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Conserved domains on  [gi|568922106|ref|XP_006501213|]
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tyrosine-protein phosphatase non-receptor type 22 isoform X1 [Mus musculus]

Protein Classification

PTPc-N22 domain-containing protein( domain architecture ID 12998656)

PTPc-N22 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 57-290 1.31e-175

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: 503.99  E-value: 1.31e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  57 KNRYKDILPYDHSLVELSLLTSDEDSSYINASFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYRILVIVMACMEFEMGK 136
Cdd:cd14602    1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 137 KKCERYWAEPGETQLQFGPFSISCEAEKKKSDYKIRTLKAKFNNETRIIYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQ 216
Cdd:cd14602   81 KKCERYWAEPGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQ 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568922106 217 EDDCVPICIHCSAGCGRTGVICAVDYTWMLLKDGIIPKNFSVFNLIQEMRTQRPSLVQTQEQYELVYSAVLELF 290
Cdd:cd14602  161 EDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIELF 234
 
Name Accession Description Interval E-value
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 57-290 1.31e-175

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: 503.99  E-value: 1.31e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  57 KNRYKDILPYDHSLVELSLLTSDEDSSYINASFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYRILVIVMACMEFEMGK 136
Cdd:cd14602    1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 137 KKCERYWAEPGETQLQFGPFSISCEAEKKKSDYKIRTLKAKFNNETRIIYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQ 216
Cdd:cd14602   81 KKCERYWAEPGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQ 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568922106 217 EDDCVPICIHCSAGCGRTGVICAVDYTWMLLKDGIIPKNFSVFNLIQEMRTQRPSLVQTQEQYELVYSAVLELF 290
Cdd:cd14602  161 EDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIELF 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
24-288 2.79e-113

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 344.64  E-value: 2.79e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106    24 FASEFLKLKRQstkykADKIYPTTVAQRPKNIKKNRYKDILPYDHSLVELSLLTsDEDSSYINASFIKGVYGPKAYIATQ 103
Cdd:smart00194   2 LEEEFEKLDRL-----KPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPP-GEGSDYINASYIDGPNGPKAYIATQ 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106   104 GPLSTTLLDFWRMIWEYRILVIVMACMEFEMGKKKCERYWAEPGETQLQFGPFSISCEAEKKKSDYKIRTLKAKF--NNE 181
Cdd:smart00194  76 GPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNtgCSE 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106   182 TRIIYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQEDDCVPICIHCSAGCGRTGVICAVDYTWMLLKDGiipKNFSVFNL 261
Cdd:smart00194 156 TRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAG---KEVDIFEI 232

                          250       260
                   ....*....|....*....|....*..
gi 568922106   262 IQEMRTQRPSLVQTQEQYELVYSAVLE 288
Cdd:smart00194 233 VKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
54-288 4.61e-104

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 319.57  E-value: 4.61e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106   54 NIKKNRYKDILPYDHSLVELSllTSDEDSSYINASFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYRILVIVMACMEFE 133
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLT--GDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  134 MGKKKCERYWAEPGETQLQFGPFSISCEAEKK-KSDYKIRTL--KAKFNNETRIIYQFHYKNWPDHDVPSSIDPILQLIW 210
Cdd:pfam00102  79 KGREKCAQYWPEEEGESLEYGDFTVTLKKEKEdEKDYTVRTLevSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568922106  211 DMRCYQEDDCV-PICIHCSAGCGRTGVICAVDYTWMLLKDGIIpknFSVFNLIQEMRTQRPSLVQTQEQYELVYSAVLE 288
Cdd:pfam00102 159 KVRKSSLDGRSgPIVVHCSAGIGRTGTFIAIDIALQQLEAEGE---VDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
22-280 4.60e-43

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 157.95  E-value: 4.60e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  22 EEFASEFLKLKRQSTKYKADKIYPTTVAQRPKNikknRYKDILPYDHSLVElslltsdEDSSYINASFIKgVYGPKAYIA 101
Cdd:COG5599   14 EKINSRLSTLTNELAPSHNDPQYLQNINGSPLN----RFRDIQPYKETALR-------ANLGYLNANYIQ-VIGNHRYIA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 102 TQGPLSTTLLDFWRMIWEYRILVIVM--ACMEFEMGKKKCERYWaepgETQLQFGPFSISCEAEKK---KSDYKIRTLKA 176
Cdd:COG5599   82 TQYPLEEQLEDFFQMLFDNNTPVLVVlaSDDEISKPKVKMPVYF----RQDGEYGKYEVSSELTESiqlRDGIEARTYVL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 177 KFNN---ETRIIYQFHYKNWPDHDVPSS--IDPILQLIWDMRCYQEDDCVPICIHCSAGCGRTGVICAVDYTWMLLKDGI 251
Cdd:COG5599  158 TIKGtgqKKIEIPVLHVKNWPDHGAISAeaLKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALV 237

                        250       260       270
                 ....*....|....*....|....*....|
gi 568922106 252 IpKNFSVFNLIQEMRTQR-PSLVQTQEQYE 280
Cdd:COG5599  238 Q-ITLSVEEIVIDMRTSRnGGMVQTSEQLD 266
PHA02738 PHA02738
hypothetical protein; Provisional
 26-286 2.74e-37

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 142.37  E-value: 2.74e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  26 SEFLKL----------KRQSTKYKADKIYPTTVAQRpKNIKKNRYKDILPYDHSLVELSllTSDEDSSYINASFIKGVYG 95
Cdd:PHA02738  12 AEFLALmeksdceeviTREHQKVISEKVDGTFNAEK-KNRKLNRYLDAVCFDHSRVILP--AERNRGDYINANYVDGFEY 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  96 PKAYIATQGPLSTTLLDFWRMIWEYRILVIVMACMEFEMGKKKCERYWAEPGETQLQFGPFSISCEAEKKKSDYKIRTLK 175
Cdd:PHA02738  89 KKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDVEQGSIRFGKFKITTTQVETHPHYVKSTLL 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 176 AKFNNE-TRIIYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQED-------------DCVPICIHCSAGCGRTGVICAVD 241
Cdd:PHA02738 169 LTDGTSaTQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRQCQKElaqeslqighnrlQPPPIVVHCNAGLGRTPCYCVVD 248

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 568922106 242 YTWMLLKDGiipKNFSVFNLIQEMRTQRPSLVQTQEQYELVYSAV 286
Cdd:PHA02738 249 ISISRFDAC---ATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAV 290
 
Name Accession Description Interval E-value
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 57-290 1.31e-175

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: 503.99  E-value: 1.31e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  57 KNRYKDILPYDHSLVELSLLTSDEDSSYINASFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYRILVIVMACMEFEMGK 136
Cdd:cd14602    1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 137 KKCERYWAEPGETQLQFGPFSISCEAEKKKSDYKIRTLKAKFNNETRIIYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQ 216
Cdd:cd14602   81 KKCERYWAEPGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQ 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568922106 217 EDDCVPICIHCSAGCGRTGVICAVDYTWMLLKDGIIPKNFSVFNLIQEMRTQRPSLVQTQEQYELVYSAVLELF 290
Cdd:cd14602  161 EDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIELF 234
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 2-294 1.20e-164

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: 478.27  E-value: 1.20e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106   2 DQREILQQLLKEAQKKKL---NSEE-FASEFLKLKRQSTKYKADKIYPTTVAQRPKNIKKNRYKDILPYDHSLVELSLLT 77
Cdd:cd14604    1 EQVEILKKFIERVQAMKStdhNGEDnFASDFMRLRRLSTKYRTEKIYPTATGEKEENVKKNRYKDILPFDHSRVKLTLKT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  78 SDEDSSYINASFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYRILVIVMACMEFEMGKKKCERYWAEPGETQLQFGPFS 157
Cdd:cd14604   81 SSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWPLYGEEPMTFGPFR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 158 ISCEAEKKKSDYKIRTLKAKFNNETRIIYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQEDDCVPICIHCSAGCGRTGVI 237
Cdd:cd14604  161 ISCEAEQARTDYFIRTLLLEFQNETRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAI 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568922106 238 CAVDYTWMLLKDGIIPKNFSVFNLIQEMRTQRPSLVQTQEQYELVYSAVLELFKRHM 294
Cdd:cd14604  241 CAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQLFEKQL 297
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 84-283 4.46e-138

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: 406.42  E-value: 4.46e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  84 YINASFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYRILVIVMACMEFEMGKKKCERYWAEPGETQLQFGPFSISCEAE 163
Cdd:cd14542    1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQLQFGPFKISLEKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 164 KKKS-DYKIRTLKAKFNNETRIIYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQEDDCVPICIHCSAGCGRTGVICAVDY 242
Cdd:cd14542   81 KRVGpDFLIRTLKVTFQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGCGRTGTICAIDY 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 568922106 243 TWMLLKDGIIPKNFSVFNLIQEMRTQRPSLVQTQEQYELVY 283
Cdd:cd14542  161 VWNLLKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVY 201
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 25-290 2.09e-127

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: 381.48  E-value: 2.09e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  25 ASEFLKLKRQSTKYKADKIYPTTVAQRPKNIKKNRYKDILPYDHSLVELