endothelial protein tyrosine phosphatase(VE-PTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRB/VE-PTP is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed specifically in vascular endothelial cells and it plays an important role in blood vessel remodeling and angiogenesis.


Pssm-ID: 350465 [Multi-domain]  Cd Length: 228  Bit Score: 254.46  E-value: 5.87e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  927 NRYGNIIAYDHSRVRLQTIEGDTNSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRV 1006
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1007 KCCKYWPDDTE--IYKDIKVTLIETELLAEYVIRTFAV-EKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKS- 1082
Cdd:cd14617    81 KCDHYWPADQDslYYGDLIVQMLSESVLPEWTIREFKIcSEEQLDAPRLVRHFHYTVWPDHGVPETTQSLIQFVRTVRDy 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157419150 1083 -KSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIH 1148
Cdd:cd14617   161 iNRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
923-1152 1.37e-75

PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs) include three vertebrate members: LAR (or PTPRF), R-PTP-delta (or PTPRD), and R-PTP-sigma (or PTPRS). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules; they bind to distinct synaptic membrane proteins and are physiologically responsible for mediating presynaptic development by shaping various synaptic adhesion pathways. They play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. LAR-RPTPs contain an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2).


Pssm-ID: 350402 [Multi-domain]  Cd Length: 238  Bit Score: 250.90  E-value: 1.37e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  923 NRMKNRYGNIIAYDHSRVRLQTIEGDTNSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVE 1002
Cdd:cd14554     6 NKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKLRE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1003 VGRVKCCKYWPDDTEI-YKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQV- 1080
Cdd:cd14554    86 MGREKCHQYWPAERSArYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVh 165
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157419150 1081 KSKSP-PSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAIL 1152
Cdd:cd14554   166 KTKEQfGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRAAL 238
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
953-1148 5.89e-75

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; Receptor-type tyrosine-protein phosphatase A (PTPRA) and E (PTPRE) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA and PTPRE share several functions including regulation of Src family kinases and voltage-gated potassium (Kv) channels. They both contain a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the first catalytic PTP domain (repeat 1).


Pssm-ID: 350399 [Multi-domain]  Cd Length: 202  Bit Score: 247.52  E-value: 5.89e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  953 YINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTE-IYKDIKVTLIETEL 1031
Cdd:cd14551     1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCwTYGNLRVRVEDTVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1032 LAEYVIRTFAVEKR----GVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCFIV 1107
Cdd:cd14551    81 LVDYTTRKFCIQKVnrgiGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGRTGTFIV 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 157419150 1108 IDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIH 1148
Cdd:cd14551   161 IDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
914-1152 9.80e-74

catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type tyrosine-protein phosphatase O (PTPRO or R-PTP-O), also known as glomerular epithelial protein 1 or protein tyrosine phosphatase U2 (PTP-U2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRO is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is essential for sustaining the structure and function of foot processes by regulating tyrosine phosphorylation of podocyte proteins. It has been identified as a synaptic cell adhesion molecule (CAM) that serves as a potent initiator of synapse formation. It is also a tumor suppressor in several types of cancer, such as hepatocellular carcinoma, lung cancer, and breast cancer.


Pssm-ID: 350462 [Multi-domain]  Cd Length: 245  Bit Score: 245.95  E-value: 9.80e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  914 PWDSAKKDENRMKNRYGNIIAYDHSRVRLQTIEGDTNSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTAS 993
Cdd:cd14614     3 PHFAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  994 IIMVTNLVEVGRVKCCKYWP--DDTEIYKDIKVTLIETELLAEYVIRTFAVEKrgVHEIREIRQFHFTGWPDHGVPY--H 1069
Cdd:cd14614    83 IVMLTQCNEKRRVKCDHYWPftEEPVAYGDITVEMLSEEEQPDWAIREFRVSY--ADEVQDVMHFNYTAWPDHGVPTanA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1070 ATGLLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHD 1149
Cdd:cd14614   161 AESILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 240

                  ...
gi 157419150 1150 AIL 1152
Cdd:cd14614   241 CVQ 243
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
927-1148 3.31e-73

catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; The kinase interaction motif (KIM) family of protein-tyrosine phosphatases (PTPs) includes tyrosine-protein phosphatases non-receptor type 7 (PTPN7) and non-receptor type 5 (PTPN5), and protein-tyrosine phosphatase receptor type R (PTPRR). PTPN7 is also called hematopoietic protein-tyrosine phosphatase (HePTP) while PTPN5 is also called striatal-enriched protein-tyrosine phosphatase (STEP). They belong to the family of classical tyrosine-specific PTPs (EC 3.1.3.48) that catalyze the dephosphorylation of phosphotyrosine peptides. KIM-PTPs are characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. They are highly specific to the MAPKs ERK1/2 (extracellular-signal-regulated kinase 1/2) and p38, over JNK (c-Jun N-terminal kinase); they dephosphorylate these kinases and thereby critically modulate cell proliferation and differentiation.


Pssm-ID: 350395 [Multi-domain]  Cd Length: 224  Bit Score: 243.46  E-value: 3.31e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  927 NRYGNIIAYDHSRVRLQTIEGDTNSDYINGNYIDGYHRPNH-YIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEvGR 1005
Cdd:cd14547     1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYDGEEKaYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTE-AK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1006 VKCCKYWPDD-TEIYKDIKVTLIETELLAEYVIRTFAVEKRGvhEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKS-- 1082
Cdd:cd14547    80 EKCAQYWPEEeNETYGDFEVTVQSVKETDGYTVRKLTLKYGG--EKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEEar 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157419150 1083 KSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIH 1148
Cdd:cd14547   158 QTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVH 223
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
927-1152 6.96e-72

catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type tyrosine-protein phosphatase V (PTPRV or R-PTP-V), also known as embryonic stem cell protein-tyrosine phosphatase (ES cell phosphatase) or osteotesticular protein-tyrosine phosphatase (OST-PTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRV is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. In rodents, it may play a role in the maintenance of pluripotency and may function in signaling pathways during bone remodeling. It is the only PTP whose function has been lost between rodent and human. The human OST-PTP gene is a pseudogene.


Pssm-ID: 350466 [Multi-domain]  Cd Length: 230  Bit Score: 239.84  E-value: 6.96e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  927 NRYGNIIAYDHSRVRLQTIEGDTNSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRV 1006
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1007 KCCKYWPDDTE--IYKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKS-- 1082
Cdd:cd14618    81 LCDHYWPSESTpvSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELVREhv 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1083 KSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAIL 1152
Cdd:cd14618   161 QATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
953-1152 5.11e-70

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type tyrosine-protein phosphatase Z (PTPRZ), also called receptor-type tyrosine-protein phosphatase zeta (R-PTP-zeta), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Three isoforms are generated by alternative splicing from a single PTPRZ gene: two transmembrane isoforms, PTPRZ-A and PTPRZ-B, and one secretory isoform, PTPRZ-S (also known as phosphacan); all are preferentially expressed in the central nervous system (CNS) as chondroitin sulfate (CS) proteoglycans. PTPRZ isoforms play important roles in maintaining oligodendrocyte precursor cells in an undifferentiated state. PTPRZ is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350506 [Multi-domain]  Cd Length: 209  Bit Score: 233.72  E-value: 5.11e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  953 YINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWP-DDTEIYKDIKVTLIETEL 1031
Cdd:cd17668     1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPaDGSEEYGNFLVTQKSVQV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1032 LAEYVIRTFAVE--------KRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPSAGPLVVHCSAGAGRTG 1103
Cdd:cd17668    81 LAYYTVRNFTLRntkikkgsQKGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSAGVGRTG 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 157419150 1104 CFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAIL 1152
Cdd:cd17668   161 TYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
953-1149 8.82e-70

fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae protein-tyrosine phosphatases 1 (PTP1) and 2 (PTP2), Schizosaccharomyces pombe PTP1, PTP2, and PTP3, and similar fungal proteins. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. PTP2, together with PTP3, is the major phosphatase that dephosphorylates and inactivates the MAP kinase HOG1 and also modulates its subcellular localization.


Pssm-ID: 350509 [Multi-domain]  Cd Length: 212  Bit Score: 232.91  E-value: 8.82e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  953 YINGNYID-GYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPD--DTEIYKDIKVTLIET 1029
Cdd:cd18533     1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSgeYEGEYGDLTVELVSE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1030 ELLAE--YVIRTFAVeKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVR--QVKSKSPPSAGPLVVHCSAGAGRTGCF 1105
Cdd:cd18533    81 EENDDggFIVREFEL-SKEDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKlkRELNDSASLDPPIIVHCSAGVGRTGTF 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 157419150 1106 IVIDIMLDMAER--------EGVVD-IYNCVRELRSRRVNMVQTEEQYVFIHD 1149
Cdd:cd18533   160 IALDSLLDELKRglsdsqdlEDSEDpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
922-1151 1.37e-68

catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11), also called SH2 domain-containing tyrosine phosphatase 2 (SHP-2 or SHP2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 promotes the activation of the RAS/Mitogen-Activated Protein Kinases (MAPK) Extracellular-Regulated Kinases 1/2 (ERK1/2) pathway, a canonical signaling cascade that plays key roles in various cellular processes, including proliferation, survival, differentiation, migration, or metabolism. It also regulates the phosphoinositide 3-kinase (PI3K)/AKT pathway, a fundamental cascade that functions in cell survival, proliferation, migration, morphogenesis, and metabolism. PTPN11 dysregulation is associated with several developmental diseases and malignancies, such as Noonan syndrome and juvenile myelomonocytic leukemia. It contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.


Pssm-ID: 350453 [Multi-domain]  Cd Length: 253  Bit Score: 231.45  E-value: 1.37e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  922 ENRMKNRYGNIIAYDHSRVRLQtiEGDTN---SDYINGNYIDGYH-------RPNH-YIATQGPMQETIYDFWRMVWHEN 990
Cdd:cd14605     1 ENKNKNRYKNILPFDHTRVVLH--DGDPNepvSDYINANIIMPEFetkcnnsKPKKsYIATQGCLQNTVNDFWRMVFQEN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  991 TASIIMVTNLVEVGRVKCCKYWPDDTEI--YKDIKVTLIETELLAEYVIRTFAVEKRGVHEI-REIRQFHFTGWPDHGVP 1067
Cdd:cd14605    79 SRVIVMTTKEVERGKSKCVKYWPDEYALkeYGVMRVRNVKESAAHDYILRELKLSKVGQGNTeRTVWQYHFRTWPDHGVP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1068 YHATGLLGFVRQV--KSKSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGV---VDIYNCVRELRSRRVNMVQTEE 1142
Cdd:cd14605   159 SDPGGVLDFLEEVhhKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMVQTEA 238

                  ....*....
gi 157419150 1143 QYVFIHDAI 1151
Cdd:cd14605   239 QYRFIYMAV 247
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
878-1153 4.85e-67

PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type tyrosine-protein phosphatase-like D (PTPRD), also known as receptor-type tyrosine-protein phosphatase delta (R-PTP-delta), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules that play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. PTPRD is involved in pre-synaptic differentiation through interaction with SLITRK2. It contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350476 [Multi-domain]  Cd Length: 292  Bit Score: 228.46  E-value: 4.85e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  878 PAIRVADLLQHITQMKCAEGY-GFKEEYESFF--EGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQTIEGDTNSDYI 954
Cdd:cd14628     4 PARNLYAYIQKLTQIETGENVtGMELEFKRLAssKAHTSRFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  955 NGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWP-DDTEIYKDIKVTLIETELLA 1033
Cdd:cd14628    84 NASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPaERSARYQYFVVDPMAEYNMP 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1034 EYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQV-KSKSP-PSAGPLVVHCSAGAGRTGCFIVIDIM 1111
Cdd:cd14628   164 QYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVhKTKEQfGQDGPISVHCSAGVGRTGVFITLSIV 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 157419150 1112 LDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 1153
Cdd:cd14628   244 LERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALE 285
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
953-1148 1.66e-66

catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type tyrosine-protein phosphatase C (PTPRC), also known as CD45, leukocyte common antigen (LCA) or GP180, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRC/CD45 is found in all nucleated hematopoietic cells and is an essential regulator of T- and B-cell antigen receptor signaling. It controls immune response, both positively and negatively, by dephosphorylating a number of signaling molecules such as the Src family kinases, the CD3zeta chain of TCY, and ZAP-70 kinase. Mutations in the human PTPRC/CD45 gene are associated with severe combined immunodeficiency (SCID) and multiple sclerosis. PTPRC/CD45 contains an extracellular receptor-like region with fibronectin type III (FN3) repeats, a short transmembrane segment, and a cytoplasmic region comprising of a membrane proximal catalytically active PTP domain (repeat 1 or D1) and a membrane distal catalytically impaired PTP-like domain (repeat 2, or D2). This model represents repeat 1.


Pssm-ID: 350405 [Multi-domain]  Cd Length: 201  Bit Score: 223.17  E-value: 1.66e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  953 YINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWP---DDTEIYKDIKVTLIET 1029
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPsmeEGSRAFGDVVVKINEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1030 ELLAEYVIRTFAV----EKRGVHEIREIRqfhFTGWPDHGVPYHATGLLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCF 1105
Cdd:cd14557    81 KICPDYIIRKLNInnkkEKGSGREVTHIQ---FTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGTY 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 157419150 1106 IVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIH 1148
Cdd:cd14557   158 IGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
927-1148 2.50e-66

catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type tyrosine-protein phosphatase Q (PTPRQ or R-PTP-Q), also called phosphatidylinositol phosphatase PTPRQ, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRQ is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats (18 in PTPRQ) and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It displays low tyrosine-protein phosphatase activity; rather, it functions as a phosphatidylinositol phosphatase required for auditory processes. It regulates the levels of phosphatidylinositol 4,5-bisphosphate (PIP2) in the basal region of hair bundles. It can dephosphorylate a broad range of phosphatidylinositol phosphates, including phosphatidylinositol 3,4,5-trisphosphate and most phosphatidylinositol monophosphates and diphosphates.


Pssm-ID: 350464 [Multi-domain]  Cd Length: 224  Bit Score: 223.63  E-value: 2.50e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  927 NRYGNIIAYDHSRVRLQTIEGDTNSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRV 1006
Cdd:cd14616     1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1007 KCCKYWPDDTE---IYKDIKVTLIETELLAEYVIRTFAVEKRGVHEIreIRQFHFTGWPDHGVPYHATGLLGFVRQVKSK 1083
Cdd:cd14616    81 RCHQYWPEDNKpvtVFGDIVITKLMEDVQIDWTIRDLKIERHGDYMM--VRQCNFTSWPEHGVPESSAPLIHFVKLVRAS 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157419150 1084 SPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIH 1148
Cdd:cd14616   159 RAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLH 223
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
1242-1443 3.24e-66

catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr (pTyr) residues, instead of pSer or pThr. This family has a distinctive active site signature motif, HCSAGxGRxG, and are characterized as either transmembrane, receptor-like or non-transmembrane (soluble) PTPs. Receptor-like PTP domains tend to occur in two copies in the cytoplasmic region of the transmembrane proteins, only one copy may be active.


Pssm-ID: 350343 [Multi-domain]  Cd Length: 200  Bit Score: 222.55  E-value: 3.24e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1242 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDP--AQLCPQYWPENG--VHRHGPIQVEFVSA 1317
Cdd:cd00047     1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEkgREKCERYWPEEGgkPLEYGDITVTLVSE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1318 DLEEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMyRDTPVSKRSFLKLIRQVDKWQEEYNGgegRTVVHCLNGGGRSG 1397
Cdd:cd00047    81 EELSDYTIRTLELSPKGCSES--REVTHLHYTGWPD-HGVPSSPEDLLALVRRVRKEARKPNG---PIVVHCSAGVGRTG 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 157419150 1398 TFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYE 1443
Cdd:cd00047   155 TFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
916-1153 5.60e-66

catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein phosphatase non-receptor type 6 (PTPN6), also called SH2 domain-containing protein-tyrosine phosphatase 1 (SHP1 or SHP-1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN6 expression is restricted mainly to hematopoietic and epithelial cells. It is an important regulator of hematopoietic cells, downregulating pathways that promote cell growth, survival, adhesion, and activation. It regulates glucose homeostasis by modulating insulin signalling in the liver and muscle, and it also negatively regulates bone resorption, affecting both the formation and the function of osteoclasts. PTPN6 contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.


Pssm-ID: 350454 [Multi-domain]  Cd Length: 266  Bit Score: 224.37  E-value: 5.60e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  916 DSAKKDENRMKNRYGNIIAYDHSRVRLQTieGDTN---SDYINGNYIDGY-----HRPNHYIATQGPMQETIYDFWRMVW 987
Cdd:cd14606    11 LEGQRPENKSKNRYKNILPFDHSRVILQG--RDSNipgSDYINANYVKNQllgpdENAKTYIASQGCLEATVNDFWQMAW 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  988 HENTASIIMVTNLVEVGRVKCCKYWPD--DTEIYKDIKVTLIETELLAEYVIRTFAVEKRGVHE-IREIRQFHFTGWPDH 1064
Cdd:cd14606    89 QENSRVIVMTTREVEKGRNKCVPYWPEvgMQRAYGPYSVTNCGEHDTTEYKLRTLQVSPLDNGElIREIWHYQYLSWPDH 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1065 GVPYHATGLLGFVRQV--KSKSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGV---VDIYNCVRELRSRRVNMVQ 1139
Cdd:cd14606   169 GVPSEPGGVLSFLDQInqRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRAQRSGMVQ 248
                         250
                  ....*....|....
gi 157419150 1140 TEEQYVFIHDAILE 1153
Cdd:cd14606   249 TEAQYKFIYVAIAQ 262
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
878-1153 1.34e-65

PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type tyrosine-protein phosphatase S (PTPRS), also known as receptor-type tyrosine-protein phosphatase sigma (R-PTP-sigma), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRS is a receptor for glycosaminoglycans, including heparan sulfate proteoglycan and neural chondroitin sulfate proteoglycans (CSPGs), which present a barrier to axon regeneration. It also plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2. PTPRS contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350475 [Multi-domain]  Cd Length: 290  Bit Score: 224.23  E-value: 1.34e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  878 PAIRVADLLQHITQMKCAEGY-GFKEEYESFF--EGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQTIEGDTNSDYI 954
Cdd:cd14627     5 PARNLYSYIQKLAQVEVGEHVtGMELEFKRLAnsKAHTSRFISANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSDYI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  955 NGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWP-DDTEIYKDIKVTLIETELLA 1033
Cdd:cd14627    85 NASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQYWPaERSARYQYFVVDPMAEYNMP 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1034 EYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQV-KSKSP-PSAGPLVVHCSAGAGRTGCFIVIDIM 1111
Cdd:cd14627   165 QYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVhKTKEQfGQDGPISVHCSAGVGRTGVFITLSIV 244
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 157419150 1112 LDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 1153
Cdd:cd14627   245 LERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALE 286
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
953-1151 9.07e-64

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; Receptor-type tyrosine-protein phosphatase A (PTPRA) and E (PTPRE) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA and PTPRE share several functions including regulation of Src family kinases and voltage-gated potassium (Kv) channels. They both contain a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350400 [Multi-domain]  Cd Length: 202  Bit Score: 215.60  E-value: 9.07e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  953 YINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEI-YKDIKVTLIETEL 1031
Cdd:cd14552     1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGSVsSGDITVELKDQTD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1032 LAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPSA-GPLVVHCSAGAGRTGCFIVIDI 1110
Cdd:cd14552    81 YEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSGnHPITVHCSAGAGRTGTFCALST 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 157419150 1111 MLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAI 1151
Cdd:cd14552   161 VLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
917-1153 1.37e-63

PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type tyrosine-protein phosphatase F (PTPRF), also known as leukocyte common antigen related (LAR), is the prototypical member of the LAR family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRF/LAR plays a role for LAR in cadherin complexes where it associates with and dephosphorylates beta-catenin, a pathway which may be critical for cadherin complex stability and cell-cell association. It also regulates focal adhesions through cyclin-dependent kinase-1 and is involved in axon guidance in the developing nervous system. It also functions in regulating insulin signaling. PTPRF contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350477 [Multi-domain]  Cd Length: 291  Bit Score: 218.44  E-value: 1.37e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  917 SAKKDENRMKNRYGNIIAYDHSRVRLQTIEGDTNSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIM 996
Cdd:cd14629    47 SANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVM 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  997 VTNLVEVGRVKCCKYWP-DDTEIYKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLG 1075
Cdd:cd14629   127 LTKLREMGREKCHQYWPaERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGEGFID 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1076 FVRQV-KSKSP-PSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 1153
Cdd:cd14629   207 FIGQVhKTKEQfGQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALE 286
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
928-1153 2.80e-63

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type tyrosine-protein phosphatase A (PTPRA), also known as receptor-type tyrosine-protein phosphatase alpha (R-PTP-alpha), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA is a positive regulator of Src and Src family kinases via dephosphorylation of the Src-inhibitory tyrosine 527. Thus, it affects transformation and tumorigenesis, inhibition of proliferation, cell cycle arrest, integrin signaling, neuronal differentiation and outgrowth, and ion channel activity. It is also involved in interleukin-1 signaling in fibroblasts through its interaction with the focal adhesion targeting domain of focal adhesion kinase. PTPRA comprises a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350471 [Multi-domain]  Cd Length: 228  Bit Score: 215.29  E-value: 2.80e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  928 RYGNIIAYDHSRVRLQTIEGDTNSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVK 1007
Cdd:cd14623     1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1008 CCKYWPDDTEI-YKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPP 1086
Cdd:cd14623    81 CAQYWPSDGSVsYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQQQ 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157419150 1087 SAG-PLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 1153
Cdd:cd14623   161 SGNhPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
953-1154 6.28e-63

catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) and type 13 (PTPN13, also known as PTPL1) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization. Human PTPN13 is an important regulator of tumor aggressiveness.


Pssm-ID: 350386 [Multi-domain]  Cd Length: 207  Bit Score: 213.39  E-value: 6.28e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  953 YINGNYI------DGYHrpnhYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTE----IYKDI 1022
Cdd:cd14538     1 YINASHIripvggDTYH----YIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNkpliCGGRL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1023 KVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSppSAGPLVVHCSAGAGRT 1102
Cdd:cd14538    77 EVSLEKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIH--NSGPIVVHCSAGIGRT 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 157419150 1103 GCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEA 1154
Cdd:cd14538   155 GVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEV 206
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
914-1151 6.43e-62

catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein phosphatase non-receptor type 12 (PTPN12), also called PTP-PEST or protein-tyrosine phosphatase G1 (PTPG1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN12 is characterized as a tumor suppressor and a pivotal regulator of EGFR/HER2 signaling. It regulates various physiological processes, including cell migration, immune response, and neuronal activity, by dephosphorylating multiple substrates including HER2, FAK, PYK2, PSTPIP, WASP, p130Cas, paxillin, Shc, catenin, c-Abl, ArgBP2, p190RhoGAP, RhoGDI, cell adhesion kinase beta, and Rho GTPase.


Pssm-ID: 350452 [Multi-domain]  Cd Length: 297  Bit Score: 214.03  E-value: 6.43e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  914 PWDSAKKDENRMKNRYGNIIAYDHSRVRLQTIEGDTNSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTAS 993
Cdd:cd14604    48 PTATGEKEENVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAI 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  994 IIMVTNLVEVGRVKCCKYWP---DDTEIYKDIKVTLIETELLAEYVIRTFAVEKRgvHEIREIRQFHFTGWPDHGVPYHA 1070
Cdd:cd14604   128 IVMACREFEMGRKKCERYWPlygEEPMTFGPFRISCEAEQARTDYFIRTLLLEFQ--NETRRLYQFHYVNWPDHDVPSSF 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1071 TGLLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAeREGVV----DIYNCVRELRSRRVNMVQTEEQYVF 1146
Cdd:cd14604   206 DSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLL-KAGKIpeefNVFNLIQEMRTQRHSAVQTKEQYEL 284

                  ....*
gi 157419150 1147 IHDAI 1151
Cdd:cd14604   285 VHRAI 289
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
926-1151 9.12e-62

catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein phosphatase non-receptor type 5 (PTPN5), also called striatum-enriched protein-tyrosine phosphatase (STEP) or neural-specific PTP, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN5/STEP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. It is a CNS-enriched protein that regulates key signaling proteins required for synaptic strengthening, as well as NMDA and AMPA receptor trafficking. PTPN5 is implicated in multiple neurologic and neuropsychiatric disorders, such as Alzheimer's disease, Parkinson's disease, schizophrenia, and fragile X syndrome.


Pssm-ID: 350461 [Multi-domain]  Cd Length: 258  Bit Score: 212.03  E-value: 9.12e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  926 KNRYGNIIAYDHSRVRLQTIE-GDTNSDYINGNYIDGY-HRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEV 1003
Cdd:cd14613    28 KNRYKTILPNPHSRVCLTSPDqDDPLSSYINANYIRGYgGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEM 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1004 GRvKCCKYWPDDTEIYKDIKVTLIETELLAEYVIRTFAVEKRGvhEIREIRQFHFTGWPDHGVPYHATGLLGFVRQV--- 1080
Cdd:cd14613   108 NE-KCTEYWPEEQVTYEGIEITVKQVIHADDYRLRLITLKSGG--EERGLKHYWYTSWPDQKTPDNAPPLLQLVQEVeea 184
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157419150 1081 KSKSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAI 1151
Cdd:cd14613   185 RQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHHVL 255
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
926-1146 2.94e-61

catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1) type 2 (PTPN2) belong to the family of classical tyrosine-specific protein tyrosine phosphatases, (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1 (or PTP-1B) is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor. PTPN2 (or TCPTP), a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner.


Pssm-ID: 350393 [Multi-domain]  Cd Length: 231  Bit Score: 209.56  E-value: 2.94e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  926 KNRYGNIIAYDHSRVRLQTIEGDtnSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGR 1005
Cdd:cd14545     1 LNRYRDRDPYDHDRSRVKLKQGD--NDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1006 VKCCKYWP---DDTEIYKD--IKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGF---V 1077
Cdd:cd14545    79 IKCAQYWPqgeGNAMIFEDtgLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFlqkV 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157419150 1078 RQVKSKSpPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGV--VDIYNCVRELRSRRVNMVQTEEQYVF 1146
Cdd:cd14545   159 RESGSLS-SDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQLRF 228
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
952-1154 1.15e-60

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; Tyrosine-protein phosphatase non-receptor type 3 (PTPN3) and type 4 (PTPN4) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN3 and PTPN4 are large modular proteins containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain. PTPN3 interacts with mitogen-activated protein kinase p38gamma and serves as its specific phosphatase. PTPN4 functions in TCR cell signaling, apoptosis, cerebellar synaptic plasticity, and innate immune responses.


Pssm-ID: 350389 [Multi-domain]  Cd Length: 212  Bit Score: 206.80  E-value: 1.15e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  952 DYINGNYID----GYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPD--DTEIYKDIKVT 1025
Cdd:cd14541     1 DYINANYVNmeipGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDlgETMQFGNLQIT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1026 LIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCF 1105
Cdd:cd14541    81 CVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCSAGIGRTGVL 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 157419150 1106 IVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEA 1154
Cdd:cd14541   161 ITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILRV 209
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
926-1153 1.21e-60

catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein phosphatase non-receptor type 22 (PTPN22), also called lymphoid phosphatase (LyP), PEST-domain phosphatase (PEP), or hematopoietic cell protein-tyrosine phosphatase 70Z-PEP, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN22 is expressed in hematopoietic cells and it functions as a key regulator of immune homeostasis by inhibiting T-cell receptor signaling through the direct dephosphorylation of Src family kinases (Lck and Fyn), ITAMs of the TCRz/CD3 complex, and other signaling molecules. Mutations in the PTPN22 gene are associated with multiple connective tissue and autoimmune diseases including type 1 diabetes mellitus, rheumatoid arthritis, and systemic lupus erythematosus. PTPN22 contains an N-terminal catalytic PTP domain and four proline-rich regions at the C-terminus.


Pssm-ID: 350450 [Multi-domain]  Cd Length: 234  Bit Score: 207.77  E-value: 1.21e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  926 KNRYGNIIAYDHSRVRLQTIEGDTNSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGR 1005
Cdd:cd14602     1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1006 VKCCKYWP---DDTEIYKDIKVTLIETELLAEYVIRTFAVEKRgvHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKS 1082
Cdd:cd14602    81 KKCERYWAepgEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFN--SETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRC 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157419150 1083 KSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAeREGVV----DIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 1153
Cdd:cd14602   159 YQEDDSVPICIHCSAGCGRTGVICAIDYTWMLL-KDGIIpenfSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIE 232
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
922-1152 2.14e-60

catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein phosphatase non-receptor type 13 (PTPN13, also known as PTPL1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN13 is an important regulator of tumor aggressiveness. It regulates breast cancer cell aggressiveness through direct inactivation of Src kinase. In hepatocellular carcinoma, PTPN13 is a tumor suppressor. PTPN13 contains a FERM domain, five PDZ domains, and a C-terminal catalytic PTP domain. With its PDZ domains, PTPN13 has numerous interacting partners that can actively participate in the regulation of its phosphatase activity or can permit direct or indirect recruitment of tyrosine phosphorylated substrates. Its FERM domain is necessary for localization to the membrane.


Pssm-ID: 350445 [Multi-domain]  Cd Length: 234  Bit Score: 206.99  E-value: 2.14e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  922 ENRMKNRYGNIIAYDHSRVRLqtieGDTNsDYINGNYID-GYHRPNH-YIATQGPMQETIYDFWRMVWHENTASIIMVTN 999
Cdd:cd14597     2 ENRKKNRYKNILPYDTTRVPL----GDEG-GYINASFIKmPVGDEEFvYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQ 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1000 LVEVGRVKCCKYWPDD----TEIYKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLG 1075
Cdd:cd14597    77 EVEGGKIKCQRYWPEIlgktTMVDNRLQLTLVRMQQLKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPEQLLT 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157419150 1076 FVRQVKSKSppSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAIL 1152
Cdd:cd14597   157 FISYMRHIH--KSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVIL 231
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
953-1149 3.98e-60

PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type tyrosine-protein phosphatase C (PTPRC), also known as CD45, leukocyte common antigen (LCA) or GP180, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRC/CD45 is found in all nucleated hematopoietic cells and is an essential regulator of T- and B-cell antigen receptor signaling. It controls immune response, both positively and negatively, by dephosphorylating a number of signaling molecules such as the Src family kinases, the CD3zeta chain of TCY, and ZAP-70 kinase. Mutations in the human PTPRC/CD45 gene are associated with severe combined immunodeficiency (SCID) and multiple sclerosis. PTPRC/CD45 contains an extracellular receptor-like region with fibronectin type III (FN3) repeats, a short transmembrane segment, and a cytoplasmic region comprising of a membrane proximal catalytically active PTP domain (repeat 1 or D1) and a membrane distal catalytically impaired PTP-like domain (repeat 2, or D2). This model represents repeat 2.


Pssm-ID: 350406 [Multi-domain]  Cd Length: 203  Bit Score: 204.93  E-value: 3.98e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  953 YINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEIYKDIKVTLIETELL 1032
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKTYGDIEVELKDTEKS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1033 AEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSP------PSAGPLVVHCSAGAGRTGCFI 1106
Cdd:cd14558    81 PTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPyknskhGRSVPIVVHCSDGSSRTGIFC 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 157419150 1107 VIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHD 1149
Cdd:cd14558   161 ALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
922-1153 4.14e-60

catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein phosphatase non-receptor type 18 (PTPN18), also called brain-derived phosphatase, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN18 regulates HER2-mediated cellular functions through defining both its phosphorylation and ubiquitination states. The N-terminal catalytic PTP domain of PTPN18 blocks lysosomal routing and delays the degradation of HER2 by dephosphorylation, and its C-terminal PEST domain promotes K48-linked HER2 ubiquitination and its destruction via the proteasome pathway.


Pssm-ID: 350451 [Multi-domain]  Cd Length: 266  Bit Score: 207.37  E-value: 4.14e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  922 ENRMKNRYGNIIAYDHSRVRLQTIEGDTNSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLV 1001
Cdd:cd14603    29 ENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVILMACREI 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1002 EVGRVKCCKYWP--DDTEIYKDIKVTLI-ETELLAEYVIRTFAVEKRgvHEIREIRQFHFTGWPDHGVPYHATGLLGFVR 1078
Cdd:cd14603   109 EMGKKKCERYWAqeQEPLQTGPFTITLVkEKRLNEEVILRTLKVTFQ--KESRSVSHFQYMAWPDHGIPDSPDCMLAMIE 186
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157419150 1079 QVKSKSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVD---IYNCVRELRSRRVNMVQTEEQYVFIHDAILE 1153
Cdd:cd14603   187 LARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPdfsIFDVVLEMRKQRPAAVQTEEQYEFLYHTVAQ 264
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
22-182 4.62e-59

Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions.


Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 200.26  E-value: 4.62e-59
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150     22 TFSGGCLFDEPySTCGYSQSEGDDFNWEQVNTLTK---PTSDPWMPSGSFMLVNASGRPEGQRAHLLLPQLKEN-DTHCI 97
Cdd:smart00137    1 TSPGNCDFEEG-STCGWHQDSNDDGHWERVSSATGipgPNRDHTTGNGHFMFFETSSGAEGQTARLLSPPLYENrSTHCL 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150     98 DFHYFvssKSNSPPGLLNVYVKVNNGPLGNPIWNISGDPTRTWNRAELAISTfWPNFYQVIFEVITS-GHQGYLAIDEVK 176
Cdd:smart00137   80 TFWYY---MYGSGSGTLNVYVRENNGSQDTLLWSRSGTQGGQWLQAEVALSS-WPQPFQVVFEGTRGkGHSGYIALDDIL 155

                    ....*.
gi 157419150    177 VLGHPC 182
Cdd:smart00137  156 LSNGPC 161
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
926-1148 1.92e-58

catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein phosphatase non-receptor type 7 (PTPN7), also called hematopoietic protein-tyrosine phosphatase (HePTP) or LC-PTP. belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN7/HePTP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. PTPN7/HePTP is found exclusively in the white blood cells in bone marrow, thymus, spleen, lymph nodes and all myeloid and lymphoid cell lines. It negatively regulates T-cell activation and proliferation, and is often dysregulated in the preleukemic disorder myelodysplastic syndrome, as well as in acute myelogenous leukemia.


Pssm-ID: 350460 [Multi-domain]  Cd Length: 247  Bit Score: 201.99  E-value: 1.92e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  926 KNRYGNIIAYDHSRVRLQTIEG-DTNSDYINGNYIDGYH-RPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEv 1003
Cdd:cd14612    18 KDRYKTILPNPQSRVCLRRAGSqEEEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITKLKE- 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1004 GRVKCCKYWPDDTEIYKDIKVTLIETELLAEYVIRTFAVEKRGvhEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKS- 1082
Cdd:cd14612    97 KKEKCVHYWPEKEGTYGRFEIRVQDMKECDGYTIRDLTIQLEE--ESRSVKHYWFSSWPDHQTPESAGPLLRLVAEVEEs 174
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157419150 1083 -KSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIH 1148
Cdd:cd14612   175 rQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLH 241
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
900-1153 4.98e-58

PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type tyrosine-protein phosphatase N2 (PTPRN2 or R-PTP-N2), also called islet cell autoantigen-related protein (IAR), ICAAR, phogrin, or IA-2beta, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). It consists of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. It is mainly expressed in neuropeptidergic neurons and peptide-secreting endocrine cells, including insulin-producing pancreatic beta-cells. It may function as a phosphatidylinositol phosphatase to regulate insulin secretion. It is also required for normal accumulation of the neurotransmitters norepinephrine, dopamine and serotonin in the brain.


Pssm-ID: 350458 [Multi-domain]  Cd Length: 283  Bit Score: 202.21  E-value: 4.98e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  900 FKEEYESFFEGQSAPWDS--AKKDENRMKNRYGNIIAYDHSRVRLQTIEGDTNSDYINGNYI-DGYHRPNHYIATQGPMQ 976
Cdd:cd14610    19 LEKEWEALCAYQAEPNATnvAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPImDHDPRNPAYIATQGPLP 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  977 ETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDD-TEIYKDIKVTLIETELLAE-YVIRTFAVEKRGVHEIREIR 1054
Cdd:cd14610    99 ATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEgSNLYHIYEVNLVSEHIWCEdFLVRSFYLKNLQTNETRTVT 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1055 QFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCFIVIDIMLD-MAEREGVVDIYNCVRELRSR 1133
Cdd:cd14610   179 QFHFLSWNDQGVPASTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNkMAKGAKEIDIAATLEHLRDQ 258
                         250       260
                  ....*....|....*....|
gi 157419150 1134 RVNMVQTEEQYVFIHDAILE 1153
Cdd:cd14610   259 RPGMVQTKEQFEFALTAVAE 278
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
909-1162 1.44e-57

catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1), also called protein-tyrosine phosphatase 1B (PTP-1B), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1/PTP-1B is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It contains an N-terminal catalytic PTP domain, followed by two tandem proline-rich motifs that mediate interaction with SH3-domain-containing proteins, and a small hydrophobic stretch that localizes the enzyme to the endoplasmic reticulum (ER). It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor.


Pssm-ID: 350456 [Multi-domain]  Cd Length: 277  Bit Score: 200.64  E-value: 1.44e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  909 EGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQTiegdTNSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWH 988
Cdd:cd14608    11 EASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQ----EDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  989 ENTASIIMVTNLVEVGRVKCCKYWPDDTE---IYKD--IKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPD 1063
Cdd:cd14608    87 QKSRGVVMLNRVMEKGSLKCAQYWPQKEEkemIFEDtnLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPD 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1064 HGVPYHATGLLGFVRQVKSKSP--PSAGPLVVHCSAGAGRTGCFIVID---IMLDMAEREGVVDIYNCVRELRSRRVNMV 1138
Cdd:cd14608   167 FGVPESPASFLNFLFKVRESGSlsPEHGPVVVHCSAGIGRSGTFCLADtclLLMDKRKDPSSVDIKKVLLEMRKFRMGLI 246
                         250       260
                  ....*....|....*....|....*.
gi 157419150 1139 QTEEQYVFIHDAILEAC--LCGDTSV 1162
Cdd:cd14608   247 QTADQLRFSYLAVIEGAkfIMGDSSV 272
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
902-1153 3.45e-57

PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type tyrosine-protein phosphatase-like N (PTPRN or R-PTP-N), also called islet cell antigen 512 (ICA512) or PTP IA-2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). It consists of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. PTPRN is located in secretory granules of neuroendocrine cells and is involved in the generation, cargo storage, traffic, exocytosis and recycling of insulin secretory granules, as well as in beta-cell proliferation. It is a major autoantigen in type 1 diabetes and is involved in the regulation of insulin secretion.


Pssm-ID: 350457 [Multi-domain]  Cd Length: 281  Bit Score: 199.88  E-value: 3.45e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  902 EEYESFFEGQSAP--WDSAKKDENRMKNRYGNIIAYDHSRVRLQTIEGDTNSDYINGN-YIDGYHRPNHYIATQGPMQET 978
Cdd:cd14609    19 KEWQALCAYQAEPntCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASpIIEHDPRMPAYIATQGPLSHT 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  979 IYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDD-TEIYKDIKVTLIETELLAE-YVIRTFAVEKRGVHEIREIRQF 1056
Cdd:cd14609    99 IADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEgSSLYHIYEVNLVSEHIWCEdFLVRSFYLKNVQTQETRTLTQF 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1057 HFTGWPDHGVPYHATGLLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCFIVIDIMLD-MAEREGVVDIYNCVRELRSRRV 1135
Cdd:cd14609   179 HFLSWPAEGIPSSTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNrMAKGVKEIDIAATLEHVRDQRP 258
                         250
                  ....*....|....*...
gi 157419150 1136 NMVQTEEQYVFIHDAILE 1153
Cdd:cd14609   259 GMVRTKDQFEFALTAVAE 276
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
926-1148 4.63e-57

catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type tyrosine-protein phosphatase-like R (PTPRR or R-PTP-R), also called protein-tyrosine phosphatase PCPTP1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRR is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. The human and mouse PTPRR gene produces multiple neuronal protein isoforms of varying sizes (in human, PTPPBS-alpha, beta, gamma and delta). All isoforms contain the KIM motif and the catalytic PTP domain. PTPRR-deficient mice show significant defects in fine motor coordination and balance skills that are reminiscent of a mild ataxia.


Pssm-ID: 350459 [Multi-domain]  Cd Length: 226  Bit Score: 197.06  E-value: 4.63e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  926 KNRYGNIIAYDHSRVRLQTIE-GDTNSDYINGNYIDGYH-RPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEV 1003
Cdd:cd14611     2 KNRYKTILPNPHSRVCLKPKNsNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1004 GRvKCCKYWPDDTEIYKDIKVTLIETELLAEYVIRTFAVeKRGVHEiREIRQFHFTGWPDHGVPYHATGLLGFVRQVKS- 1082
Cdd:cd14611    82 NE-KCVLYWPEKRGIYGKVEVLVNSVKECDNYTIRNLTL-KQGSQS-RSVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEd 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157419150 1083 -KSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIH 1148
Cdd:cd14611   159 rLASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
953-1148 8.53e-57

catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; Tyrosine-protein phosphatase non-receptor type 22 (PTPN22), type 18 (PTPN18) and type 12 (PTPN12) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN22 is expressed in hematopoietic cells and it functions as a key regulator of immune homeostasis by inhibiting T-cell receptor signaling through the direct dephosphorylation of Src family kinases (Lck and Fyn), ITAMs of the TCRz/CD3 complex, and other signaling molecules. TPN18 regulates HER2-mediated cellular functions through defining both its phosphorylation and ubiquitination states. PTPN12 is characterized as a tumor suppressor and a pivotal regulator of EGFR/HER2 signaling.


Pssm-ID: 350390 [Multi-domain]  Cd Length: 202  Bit Score: 195.33  E-value: 8.53e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  953 YINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWP---DDTEIYKDIKVTLIET 1029
Cdd:cd14542     1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPeegEEQLQFGPFKISLEKE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1030 ELLAE-YVIRTFAVEKRgvHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCFIVI 1108
Cdd:cd14542    81 KRVGPdFLIRTLKVTFQ--KESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGCGRTGTICAI 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 157419150 1109 DIMLDMAEREGVVD---IYNCVRELRSRRVNMVQTEEQYVFIH 1148
Cdd:cd14542   159 DYVWNLLKTGKIPEefsLFDLVREMRKQRPAMVQTKEQYELVY 201
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
952-1151 1.73e-56

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type tyrosine-protein phosphatase E (PTPRE), also known as receptor-type tyrosine-protein phosphatase epsilon (R-PTP-epsilon), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. The PTPRE gene contains two distinct promoters that generate the two major isoforms: transmembrane (receptor type RPTPe or PTPeM) and cytoplasmic (cyt-PTPe or PTPeC). Receptor type RPTPe plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells, and may also play a role in osteoclast formation and function. It also negatively regulates PDGFRbeta-mediated signaling pathways that are crucial for the pathogenesis of atherosclerosis. cyt-PTPe acts as a negative regulator of insulin receptor signaling in skeletal muscle. It regulates insulin-induced phosphorylation of proteins downstream of the insulin receptor. Receptor type RPTPe contains a small extracellular region, a single transmembrane segment, and an intracellular region two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350470 [Multi-domain]  Cd Length: 205  Bit Score: 194.84  E-value: 1.73e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  952 DYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEI-YKDIKVTLIETE 1030
Cdd:cd14622     1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGSVtHGEITIEIKNDT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1031 LLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPSAG-PLVVHCSAGAGRTGCFIVID 1109
Cdd:cd14622    81 LLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQTGNhPIVVHCSAGAGRTGTFIALS 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 157419150 1110 IMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAI 1151
Cdd:cd14622   161 NILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
1208-1446 1.02e-55

PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs) include three vertebrate members: LAR (or PTPRF), R-PTP-delta (or PTPRD), and R-PTP-sigma (or PTPRS). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules; they bind to distinct synaptic membrane proteins and are physiologically responsible for mediating presynaptic development by shaping various synaptic adhesion pathways. They play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. LAR-RPTPs contain an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2).


Pssm-ID: 350402 [Multi-domain]  Cd Length: 238  Bit Score: 193.89  E-value: 1.02e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1208 ALLPRNHEKNRCMDILPPDRCLPFLITIDG-ESSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVML 1286
Cdd:cd14554     1 ANLPCNKFKNRLVNILPYESTRVCLQPIRGvEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1287 NDVDPA--QLCPQYWPENGVHRHGPIQVEFVSADLEEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMyRDTPVSKRSF 1364
Cdd:cd14554    81 TKLREMgrEKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQS--RTVRQFQFTDWPE-QGVPKSGEGF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1365 LKLIRQVDKWQEEYnGGEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEV 1444
Cdd:cd14554   158 IDFIGQVHKTKEQF-GQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRA 236

                  ..
gi 157419150 1445 AL 1446
Cdd:cd14554   237 AL 238
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
918-1152 1.20e-54

catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein phosphatase non-receptor type 3 (PTPN3), also called protein-tyrosine phosphatase H1 (PTP-H1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN3 interacts with mitogen-activated protein kinase p38gamma and serves as its specific phosphatase. PTPN3 and p38gamma cooperate to promote Ras-induced oncogenesis. PTPN3 is a large modular protein containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain. Its PDZ domain binds with the PDZ-binding motif of p38gamma and enables efficient tyrosine dephosphorylation.


Pssm-ID: 350448 [Multi-domain]  Cd Length: 274  Bit Score: 191.99  E-value: 1.20e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  918 AKKDENRMKNRYGNIIAYDHSRVRLQTiegdtNSDYINGNYID----GYHRPNHYIATQGPMQETIYDFWRMVWHENTAS 993
Cdd:cd14600    35 AKLPQNMDKNRYKDVLPYDATRVVLQG-----NEDYINASYVNmeipSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSL 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  994 IIMVTNLVEVGRVKCCKYWPDDTEI--YKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHAT 1071
Cdd:cd14600   110 IVMLTTLTERGRTKCHQYWPDPPDVmeYGGFRVQCHSEDCTIAYVFREMLLTNTQTGEERTVTHLQYVAWPDHGVPDDSS 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1072 GLLGFVRQVKSKSPPSAgPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAI 1151
Cdd:cd14600   190 DFLEFVNYVRSKRVENE-PVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAI 268

                  .
gi 157419150 1152 L 1152
Cdd:cd14600   269 L 269
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
909-1151 2.03e-54

catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein phosphatase non-receptor type 2 (PTPN2), also called T-cell protein-tyrosine phosphatase (TCPTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN2, a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner. It is deleted in 6% of all T-cell acute lymphoblastic leukemias and is associated with constitutive JAK1/STAT5 signaling and tumorigenesis.


Pssm-ID: 350455 [Multi-domain]  Cd Length: 257  Bit Score: 190.95  E-value: 2.03e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  909 EGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQtiegDTNSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWH 988
Cdd:cd14607    10 ESHDYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQ----NTENDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQ 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  989 ENTASIIMVTNLVEVGRVKCCKYWPDDTE---IYKD--IKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPD 1063
Cdd:cd14607    86 QKTKAVVMLNRIVEKDSVKCAQYWPTDEEevlSFKEtgFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFHYTTWPD 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1064 HGVPYHATGLLGF---VRQVKSKSPPSaGPLVVHCSAGAGRTGCFIVIDIMLDMAEREG--VVDIYNCVRELRSRRVNMV 1138
Cdd:cd14607   166 FGVPESPASFLNFlfkVRESGSLSPEH-GPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRKYRMGLI 244
                         250
                  ....*....|...
gi 157419150 1139 QTEEQYVFIHDAI 1151
Cdd:cd14607   245 QTPDQLRFSYMAV 257
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
1242-1444 2.40e-53

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; Receptor-type tyrosine-protein phosphatase A (PTPRA) and E (PTPRE) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA and PTPRE share several functions including regulation of Src family kinases and voltage-gated potassium (Kv) channels. They both contain a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350400 [Multi-domain]  Cd Length: 202  Bit Score: 185.55  E-value: 2.40e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1242 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDP--AQLCPQYWPENGVHRHGPIQVEFVSADL 1319
Cdd:cd14552     1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKErsQNKCAQYWPEDGSVSSGDITVELKDQTD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1320 EEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEynGGEGRTVVHCLNGGGRSGTF 1399
Cdd:cd14552    81 YEDYTLRDFLVTKGKGGST--RTVRQFHFHGWPEV-GIPDNGKGMIDLIAAVQKQQQQ--SGNHPITVHCSAGAGRTGTF 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 157419150 1400 CAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEV 1444
Cdd:cd14552   156 CALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKV 200
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
1159-1451 3.51e-53

PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type tyrosine-protein phosphatase S (PTPRS), also known as receptor-type tyrosine-protein phosphatase sigma (R-PTP-sigma), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRS is a receptor for glycosaminoglycans, including heparan sulfate proteoglycan and neural chondroitin sulfate proteoglycans (CSPGs), which present a barrier to axon regeneration. It also plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2. PTPRS contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350475 [Multi-domain]  Cd Length: 290  Bit Score: 188.40  E-value: 3.51e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1159 DTSVPAsqvRSLYYDMNKL---DPQTNSSQIKEEFRTL-NMVTPTLRVEDcsiALLPRNHEKNRCMDILPPDRCLPFLIT 1234
Cdd:cd14627     1 NTEVPA---RNLYSYIQKLaqvEVGEHVTGMELEFKRLaNSKAHTSRFIS---ANLPCNKFKNRLVNIMPYETTRVCLQP 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1235 IDG-ESSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDPA--QLCPQYWPengVHRHGPIQ 1311
Cdd:cd14627    75 IRGvEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMgrEKCHQYWP---AERSARYQ 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1312 VEFVSADLEEDIISRIFRIYNAARPQDGY-RMVQQFQFLGWPMyRDTPVSKRSFLKLIRQVDKWQEEYnGGEGRTVVHCL 1390
Cdd:cd14627   152 YFVVDPMAEYNMPQYILREFKVTDARDGQsRTVRQFQFTDWPE-QGVPKSGEGFIDFIGQVHKTKEQF-GQDGPISVHCS 229
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157419150 1391 NGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALEYLNS 1451
Cdd:cd14627   230 AGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEYLGS 290
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
1160-1451 1.15e-51

PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type tyrosine-protein phosphatase-like D (PTPRD), also known as receptor-type tyrosine-protein phosphatase delta (R-PTP-delta), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules that play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. PTPRD is involved in pre-synaptic differentiation through interaction with SLITRK2. It contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350476 [Multi-domain]  Cd Length: 292  Bit Score: 184.16  E-value: 1.15e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1160 TSVPASQVRSLYYDMNKLDPQTNSSQIKEEFRTLnmVTPTLRVEDCSIALLPRNHEKNRCMDILPPDRCLPFLITIDG-E 1238
Cdd:cd14628     1 TEVPARNLYAYIQKLTQIETGENVTGMELEFKRL--ASSKAHTSRFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGvE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1239 SSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDPA--QLCPQYWPengVHRHGPIQVEFVS 1316
Cdd:cd14628    79 GSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMgrEKCHQYWP---AERSARYQYFVVD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1317 ADLEEDIISRIFRIYNAARPQDGY-RMVQQFQFLGWPMyRDTPVSKRSFLKLIRQVDKWQEEYnGGEGRTVVHCLNGGGR 1395
Cdd:cd14628   156 PMAEYNMPQYILREFKVTDARDGQsRTVRQFQFTDWPE-QGVPKSGEGFIDFIGQVHKTKEQF-GQDGPISVHCSAGVGR 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 157419150 1396 SGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALEYLNS 1451
Cdd:cd14628   234 TGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYLGS 289
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
1160-1451 1.98e-51

PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type tyrosine-protein phosphatase F (PTPRF), also known as leukocyte common antigen related (LAR), is the prototypical member of the LAR family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRF/LAR plays a role for LAR in cadherin complexes where it associates with and dephosphorylates beta-catenin, a pathway which may be critical for cadherin complex stability and cell-cell association. It also regulates focal adhesions through cyclin-dependent kinase-1 and is involved in axon guidance in the developing nervous system. It also functions in regulating insulin signaling. PTPRF contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350477 [Multi-domain]  Cd Length: 291  Bit Score: 183.39  E-value: 1.98e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1160 TSVPAsqvRSLYYDMNKLD---PQTNSSQIKEEFRTLnmVTPTLRVEDCSIALLPRNHEKNRCMDILPPDRCLPFLITID 1236
Cdd:cd14629     2 TEVPA---RNLYAHIQKLTqvpPGESVTAMELEFKLL--ANSKAHTSRFISANLPCNKFKNRLVNIMPYELTRVCLQPIR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1237 G-ESSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDPA--QLCPQYWPengVHRHGPIQVE 1313
Cdd:cd14629    77 GvEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMgrEKCHQYWP---AERSARYQYF 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1314 FVSADLEEDIISRIFRIYNAARPQDGY-RMVQQFQFLGWPMyRDTPVSKRSFLKLIRQVDKWQEEYnGGEGRTVVHCLNG 1392
Cdd:cd14629   154 VVDPMAEYNMPQYILREFKVTDARDGQsRTIRQFQFTDWPE-QGVPKTGEGFIDFIGQVHKTKEQF-GQDGPITVHCSAG 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 157419150 1393 GGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALEYLNS 1451
Cdd:cd14629   232 VGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALEYLGS 290
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
1241-1448 1.03e-50

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type tyrosine-protein phosphatase E (PTPRE), also known as receptor-type tyrosine-protein phosphatase epsilon (R-PTP-epsilon), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. The PTPRE gene contains two distinct promoters that generate the two major isoforms: transmembrane (receptor type RPTPe or PTPeM) and cytoplasmic (cyt-PTPe or PTPeC). Receptor type RPTPe plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells, and may also play a role in osteoclast formation and function. It also negatively regulates PDGFRbeta-mediated signaling pathways that are crucial for the pathogenesis of atherosclerosis. cyt-PTPe acts as a negative regulator of insulin receptor signaling in skeletal muscle. It regulates insulin-induced phosphorylation of proteins downstream of the insulin receptor. Receptor type RPTPe contains a small extracellular region, a single transmembrane segment, and an intracellular region two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350470 [Multi-domain]  Cd Length: 205  Bit Score: 178.28  E-value: 1.03e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1241 NYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDPAQL--CPQYWPENGVHRHGPIQVEFVSAD 1318
Cdd:cd14622     1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQekCVQYWPSEGSVTHGEITIEIKNDT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1319 LEEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEynGGEGRTVVHCLNGGGRSGT 1398
Cdd:cd14622    81 LLETISIRDFLVTYNQEKQT--RLVRQFHFHGWPEI-GIPAEGKGMIDLIAAVQKQQQQ--TGNHPIVVHCSAGAGRTGT 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 157419150 1399 FCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALEY 1448
Cdd:cd14622   156 FIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQDF 205
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
953-1153 4.87e-50

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; Tyrosine-protein phosphatase non-receptor type 21 (PTPN21) and type 14 (PTPN14) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Both PTPN21 and PTPN14 contain an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350388 [Multi-domain]  Cd Length: 219  Bit Score: 176.88  E-value: 4.87e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  953 YINGNYI----DGYHRpnHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPD-----DTEIYKDIK 1023
Cdd:cd14540     1 YINASHItatvGGKQR--FYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTlggehDALTFGEYK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1024 VTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKS-----------KSPPSagPLV 1092
Cdd:cd14540    79 VSTKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSvrrhtnqdvagHNRNP--PTL 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157419150 1093 VHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 1153
Cdd:cd14540   157 VHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQ 217
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
953-1154 1.10e-49

catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization.


Pssm-ID: 350444 [Multi-domain]  Cd Length: 207  Bit Score: 175.32  E-value: 1.10e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  953 YINGNYI-----DGYHRpnhYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPD---DTEIYKDIKV 1024
Cdd:cd14596     1 YINASYItmpvgEEELF---YIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPEtlqEPMELENYQL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1025 TLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSppSAGPLVVHCSAGAGRTGC 1104
Cdd:cd14596    78 RLENYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVH--NTGPIVVHCSAGIGRAGV 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 157419150 1105 FIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEA 1154
Cdd:cd14596   156 LICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEV 205
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
1184-1442 1.52e-49

catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein phosphatase non-receptor type 9 (PTPN9), also called protein-tyrosine phosphatase MEG2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN9 plays an important role in promoting intracellular secretary vesicle fusion in hematopoietic cells and promotes the dephosphorylation of ErbB2 and EGFR in breast cancer cells, leading to impaired activation of STAT5 and STAT3. It also directly dephosphorylates STAT3 at the Tyr705 residue, resulting in its inactivation. PTPN9 has been found to be dysregulated in various human cancers, including breast, colorectal, and gastric cancer.


Pssm-ID: 350391 [Multi-domain]  Cd Length: 271  Bit Score: 177.17  E-value: 1.52e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1184 SQIKEEFRTLNMVTPTLRVEdCSiaLLPRNHEKNRCMDILPPDRCLPFLITIDG-ESSNYINAALMDSYKQPSAFIVTQH 1262
Cdd:cd14543     3 RGIYEEYEDIRREPPAGTFL-CS--LAPANQEKNRYGDVLCLDQSRVKLPKRNGdERTDYINANFMDGYKQKNAYIATQG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1263 PLPNTVKDFWRLVLDYHCTSVVMLNDVDPA--QLCPQYWP--ENGVHRHGPIQVEFVSADLEEDIISRIFRIYNAArpQD 1338
Cdd:cd14543    80 PLPKTYSDFWRMVWEQKVLVIVMTTRVVERgrVKCGQYWPleEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTE--TD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1339 GYRMVQQFQFLGWPMYrDTPVSKRS---FLKLIRQ---------VDKWQEEYNGGEgrTVVHCLNGGGRSGTFCAISIVC 1406
Cdd:cd14543   158 ESRQVTHFQFTSWPDF-GVPSSAAAlldFLGEVRQqqalavkamGDRWKGHPPGPP--IVVHCSAGIGRTGTFCTLDICL 234
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 157419150 1407 EMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCY 1442
Cdd:cd14543   235 SQLEDVGTLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270
PHA02738 PHA02738
hypothetical protein; Provisional
923-1151 2.09e-49

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 178.58  E-value: 2.09e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  923 NRMKNRYGNIIAYDHSRVRLQTIEgdTNSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVE 1002
Cdd:PHA02738   49 NRKLNRYLDAVCFDHSRVILPAER--NRGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKE 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1003 VGRVKCCKYWPD---DTEIYKDIKVTLIETELLAEYVIRTFAVEKrGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQ 1079
Cdd:PHA02738  127 NGREKCFPYWSDveqGSIRFGKFKITTTQVETHPHYVKSTLLLTD-GTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVLE 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1080 VKS----------------KSPPsagPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQ 1143
Cdd:PHA02738  206 VRQcqkelaqeslqighnrLQPP---PIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQ 282

                  ....*...
gi 157419150 1144 YVFIHDAI 1151
Cdd:PHA02738  283 YFFCYRAV 290
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
953-1153 8.62e-49

PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type tyrosine-protein phosphatase-like N (PTPRN) and N2 (PTPRN2) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). They consist of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. They are mainly expressed in neuropeptidergic neurons and peptide-secreting endocrine cells, including insulin-producing pancreatic beta-cells, and are involved in involved in the generation, cargo storage, traffic, exocytosis and recycling of insulin secretory granules, as well as in beta-cell proliferation. They also are major autoantigens in type 1 diabetes and are involved in the regulation of insulin secretion.


Pssm-ID: 350394 [Multi-domain]  Cd Length: 208  Bit Score: 172.63  E-value: 8.62e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  953 YINGNYI-DGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDD-TEIYKDIKVTLI-ET 1029
Cdd:cd14546     1 YINASTIyDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEgSEVYHIYEVHLVsEH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1030 ELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCFIVID 1109
Cdd:cd14546    81 IWCDDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSCPIVVHCSDGAGRTGTYILID 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 157419150 1110 IMLD-MAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 1153
Cdd:cd14546   161 MVLNrMAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAE 205
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
952-1153 5.24e-48

catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein phosphatase non-receptor type 4 (PTPN4), also called protein-tyrosine phosphatase MEG1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN4 functions in TCR cell signaling, apoptosis, cerebellar synaptic plasticity, and innate immune responses. It specifically inhibits the TRIF-dependent TLR4 pathway by suppressing tyrosine phosphorylation of TRAM. It is a large modular protein containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain; the PDZ domain regulates the catalytic activity of PTPN4.


Pssm-ID: 350449 [Multi-domain]  Cd Length: 212  Bit Score: 170.51  E-value: 5.24e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  952 DYINGNYIDgYHRP-----NHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPD--DTEIYKDIKV 1024
Cdd:cd14601     1 DYINANYIN-MEIPsssiiNRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEpsGSSSYGGFQV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1025 TLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGC 1104
Cdd:cd14601    80 TCHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVHCSAGIGRTGV 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 157419150 1105 FIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 1153
Cdd:cd14601   160 LITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILK 208
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
27-182 7.30e-48

Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region.


Pssm-ID: 99706  Cd Length: 157  Bit Score: 167.94  E-value: 7.30e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150   27 CLFDEPysTCGYSQSEGDDFNWEQVNTLTKPTSDP-----WMPSGSFMLVNASGRPEGQRAHLLLPQLKEN-DTHCIDFH 100
Cdd:cd06263     1 CDFEDG--LCGWTQDSTDDFDWTRVSGSTPSPGTPpdhthGTGSGHYLYVESSSGREGQKARLLSPLLPPPrSSHCLSFW 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  101 YFVSSksnSPPGLLNVYVKVNNGPLGNPIWNISGDPTRTWNRAELAISTFWpNFYQVIFEVIT-SGHQGYLAIDEVKVLG 179
Cdd:cd06263    79 YHMYG---SGVGTLNVYVREEGGGLGTLLWSASGGQGNQWQEAEVTLSASS-KPFQVVFEGVRgSGSRGDIALDDISLSP 154

                  ...
gi 157419150  180 HPC 182
Cdd:cd06263   155 GPC 157
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
880-1148 8.33e-48

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 173.65  E-value: 8.33e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  880 IRVADLLQHITQMKCAeGYGFKEEYESFFEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQTIEGDTnSDYINGNYI 959
Cdd:PHA02747    9 CRAIDFLKRRNQLNCF-GIIRDEHHQIILKPFDGLIANFEKPENQPKNRYWDIPCWDHNRVILDSGGGST-SDYIHANWI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  960 DGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEV-GRVKCCKYW---PDDTEIYKDIKVTLIETELLAEY 1035
Cdd:PHA02747   87 DGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTPTKGTnGEEKCYQYWclnEDGNIDMEDFRIETLKTSVRAKY 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1036 VIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGF------VRQVKSK--SPPSA--GPLVVHCSAGAGRTGCF 1105
Cdd:PHA02747  167 ILTLIEITDKILKDSRKISHFQCSEWFEDETPSDHPDFIKFikiidiNRKKSGKlfNPKDAllCPIVVHCSDGVGKTGIF 246
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 157419150 1106 IVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIH 1148
Cdd:PHA02747  247 CAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDYLFIQ 289
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
1242-1443 1.65e-47

PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type tyrosine-protein phosphatase C (PTPRC), also known as CD45, leukocyte common antigen (LCA) or GP180, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRC/CD45 is found in all nucleated hematopoietic cells and is an essential regulator of T- and B-cell antigen receptor signaling. It controls immune response, both positively and negatively, by dephosphorylating a number of signaling molecules such as the Src family kinases, the CD3zeta chain of TCY, and ZAP-70 kinase. Mutations in the human PTPRC/CD45 gene are associated with severe combined immunodeficiency (SCID) and multiple sclerosis. PTPRC/CD45 contains an extracellular receptor-like region with fibronectin type III (FN3) repeats, a short transmembrane segment, and a cytoplasmic region comprising of a membrane proximal catalytically active PTP domain (repeat 1 or D1) and a membrane distal catalytically impaired PTP-like domain (repeat 2, or D2). This model represents repeat 2.


Pssm-ID: 350406 [Multi-domain]  Cd Length: 203  Bit Score: 168.73  E-value: 1.65e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1242 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDV--DPAQLCPQYWPENGvHRHGPIQVEFVSADL 1319
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELkeGDQEQCAQYWGDEK-KTYGDIEVELKDTEK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1320 EEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMyRDTPVSKRSFLKLIRQVDKWQEEYNGGEGRT---VVHCLNGGGRS 1396
Cdd:cd14558    80 SPTYTVRVFEITHLKRKDS--RTVYQYQYHKWKG-EELPEKPKDLVDMIKSIKQKLPYKNSKHGRSvpiVVHCSDGSSRT 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 157419150 1397 GTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYE 1443
Cdd:cd14558   157 GIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
953-1149 2.21e-46

PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The type IIb (or R2B) subfamily of receptor protein tyrosine phosphatases (RPTPs) include the prototypical member PTPmu (or PTPRM), PCP-2 (or PTPRU), PTPrho (or PTPRT), and PTPkappa (or PTPRK). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Type IIb RPTPs mediate cell-cell adhesion though homophilic interactions; their ligand is an identical molecule on an adjacent cell. No heterophilic interactions between the subfamily members have been observed. They also commonly function as tumor suppressors. They contain an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350404 [Multi-domain]  Cd Length: 201  Bit Score: 165.66  E-value: 2.21e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  953 YINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVtNLVEVGRVKCCKYWPDDTE-IYKDIKVTLIETEL 1031
Cdd:cd14556     1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVML-NQLDPKDQSCPQYWPDEGSgTYGPIQVEFVSTTI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1032 LAEYVIRTFAVE--KRGVHEIREIRQFHFTGWPDHG-VPYHATGLLGFVRQV-KSKSPPSAGPLVVHCSAGAGRTGCFIV 1107
Cdd:cd14556    80 DEDVISRIFRLQntTRPQEGYRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVeKWQEQSGEGPIVVHCLNGVGRSGVFCA 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 157419150 1108 IDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHD 1149
Cdd:cd14556   160 ISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
1238-1447 3.03e-46

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type tyrosine-protein phosphatase A (PTPRA), also known as receptor-type tyrosine-protein phosphatase alpha (R-PTP-alpha), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA is a positive regulator of Src and Src family kinases via dephosphorylation of the Src-inhibitory tyrosine 527. Thus, it affects transformation and tumorigenesis, inhibition of proliferation, cell cycle arrest, integrin signaling, neuronal differentiation and outgrowth, and ion channel activity. It is also involved in interleukin-1 signaling in fibroblasts through its interaction with the focal adhesion targeting domain of focal adhesion kinase. PTPRA comprises a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350471 [Multi-domain]  Cd Length: 228  Bit Score: 166.37  E-value: 3.03e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1238 ESSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDP--AQLCPQYWPENGVHRHGPIQVEFV 1315
Cdd:cd14623    22 ENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEErgQEKCAQYWPSDGSVSYGDITIELK 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1316 SADLEEDIISRIFRIYNAArpQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEynGGEGRTVVHCLNGGGR 1395
Cdd:cd14623   102 KEEECESYTVRDLLVTNTR--ENKSRQIRQFHFHGWPEV-GIPSDGKGMINIIAAVQKQQQQ--SGNHPITVHCSAGAGR 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 157419150 1396 SGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 1447
Cdd:cd14623   177 TGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
922-1147 4.99e-46

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 167.58  E-value: 4.99e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  922 ENRMKNRYGNIIAYDHSRVRlqtiegdTNSDYINGNYIDGYhRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLV 1001
Cdd:COG5599    41 NGSPLNRFRDIQPYKETALR-------ANLGYLNANYIQVI-GNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDD 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1002 EVG--RVKCCKYWPDDTEIYK-DIKVTLIETELLAEYV-IRTFAVEKRGV-HEIREIRQFHFTGWPDHGVP----YHAtg 1072
Cdd:COG5599   113 EISkpKVKMPVYFRQDGEYGKyEVSSELTESIQLRDGIeARTYVLTIKGTgQKKIEIPVLHVKNWPDHGAIsaeaLKN-- 190
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157419150 1073 LLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDM--AEREGVVDIYNCVRELR-SRRVNMVQTEEQYVFI 1147
Cdd:COG5599   191 LADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSinALVQITLSVEEIVIDMRtSRNGGMVQTSEQLDVL 268
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
27-182 1.65e-45

MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 161.38  E-value: 1.65e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150    27 CLFDEPySTCGYSQSEGDDFNWEQVNTL---TKPTSDPWM--PSGSFMLVNASGRPEGQRAHLLLPQLKENDT-HCIDFH 100
Cdd:pfam00629    1 CDFEDG-NLCGWTQDSSDDFDWERVSGPsvkTGPSSDHTQgtGSGHFMYVDTSSGAPGQTARLLSPLLPPSRSpQCLRFW 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150   101 YFVSSksnSPPGLLNVYVKVNNGPLGNPIWNISGDPTRTWNRAELAISTFwPNFYQVIFEVI-TSGHQGYLAIDEVKVLG 179
Cdd:pfam00629   80 YHMSG---SGVGTLRVYVRENGGTLDTLLWSISGDQGPSWKEARVTLSSS-TQPFQVVFEGIrGGGSRGGIALDDISLSS 155

                   ...
gi 157419150   180 HPC 182
Cdd:pfam00629  156 GPC 158
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
900-1153 1.80e-44

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 163.63  E-value: 1.80e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  900 FKEEYESFFEGQSA-PWDSAKKDENRMKNRYGNIIAYDHSRVRLQTIEGdtNSDYINGNYIDGYHRPNHYIATQGPMQET 978
Cdd:PHA02742   28 LKEEHEHIMQEIVAfSCNESLELKNMKKCRYPDAPCFDRNRVILKIEDG--GDDFINASYVDGHNAKGRFICTQAPLEET 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  979 IYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYW---PDDTEIYKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQ 1055
Cdd:PHA02742  106 ALDFWQAIFQDQVRVIVMITKIMEDGKEACYPYWmphERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLDIKH 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1056 FHFTGWPDHGVPYHATGLLGFVRQV-----------KSKSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIY 1124
Cdd:PHA02742  186 FAYEDWPHGGLPRDPNKFLDFVLAVreadlkadvdiKGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLL 265
                         250       260
                  ....*....|....*....|....*....
gi 157419150 1125 NCVRELRSRRVNMVQTEEQYVFIHDAILE 1153
Cdd:PHA02742  266 SIVRDLRKQRHNCLSLPQQYIFCYFIVLI 294
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
1213-1451 1.29e-43

catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs) include three vertebrate members: LAR (or PTPRF), R-PTP-delta (or PTPRD), and R-PTP-sigma (or PTPRS). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules; they bind to distinct synaptic membrane proteins and are physiologically responsible for mediating presynaptic development by shaping various synaptic adhesion pathways. They play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. LAR-RPTPs contain an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350401 [Multi-domain]  Cd Length: 238  Bit Score: 159.10  E-value: 1.29e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1213 NHEKNRCMDILPPDRCLPFLITIDG-ESSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDP 1291
Cdd:cd14553     3 NKPKNRYANVIAYDHSRVILQPIEGvPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1292 AQL--CPQYWPENGVHRHGPIQVEFV-SADLEEDIIsRIFRIYNAARPQDgyRMVQQFQFLGWPMYrDTPVSKRSFLKLI 1368
Cdd:cd14553    83 RSRvkCDQYWPTRGTETYGLIQVTLLdTVELATYTV-RTFALHKNGSSEK--REVRQFQFTAWPDH-GVPEHPTPFLAFL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1369 RQVdkwQEEYNGGEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALEY 1448
Cdd:cd14553   159 RRV---KACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLEA 235

                  ...
gi 157419150 1449 LNS 1451
Cdd:cd14553   236 VTC 238
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
1218-1440 1.83e-43

catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar proteins; R3 subfamily receptor-type phosphotyrosine phosphatases (RPTP) are characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. Vertebrate members include receptor-type tyrosine-protein phosphatase-like O (PTPRO), J (PTPRJ), Q (PTPRQ), B (PTPRB), V (PTPRV) and H (PTPRH). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Most members are PTPs, except for PTPRQ, which dephosphorylates phosphatidylinositide substrates. PTPRV is characterized only in rodents; its function has been lost in humans. Both vertebrate and invertebrate R3 subfamily RPTPs are involved in the control of a variety of cellular processes, including cell growth, differentiation, mitotic cycle and oncogenic transformation.


Pssm-ID: 350396 [Multi-domain]  Cd Length: 222  Bit Score: 157.90  E-value: 1.83e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1218 RCMDILPPDRCLPFLITIDGES-SNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDPA--QL 1294
Cdd:cd14548     1 RYTNILPYDHSRVKLIPINEEEgSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKgrVK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1295 CPQYWPENGVHR-HGPIQVEFVSADLEEDIISRIFRIYNAarpqDGYRMVQQFQFLGWPMYR--DTPVSKRSFLKLIRQv 1371
Cdd:cd14548    81 CDHYWPFDQDPVyYGDITVTMLSESVLPDWTIREFKLERG----DEVRSVRQFHFTAWPDHGvpEAPDSLLRFVRLVRD- 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157419150 1372 dkwqeEYNGGEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKF 1440
Cdd:cd14548   156 -----YIKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIF 219
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
953-1149 6.16e-43

PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein phosphatase non-receptor type 23 (PTPN23), also called His domain-containing protein tyrosine phosphatase (HD-PTP) or protein tyrosine phosphatase TD14 (PTP-TD14), is a catalytically inactive member of the tyrosine-specific protein tyrosine phosphatase (PTP) family. Human PTPN23 may be involved in the regulation of small nuclear ribonucleoprotein assembly and pre-mRNA splicing by modifying the survival motor neuron (SMN) complex. It plays a role in ciliogenesis and is part of endosomal sorting complex required for transport (ESCRT) pathways. PTPN23 contains five domains: a BRO1-like domain that plays a role in endosomal sorting; a V-domain that interacts with Lys63-linked polyubiquitinated substrates; a central proline-rich region that might recruit SH3-containing proteins; a PTP-like domain; and a proteolytic degradation-targeting motif, also known as a PEST sequence.


Pssm-ID: 350387 [Multi-domain]  Cd Length: 205  Bit Score: 156.00  E-value: 6.16e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  953 YINGNYIDGY--HRPNhYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDD---TEIYKDIKVTLI 1027
Cdd:cd14539     1 YINASLIEDLtpYCPR-FIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTErgqALVYGAITVSLQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1028 ETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKS---KSPPSAGPLVVHCSAGAGRTGC 1104
Cdd:cd14539    80 SVRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHShylQQRSLQTPIVVHCSSGVGRTGA 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 157419150 1105 F-IVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHD 1149
Cdd:cd14539   160 FcLLYAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
902-1153 3.14e-42

catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein phosphatase non-receptor type 14 (PTPN14), also called protein-tyrosine phosphatase pez, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN14 is a potential tumor suppressor and plays a regulatory role in the Hippo and Wnt/beta-catenin signaling pathways. It contains an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350447 [Multi-domain]  Cd Length: 287  Bit Score: 156.70  E-value: 3.14e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  902 EEYESFFEGQSAP-------WDSAKKDENRMKNRYGNIIAYDHSRVRLQTIEgDTNSDYINGNYIDGYHRPN--HYIATQ 972
Cdd:cd14599    10 EEGMVFTEYEQIPkkkadgvFTTATLPENAERNRIREVVPYEENRVELVPTK-ENNTGYINASHIKVTVGGEewHYIATQ 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  973 GPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPD-----DTEIYKDIKVTLIETELLAEYVIRTFAVEKRGV 1047
Cdd:cd14599    89 GPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKlgskhSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLS 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1048 HEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKS----------KSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAER 1117
Cdd:cd14599   169 GQERTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSvrrhtnsmldSTKNCNPPIVVHCSAGVGRTGVVILTELMIGCLEH 248
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 157419150 1118 EGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 1153
Cdd:cd14599   249 NEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQ 284
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
1242-1443 8.51e-42

PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 subfamily of receptor-type phosphotyrosine phosphatases (RPTP) is composed of receptor-type tyrosine-protein phosphatase Z (PTPRZ) and G (PTPRG). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. They are type 1 integral membrane proteins consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350398 [Multi-domain]  Cd Length: 200  Bit Score: 152.48  E-value: 8.51e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1242 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDPAQLCPQYWPENGVHRH-GPIQVEFVSADL- 1319
Cdd:cd14550     1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNEDEPIYWPTKEKPLEcETFKVTLSGEDHs 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1320 ----EEDIISRIFRIYNAarpQDGYRM-VQQFQFLGWPmYRDTPVSkrSFLKLIRQVDKWQEEYNGGegrTVVHCLNGGG 1394
Cdd:cd14550    81 clsnEIRLIVRDFILEST---QDDYVLeVRQFQCPSWP-NPCSPIH--TVFELINTVQEWAQQRDGP---IVVHDRYGGV 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 157419150 1395 RSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYE 1443
Cdd:cd14550   152 QAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
953-1148 1.17e-40

protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis thaliana protein tyrosine phosphatase 1 (AtPTP1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. AtPTP1 dephosphorylates and inhibits MAP kinase 6 (MPK6) in non-oxidative stress conditions. Together with MAP kinase phosphatase 1 (MKP1) it expresses salicylic acid (SA) and camalexin biosynthesis, and therefore, modulating defense response.


Pssm-ID: 350496 [Multi-domain]  Cd Length: 206  Bit Score: 149.54  E-value: 1.17e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  953 YINGNYIDGYHRPNH--YIATQGPMQETIYDFWRMVWHENTASIIMVTNLVE-VGRVKCCKYWPD---DTEIYKDIKVTl 1026
Cdd:cd17658     1 YINASLVETPASESLpkFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDnYSTAKCADYFPAeenESREFGRISVT- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1027 IETELLAEYVI--RTFAVEKRGVHE-IREIRQFHFTGWPDHGVPyHATgllGFVRQVKSKS---PPSAGPLVVHCSAGAG 1100
Cdd:cd17658    80 NKKLKHSQHSItlRVLEVQYIESEEpPLSVLHIQYPEWPDHGVP-KDT---RSVRELLKRLygiPPSAGPIVVHCSAGIG 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 157419150 1101 RTGCFIVID-----IML-DMAeregVVDIYNCVRELRSRRVNMVQTEEQYVFIH 1148
Cdd:cd17658   156 RTGAYCTIHntirrILEgDMS----AVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
1205-1451 2.04e-40

PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type tyrosine-protein phosphatase N2 (PTPRN2 or R-PTP-N2), also called islet cell autoantigen-related protein (IAR), ICAAR, phogrin, or IA-2beta, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). It consists of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. It is mainly expressed in neuropeptidergic neurons and peptide-secreting endocrine cells, including insulin-producing pancreatic beta-cells. It may function as a phosphatidylinositol phosphatase to regulate insulin secretion. It is also required for normal accumulation of the neurotransmitters norepinephrine, dopamine and serotonin in the brain.


Pssm-ID: 350458 [Multi-domain]  Cd Length: 283  Bit Score: 151.36  E-value: 2.04e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1205 CSIALLPRNHEKNRCMDILPPDRCLPFLITIDGES-SNYINAA-LMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTS 1282
Cdd:cd14610    36 TNVAQREENVQKNRSLAVLPYDHSRIILKAENSHShSDYINASpIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCVV 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1283 VVMLNDV--DPAQLCPQYWPENGVHRHGPIQVEFVSADLE-EDIISRIFRIYNAARPQDgyRMVQQFQFLGWpMYRDTPV 1359
Cdd:cd14610   116 IVMLTPLaeNGVKQCYHYWPDEGSNLYHIYEVNLVSEHIWcEDFLVRSFYLKNLQTNET--RTVTQFHFLSW-NDQGVPA 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1360 SKRSFLKLIRQVDKWqeeYNGGEGRTVVHCLNGGGRSGTFCAISIVC-EMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQY 1438
Cdd:cd14610   193 STRSLLDFRRKVNKC---YRGRSCPIIVHCSDGAGRSGTYILIDMVLnKMAKGAKEIDIAATLEHLRDQRPGMVQTKEQF 269
                         250
                  ....*....|...
gi 157419150 1439 KFCYEVALEYLNS 1451
Cdd:cd14610   270 EFALTAVAEEVNA 282
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
1052-1153 2.88e-40

Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine phosphatases. Homologues detected by this profile and not by those of "PTPc" or "DSPc" are predicted to be protein phosphatases with a similar fold to DSPs and PTPs, yet with unpredicted specificities.


Pssm-ID: 214469 [Multi-domain]  Cd Length: 105  Bit Score: 144.42  E-value: 2.88e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150   1052 EIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPSA--GPLVVHCSAGAGRTGCFIVIDIMLDMAERE-GVVDIYNCVR 1128
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSEssGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80
                            90       100
                    ....*....|....*....|....*
gi 157419150   1129 ELRSRRVNMVQTEEQYVFIHDAILE 1153
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1052-1153 2.88e-40

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 144.42  E-value: 2.88e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150   1052 EIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPSA--GPLVVHCSAGAGRTGCFIVIDIMLDMAERE-GVVDIYNCVR 1128
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSEssGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80
                            90       100
                    ....*....|....*....|....*
gi 157419150   1129 ELRSRRVNMVQTEEQYVFIHDAILE 1153
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
1213-1447 3.29e-40

catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type tyrosine-protein phosphatase F (PTPRF), also known as leukocyte common antigen related (LAR), is the prototypical member of the LAR family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRF/LAR plays a role for LAR in cadherin complexes where it associates with and dephosphorylates beta-catenin, a pathway which may be critical for cadherin complex stability and cell-cell association. It also regulates focal adhesions through cyclin-dependent kinase-1 and is involved in axon guidance in the developing nervous system. It also functions in regulating insulin signaling. PTPRF contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350474 [Multi-domain]  Cd Length: 276  Bit Score: 150.57  E-value: 3.29e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1213 NHEKNRCMDILPPDRCLPFLITIDG-ESSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDP 1291
Cdd:cd14626    41 NKPKNRYANVIAYDHSRVILTSVDGvPGSDYINANYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEE 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1292 AQL--CPQYWPENGVHRHGPIQVEFVSADLEEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMY--RDTPVSKRSFLKL 1367
Cdd:cd14626   121 KSRvkCDQYWPIRGTETYGMIQVTLLDTVELATYSVRTFALYKNGSSEK--REVRQFQFMAWPDHgvPEYPTPILAFLRR 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1368 IRQVDKwqeeynGGEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 1447
Cdd:cd14626   199 VKACNP------PDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLE 272
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
920-1151 1.12e-38

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 147.48  E-value: 1.12e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  920 KDENRMKNRYGNIIAYDHSRV-------------------RLQTIEGDTNSDYINGNYIDGYHRPNHYIATQGPMQETIY 980
Cdd:PHA02746   48 KKENLKKNRFHDIPCWDHSRVvinaheslkmfdvgdsdgkKIEVTSEDNAENYIHANFVDGFKEANKFICAQGPKEDTSE 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  981 DFWRMVWHENTASIIMVTNlVEVGRVKCCKYW--PDDTEI-YKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFH 1057
Cdd:PHA02746  128 DFFKLISEHESQVIVSLTD-IDDDDEKCFELWtkEEDSELaFGRFVAKILDIIEELSFTKTRLMITDKISDTSREIHHFW 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1058 FTGWPDHGVPYHATGLLGFVRQVKSK----------SPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCV 1127
Cdd:PHA02746  207 FPDWPDNGIPTGMAEFLELINKVNEEqaelikqadnDPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIV 286
                         250       260
                  ....*....|....*....|....
gi 157419150 1128 RELRSRRVNMVQTEEQYVFIHDAI 1151
Cdd:PHA02746  287 LKIRKQRHSSVFLPEQYAFCYKAL 310
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
1221-1447 2.98e-38

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type tyrosine-protein phosphatase E (PTPRE), also known as receptor-type tyrosine-protein phosphatase epsilon (R-PTP-epsilon), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. The PTPRE gene contains two distinct promoters that generate the two major isoforms: transmembrane (receptor type RPTPe or PTPeM) and cytoplasmic (cyt-PTPe or PTPeC). Receptor type RPTPe plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells, and may also play a role in osteoclast formation and function. It also negatively regulates PDGFRbeta-mediated signaling pathways that are crucial for the pathogenesis of atherosclerosis. cyt-PTPe acts as a negative regulator of insulin receptor signaling in skeletal muscle. It regulates insulin-induced phosphorylation of proteins downstream of the insulin receptor. Receptor type RPTPe contains a small extracellular region, a single transmembrane segment, and an intracellular region two tandem catalytic PTP domains. This model represents the first PTP domain (repeat 1).


Pssm-ID: 350468 [Multi-domain]  Cd Length: 229  Bit Score: 143.16  E-value: 2.98e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1221 DILPPDRCLPFLITIDG-ESSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVD--PAQLCPQ 1297
Cdd:cd14620     3 NILPYDHSRVILSQLDGiPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKerKEEKCYQ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1298 YWPENGVHRHGPIQVEFVSADLEEDIISRIFRI-YNAARPQDGYRMVQQFQFLGWPMYRD--TPVSKRSFLKLIRQVDKW 1374
Cdd:cd14620    83 YWPDQGCWTYGNIRVAVEDCVVLVDYTIRKFCIqPQLPDGCKAPRLVTQLHFTSWPDFGVpfTPIGMLKFLKKVKSVNPV 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157419150 1375 QEeynggeGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 1447
Cdd:cd14620   163 HA------GPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
1217-1446 5.05e-38

catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type tyrosine-protein phosphatase V (PTPRV or R-PTP-V), also known as embryonic stem cell protein-tyrosine phosphatase (ES cell phosphatase) or osteotesticular protein-tyrosine phosphatase (OST-PTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRV is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. In rodents, it may play a role in the maintenance of pluripotency and may function in signaling pathways during bone remodeling. It is the only PTP whose function has been lost between rodent and human. The human OST-PTP gene is a pseudogene.


Pssm-ID: 350466 [Multi-domain]  Cd Length: 230  Bit Score: 142.77  E-value: 5.05e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1217 NRCMDILPPDRCLPFLITIDGES-SNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDV--DPAQ 1293
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQLGGEPhSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGmeNGRV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1294 LCPQYWPENGVH-RHGPIQVEFVSADLEEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMYR--DTPVSKRSFLKLIRQ 1370
Cdd:cd14618    81 LCDHYWPSESTPvSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKE--RRVKHLHYTAWPDHGipESTSSLMAFRELVRE 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157419150 1371 vdkwQEEYNGGEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVAL 1446
Cdd:cd14618   159 ----HVQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
1163-1448 7.34e-38

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type tyrosine-protein phosphatase A (PTPRA), also known as receptor-type tyrosine-protein phosphatase alpha (R-PTP-alpha), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA is a positive regulator of Src and Src family kinases via dephosphorylation of the Src-inhibitory tyrosine 527. Thus, it affects transformation and tumorigenesis, inhibition of proliferation, cell cycle arrest, integrin signaling, neuronal differentiation and outgrowth, and ion channel activity. It is also involved in interleukin-1 signaling in fibroblasts through its interaction with the focal adhesion targeting domain of focal adhesion kinase. PTPRA comprises a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the first catalytic PTP domain (repeat 1).


Pssm-ID: 350469 [Multi-domain]  Cd Length: 296  Bit Score: 144.40  E-value: 7.34e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1163 PASQVRSLYYDMNKLDPQTNSsQIKEEFRTLnmvtPTLRVE-DCSIALLPRNHEKNRCMDILPPDRCLPFLITIDG-ESS 1240
Cdd:cd14621     6 PPLPVDKLEEEINRRMADDNK-LFREEFNAL----PACPIQaTCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGvPDS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1241 NYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDPAQ--LCPQYWPENGVHRHGPIQVEFVSAD 1318
Cdd:cd14621    81 DYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKecKCAQYWPDQGCWTYGNIRVSVEDVT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1319 LEEDIISRIFRIYNAA-----RPQdgyRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEYNGGegrTVVHCLNGG 1393
Cdd:cd14621   161 VLVDYTVRKFCIQQVGdvtnkKPQ---RLITQFHFTSWPDF-GVPFTPIGMLKFLKKVKNCNPQYAGA---IVVHCSAGV 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 157419150 1394 GRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALEY 1448
Cdd:cd14621   234 GRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEH 288
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
1205-1451 1.15e-37

PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type tyrosine-protein phosphatase-like N (PTPRN or R-PTP-N), also called islet cell antigen 512 (ICA512) or PTP IA-2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). It consists of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. PTPRN is located in secretory granules of neuroendocrine cells and is involved in the generation, cargo storage, traffic, exocytosis and recycling of insulin secretory granules, as well as in beta-cell proliferation. It is a major autoantigen in type 1 diabetes and is involved in the regulation of insulin secretion.


Pssm-ID: 350457 [Multi-domain]  Cd Length: 281  Bit Score: 143.25  E-value: 1.15e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1205 CSIALLPRNHEKNRCMDILPPDRC-LPFLITIDGESSNYINAA-LMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTS 1282
Cdd:cd14609    34 CSTAQGEANVKKNRNPDFVPYDHArIKLKAESNPSRSDYINASpIIEHDPRMPAYIATQGPLSHTIADFWQMVWENGCTV 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1283 VVMLNDV--DPAQLCPQYWPENGVHRHGPIQVEFVSADLE-EDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMyRDTPV 1359
Cdd:cd14609   114 IVMLTPLveDGVKQCDRYWPDEGSSLYHIYEVNLVSEHIWcEDFLVRSFYLKNVQTQET--RTLTQFHFLSWPA-EGIPS 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1360 SKRSFLKLIRQVDKWqeeYNGGEGRTVVHCLNGGGRSGTFCAISIVC-EMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQY 1438
Cdd:cd14609   191 STRPLLDFRRKVNKC---YRGRSCPIIVHCSDGAGRTGTYILIDMVLnRMAKGVKEIDIAATLEHVRDQRPGMVRTKDQF 267
                         250
                  ....*....|...
gi 157419150 1439 KFCYEVALEYLNS 1451
Cdd:cd14609   268 EFALTAVAEEVNA 280
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
953-1153 2.10e-37

catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein phosphatase non-receptor type 21 (PTPN21), also called protein-tyrosine phosphatase D1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN21 is a component of a multivalent scaffold complex nucleated by focal adhesion kinase (FAK) at specific intracellular sites. It promotes cytoskeleton events that induce cell adhesion and migration by modulating Src-FAK signaling. It can also selectively associate with and stimulate Tec family kinases and modulate Stat3 activation. Human PTPN21 may also play a pathologic role in gastrointestinal tract tumorigenesis. PTPN21 contains an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350446 [Multi-domain]  Cd Length: 220  Bit Score: 140.50  E-value: 2.10e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  953 YINGNYIDGYHRPNH--YIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWP-----DDTEIYKDIKVT 1025
Cdd:cd14598     1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPrlgsrHNTVTYGRFKIT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1026 LIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKS-----------KSPPSagPLVVH 1094
Cdd:cd14598    81 TRFRTDSGCYATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSvrrhtnstidpKSPNP--PVLVH 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 157419150 1095 CSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 1153
Cdd:cd14598   159 CSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQ 217
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
1210-1452 4.07e-37

catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type tyrosine-protein phosphatase D (PTPRD), also known as receptor-type tyrosine-protein phosphatase delta (R-PTP-delta), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules that play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. PTPRD is involved in pre-synaptic differentiation through interaction with SLITRK2. It contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350472 [Multi-domain]  Cd Length: 284  Bit Score: 141.79  E-value: 4.07e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1210 LPRNHEKNRCMDILPPDRCLPFLITIDG-ESSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLND 1288
Cdd:cd14624    44 LEVNKPKNRYANVIAYDHSRVLLSAIEGiPGSDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTK 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1289 VDPAQL--CPQYWPENGVHRHGPIQVEFVSADLEEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMYrDTPVSKRSFLK 1366
Cdd:cd14624   124 LEERSRvkCDQYWPSRGTETYGLIQVTLLDTVELATYCVRTFALYKNGSSEK--REVRQFQFTAWPDH-GVPEHPTPFLA 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1367 LIRQVDKWQEEyngGEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVAL 1446
Cdd:cd14624   201 FLRRVKTCNPP---DAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALL 277

                  ....*.
gi 157419150 1447 EYLNSG 1452
Cdd:cd14624   278 EAVTCG 283
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
1210-1447 5.65e-37

catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type tyrosine-protein phosphatase S (PTPRS), also known as receptor-type tyrosine-protein phosphatase sigma (R-PTP-sigma), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRS is a receptor for glycosaminoglycans, including heparan sulfate proteoglycan and neural chondroitin sulfate proteoglycans (CSPGs), which present a barrier to axon regeneration. It also plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2. PTPRS contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350473 [Multi-domain]  Cd Length: 282  Bit Score: 141.38  E-value: 5.65e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1210 LPRNHEKNRCMDILPPDRCLPFLITIDG-ESSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLND 1288
Cdd:cd14625    44 LEVNKPKNRYANVIAYDHSRVILQPIEGiMGSDYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTK 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1289 VDPAQL--CPQYWPENGVHRHGPIQVEFVSADLEEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMYrDTPVSKRSFLK 1366
Cdd:cd14625   124 LEEKSRikCDQYWPSRGTETYGMIQVTLLDTIELATFCVRTFSLHKNGSSEK--REVRQFQFTAWPDH-GVPEYPTPFLA 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1367 LIRQVDKWQEEyngGEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVAL 1446
Cdd:cd14625   201 FLRRVKTCNPP---DAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALL 277

                  .
gi 157419150 1447 E 1447
Cdd:cd14625   278 E 278
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
1242-1450 1.02e-36

PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type tyrosine-protein phosphatase-like N (PTPRN) and N2 (PTPRN2) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). They consist of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. They are mainly expressed in neuropeptidergic neurons and peptide-secreting endocrine cells, including insulin-producing pancreatic beta-cells, and are involved in involved in the generation, cargo storage, traffic, exocytosis and recycling of insulin secretory granules, as well as in beta-cell proliferation. They also are major autoantigens in type 1 diabetes and are involved in the regulation of insulin secretion.


Pssm-ID: 350394 [Multi-domain]  Cd Length: 208  Bit Score: 137.96  E-value: 1.02e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1242 YINAA-LMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVML-----NDVDpaqLCPQYWPENGVHRHGPIQVEFV 1315
Cdd:cd14546     1 YINAStIYDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLtrlqeNGVK---QCARYWPEEGSEVYHIYEVHLV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1316 SADL-EEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPmYRDTPVSKRSFLKLIRQVDKwqeEYNGGEGRTVVHCLNGGG 1394
Cdd:cd14546    78 SEHIwCDDYLVRSFYLKNLQTSET--RTVTQFHFLSWP-DEGIPASAKPLLEFRRKVNK---SYRGRSCPIVVHCSDGAG 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 157419150 1395 RSGTFCAISIVCE-MLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALEYLN 1450
Cdd:cd14546   152 RTGTYILIDMVLNrMAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAEEVN 208
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
1242-1443 1.80e-36

catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 subfamily of receptor-type phosphotyrosine phosphatases (RPTP) is composed of receptor-type tyrosine-protein phosphatase Z (PTPRZ) and G (PTPRG). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. They are type 1 integral membrane proteins consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350397 [Multi-domain]  Cd Length: 204  Bit Score: 137.10  E-value: 1.80e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1242 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVML-NDVDPAQL-CPQYWPENGVHRHGPIQVEFVSADL 1319
Cdd:cd14549     1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMItNLVERGRRkCDQYWPKEGTETYGNIQVTLLSTEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1320 EEDIISRIFRIYNA----ARPQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQeeyNGGEGRTVVHCLNGGGR 1395
Cdd:cd14549    81 LATYTVRTFSLKNLklkkVKGRSSERVVYQYHYTQWPDH-GVPDYTLPVLSFVRKSSAAN---PPGAGPIVVHCSAGVGR 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 157419150 1396 SGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYE 1443
Cdd:cd14549   157 TGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
1242-1443 4.60e-36

fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae protein-tyrosine phosphatases 1 (PTP1) and 2 (PTP2), Schizosaccharomyces pombe PTP1, PTP2, and PTP3, and similar fungal proteins. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. PTP2, together with PTP3, is the major phosphatase that dephosphorylates and inactivates the MAP kinase HOG1 and also modulates its subcellular localization.


Pssm-ID: 350509 [Multi-domain]  Cd Length: 212  Bit Score: 136.22  E-value: 4.60e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1242 YINAALMD-SYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDPAQL--CPQYWPENGVH-RHGPIQVEFVSA 1317
Cdd:cd18533     1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGRekCDQYWPSGEYEgEYGDLTVELVSE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1318 DLEED--IISRIFRIynaARPQDGYRMVQQFQFLGWPmyrD--TPVSKRSFLKLIRQVDKWQEEyNGGEGRTVVHCLNGG 1393
Cdd:cd18533    81 EENDDggFIVREFEL---SKEDGKVKKVYHIQYKSWP---DfgVPDSPEDLLTLIKLKRELNDS-ASLDPPIIVHCSAGV 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 157419150 1394 GRSGTFCAISIVCEMLRHQRTVD---------VFHAVKTLRNNKPNMVDLLDQYKFCYE 1443
Cdd:cd18533   154 GRTGTFIALDSLLDELKRGLSDSqdledsedpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
1242-1447 1.41e-35

catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The type II (or R2B) subfamily of receptor protein tyrosine phosphatases (RPTPs) include the prototypical member PTPmu (or PTPRM), PCP-2 (or PTPRU), PTPrho (or PTPRT), and PTPkappa (or PTPRK). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Type IIb RPTPs mediate cell-cell adhesion though homophilic interactions; their ligand is an identical molecule on an adjacent cell. No heterophilic interactions between the subfamily members have been observed. They also commonly function as tumor suppressors. They contain an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350403 [Multi-domain]  Cd Length: 204  Bit Score: 134.66  E-value: 1.41e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1242 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVML-NDVDPAQL-CPQYWPENgVHRHGPIQVEFVSADL 1319
Cdd:cd14555     1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVtNLVEVGRVkCSRYWPDD-TEVYGDIKVTLVETEP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1320 EEDIISRIFRIynAARPQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVdkwQEEYNGGEGRTVVHCLNGGGRSGTF 1399
Cdd:cd14555    80 LAEYVVRTFAL--ERRGYHEIREVRQFHFTGWPDH-GVPYHATGLLGFIRRV---KASNPPSAGPIVVHCSAGAGRTGCY 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 157419150 1400 CAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 1447
Cdd:cd14555   154 IVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
1217-1447 5.53e-35

catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type tyrosine-protein phosphatase J (PTPRJ or R-PTP-J), also known as receptor-type tyrosine-protein phosphatase eta (R-PTP-eta) or density-enhanced phosphatase 1 (DEP-1) OR CD148, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRJ is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats (eight in PTPRJ) and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed in various cell types including epithelial, hematopoietic, and endothelial cells. It plays a role in cell adhesion, migration, proliferation and differentiation. It dephosphorylates or contributes to the dephosphorylation of various substrates including protein kinases such as FLT3, PDGFRB, MET, RET (variant MEN2A), VEGFR-2, LYN, SRC, MAPK1, MAPK3, and EGFR, as well as PIK3R1 and PIK3R2.


Pssm-ID: 350463 [Multi-domain]  Cd Length: 229  Bit Score: 133.79  E-value: 5.53e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1217 NRCMDILPPDRCLPFLITIDGESSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLND-VDPAQL- 1294
Cdd:cd14615     1 NRYNNVLPYDISRVKLSVQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKcVEQGRTk 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1295 CPQYWPENGVHRHGPIQVEFVSADLEEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPmyrDTPVSKRS-----FLKLIR 1369
Cdd:cd14615    81 CEEYWPSKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNES--RTVRHFHFTSWP---DHGVPETTdllinFRHLVR 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157419150 1370 QVDKwqeeYNGGEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 1447
Cdd:cd14615   156 EYMK----QNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCALD 229
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
1217-1440 6.81e-35

catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; The kinase interaction motif (KIM) family of protein-tyrosine phosphatases (PTPs) includes tyrosine-protein phosphatases non-receptor type 7 (PTPN7) and non-receptor type 5 (PTPN5), and protein-tyrosine phosphatase receptor type R (PTPRR). PTPN7 is also called hematopoietic protein-tyrosine phosphatase (HePTP) while PTPN5 is also called striatal-enriched protein-tyrosine phosphatase (STEP). They belong to the family of classical tyrosine-specific PTPs (EC 3.1.3.48) that catalyze the dephosphorylation of phosphotyrosine peptides. KIM-PTPs are characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. They are highly specific to the MAPKs ERK1/2 (extracellular-signal-regulated kinase 1/2) and p38, over JNK (c-Jun N-terminal kinase); they dephosphorylate these kinases and thereby critically modulate cell proliferation and differentiation.


Pssm-ID: 350395 [Multi-domain]  Cd Length: 224  Bit Score: 133.29  E-value: 6.81e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1217 NRCMDILPPDR---CLPflITIDGESSNYINAALMDSYK-QPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVML-NDVDP 1291
Cdd:cd14547     1 NRYKTILPNEHsrvCLP--SVDDDPLSSYINANYIRGYDgEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMItNLTEA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1292 AQLCPQYWPENGVHRHGPIQVEFVSADLEEDIISRIFRIYNaarpQDGYRMVQQFQFLGWPMYRdTPVSKRSFLKLIRQV 1371
Cdd:cd14547    79 KEKCAQYWPEEENETYGDFEVTVQSVKETDGYTVRKLTLKY----GGEKRYLKHYWYTSWPDHK-TPEAAQPLLSLVQEV 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157419150 1372 DKWQEEYNGgEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKF 1440
Cdd:cd14547   154 EEARQTEPH-RGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEF 221
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
1242-1443 8.83e-35

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; Receptor-type tyrosine-protein phosphatase A (PTPRA) and E (PTPRE) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA and PTPRE share several functions including regulation of Src family kinases and voltage-gated potassium (Kv) channels. They both contain a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the first catalytic PTP domain (repeat 1).


Pssm-ID: 350399 [Multi-domain]  Cd Length: 202  Bit Score: 132.34  E-value: 8.83e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1242 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDP--AQLCPQYWPENGVHRHGPIQVEFVSADL 1319
Cdd:cd14551     1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKErkEKKCSQYWPDQGCWTYGNLRVRVEDTVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1320 EEDIISRIF------RIYNAARPqdgyRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEYNGGegrTVVHCLNGG 1393
Cdd:cd14551    81 LVDYTTRKFciqkvnRGIGEKRV----RLVTQFHFTSWPDF-GVPFTPIGMLKFLKKVKSANPPRAGP---IVVHCSAGV 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 157419150 1394 GRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYE 1443
Cdd:cd14551   153 GRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
1208-1443 1.60e-34

catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type tyrosine-protein phosphatase O (PTPRO or R-PTP-O), also known as glomerular epithelial protein 1 or protein tyrosine phosphatase U2 (PTP-U2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRO is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is essential for sustaining the structure and function of foot processes by regulating tyrosine phosphorylation of podocyte proteins. It has been identified as a synaptic cell adhesion molecule (CAM) that serves as a potent initiator of synapse formation. It is also a tumor suppressor in several types of cancer, such as hepatocellular carcinoma, lung cancer, and breast cancer.


Pssm-ID: 350462 [Multi-domain]  Cd Length: 245  Bit Score: 133.09  E-value: 1.60e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1208 ALLPRNHEKNRCMDILPPDRCLPFLITI-DGESSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVML 1286
Cdd:cd14614     7 ADLPVNRCKNRYTNILPYDFSRVKLVSMhEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVML 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1287 NDVDPAQL--CPQYWP--ENGVHrHGPIQVEFVSADLEEDIISRIFRIYNAARPQDgyrmVQQFQFLGWPMY----RDTP 1358
Cdd:cd14614    87 TQCNEKRRvkCDHYWPftEEPVA-YGDITVEMLSEEEQPDWAIREFRVSYADEVQD----VMHFNYTAWPDHgvptANAA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1359 VSKRSFLKLIRQvdkwqeEYNGGEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQY 1438
Cdd:cd14614   162 ESILQFVQMVRQ------QAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQY 235

                  ....*
gi 157419150 1439 KFCYE 1443
Cdd:cd14614   236 IFIHQ 240
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
1213-1447 1.61e-34

catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350478 [Multi-domain]  Cd Length: 237  Bit Score: 132.84  E-value: 1.61e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1213 NHEKNRCMDILPPDRCLPFLITIDGES-SNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVML-NDVD 1290
Cdd:cd14630     3 NRNKNRYGNIISYDHSRVRLQLLDGDPhSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVtNLVE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1291 PAQL-CPQYWPENgVHRHGPIQVEFVSADLEEDIISRIFRIYNAARPQdgYRMVQQFQFLGWPMYrDTPVSKRSFLKLIR 1369
Cdd:cd14630    83 VGRVkCVRYWPDD-TEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHE--IREIRQFHFTSWPDH-GVPCYATGLLGFVR 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157419150 1370 QVdKWQEEYNGGEgrTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 1447
Cdd:cd14630   159 QV-KFLNPPDAGP--IVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILE 233
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
1217-1449 2.19e-34

catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type tyrosine-protein phosphatase H (PTPRH or R-PTP-H), also known as stomach cancer-associated protein tyrosine phosphatase 1 (SAP-1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRH is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is localized specifically at microvilli of the brush border in gastrointestinal epithelial cells. It plays a role in intestinal immunity by regulating CEACAM20 through tyrosine dephosphorylation. It is also a negative regulator of integrin-mediated signaling and may contribute to contact inhibition of cell growth and motility.


Pssm-ID: 350467 [Multi-domain]  Cd Length: 233  Bit Score: 132.32  E-value: 2.19e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1217 NRCMDILPPDRCLPFLITIDGE-SSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDPAQL- 1294
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKPIHEEpGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRv 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1295 -CPQYWPENGVH-RHGPIQVEFVSADLEEDIISRIFRIYNAArpQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVD 1372
Cdd:cd14619    81 kCEHYWPLDYTPcTYGHLRVTVVSEEVMENWTVREFLLKQVE--EQKTLSVRHFHFTAWPDH-GVPSSTDTLLAFRRLLR 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157419150 1373 KWQEEYNGGeGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALEYL 1449
Cdd:cd14619   158 QWLDQTMSG-GPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDFL 233
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
953-1153 2.84e-34

PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350482 [Multi-domain]  Cd Length: 206  Bit Score: 130.91  E-value: 2.84e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  953 YINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVtNLVEVGRVkCCKYWPDDTE-IYKDIKVTLIETEL 1031
Cdd:cd14634     1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVML-NEMDAAQL-CMQYWPEKTScCYGPIQVEFVSADI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1032 LAEYVIRTFAV--EKRGVHEIREIRQFHFTGWPDH-GVPYHATGLLGFVRQV---KSKSPPSAGPLVVHCSAGAGRTGCF 1105
Cdd:cd14634    79 DEDIISRIFRIcnMARPQDGYRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLekwQEQYDGREGRTVVHCLNGGGRSGTF 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 157419150 1106 IVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 1153
Cdd:cd14634   159 CAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
953-1153 1.21e-33

PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350484 [Multi-domain]  Cd Length: 206  Bit Score: 129.37  E-value: 1.21e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  953 YINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMvtnLVEVGRVKCC-KYWPDDTEI-YKDIKVTLIETE 1030
Cdd:cd14636     1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVM---LNEVDLAQGCpQYWPEEGMLrYGPIQVECMSCS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1031 LLAEYVIRTFAV--EKRGVHEIREIRQFHFTGWPDH-GVPYHATGLLGFVRQV---KSKSPPSAGPLVVHCSAGAGRTGC 1104
Cdd:cd14636    78 MDCDVISRIFRIcnLTRPQEGYLMVQQFQYLGWASHrEVPGSKRSFLKLILQVekwQEECDEGEGRTIIHCLNGGGRSGM 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 157419150 1105 FIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 1153
Cdd:cd14636   158 FCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
1236-1447 1.58e-33

catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350479 [Multi-domain]  Cd Length: 218  Bit Score: 129.37  E-value: 1.58e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1236 DGESSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVML-NDVDPAQL-CPQYWPENgVHRHGPIQVE 1313
Cdd:cd14631     9 DDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVtNLVEVGRVkCYKYWPDD-TEVYGDFKVT 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1314 FVSADLEEDIISRIFRIynAARPQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVdkwQEEYNGGEGRTVVHCLNGG 1393
Cdd:cd14631    88 CVEMEPLAEYVVRTFTL--ERRGYNEIREVKQFHFTGWPDH-GVPYHATGLLSFIRRV---KLSNPPSAGPIVVHCSAGA 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 157419150 1394 GRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 1447
Cdd:cd14631   162 GRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
1211-1447 3.44e-33

catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein phosphatase non-receptor type 18 (PTPN18), also called brain-derived phosphatase, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN18 regulates HER2-mediated cellular functions through defining both its phosphorylation and ubiquitination states. The N-terminal catalytic PTP domain of PTPN18 blocks lysosomal routing and delays the degradation of HER2 by dephosphorylation, and its C-terminal PEST domain promotes K48-linked HER2 ubiquitination and its destruction via the proteasome pathway.


Pssm-ID: 350451 [Multi-domain]  Cd Length: 266  Bit Score: 129.95  E-value: 3.44e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1211 PRNHEKNRCMDILPPDR---CLPFLItiDGESSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVM-L 1286
Cdd:cd14603    28 KENVKKNRYKDILPYDQtrvILSLLQ--EEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVILMaC 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1287 NDVDPA-QLCPQYWP-ENGVHRHGPIQVEFVSAD-LEEDIISRIFRIynaaRPQDGYRMVQQFQFLGWPmYRDTPVSKRS 1363
Cdd:cd14603   106 REIEMGkKKCERYWAqEQEPLQTGPFTITLVKEKrLNEEVILRTLKV----TFQKESRSVSHFQYMAWP-DHGIPDSPDC 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1364 FLKLIRQVDKWQeeyngGEGRT--VVHCLNGGGRSGTFCAISIVCEMLRHQRTVD---VFHAVKTLRNNKPNMVDLLDQY 1438
Cdd:cd14603   181 MLAMIELARRLQ-----GSGPEplCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPdfsIFDVVLEMRKQRPAAVQTEEQY 255

                  ....*....
gi 157419150 1439 KFCYEVALE 1447
Cdd:cd14603   256 EFLYHTVAQ 264
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
1213-1447 1.24e-32

catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350481 [Multi-domain]  Cd Length: 273  Bit Score: 128.62  E-value: 1.24e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1213 NHEKNRCMDILPPDRCLPFLITIDGES-SNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVML-NDVD 1290
Cdd:cd14633    40 NRMKNRYGNIIAYDHSRVRLQPIEGETsSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVtNLVE 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1291 PAQL-CPQYWPENgVHRHGPIQVEFVSADLEEDIISRIFRIynAARPQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIR 1369
Cdd:cd14633   120 VGRVkCCKYWPDD-TEIYKDIKVTLIETELLAEYVIRTFAV--EKRGVHEIREIRQFHFTGWPDH-GVPYHATGLLGFVR 195
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157419150 1370 QVdkwQEEYNGGEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 1447
Cdd:cd14633   196 QV---KSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 270
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
953-1147 1.30e-32

PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 subfamily of receptor-type phosphotyrosine phosphatases (RPTP) is composed of receptor-type tyrosine-protein phosphatase Z (PTPRZ) and G (PTPRG). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. They are type 1 integral membrane proteins consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350398 [Multi-domain]  Cd Length: 200  Bit Score: 125.90  E-value: 1.30e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  953 YINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGrvKCCKYWPD-DTEIYKD-IKVTLIETE 1030
Cdd:cd14550     1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWPTkEKPLECEtFKVTLSGED 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1031 LL-----AEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATglLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCF 1105
Cdd:cd14550    79 HSclsneIRLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPIHTV--FELINTVQEWAQQRDGPIVVHDRYGGVQAATF 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 157419150 1106 IVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFI 1147
Cdd:cd14550   157 CALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFL 198
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
1242-1447 2.11e-32

catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type tyrosine-protein phosphatase U (PTPRU), also known as pancreatic carcinoma phosphatase 2 (PCP-2), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRU/PCP-2 is the most distant member of the type IIb subfamily and may have a distinct biological function other than cell-cell aggregation. It localizes to the adherens junctions and directly binds and dephosphorylates beta-catenin, and regulates the balance between signaling and adhesive beta-catenin. It plays an important role in the maintenance of epithelial integrity. PTPRU contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350480 [Multi-domain]  Cd Length: 205  Bit Score: 125.55  E-value: 2.11e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1242 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLND-VDPAQL-CPQYWPENGvHRHGPIQVEFVSADL 1319
Cdd:cd14632     1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKlVEVGRVkCSKYWPDDS-DTYGDIKITLLKTET 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1320 EEDIISRIFriynaARPQDGYRM---VQQFQFLGWPMYrDTPVSKRSFLKLIRQVdkwQEEYNGGEGRTVVHCLNGGGRS 1396
Cdd:cd14632    80 LAEYSVRTF-----ALERRGYSArheVKQFHFTSWPEH-GVPYHATGLLAFIRRV---KASTPPDAGPVVVHCSAGAGRT 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 157419150 1397 GTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 1447
Cdd:cd14632   151 GCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
1211-1449 3.42e-32

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 128.58  E-value: 3.42e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1211 PRNHEKNRCMDILPPDRCLPFLITIDGESSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLN--- 1287
Cdd:PHA02747   49 PENQPKNRYWDIPCWDHNRVILDSGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTptk 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1288 DVDPAQLCPQYW--PENGVHRHGPIQVEFVSADLEEDIISRIFRIYNaaRPQDGYRMVQQFQFLGWPMYrDTPVSKRSFL 1365
Cdd:PHA02747  129 GTNGEEKCYQYWclNEDGNIDMEDFRIETLKTSVRAKYILTLIEITD--KILKDSRKISHFQCSEWFED-ETPSDHPDFI 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1366 KLIRQVD----KWQEEYNGGEG---RTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQY 1438
Cdd:PHA02747  206 KFIKIIDinrkKSGKLFNPKDAllcPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDY 285
                         250
                  ....*....|....
gi 157419150 1439 KF---CYEVALEYL 1449
Cdd:PHA02747  286 LFiqpGYEVLHYFL 299
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
1216-1444 1.29e-31

catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein phosphatase non-receptor type 5 (PTPN5), also called striatum-enriched protein-tyrosine phosphatase (STEP) or neural-specific PTP, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN5/STEP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. It is a CNS-enriched protein that regulates key signaling proteins required for synaptic strengthening, as well as NMDA and AMPA receptor trafficking. PTPN5 is implicated in multiple neurologic and neuropsychiatric disorders, such as Alzheimer's disease, Parkinson's disease, schizophrenia, and fragile X syndrome.


Pssm-ID: 350461 [Multi-domain]  Cd Length: 258  Bit Score: 124.97  E-value: 1.29e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1216 KNRCMDILPPDRCLPFLITIDGES--SNYINAALMDSY-KQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDPA 1292
Cdd:cd14613    28 KNRYKTILPNPHSRVCLTSPDQDDplSSYINANYIRGYgGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEM 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1293 -QLCPQYWPENGVHRHGpIQVEFVSADLEEDIISRIFRIynaaRPQDGYRMVQQFQFLGWPMYRdTPVSKRSFLKLIRQV 1371
Cdd:cd14613   108 nEKCTEYWPEEQVTYEG-IEITVKQVIHADDYRLRLITL----KSGGEERGLKHYWYTSWPDQK-TPDNAPPLLQLVQEV 181
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157419150 1372 DKWQEEYNGGEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEV 1444
Cdd:cd14613   182 EEARQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHHV 254
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
1205-1447 1.79e-31

catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1), also called protein-tyrosine phosphatase 1B (PTP-1B), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1/PTP-1B is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It contains an N-terminal catalytic PTP domain, followed by two tandem proline-rich motifs that mediate interaction with SH3-domain-containing proteins, and a small hydrophobic stretch that localizes the enzyme to the endoplasmic reticulum (ER). It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor.


Pssm-ID: 350456 [Multi-domain]  Cd Length: 277  Bit Score: 125.14  E-value: 1.79e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1205 CSIALLPRNHEKNRCMDILPPDRCLpflITIDGESSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVV 1284
Cdd:cd14608    17 CRVAKLPKNKNRNRYRDVSPFDHSR---IKLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVV 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1285 MLNDV--DPAQLCPQYWPEN----GVHRHGPIQVEFVSADLEEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMY--RD 1356
Cdd:cd14608    94 MLNRVmeKGSLKCAQYWPQKeekeMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQET--REILHFHYTTWPDFgvPE 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1357 TPVSKRSFLKLIRQVDKWQEEYnggeGRTVVHCLNGGGRSGTFCAISiVCEMLRHQR----TVDVFHAVKTLRNNKPNMV 1432
Cdd:cd14608   172 SPASFLNFLFKVRESGSLSPEH----GPVVVHCSAGIGRSGTFCLAD-TCLLLMDKRkdpsSVDIKKVLLEMRKFRMGLI 246
                         250
                  ....*....|....*
gi 157419150 1433 DLLDQYKFCYEVALE 1447
Cdd:cd14608   247 QTADQLRFSYLAVIE 261
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
1242-1443 2.84e-31

PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein phosphatase non-receptor type 23 (PTPN23), also called His domain-containing protein tyrosine phosphatase (HD-PTP) or protein tyrosine phosphatase TD14 (PTP-TD14), is a catalytically inactive member of the tyrosine-specific protein tyrosine phosphatase (PTP) family. Human PTPN23 may be involved in the regulation of small nuclear ribonucleoprotein assembly and pre-mRNA splicing by modifying the survival motor neuron (SMN) complex. It plays a role in ciliogenesis and is part of endosomal sorting complex required for transport (ESCRT) pathways. PTPN23 contains five domains: a BRO1-like domain that plays a role in endosomal sorting; a V-domain that interacts with Lys63-linked polyubiquitinated substrates; a central proline-rich region that might recruit SH3-containing proteins; a PTP-like domain; and a proteolytic degradation-targeting motif, also known as a PEST sequence.


Pssm-ID: 350387 [Multi-domain]  Cd Length: 205  Bit Score: 122.49  E-value: 2.84e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1242 YINAALMDSYKQPSA-FIVTQHPLPNTVKDFWRLVLDYHCTSVVMLndVDPAQLCPQ----YWPEN-GVH-RHGPIQVEF 1314
Cdd:cd14539     1 YINASLIEDLTPYCPrFIATQAPLPGTAADFWLMVYEQQVSVIVML--VSEQENEKQkvhrYWPTErGQAlVYGAITVSL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1315 VSADLEEDIISRIFRIYNaaRPQDGYRMVQQFQFLGWPMYRdTPVSKRSFLKLIRQVDKWQEEYNGGEGRTVVHCLNGGG 1394
Cdd:cd14539    79 QSVRTTPTHVERIISIQH--KDTRLSRSVVHLQFTTWPELG-LPDSPNPLLRFIEEVHSHYLQQRSLQTPIVVHCSSGVG 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 157419150 1395 RSGTFC-AISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYE 1443
Cdd:cd14539   156 RTGAFClLYAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
953-1153 5.09e-31

PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350483 [Multi-domain]  Cd Length: 206  Bit Score: 121.72  E-value: 5.09e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  953 YINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVtNLVEVGRVkCCKYWPDD-TEIYKDIKVTLIETEL 1031
Cdd:cd14635     1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVML-NDVDPAQL-CPQYWPENgVHRHGPIQVEFVSADL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1032 LAEYVIRTFAV--EKRGVHEIREIRQFHFTGWPDH-GVPYHATGLLGFVRQV---KSKSPPSAGPLVVHCSAGAGRTGCF 1105
Cdd:cd14635    79 EEDIISRIFRIynAARPQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVdkwQEEYNGGEGRTVVHCLNGGGRSGTF 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 157419150 1106 IVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 1153
Cdd:cd14635   159 CAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
1242-1442 5.71e-31

catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; Tyrosine-protein phosphatase non-receptor type 22 (PTPN22), type 18 (PTPN18) and type 12 (PTPN12) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN22 is expressed in hematopoietic cells and it functions as a key regulator of immune homeostasis by inhibiting T-cell receptor signaling through the direct dephosphorylation of Src family kinases (Lck and Fyn), ITAMs of the TCRz/CD3 complex, and other signaling molecules. TPN18 regulates HER2-mediated cellular functions through defining both its phosphorylation and ubiquitination states. PTPN12 is characterized as a tumor suppressor and a pivotal regulator of EGFR/HER2 signaling.


Pssm-ID: 350390 [Multi-domain]  Cd Length: 202  Bit Score: 121.38  E-value: 5.71e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1242 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVML-NDVDPAQL-CPQYWPENG--VHRHGPIQVEFVSA 1317
Cdd:cd14542     1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMAcREFEMGKKkCERYWPEEGeeQLQFGPFKISLEKE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1318 D-LEEDIISRIFRiynaARPQDGYRMVQQFQFLGWPMyRDTPVSKRSFLKLIRQVDKWQEEyngGEGRTVVHCLNGGGRS 1396
Cdd:cd14542    81 KrVGPDFLIRTLK----VTFQKESRTVYQFHYTAWPD-HGVPSSVDPILDLVRLVRDYQGS---EDVPICVHCSAGCGRT 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 157419150 1397 GTFCAISIVCEMLRHQRTVD---VFHAVKTLRNNKPNMVDLLDQYKFCY 1442
Cdd:cd14542   153 GTICAIDYVWNLLKTGKIPEefsLFDLVREMRKQRPAMVQTKEQYELVY 201
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
1242-1449 1.40e-30

catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) and type 13 (PTPN13, also known as PTPL1) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization. Human PTPN13 is an important regulator of tumor aggressiveness.


Pssm-ID: 350386 [Multi-domain]  Cd Length: 207  Bit Score: 120.56  E-value: 1.40e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1242 YINAalmdSY------KQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLN-DVDPAQL-CPQYWPEN---GVHRHGPI 1310
Cdd:cd14538     1 YINA----SHiripvgGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTqDVEGGKVkCHRYWPDSlnkPLICGGRL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1311 QVEFVSADLEEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEynggeGRTVVHCL 1390
Cdd:cd14538    77 EVSLEKYQSLQDFVIRRISLRDKETGEV--HHITHLNFTTWPDH-GTPQSADPLLRFIRYMRRIHNS-----GPIVVHCS 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 157419150 1391 NGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALEYL 1449
Cdd:cd14538   149 AGIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
1242-1446 2.18e-30

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type tyrosine-protein phosphatase Z (PTPRZ), also called receptor-type tyrosine-protein phosphatase zeta (R-PTP-zeta), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Three isoforms are generated by alternative splicing from a single PTPRZ gene: two transmembrane isoforms, PTPRZ-A and PTPRZ-B, and one secretory isoform, PTPRZ-S (also known as phosphacan); all are preferentially expressed in the central nervous system (CNS) as chondroitin sulfate (CS) proteoglycans. PTPRZ isoforms play important roles in maintaining oligodendrocyte precursor cells in an undifferentiated state. PTPRZ is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350507 [Multi-domain]  Cd Length: 204  Bit Score: 119.71  E-value: 2.18e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1242 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDV-DPAQLCPQYWPengvHRHGPIQVEFVSADL- 1319
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGqNMAEDEFVYWP----NKDEPINCETFKVTLi 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1320 ---------EEDIISRIFrIYNAArpQDGYRM-VQQFQFLGWPmYRDTPVSKRsfLKLIRQVdkwQEEYNGGEGRTVVHC 1389
Cdd:cd17669    77 aeehkclsnEEKLIIQDF-ILEAT--QDDYVLeVRHFQCPKWP-NPDSPISKT--FELISII---KEEAANRDGPMIVHD 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 157419150 1390 LNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVAL 1446
Cdd:cd17669   148 EHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
1216-1442 4.00e-30

catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1) type 2 (PTPN2) belong to the family of classical tyrosine-specific protein tyrosine phosphatases, (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1 (or PTP-1B) is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor. PTPN2 (or TCPTP), a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner.


Pssm-ID: 350393 [Multi-domain]  Cd Length: 231  Bit Score: 119.80  E-value: 4.00e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1216 KNRCMDILPPDRCLpflITIDGESSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDV--DPAQ 1293
Cdd:cd14545     3 RYRDRDPYDHDRSR---VKLKQGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLmeKGQI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1294 LCPQYWPENGVH----RHGPIQVEFVSADLEEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMYrDTPVSKRSFLKLIR 1369
Cdd:cd14545    80 KCAQYWPQGEGNamifEDTGLKVTLLSEEDKSYYTVRTLELENLKTQET--REVLHFHYTTWPDF-GVPESPAAFLNFLQ 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157419150 1370 QVdKWQEEYNGGEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRT--VDVFHAVKTLRNNKPNMVDLLDQYKFCY 1442
Cdd:cd14545   157 KV-RESGSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQLRFSY 230
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
1210-1442 4.42e-30

catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein phosphatase non-receptor type 7 (PTPN7), also called hematopoietic protein-tyrosine phosphatase (HePTP) or LC-PTP. belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN7/HePTP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. PTPN7/HePTP is found exclusively in the white blood cells in bone marrow, thymus, spleen, lymph nodes and all myeloid and lymphoid cell lines. It negatively regulates T-cell activation and proliferation, and is often dysregulated in the preleukemic disorder myelodysplastic syndrome, as well as in acute myelogenous leukemia.


Pssm-ID: 350460 [Multi-domain]  Cd Length: 247  Bit Score: 120.33  E-value: 4.42e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1210 LPRNHEKNRCMDILP-PDR--CLPFLITIDgESSNYINAALMDSYK-QPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVM 1285
Cdd:cd14612    12 IPGHASKDRYKTILPnPQSrvCLRRAGSQE-EEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVM 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1286 LNDV-DPAQLCPQYWPENGvHRHGPIQVEFVSADLEEDIISRIFRIynaaRPQDGYRMVQQFQFLGWPMYRdTPVSKRSF 1364
Cdd:cd14612    91 ITKLkEKKEKCVHYWPEKE-GTYGRFEIRVQDMKECDGYTIRDLTI----QLEEESRSVKHYWFSSWPDHQ-TPESAGPL 164
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157419150 1365 LKLIRQVDKwQEEYNGGEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCY 1442
Cdd:cd14612   165 LRLVAEVEE-SRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLH 241
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
1242-1438 1.89e-29

catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type tyrosine-protein phosphatase C (PTPRC), also known as CD45, leukocyte common antigen (LCA) or GP180, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRC/CD45 is found in all nucleated hematopoietic cells and is an essential regulator of T- and B-cell antigen receptor signaling. It controls immune response, both positively and negatively, by dephosphorylating a number of signaling molecules such as the Src family kinases, the CD3zeta chain of TCY, and ZAP-70 kinase. Mutations in the human PTPRC/CD45 gene are associated with severe combined immunodeficiency (SCID) and multiple sclerosis. PTPRC/CD45 contains an extracellular receptor-like region with fibronectin type III (FN3) repeats, a short transmembrane segment, and a cytoplasmic region comprising of a membrane proximal catalytically active PTP domain (repeat 1 or D1) and a membrane distal catalytically impaired PTP-like domain (repeat 2, or D2). This model represents repeat 1.


Pssm-ID: 350405 [Multi-domain]  Cd Length: 201  Bit Score: 116.85  E-value: 1.89e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1242 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDPAQL--CPQYWP--ENGVHRHGPIQVEFVSA 1317
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRnkCAQYWPsmEEGSRAFGDVVVKINEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1318 DLEEDIISRIFRIYNaARPQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQeeyNGGEGRTVVHCLNGGGRSG 1397
Cdd:cd14557    81 KICPDYIIRKLNINN-KKEKGSGREVTHIQFTSWPDH-GVPEDPHLLLKLRRRVNAFN---NFFSGPIVVHCSAGVGRTG 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 157419150 1398 TFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQY 1438
Cdd:cd14557   156 TYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQY 196
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
953-1152 1.96e-29

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type tyrosine-protein phosphatase Z (PTPRZ), also called receptor-type tyrosine-protein phosphatase zeta (R-PTP-zeta), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Three isoforms are generated by alternative splicing from a single PTPRZ gene: two transmembrane isoforms, PTPRZ-A and PTPRZ-B, and one secretory isoform, PTPRZ-S (also known as phosphacan); all are preferentially expressed in the central nervous system (CNS) as chondroitin sulfate (CS) proteoglycans. PTPRZ isoforms play important roles in maintaining oligodendrocyte precursor cells in an undifferentiated state. PTPRZ is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350507 [Multi-domain]  Cd Length: 204  Bit Score: 117.02  E-value: 1.96e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  953 YINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCkYWPDDTE--IYKDIKVTLIETE 1030
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWPNKDEpiNCETFKVTLIAEE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1031 LLA-----EYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATglLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCF 1105
Cdd:cd17669    80 HKClsneeKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKT--FELISIIKEEAANRDGPMIVHDEHGGVTAGTF 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 157419150 1106 IVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAIL 1152
Cdd:cd17669   158 CALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
1211-1447 3.02e-29

catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type tyrosine-protein phosphatase G (PTPRG), also called protein-tyrosine phosphatase gamma (R-PTP-gamma), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRG is an important tumor suppressor gene in multiple human cancers such as lung, ovarian, and breast cancers. It is widely expressed in many tissues, including the central nervous system, where it plays a role during neuroinflammation processes. It can dephosphorylate platelet-derived growth factor receptor beta (PDGFRB) and may play a role in PDGFRB-related infantile myofibromatosis. PTPRG has four splicing isoforms: three transmembrane isoforms, PTPRG-A, B, and C, and one secretory isoform, PTPRG-S, which are expressed in many tissues including the brain. PTPRG is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350505 [Multi-domain]  Cd Length: 274  Bit Score: 118.60  E-value: 3.02e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1211 PRNHEKNRCMDILPPDRC---LPFLITIDGESSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVML- 1286
Cdd:cd17667    25 PDNKHKNRYINILAYDHSrvkLRPLPGKDSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMIt 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1287 NDVDPAQL-CPQYWPENGVHRHGPIQVEFVSADLEEDIISRIFRIYNAA--RPQDG-------YRMVQQFQFLGWPmyrD 1356
Cdd:cd17667   105 NLVEKGRRkCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTKvkKGQKGnpkgrqnERTVIQYHYTQWP---D 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1357 TPVSKRSfLKLIRQVDKWQEEYNGGEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLD 1436
Cdd:cd17667   182 MGVPEYA-LPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEE 260
                         250
                  ....*....|.
gi 157419150 1437 QYKFCYEVALE 1447
Cdd:cd17667   261 QYIFIHDALLE 271
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
1240-1443 5.38e-29

catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type tyrosine-protein phosphatase Q (PTPRQ or R-PTP-Q), also called phosphatidylinositol phosphatase PTPRQ, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRQ is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats (18 in PTPRQ) and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It displays low tyrosine-protein phosphatase activity; rather, it functions as a phosphatidylinositol phosphatase required for auditory processes. It regulates the levels of phosphatidylinositol 4,5-bisphosphate (PIP2) in the basal region of hair bundles. It can dephosphorylate a broad range of phosphatidylinositol phosphates, including phosphatidylinositol 3,4,5-trisphosphate and most phosphatidylinositol monophosphates and diphosphates.


Pssm-ID: 350464 [Multi-domain]  Cd Length: 224  Bit Score: 116.54  E-value: 5.38e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1240 SNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDV-DPAQL-CPQYWPENG--VHRHGPIQVEFV 1315
Cdd:cd14616    25 SDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCfEKGRIrCHQYWPEDNkpVTVFGDIVITKL 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1316 SADLEEDIISRIFRIynaaRPQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEYNggeGRTVVHCLNGGGR 1395
Cdd:cd14616   105 MEDVQIDWTIRDLKI----ERHGDYMMVRQCNFTSWPEH-GVPESSAPLIHFVKLVRASRAHDN---TPMIVHCSAGVGR 176
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 157419150 1396 SGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYE 1443
Cdd:cd14616   177 TGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
953-1153 6.19e-29

PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type tyrosine-protein phosphatase U (PTPRU), also known as pancreatic carcinoma phosphatase 2 (PCP-2), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRU/PCP-2 is the most distant member of the type IIb subfamily and may have a distinct biological function other than cell-cell aggregation. It localizes to the adherens junctions and directly binds and dephosphorylates beta-catenin, and regulates the balance between signaling and adhesive beta-catenin. It plays an important role in the maintenance of epithelial integrity. PTPRU contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350485 [Multi-domain]  Cd Length: 207  Bit Score: 115.78  E-value: 6.19e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  953 YINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRV-KCCKYWPDD-TEIYKDIKVTLIETE 1030
Cdd:cd14637     1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEPgLQQYGPMEVEFVSGS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1031 LLAEYVIRTFAVEK--RGVHEIREIRQFHFTGW-PDHGVPYHATGLLGFVRQV-KSKSPPSAGPLVVHCSAGAGRTGCFI 1106
Cdd:cd14637    81 ADEDIVTRLFRVQNitRLQEGHLMVRHFQFLRWsAYRDTPDSKKAFLHLLASVeKWQRESGEGRTVVHCLNGGGRSGTYC 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 157419150 1107 VIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 1153
Cdd:cd14637   161 ASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
1217-1443 1.38e-28

catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type tyrosine-protein phosphatase B (PTPRB), also known as receptor-type tyrosine-protein phosphatase beta (R-PTP-beta) or vascular endothelial protein tyrosine phosphatase(VE-PTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRB/VE-PTP is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed specifically in vascular endothelial cells and it plays an important role in blood vessel remodeling and angiogenesis.


Pssm-ID: 350465 [Multi-domain]  Cd Length: 228  Bit Score: 115.40  E-value: 1.38e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1217 NRCMDILPPDRCLPFLITIDGES-SNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLND-VDPAQL 1294
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNVDDDPcSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQcVEKGRV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1295 -CPQYWP-ENGVHRHGPIQVEFVSADLEEDIISRIFRIYNAARpQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVD 1372
Cdd:cd14617    81 kCDHYWPaDQDSLYYGDLIVQMLSESVLPEWTIREFKICSEEQ-LDAPRLVRHFHYTVWPDH-GVPETTQSLIQFVRTVR 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157419150 1373 KWQEEYNGgEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYE 1443
Cdd:cd14617   159 DYINRTPG-SGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
1242-1446 1.84e-28

PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type tyrosine-protein phosphatase G (PTPRG), also called protein-tyrosine phosphatase gamma (R-PTP-gamma), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRG is an important tumor suppressor gene in multiple human cancers such as lung, ovarian, and breast cancers. It is widely expressed in many tissues, including the central nervous system, where it plays a role during neuroinflammation processes. It can dephosphorylate platelet-derived growth factor receptor beta (PDGFRB) and may play a role in PDGFRB-related infantile myofibromatosis. PTPRG is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350508 [Multi-domain]  Cd Length: 205  Bit Score: 114.39  E-value: 1.84e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1242 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLND-VDPAQLCPQYWPEngvhRHGPIQVEFVSADL- 1319
Cdd:cd17670     1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDnQGLAEDEFVYWPS----REESMNCEAFTVTLi 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1320 ---------EEDIISRIFrIYNAArpQDGYRM-VQQFQFLGWPmYRDTPVSkrSFLKLIRQVdkwQEEYNGGEGRTVVHC 1389
Cdd:cd17670    77 skdrlclsnEEQIIIHDF-ILEAT--QDDYVLeVRHFQCPKWP-NPDAPIS--STFELINVI---KEEALTRDGPTIVHD 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 157419150 1390 LNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVAL 1446
Cdd:cd17670   148 EFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
1216-1447 3.39e-28

catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein phosphatase non-receptor type 22 (PTPN22), also called lymphoid phosphatase (LyP), PEST-domain phosphatase (PEP), or hematopoietic cell protein-tyrosine phosphatase 70Z-PEP, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN22 is expressed in hematopoietic cells and it functions as a key regulator of immune homeostasis by inhibiting T-cell receptor signaling through the direct dephosphorylation of Src family kinases (Lck and Fyn), ITAMs of the TCRz/CD3 complex, and other signaling molecules. Mutations in the PTPN22 gene are associated with multiple connective tissue and autoimmune diseases including type 1 diabetes mellitus, rheumatoid arthritis, and systemic lupus erythematosus. PTPN22 contains an N-terminal catalytic PTP domain and four proline-rich regions at the C-terminus.


Pssm-ID: 350450 [Multi-domain]  Cd Length: 234  Bit Score: 114.55  E-value: 3.39e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1216 KNRCMDILPPDRCLP--FLITIDgESSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVM--LNDVDP 1291
Cdd:cd14602     1 KNRYKDILPYDHSRVelSLITSD-EDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMacMEFEMG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1292 AQLCPQYWPENGVH--RHGPIQVEFVSADLEEDIISRIFRiynaARPQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIR 1369
Cdd:cd14602    80 KKKCERYWAEPGEMqlEFGPFSVTCEAEKRKSDYIIRTLK----VKFNSETRTIYQFHYKNWPDH-DVPSSIDPILELIW 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1370 QVDKWQEEyngGEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQ---RTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVAL 1446
Cdd:cd14602   155 DVRCYQED---DSVPICIHCSAGCGRTGVICAIDYTWMLLKDGiipENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAVI 231

                  .
gi 157419150 1447 E 1447
Cdd:cd14602   232 E 232
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
953-1152 4.59e-28

PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type tyrosine-protein phosphatase G (PTPRG), also called protein-tyrosine phosphatase gamma (R-PTP-gamma), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRG is an important tumor suppressor gene in multiple human cancers such as lung, ovarian, and breast cancers. It is widely expressed in many tissues, including the central nervous system, where it plays a role during neuroinflammation processes. It can dephosphorylate platelet-derived growth factor receptor beta (PDGFRB) and may play a role in PDGFRB-related infantile myofibromatosis. PTPRG is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350508 [Multi-domain]  Cd Length: 205  Bit Score: 113.23  E-value: 4.59e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  953 YINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTN---LVEVGRVkcckYWPDDTEIY--KDIKVTLI 1027
Cdd:cd17670     1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDnqgLAEDEFV----YWPSREESMncEAFTVTLI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1028 ETELLA-----EYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATglLGFVRQVKSKSPPSAGPLVVHCSAGAGRT 1102
Cdd:cd17670    77 SKDRLClsneeQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISST--FELINVIKEEALTRDGPTIVHDEFGAVSA 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 157419150 1103 GCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAIL 1152
Cdd:cd17670   155 GTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
1342-1447 2.34e-27

Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine phosphatases. Homologues detected by this profile and not by those of "PTPc" or "DSPc" are predicted to be protein phosphatases with a similar fold to DSPs and PTPs, yet with unpredicted specificities.


Pssm-ID: 214469 [Multi-domain]  Cd Length: 105  Bit Score: 107.44  E-value: 2.34e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150   1342 MVQQFQFLGWPmYRDTPVSKRSFLKLIRQVDKWQEEYNGGeGRTVVHCLNGGGRSGTFCAISIVCEMLRH-QRTVDVFHA 1420
Cdd:smart00012    1 TVKHYHYTGWP-DHGVPESPDSILELLRAVKKNLNQSESS-GPVVVHCSAGVGRTGTFVAIDILLQQLEAeAGEVDIFDT 78
                            90       100
                    ....*....|....*....|....*..
gi 157419150   1421 VKTLRNNKPNMVDLLDQYKFCYEVALE 1447
Cdd:smart00012   79 VKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1342-1447 2.34e-27

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 107.44  E-value: 2.34e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150   1342 MVQQFQFLGWPmYRDTPVSKRSFLKLIRQVDKWQEEYNGGeGRTVVHCLNGGGRSGTFCAISIVCEMLRH-QRTVDVFHA 1420
Cdd:smart00404    1 TVKHYHYTGWP-DHGVPESPDSILELLRAVKKNLNQSESS-GPVVVHCSAGVGRTGTFVAIDILLQQLEAeAGEVDIFDT 78
                            90       100
                    ....*....|....*....|....*..
gi 157419150   1421 VKTLRNNKPNMVDLLDQYKFCYEVALE 1447
Cdd:smart00404   79 VKELRSQRPGMVQTEEQYLFLYRALLE 105
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
1216-1442 3.63e-27

catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type tyrosine-protein phosphatase-like R (PTPRR or R-PTP-R), also called protein-tyrosine phosphatase PCPTP1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRR is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. The human and mouse PTPRR gene produces multiple neuronal protein isoforms of varying sizes (in human, PTPPBS-alpha, beta, gamma and delta). All isoforms contain the KIM motif and the catalytic PTP domain. PTPRR-deficient mice show significant defects in fine motor coordination and balance skills that are reminiscent of a mild ataxia.


Pssm-ID: 350459 [Multi-domain]  Cd Length: 226  Bit Score: 111.16  E-value: 3.63e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1216 KNRCMDILPPDRCLPFLIT--IDGESSNYINAALMDSYK-QPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDV-DP 1291
Cdd:cd14611     2 KNRYKTILPNPHSRVCLKPknSNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLkEK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1292 AQLCPQYWPEN-GVHrhGPIQVEFVSADLEEDIISRIFRIYNAARPqdgyRMVQQFQFLGWPMYRdTPVSKRSFLKLIRQ 1370
Cdd:cd14611    82 NEKCVLYWPEKrGIY--GKVEVLVNSVKECDNYTIRNLTLKQGSQS----RSVKHYWYTSWPDHK-TPDSAQPLLQLMLD 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157419150 1371 VDKWQEEYNGgEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCY 1442
Cdd:cd14611   155 VEEDRLASPG-RGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
1213-1451 4.03e-27

catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11), also called SH2 domain-containing tyrosine phosphatase 2 (SHP-2 or SHP2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 promotes the activation of the RAS/Mitogen-Activated Protein Kinases (MAPK) Extracellular-Regulated Kinases 1/2 (ERK1/2) pathway, a canonical signaling cascade that plays key roles in various cellular processes, including proliferation, survival, differentiation, migration, or metabolism. It also regulates the phosphoinositide 3-kinase (PI3K)/AKT pathway, a fundamental cascade that functions in cell survival, proliferation, migration, morphogenesis, and metabolism. PTPN11 dysregulation is associated with several developmental diseases and malignancies, such as Noonan syndrome and juvenile myelomonocytic leukemia. It contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.


Pssm-ID: 350453 [Multi-domain]  Cd Length: 253  Bit Score: 112.03  E-value: 4.03e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1213 NHEKNRCMDILPPDRCLpfLITIDGE----SSNYINAALM--------DSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHC 1280
Cdd:cd14605     2 NKNKNRYKNILPFDHTR--VVLHDGDpnepVSDYINANIImpefetkcNNSKPKKSYIATQGCLQNTVNDFWRMVFQENS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1281 TSVVMLN-DVDPAQL-CPQYWP-ENGVHRHGPIQVEFVSADLEEDIISRIFRIYNAARpQDGYRMVQQFQFLGWPMYrDT 1357
Cdd:cd14605    80 RVIVMTTkEVERGKSkCVKYWPdEYALKEYGVMRVRNVKESAAHDYILRELKLSKVGQ-GNTERTVWQYHFRTWPDH-GV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1358 PVSKRSFLKLIRQVDKWQEEYNGGeGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRT---VDVFHAVKTLRNNKPNMVDL 1434
Cdd:cd14605   158 PSDPGGVLDFLEEVHHKQESIMDA-GPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMVQT 236
                         250
                  ....*....|....*..
gi 157419150 1435 LDQYKFCYEVALEYLNS 1451
Cdd:cd14605   237 EAQYRFIYMAVQHYIET 253
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
1233-1444 1.42e-26

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 112.43  E-value: 1.42e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1233 ITIDGESSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVD-PAQLCPQYW--PENGVHRHGP 1309
Cdd:PHA02746   91 VTSEDNAENYIHANFVDGFKEANKFICAQGPKEDTSEDFFKLISEHESQVIVSLTDIDdDDEKCFELWtkEEDSELAFGR 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1310 IQVEFVSADLEEDIISRIFRIYNAArpQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEY-------NGGE 1382
Cdd:PHA02746  171 FVAKILDIIEELSFTKTRLMITDKI--SDTSREIHHFWFPDWPDN-GIPTGMAEFLELINKVNEEQAELikqadndPQTL 247
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157419150 1383 GRTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEV 1444
Cdd:PHA02746  248 GPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKA 309
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
1242-1449 2.47e-26

catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization.


Pssm-ID: 350444 [Multi-domain]  Cd Length: 207  Bit Score: 108.30  E-value: 2.47e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1242 YINAA--LMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLN-DVDPAQL-CPQYWPENgvhRHGPIQVEFVSA 1317
Cdd:cd14596     1 YINASyiTMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTrEVERGKVkCHRYWPET---LQEPMELENYQL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1318 DLE-----EDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEynggeGRTVVHCLNG 1392
Cdd:cd14596    78 RLEnyqalQYFIIRIIKLVEKETGEN--RLIKHLQFTTWPDH-GTPQSSDQLVKFICYMRKVHNT-----GPIVVHCSAG 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 157419150 1393 GGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALEYL 1449
Cdd:cd14596   150 IGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVL 206
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
1242-1443 3.26e-26

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type tyrosine-protein phosphatase Z (PTPRZ), also called receptor-type tyrosine-protein phosphatase zeta (R-PTP-zeta), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Three isoforms are generated by alternative splicing from a single PTPRZ gene: two transmembrane isoforms, PTPRZ-A and PTPRZ-B, and one secretory isoform, PTPRZ-S (also known as phosphacan); all are preferentially expressed in the central nervous system (CNS) as chondroitin sulfate (CS) proteoglycans. PTPRZ isoforms play important roles in maintaining oligodendrocyte precursor cells in an undifferentiated state. PTPRZ is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350506 [Multi-domain]  Cd Length: 209  Bit Score: 107.76  E-value: 3.26e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1242 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVML-NDVDPAQL-CPQYWPENGVHRHGPIQVEFVSADL 1319
Cdd:cd17668     1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMItNLVEKGRRkCDQYWPADGSEEYGNFLVTQKSVQV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1320 EEDIISRIFRIYNA--------ARPQDgyRMVQQFQFLGWPmyrDTPVSKRSfLKLIRQVDKWQEEYNGGEGRTVVHCLN 1391
Cdd:cd17668    81 LAYYTVRNFTLRNTkikkgsqkGRPSG--RVVTQYHYTQWP---DMGVPEYT-LPVLTFVRKASYAKRHAVGPVVVHCSA 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 157419150 1392 GGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYE 1443
Cdd:cd17668   155 GVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHD 206
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
1213-1442 3.55e-26

catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein phosphatase non-receptor type 12 (PTPN12), also called PTP-PEST or protein-tyrosine phosphatase G1 (PTPG1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN12 is characterized as a tumor suppressor and a pivotal regulator of EGFR/HER2 signaling. It regulates various physiological processes, including cell migration, immune response, and neuronal activity, by dephosphorylating multiple substrates including HER2, FAK, PYK2, PSTPIP, WASP, p130Cas, paxillin, Shc, catenin, c-Abl, ArgBP2, p190RhoGAP, RhoGDI, cell adhesion kinase beta, and Rho GTPase.


Pssm-ID: 350452 [Multi-domain]  Cd Length: 297  Bit Score: 110.41  E-value: 3.55e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1213 NHEKNRCMDILPPDRC-LPFLITIDGESSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVM-LNDVD 1290
Cdd:cd14604    57 NVKKNRYKDILPFDHSrVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMaCREFE 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1291 PA-QLCPQYWPENGVH--RHGPIQVEFVSADLEEDIISRIFRIynaaRPQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKL 1367
Cdd:cd14604   137 MGrKKCERYWPLYGEEpmTFGPFRISCEAEQARTDYFIRTLLL----EFQNETRRLYQFHYVNWPDH-DVPSSFDSILDM 211
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157419150 1368 IRQVDKWQEEyngGEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRT---VDVFHAVKTLRNNKPNMVDLLDQYKFCY 1442
Cdd:cd14604   212 ISLMRKYQEH---EDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKEQYELVH 286
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
1207-1442 3.61e-26

catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein phosphatase non-receptor type 2 (PTPN2), also called T-cell protein-tyrosine phosphatase (TCPTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN2, a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner. It is deleted in 6% of all T-cell acute lymphoblastic leukemias and is associated with constitutive JAK1/STAT5 signaling and tumorigenesis.


Pssm-ID: 350455 [Multi-domain]  Cd Length: 257  Bit Score: 109.29  E-value: 3.61e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1207 IALLPRNHEKNRCMDILPPDRCLpflITIDGESSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVML 1286
Cdd:cd14607    18 VAKYPENRNRNRYRDVSPYDHSR---VKLQNTENDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVML 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1287 NDV--DPAQLCPQYWPENG----VHRHGPIQVEFVSADLEEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMYrDTPVS 1360
Cdd:cd14607    95 NRIveKDSVKCAQYWPTDEeevlSFKETGFSVKLLSEDVKSYYTVHLLQLENINSGET--RTISHFHYTTWPDF-GVPES 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1361 KRSFLKLIRQVdKWQEEYNGGEGRTVVHCLNGGGRSGTFCAISiVCEMLRHQR---TVDVFHAVKTLRNNKPNMVDLLDQ 1437
Cdd:cd14607   172 PASFLNFLFKV-RESGSLSPEHGPAVVHCSAGIGRSGTFSLVD-TCLVLMEKKdpdSVDIKQVLLDMRKYRMGLIQTPDQ 249

                  ....*
gi 157419150 1438 YKFCY 1442
Cdd:cd14607   250 LRFSY 254
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
1242-1443 8.18e-26

protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis thaliana protein tyrosine phosphatase 1 (AtPTP1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. AtPTP1 dephosphorylates and inhibits MAP kinase 6 (MPK6) in non-oxidative stress conditions. Together with MAP kinase phosphatase 1 (MKP1) it expresses salicylic acid (SA) and camalexin biosynthesis, and therefore, modulating defense response.


Pssm-ID: 350496 [Multi-domain]  Cd Length: 206  Bit Score: 106.78  E-value: 8.18e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1242 YINAALM--DSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDPAQL---CPQYWP--ENGVHRHGPIQVEF 1314
Cdd:cd17658     1 YINASLVetPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYStakCADYFPaeENESREFGRISVTN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1315 VSADLEEDIISRIFRIYNAARPQDGYRMVQQFQFLGWPMY--RDTPVSKRSFLKLIRQVDKwqeeyngGEGRTVVHCLNG 1392
Cdd:cd17658    81 KKLKHSQHSITLRVLEVQYIESEEPPLSVLHIQYPEWPDHgvPKDTRSVRELLKRLYGIPP-------SAGPIVVHCSAG 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 157419150 1393 GGRSGTFCAISIVCE--MLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYE 1443
Cdd:cd17658   154 IGRTGAYCTIHNTIRriLEGDMSAVDLSKTVRKFRSQRIGMVQTQDQYIFCYA 206
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
1242-1446 1.17e-25

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; Tyrosine-protein phosphatase non-receptor type 3 (PTPN3) and type 4 (PTPN4) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN3 and PTPN4 are large modular proteins containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain. PTPN3 interacts with mitogen-activated protein kinase p38gamma and serves as its specific phosphatase. PTPN4 functions in TCR cell signaling, apoptosis, cerebellar synaptic plasticity, and innate immune responses.


Pssm-ID: 350389 [Multi-domain]  Cd Length: 212  Bit Score: 106.26  E-value: 1.17e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1242 YINAALMDSYKQPSA----FIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDV--DPAQLCPQYWPE-NGVHRHGPIQVEF 1314
Cdd:cd14541     2 YINANYVNMEIPGSGivnrYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLveRGRVKCHQYWPDlGETMQFGNLQITC 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1315 VSADLEEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEeynGGEGRTVVHCLNGGG 1394
Cdd:cd14541    82 VSEEVTPSFAFREFILTNTNTGEE--RHITQMQYLAWPDH-GVPDDSSDFLDFVKRVRQNRV---GMVEPTVVHCSAGIG 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 157419150 1395 RSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVAL 1446
Cdd:cd14541   156 RTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAIL 207
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
1257-1449 1.54e-25

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; Tyrosine-protein phosphatase non-receptor type 21 (PTPN21) and type 14 (PTPN14) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Both PTPN21 and PTPN14 contain an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350388 [Multi-domain]  Cd Length: 219  Bit Score: 106.39  E-value: 1.54e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1257 FIVTQHPLPNTVKDFWRLVLDYHCTSVVMLND--VDPAQLCPQYWPENGVHRH----GPIQVEFVSADLEEDIISRIFRI 1330
Cdd:cd14540    18 YIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAeeEGGREKCFRYWPTLGGEHDaltfGEYKVSTKFSVSSGCYTTTGLRV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1331 YNAarPQDGYRMVQQFQFLGWPMYR--DTPVSKRSFLKLIRQVDKWQEEYNGGEGR---TVVHCLNGGGRSGT--FCAIS 1403
Cdd:cd14540    98 KHT--LSGQSRTVWHLQYTDWPDHGcpEDVSGFLDFLEEINSVRRHTNQDVAGHNRnppTLVHCSAGVGRTGVviLADLM 175
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 157419150 1404 IVCemLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALEYL 1449
Cdd:cd14540   176 LYC--LDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQYL 219
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
1213-1449 2.24e-25

catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein phosphatase non-receptor type 13 (PTPN13, also known as PTPL1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN13 is an important regulator of tumor aggressiveness. It regulates breast cancer cell aggressiveness through direct inactivation of Src kinase. In hepatocellular carcinoma, PTPN13 is a tumor suppressor. PTPN13 contains a FERM domain, five PDZ domains, and a C-terminal catalytic PTP domain. With its PDZ domains, PTPN13 has numerous interacting partners that can actively participate in the regulation of its phosphatase activity or can permit direct or indirect recruitment of tyrosine phosphorylated substrates. Its FERM domain is necessary for localization to the membrane.


Pssm-ID: 350445 [Multi-domain]  Cd Length: 234  Bit Score: 106.45  E-value: 2.24e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1213 NHEKNRCMDILPPDRCLPFLitidGESSNYINAAL--MDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVML-NDV 1289
Cdd:cd14597     3 NRKKNRYKNILPYDTTRVPL----GDEGGYINASFikMPVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMtQEV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1290 DPAQL-CPQYWPE---NGVHRHGPIQVEFVSADLEEDIISRIFRIYNAARPQdgYRMVQQFQFLGWPMYrDTPVSKRSFL 1365
Cdd:cd14597    79 EGGKIkCQRYWPEilgKTTMVDNRLQLTLVRMQQLKNFVIRVLELEDIQTRE--VRHITHLNFTAWPDH-DTPSQPEQLL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1366 KLI---RQVDKwqeeynggEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCY 1442
Cdd:cd14597   156 TFIsymRHIHK--------SGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCY 227

                  ....*..
gi 157419150 1443 EVALEYL 1449
Cdd:cd14597   228 QVILYVL 234
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
1213-1449 1.52e-24

catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) and type 6 (PTPN6) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 and PTPN6, are also called SH2 domain-containing tyrosine phosphatase 2 (SHP2) and 1 (SHP1), respectively. They contain two tandem SH2 domains: a catalytic PTP domain, and a C-terminal tail with regulatory properties. Although structurally similar, they have different localization and different roles in signal transduction. PTPN11/SHP2 is expressed ubiquitously and plays a positive role in cell signaling, leading to cell activation, while PTPN6/SHP1 expression is restricted mainly to hematopoietic and epithelial cells and functions as a negative regulator of signaling events.


Pssm-ID: 350392 [Multi-domain]  Cd Length: 251  Bit Score: 104.47  E-value: 1.52e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1213 NHEKNRCMDILPPDRCLPFLITIDGE--SSNYINA----------ALMDSYKqpsAFIVTQHPLPNTVKDFWRLVLDYHC 1280
Cdd:cd14544     1 NKGKNRYKNILPFDHTRVILKDRDPNvpGSDYINAnyirnenegpTTDENAK---TYIATQGCLENTVSDFWSMVWQENS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1281 TSVVML-NDVDPAQ-LCPQYWP-ENGVHRHGPIQVEFVSADLEEDIISRIFRIYNAARPQDGyRMVQQFQFLGWPMYrDT 1357
Cdd:cd14544    78 RVIVMTtKEVERGKnKCVRYWPdEGMQKQYGPYRVQNVSEHDTTDYTLRELQVSKLDQGDPI-REIWHYQYLSWPDH-GV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1358 PVSKRSFLKLIRQVDKWQEEYNGgEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQR---TVDVFHAVKTLRNNKPNMVDL 1434
Cdd:cd14544   156 PSDPGGVLNFLEDVNQRQESLPH-AGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDIDIQKTIQMVRSQRSGMVQT 234
                         250
                  ....*....|....*
gi 157419150 1435 LDQYKFCYEVALEYL 1449
Cdd:cd14544   235 EAQYKFIYVAVAQYI 249
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
1211-1451 1.16e-23

catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein phosphatase non-receptor type 6 (PTPN6), also called SH2 domain-containing protein-tyrosine phosphatase 1 (SHP1 or SHP-1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN6 expression is restricted mainly to hematopoietic and epithelial cells. It is an important regulator of hematopoietic cells, downregulating pathways that promote cell growth, survival, adhesion, and activation. It regulates glucose homeostasis by modulating insulin signalling in the liver and muscle, and it also negatively regulates bone resorption, affecting both the formation and the function of osteoclasts. PTPN6 contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.


Pssm-ID: 350454 [Multi-domain]  Cd Length: 266  Bit Score: 102.27  E-value: 1.16e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1211 PRNHEKNRCMDILPPDRCLPFLITIDGE-------SSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSV 1283
Cdd:cd14606    16 PENKSKNRYKNILPFDHSRVILQGRDSNipgsdyiNANYVKNQLLGPDENAKTYIASQGCLEATVNDFWQMAWQENSRVI 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1284 VMLN-DVDPAQ-LCPQYWPENGVHR-HGPIQVEFVSadlEEDIISRIFRIYNAARPQDG--YRMVQQFQFLGWPMYrDTP 1358
Cdd:cd14606    96 VMTTrEVEKGRnKCVPYWPEVGMQRaYGPYSVTNCG---EHDTTEYKLRTLQVSPLDNGelIREIWHYQYLSWPDH-GVP 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1359 VSKRSFLKLIRQVDKWQEEYNGGeGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRT---VDVFHAVKTLRNNKPNMVDLL 1435
Cdd:cd14606   172 SEPGGVLSFLDQINQRQESLPHA-GPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRAQRSGMVQTE 250
                         250
                  ....*....|....*.
gi 157419150 1436 DQYKFCYEVALEYLNS 1451
Cdd:cd14606   251 AQYKFIYVAIAQFIET 266
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
1205-1448 1.47e-23

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 102.77  E-value: 1.47e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1205 CSIALLPRNHEKNRCMDILPPDRCLPFLITIDGeSSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVV 1284
Cdd:PHA02742   44 CNESLELKNMKKCRYPDAPCFDRNRVILKIEDG-GDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIV 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1285 MLNDV--DPAQLCPQYW--PENGVHRHGPIQVEFVSAdleediisRIFRIYNAARPQ-----DGYRM-VQQFQFLGWPmY 1354
Cdd:PHA02742  123 MITKImeDGKEACYPYWmpHERGKATHGEFKIKTKKI--------KSFRNYAVTNLCltdtnTGASLdIKHFAYEDWP-H 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1355 RDTPVSKRSFLKLI---RQVDKWQEEYNGGEGRT-----VVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRN 1426
Cdd:PHA02742  194 GGLPRDPNKFLDFVlavREADLKADVDIKGENIVkeppiLVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRK 273
                         250       260
                  ....*....|....*....|..
gi 157419150 1427 NKPNMVDLLDQYKFCYEVALEY 1448
Cdd:PHA02742  274 QRHNCLSLPQQYIFCYFIVLIF 295
PHA02738 PHA02738
hypothetical protein; Provisional
1212-1451 2.86e-22

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 99.61  E-value: 2.86e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1212 RNHEKNR-----CMD----ILPPDRclpflitidgESSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTS 1282
Cdd:PHA02738   48 KNRKLNRyldavCFDhsrvILPAER----------NRGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQI 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1283 VVML--NDVDPAQLCPQYWP--ENGVHRHGPIQVEFVSADLEEDIISRIFRIYNAArpqDGYRMVQQFQFLGWPMYrDTP 1358
Cdd:PHA02738  118 IVMLckKKENGREKCFPYWSdvEQGSIRFGKFKITTTQVETHPHYVKSTLLLTDGT---SATQTVTHFNFTAWPDH-DVP 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1359 VSKRSFLKLIRQV-----DKWQEEYNGGEGRT-----VVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNK 1428
Cdd:PHA02738  194 KNTSEFLNFVLEVrqcqkELAQESLQIGHNRLqpppiVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQR 273
                         250       260
                  ....*....|....*....|...
gi 157419150 1429 PNMVDLLDQYKFCYEVALEYLNS 1451
Cdd:PHA02738  274 YYSLFIPFQYFFCYRAVKRYVNL 296
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
1174-1446 2.89e-21

catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein phosphatase non-receptor type 3 (PTPN3), also called protein-tyrosine phosphatase H1 (PTP-H1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN3 interacts with mitogen-activated protein kinase p38gamma and serves as its specific phosphatase. PTPN3 and p38gamma cooperate to promote Ras-induced oncogenesis. PTPN3 is a large modular protein containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain. Its PDZ domain binds with the PDZ-binding motif of p38gamma and enables efficient tyrosine dephosphorylation.


Pssm-ID: 350448 [Multi-domain]  Cd Length: 274  Bit Score: 95.30  E-value: 2.89e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1174 MNKLDPQTNSSQIKEEFRTLNMVTPTLRVedcSIALLPRNHEKNRCMDILPPDRCLPFLitidGESSNYINAALMDSyKQ 1253
Cdd:cd14600     4 MAQLKKGLESGTVLIQFEQLYRKKPGLAI---TCAKLPQNMDKNRYKDVLPYDATRVVL----QGNEDYINASYVNM-EI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1254 PSA-----FIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDPA--QLCPQYWPE-NGVHRHGPIQVEFVSadlEEDIIS 1325
Cdd:cd14600    76 PSAnivnkYIATQGPLPHTCAQFWQVVWEQKLSLIVMLTTLTERgrTKCHQYWPDpPDVMEYGGFRVQCHS---EDCTIA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1326 RIFRIYNAARPQDG-YRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEynggEGRTVVHCLNGGGRSGTFCAISI 1404
Cdd:cd14600   153 YVFREMLLTNTQTGeERTVTHLQYVAWPDH-GVPDDSSDFLEFVNYVRSKRVE----NEPVLVHCSAGIGRTGVLVTMET 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 157419150 1405 VCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVAL 1446
Cdd:cd14600   228 AMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAIL 269
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
1239-1447 3.77e-20

catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein phosphatase non-receptor type 4 (PTPN4), also called protein-tyrosine phosphatase MEG1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN4 functions in TCR cell signaling, apoptosis, cerebellar synaptic plasticity, and innate immune responses. It specifically inhibits the TRIF-dependent TLR4 pathway by suppressing tyrosine phosphorylation of TRAM. It is a large modular protein containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain; the PDZ domain regulates the catalytic activity of PTPN4.


Pssm-ID: 350449 [Multi-domain]  Cd Length: 212  Bit Score: 90.39  E-value: 3.77e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1239 SSNYINAALmDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVML-NDVDPAQL-CPQYWPE-NGVHRHGPIQVEFV 1315
Cdd:cd14601     4 NANYINMEI-PSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLtTQVERGRVkCHQYWPEpSGSSSYGGFQVTCH 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1316 SADLEEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVdkwQEEYNGGEGRTVVHCLNGGGR 1395
Cdd:cd14601    83 SEEGNPAYVFREMTLTNLEKNES--RPLTQIQYIAWPDH-GVPDDSSDFLDFVCLV---RNKRAGKDEPVVVHCSAGIGR 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 157419150 1396 SGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 1447
Cdd:cd14601   157 TGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILK 208
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
1206-1449 9.47e-19

catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein phosphatase non-receptor type 14 (PTPN14), also called protein-tyrosine phosphatase pez, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN14 is a potential tumor suppressor and plays a regulatory role in the Hippo and Wnt/beta-catenin signaling pathways. It contains an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350447 [Multi-domain]  Cd Length: 287  Bit Score: 88.52  E-value: 9.47e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1206 SIALLPRNHEKNRCMDILPPDRCLPFLITIDGESSNYINAALMDSYKQPSA--FIVTQHPLPNTVKDFWRLVLDYHCTSV 1283
Cdd:cd14599    31 TTATLPENAERNRIREVVPYEENRVELVPTKENNTGYINASHIKVTVGGEEwhYIATQGPLPHTCHDFWQMVWEQGVNVI 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1284 VMLNDVDPA--QLCPQYWPENGVHRHGPIQVEF-VSADLEED---IISRIFRIYNAARPQDgyRMVQQFQFLGWPMYrDT 1357
Cdd:cd14599   111 AMVTAEEEGgrSKSHRYWPKLGSKHSSATYGKFkVTTKFRTDsgcYATTGLKVKHLLSGQE--RTVWHLQYTDWPDH-GC 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1358 PVSKRSFLKLIRQVDKWQEEYNGGEGRT-------VVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPN 1430
Cdd:cd14599   188 PEEVQGFLSYLEEIQSVRRHTNSMLDSTkncnppiVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVPVMLRHLREQRMF 267
                         250
                  ....*....|....*....
gi 157419150 1431 MVDLLDQYKFCYEVALEYL 1449
Cdd:cd14599   268 MIQTIAQYKFVYQVLIQFL 286
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
880-1151 3.35e-16

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 81.17  E-value: 3.35e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  880 IRVADLLQHITQmkcaEGYGFKEEYESffEGQSapwdSAKKDENRMKNRYG--NIIAYDHSRVRLQTIEgdtnsDYINGN 957
Cdd:PHA02740   18 INKPDLLSCIIK----EYRAIVPEHED--EANK----ACAQAENKAKDENLalHITRLLHRRIKLFNDE-----KVLDAR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  958 YIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEvgrvKCC--KYWPDD---TEIYKDIKVTLIETELL 1032
Cdd:PHA02740   83 FVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHAD----KKCfnQFWSLKegcVITSDKFQIETLEIIIK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1033 AEYVIRTFAV-EKRGvhEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKS--------KSPPSAGPLVVHCSAGAGRTG 1103
Cdd:PHA02740  159 PHFNLTLLSLtDKFG--QAQKISHFQYTAWPADGFSHDPDAFIDFFCNIDDlcadlekhKADGKIAPIIIDCIDGISSSA 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 157419150 1104 CFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAI 1151
Cdd:PHA02740  237 VFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLI 284
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
1257-1449 3.59e-14

catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein phosphatase non-receptor type 21 (PTPN21), also called protein-tyrosine phosphatase D1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN21 is a component of a multivalent scaffold complex nucleated by focal adhesion kinase (FAK) at specific intracellular sites. It promotes cytoskeleton events that induce cell adhesion and migration by modulating Src-FAK signaling. It can also selectively associate with and stimulate Tec family kinases and modulate Stat3 activation. Human PTPN21 may also play a pathologic role in gastrointestinal tract tumorigenesis. PTPN21 contains an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350446 [Multi-domain]  Cd Length: 220  Bit Score: 73.47  E-value: 3.59e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1257 FIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDPA--QLCPQYWPENGvHRHGPIQV-EFvsadleeDIISRiFRIYNA 1333
Cdd:cd14598    18 YIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGgrEKSFRYWPRLG-SRHNTVTYgRF-------KITTR-FRTDSG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1334 ARPQDGY----------RMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEYN------GGEGRTVVHCLNGGGRSG 1397
Cdd:cd14598    89 CYATTGLkikhlltgqeRTVWHLQYTDWPEH-GCPEDLKGFLSYLEEIQSVRRHTNstidpkSPNPPVLVHCSAGVGRTG 167
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 157419150 1398 TFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALEYL 1449
Cdd:cd14598   168 VVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFL 219
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
192-274 3.93e-13

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 66.45  E-value: 3.93e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150   192 QNVEVNAGQFATFQCSAIGRTVAGDRLWLQGIDVRDAPLKeIKVTSSRRFIASFNVVNTTKRDAGKYRCMIRTEGGVGIS 271
Cdd:pfam00047    4 PTVTVLEGDSATLTCSASTGSPGPDVTWSKEGGTLIESLK-VKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGSATL 82

                   ...
gi 157419150   272 NYA 274
Cdd:pfam00047   83 STS 85
fn3 pfam00041
Fibronectin type III domain;
499-574 2.76e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 60.89  E-value: 2.76e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157419150   499 IFLQWREPTQTYGVITLYEITYKAVSSFDPEIDLSNqsgrvskLGNETHFLFFGLYPGTTYSFTIRASTAKGFGPP 574
Cdd:pfam00041   16 LTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITV-------PGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGPP 84
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
155-638 4.82e-11

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 67.33  E-value: 4.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  155 YQVIFEVITSGHQGYLAIDEVKVLGHPCTRTPHFLRIQNVEVNAGQFATFqcSAIGRTVAGDRLWlqGIDVRDAPLKEIK 234
Cdd:COG3401    21 TAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTG--GRAGTTSGVAAVA--VAAAPPTATGLTT 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  235 VTSSRRFIASFNVVNTTKRDAGKYRCMIRTEGGVGISNYAELVVKEPPVPIAPPQLASVGATYlwiqlnANSINGDGPIV 314
Cdd:COG3401    97 LTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTT------ASSVAGAGVVV 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  315 AREVEYCTASGSWNDRQPVDSTSYKIGHLDPDTEYEISVLLTrpGEGGTGSPGPALRTRTKCADPMRgPRKLEVVEVKSR 394
Cdd:COG3401   171 SPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAAT--DTGGESAPSNEVSVTTPTTPPSA-PTGLTATADTPG 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  395 QITIRWEP-FGYNVTrchSYNLtvhycYQVGGQEQVREEVSWDTENSHpqhTITNLSPYTNVSVKLILMNPEGRK--ESQ 471
Cdd:COG3401   248 SVTLSWDPvTESDAT---GYRV-----YRSNSGDGPFTKVATVTTTSY---TDTGLTNGTTYYYRVTAVDAAGNEsaPSN 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  472 ELIVQTDEDLPGAvPTESIQGSTFEEKIFLQWREPTQTYgvITLYEITYKAVSSFDPEidlsnqsgRVSKLGNETHFLFF 551
Cdd:COG3401   317 VVSVTTDLTPPAA-PSGLTATAVGSSSITLSWTASSDAD--VTGYNVYRSTSGGGTYT--------KIAETVTTTSYTDT 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  552 GLYPGTTYSFTIRASTAKGFGPPATNQFT-TKISAPSMPAYELETPLNQTDNTVTVMLKPAHSRGAPVSVYQIVVEEERP 630
Cdd:COG3401   386 GLTPGTTYYYKVTAVDAAGNESAPSEEVSaTTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTG 465

                  ....*...
gi 157419150  631 RRTKKTTE 638
Cdd:COG3401   466 NAVPFTTT 473
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
499-581 1.44e-10

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 59.05  E-value: 1.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  499 IFLQWREPTQTYGVITLYEITYKAVSSfdpeidlsNQSGRVSK-LGNETHFLFFGLYPGTTYSFTIRASTAKGFGPPATN 577
Cdd:cd00063    17 VTLSWTPPEDDGGPITGYVVEYREKGS--------GDWKEVEVtPGSETSYTLTGLKPGTEYEFRVRAVNGGGESPPSES 88

                  ....*
gi 157419150  578 -QFTT 581
Cdd:cd00063    89 vTVTT 93
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
954-1145 4.23e-10

YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. YopH is an essential virulence determinant of the pathogenic bacterium by dephosphorylating several focal adhesion proteins including p130Cas in human epithelial cells, resulting in the disruption of focal adhesions and cell detachment from the extracellular matrix. It contains an N-terminal domain that contains signals required for TTSS-mediated delivery of YopH into host cells and a C-terminal catalytic PTP domain.


Pssm-ID: 350407 [Multi-domain]  Cd Length: 227  Bit Score: 61.65  E-value: 4.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  954 INGNY--IDGYHRpnhYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYW-PDDTeiYKDIKVT----- 1025
Cdd:cd14559    18 LNANRvqIGNKNV---AIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPPYFrQSGT--YGSVTVKskktg 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1026 ---LIETELLAEYVIRTFAVEKRgvheiREIRQFHFTGWPDHG-VPYHAT----GLLGFVRQVKSKSPPSAGPL------ 1091
Cdd:cd14559    93 kdeLVDGLKADMYNLKITDGNKT-----ITIPVVHVTNWPDHTaISSEGLkelaDLVNKSAEEKRNFYKSKGSSaindkn 167
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 157419150 1092 ----VVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIyncVRELR-SRRVNMVQTEEQYV 1145
Cdd:cd14559   168 kllpVIHCRAGVGRTGQLAAAMELNKSPNNLSVEDI---VSDMRtSRNGKMVQKDEQLD 223
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
1213-1449 2.64e-09

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 60.37  E-value: 2.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1213 NHEKNRCMD---ILPPDRCLPFLITIDGESsNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDV 1289
Cdd:PHA02740   47 AQAENKAKDenlALHITRLLHRRIKLFNDE-KVLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRH 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1290 DPAQLCPQYWP--ENGVHRHGPIQVEFVsadleeDIISRIFRIYNAARPQDGY---RMVQQFQFLGWPM--YRDTPvskR 1362
Cdd:PHA02740  126 ADKKCFNQFWSlkEGCVITSDKFQIETL------EIIIKPHFNLTLLSLTDKFgqaQKISHFQYTAWPAdgFSHDP---D 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1363 SFLKLIRQVDKW-----QEEYNGGEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQ 1437
Cdd:PHA02740  197 AFIDFFCNIDDLcadleKHKADGKIAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDD 276
                         250
                  ....*....|..
gi 157419150 1438 YKFCYEVALEYL 1449
Cdd:PHA02740  277 YVFCYHLIAAYL 288
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
1051-1149 1.55e-07

protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine phosphatase domain-containing protein 1 (PTPDC1) is an uncharacterized non-receptor class protein-tyrosine phosphatase (PTP). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Small interfering RNA (siRNA) knockdown of the ptpdc1 gene is associated with elongated cilia.


Pssm-ID: 350356 [Multi-domain]  Cd Length: 206  Bit Score: 53.51  E-value: 1.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1051 REIRQFHFtGWPDHGVPYHATgLLGFVrQVKSKSPPSAGPLVVHCSAGAGRTG----CFIVidIMLDMAEREgvvdiynC 1126
Cdd:cd14506    75 AGIYFYNF-GWKDYGVPSLTT-ILDIV-KVMAFALQEGGKVAVHCHAGLGRTGvliaCYLV--YALRMSADQ-------A 142
                          90       100
                  ....*....|....*....|...
gi 157419150 1127 VRELRSRRVNMVQTEEQYVFIHD 1149
Cdd:cd14506   143 IRLVRSKRPNSIQTRGQVLCVRE 165
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
1076-1149 4.07e-07

cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This superfamily is composed of cys-based phosphatases, which includes classical protein tyrosine phosphatases (PTPs) as well as dual-specificity phosphatases (DUSPs or DSPs). They are characterized by a CxxxxxR conserved catalytic loop (where C is the catalytic cysteine, x is any amino acid, and R is an arginine). PTPs are part of the tyrosine phosphorylation/dephosphorylation regulatory mechanism, and are important in the response of the cells to physiologic and pathologic changes in their environment. DUSPs show more substrate diversity (including RNA and lipids) and include pTyr, pSer, and pThr phosphatases.


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 50.04  E-value: 4.07e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157419150 1076 FVRQVKSKSPPSaGPLVVHCSAGAGRTGCFIVIDIMLDMaeREGVVDIyncVRELRSRRVN-MVQTEEQYVFIHD 1149
Cdd:cd14494    45 FLEVLDQAEKPG-EPVLVHCKAGVGRTGTLVACYLVLLG--GMSAEEA---VRIVRLIRPGgIPQTIEQLDFLIK 113
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
383-477 5.32e-07

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 49.03  E-value: 5.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  383 PRKLEVVEVKSRQITIRWEPFGYNVTRCHSYNLtvhYCYQVGGQEQVREEVSWDTENShpqHTITNLSPYTNVSVKLILM 462
Cdd:cd00063     4 PTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVV---EYREKGSGDWKEVEVTPGSETS---YTLTGLKPGTEYEFRVRAV 77
                          90
                  ....*....|....*.
gi 157419150  463 NPEGR-KESQELIVQT 477
Cdd:cd00063    78 NGGGEsPPSESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
383-467 5.58e-07

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 48.76  E-value: 5.58e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150    383 PRKLEVVEVKSRQITIRWEPFGYNVTRchSYNLTvhycYQVGGQEQVREEVSWDTENSHPQHTITNLSPYTNVSVKLILM 462
Cdd:smart00060    4 PSNLRVTDVTSTSVTLSWEPPPDDGIT--GYIVG----YRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77

                    ....*
gi 157419150    463 NPEGR 467
Cdd:smart00060   78 NGAGE 82
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
482-572 1.40e-06

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 47.61  E-value: 1.40e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150    482 PGAVPTESIQGSTfEEKIFLQWREPTqtYGVITLYEITYKAVSSfdpeiDLSNQSGRVSKLGNETHFLFFGLYPGTTYSF 561
Cdd:smart00060    1 PSPPSNLRVTDVT-STSVTLSWEPPP--DDGITGYIVGYRVEYR-----EEGSEWKEVNVTPSSTSYTLTGLKPGTEYEF 72
                            90
                    ....*....|.
gi 157419150    562 TIRASTAKGFG 572
Cdd:smart00060   73 RVRAVNGAGEG 83
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1031-1149 2.72e-06

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 48.43  E-value: 2.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1031 LLAEYVIRTFAVEKRGVheireirQFHFTGWPDHGVPyHATGLLGFVRQVKSKSPPSaGPLVVHCSAGAGRTGCFIvidI 1110
Cdd:COG2453    32 LTEEEELLLGLLEEAGL-------EYLHLPIPDFGAP-DDEQLQEAVDFIDEALREG-KKVLVHCRGGIGRTGTVA---A 99
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 157419150 1111 MLDMAEREGVVDIYNCVRELRSRRvnmVQTEEQYVFIHD 1149
Cdd:COG2453   100 AYLVLLGLSAEEALARVRAARPGA---VETPAQRAFLER 135
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
282-361 1.80e-05

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 44.53  E-value: 1.80e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150    282 PVPIAPPQLASVGATYLWIQ-LNANSINGDGPIVAREVEYCTASGSWND-RQPVDSTSYKIGHLDPDTEYEISVL-LTRP 358
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSwEPPPDDGITGYIVGYRVEYREEGSEWKEvNVTPSSTSYTLTGLKPGTEYEFRVRaVNGA 80

                    ...
gi 157419150    359 GEG 361
Cdd:smart00060   81 GEG 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
192-278 1.83e-05

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 44.42  E-value: 1.83e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150    192 QNVEVNAGQFATFQCSAIGRTVAgDRLWLQGIDVRDAPLKEIKVTSSRrFIASFNVVNTTKRDAGKYRCMIRTEGGVGIS 271
Cdd:smart00410    2 PSVTVKEGESVTLSCEASGSPPP-EVTWYKQGGKLLAESGRFSVSRSG-STSTLTISNVTPEDSGTYTCAATNSSGSASS 79

                    ....*..
gi 157419150    272 NyAELVV 278
Cdd:smart00410   80 G-TTLTV 85
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
1357-1443 2.26e-05

cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This superfamily is composed of cys-based phosphatases, which includes classical protein tyrosine phosphatases (PTPs) as well as dual-specificity phosphatases (DUSPs or DSPs). They are characterized by a CxxxxxR conserved catalytic loop (where C is the catalytic cysteine, x is any amino acid, and R is an arginine). PTPs are part of the tyrosine phosphorylation/dephosphorylation regulatory mechanism, and are important in the response of the cells to physiologic and pathologic changes in their environment. DUSPs show more substrate diversity (including RNA and lipids) and include pTyr, pSer, and pThr phosphatases.


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 45.03  E-value: 2.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1357 TPVSKRSFLKLIRQVDKwqeeyngGEGRTVVHCLNGGGRSGTFCAisivCEMLRHQRTvDVFHAVKTLRNNKPN-MVDLL 1435
Cdd:cd14494    38 TLAMVDRFLEVLDQAEK-------PGEPVLVHCKAGVGRTGTLVA----CYLVLLGGM-SAEEAVRIVRLIRPGgIPQTI 105

                  ....*...
gi 157419150 1436 DQYKFCYE 1443
Cdd:cd14494   106 EQLDFLIK 113
I-set pfam07679
Immunoglobulin I-set domain;
186-267 1.38e-04

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 42.24  E-value: 1.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150   186 PHFLR-IQNVEVNAGQFATFQCSAIGR---TVAgdrlWLQGidvrDAPLKeikvtSSRRF-------IASFNVVNTTKRD 254
Cdd:pfam07679    1 PKFTQkPKDVEVQEGESARFTCTVTGTpdpEVS----WFKD----GQPLR-----SSDRFkvtyeggTYTLTISNVQPDD 67
                           90
                   ....*....|...
gi 157419150   255 AGKYRCMIRTEGG 267
Cdd:pfam07679   68 SGKYTCVATNSAG 80
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
1076-1147 1.46e-04

dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as VH1-like phosphatase Z (VHZ) or low molecular mass dual specificity phosphatase 3 (LDP-3), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. DUSP23 is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. It is able to enhance activation of JNK and p38 MAPK, and has been shown to dephosphorylate p44-ERK1 (MAPK3) in vitro. It has been associated with cell growth and human primary cancers. It has also been identified as a cell-cell adhesion regulatory protein; it promotes the dephosphorylation of beta-catenin at Tyr 142 and enhances the interaction between alpha- and beta-catenin.


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 43.42  E-value: 1.46e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157419150 1076 FVRQVKsKSPPSAGPLVVHCSAGAGRTG----CFIVIDIMLDMAEregvvdiynCVRELRSRRVNMVQTEEQYVFI 1147
Cdd:cd14504    71 FLDIVE-EANAKNEAVLVHCLAGKGRTGtmlaCYLVKTGKISAVD---------AINEIRRIRPGSIETSEQEKFV 136
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
282-374 1.73e-04

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 42.10  E-value: 1.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150  282 PVPIAPPQLASVGATYLWIQLNANSINGdGPIVAREVEYCTA-SGSWN--DRQPVDSTSYKIGHLDPDTEYEISVLLTRp 358
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDG-GPITGYVVEYREKgSGDWKevEVTPGSETSYTLTGLKPGTEYEFRVRAVN- 78
                          90
                  ....*....|....*.
gi 157419150  359 gEGGTGSPGPALRTRT 374
Cdd:cd00063    79 -GGGESPPSESVTVTT 93
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
1257-1439 1.92e-04

YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. YopH is an essential virulence determinant of the pathogenic bacterium by dephosphorylating several focal adhesion proteins including p130Cas in human epithelial cells, resulting in the disruption of focal adhesions and cell detachment from the extracellular matrix. It contains an N-terminal domain that contains signals required for TTSS-mediated delivery of YopH into host cells and a C-terminal catalytic PTP domain.


Pssm-ID: 350407 [Multi-domain]  Cd Length: 227  Bit Score: 44.70  E-value: 1.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1257 FIVTQHPLPNTVKDFWRLVLDYHCTSVVML--NDVDPAQLCPQYWPENGvhRHGPIQV--EFVSADLEEDIISriFRIYN 1332
Cdd:cd14559    31 AIACQYPKNEQLEDHLKMLADNRTPCLVVLasNKDIQRKGLPPYFRQSG--TYGSVTVksKKTGKDELVDGLK--ADMYN 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1333 AARPQDGYRM-VQQFQFLGWPmyrD-TPVSKRSFLKLIRQVDKWQEEYNGG-------------EGRTVVHCLNGGGRSG 1397
Cdd:cd14559   107 LKITDGNKTItIPVVHVTNWP---DhTAISSEGLKELADLVNKSAEEKRNFykskgssaindknKLLPVIHCRAGVGRTG 183
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 157419150 1398 TFCAisiVCEMLRHQRTV---DVFHAVKTLRNNKpnMVDLLDQYK 1439
Cdd:cd14559   184 QLAA---AMELNKSPNNLsveDIVSDMRTSRNGK--MVQKDEQLD 223
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
1024-1149 4.24e-04

cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of eukaryotic cyclin-dependent kinase inhibitor 3 (CDKN3) and related archaeal and bacterial proteins. CDKN3 is also known as kinase-associated phosphatase (KAP), CDK2-associated dual-specificity phosphatase, cyclin-dependent kinase interactor 1 (CDI1), or cyclin-dependent kinase-interacting protein 2 (CIP2). It has been characterized as dual-specificity phosphatase, which function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and protein-tyrosine-phosphatase (EC 3.1.3.48). It dephosphorylates CDK2 at a threonine residue in a cyclin-dependent manner, resulting in the inhibition of G1/S cell cycle progression. It also interacts with CDK1 and controls progression through mitosis by dephosphorylating CDC2. CDKN3 may also function as a tumor suppressor; its loss of function was found in a variety of cancers including glioblastoma and hepatocellular carcinoma. However, it has also been found over-expressed in many cancers such as breast, cervical, lung and prostate cancers, and may also have an oncogenic function.


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 42.64  E-value: 4.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1024 VTLIETELLAEYVIRTF--AVEKRGvheireIRQFHFTgWPDHGVP----YHATgLLGFVRQVKSKSppsaGPLVVHCSA 1097
Cdd:cd14505    48 VTLCTDGELEELGVPDLleQYQQAG------ITWHHLP-IPDGGVPsdiaQWQE-LLEELLSALENG----KKVLIHCKG 115
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 157419150 1098 GAGRTGcFIVIDIMLDMAEREGVVDIYNCVRELRSRrvnMVQTEEQYVFIHD 1149
Cdd:cd14505   116 GLGRTG-LIAACLLLELGDTLDPEQAIAAVRALRPG---AIQTPKQENFLHQ 163
PTPLP-like cd14495
Protein tyrosine phosphatase-like domains of phytases and similar domains; This subfamily ...
1010-1114 6.81e-04

Protein tyrosine phosphatase-like domains of phytases and similar domains; This subfamily contains the tandem protein tyrosine phosphatase (PTP)-like domains of protein tyrosine phosphatase-like phytases (PTPLPs) and similar domains including the PTP domain of Pseudomonas syringae tyrosine-protein phosphatase hopPtoD2. PTPLPs, also known as cysteine phytases, are one of four known classes of phytases, enzymes that degrade phytate (inositol hexakisphosphate [InsP(6)]) to less-phosphorylated myo-inositol derivatives. Phytate is the most abundant cellular inositol phosphate and plays important roles in a broad scope of cellular processes, including DNA repair, RNA processing and export, development, apoptosis, and pathogenicity. PTPLPs adopt a PTP fold, including the active-site signature sequence (CX5R(S/T)) and utilize a classical PTP reaction mechanism. However, these enzymes display no catalytic activity against classical PTP substrates due to several unique structural features that confer specificity for myo-inositol polyphosphates.


Pssm-ID: 350345  Cd Length: 278  Bit Score: 43.13  E-value: 6.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1010 KYWPDDTEIYKDIKVTLIETEllaEYVirtfaVEKRGVHEIREIRQFHFtgWPDhgvPYHATGLLGFVRQVksksPPSAG 1089
Cdd:cd14495   126 KDKKKSPSQPKTVKVESVRTE---EEL-----VKKKGAHYVRIAATDHV--WPD---DEEIDAFVAFYRSL----PADAW 188
                          90       100
                  ....*....|....*....|....*
gi 157419150 1090 pLVVHCSAGAGRTGCFIVidiMLDM 1114
Cdd:cd14495   189 -LHFHCRAGKGRTTTFMV---MYDM 209
fn3 pfam00041
Fibronectin type III domain;
284-361 1.15e-03

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 39.32  E-value: 1.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150   284 PIAPPQLASVGATYLWIQLNANSiNGDGPIVAREVEYCTASGSWNDRQ---PVDSTSYKIGHLDPDTEYEISVlLTRPGE 360
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPP-DGNGPITGYEVEYRPKNSGEPWNEitvPGTTTSVTLTGLKPGTEYEVRV-QAVNGG 79

                   .
gi 157419150   361 G 361
Cdd:pfam00041   80 G 80
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
1357-1443 1.81e-03

cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of eukaryotic cyclin-dependent kinase inhibitor 3 (CDKN3) and related archaeal and bacterial proteins. CDKN3 is also known as kinase-associated phosphatase (KAP), CDK2-associated dual-specificity phosphatase, cyclin-dependent kinase interactor 1 (CDI1), or cyclin-dependent kinase-interacting protein 2 (CIP2). It has been characterized as dual-specificity phosphatase, which function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and protein-tyrosine-phosphatase (EC 3.1.3.48). It dephosphorylates CDK2 at a threonine residue in a cyclin-dependent manner, resulting in the inhibition of G1/S cell cycle progression. It also interacts with CDK1 and controls progression through mitosis by dephosphorylating CDC2. CDKN3 may also function as a tumor suppressor; its loss of function was found in a variety of cancers including glioblastoma and hepatocellular carcinoma. However, it has also been found over-expressed in many cancers such as breast, cervical, lung and prostate cancers, and may also have an oncogenic function.


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 40.71  E-value: 1.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1357 TPVSKRSFLKLIRQVdkwQEEYNGGEgRTVVHCLNGGGRSGTFCAisivCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLD 1436
Cdd:cd14505    85 VPSDIAQWQELLEEL---LSALENGK-KVLIHCKGGLGRTGLIAA----CLLLELGDTLDPEQAIAAVRALRPGAIQTPK 156

                  ....*..
gi 157419150 1437 QYKFCYE 1443
Cdd:cd14505   157 QENFLHQ 163
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1346-1440 1.89e-03

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 39.95  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150 1346 FQFLGWPMYRDTPVSKRSFLKLIRQVDKWQEEynggEGRTVVHCLNGGGRSGTFCAisivCEMLRHQRTVDvfHAVKTLR 1425
Cdd:COG2453    48 LEYLHLPIPDFGAPDDEQLQEAVDFIDEALRE----GKKVLVHCRGGIGRTGTVAA----AYLVLLGLSAE--EALARVR 117
                          90
                  ....*....|....*
gi 157419150 1426 NNKPNMVDLLDQYKF 1440
Cdd:COG2453   118 AARPGAVETPAQRAF 132
fn3 pfam00041
Fibronectin type III domain;
383-463 2.38e-03

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 38.55  E-value: 2.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157419150   383 PRKLEVVEVKSRQITIRWEP--------FGYNVTrchsynltvhyCYQVGGQEQVREEvswDTENSHPQHTITNLSPYTN 454
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPppdgngpiTGYEVE-----------YRPKNSGEPWNEI---TVPGTTTSVTLTGLKPGTE 68

                   ....*....
gi 157419150   455 VSVKLILMN 463
Cdd:pfam00041   69 YEVRVQAVN 77
DUSP14-like cd14514
dual specificity protein phosphatases 14, 18, 21, 28 and similar proteins; This family is ...
1369-1430 3.80e-03

dual specificity protein phosphatases 14, 18, 21, 28 and similar proteins; This family is composed of dual specificity protein phosphatase 14 (DUSP14, also known as MKP-6), 18 (DUSP18), 21 (DUSP21), 28 (DUSP28), and similar proteins. They function as protein-serine/threonine phosphatases (EC 3.1.3.16) and protein-tyrosine-phosphatases (EC 3.1.3.48), and are atypical DUSPs. They contain the catalytic dual specificity phosphatase domain but lack the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. DUSP14 directly interacts and dephosphorylates TGF-beta-activated kinase 1 (TAK1)-binding protein 1 (TAB1) in T cells, and negatively regulates TCR signaling and immune responses. DUSP18 has been shown to interact and dephosphorylate SAPK/JNK, and may play a role in regulating the SAPK/JNK pathway. DUSP18 and DUSP21 target to opposing sides of the mitochondrial inner membrane. DUSP28 has been implicated in hepatocellular carcinoma progression and in migratory activity and drug resistance of pancreatic cancer cells.


Pssm-ID: 350364 [Multi-domain]  Cd Length: 133  Bit Score: 39.07  E-value: 3.80e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157419150 1369 RQVDKWQEEYNGGeGRTVVHCLNGGGRSGTFCAISIVCemLRHQRTVDVFHAVKTLRNN-KPN 1430
Cdd:cd14514    65 EVADKIHQVKRRG-GRTLVHCVAGVSRSATLCLAYLMK--YEGMTLREAYKHVKAARPIiRPN 124
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH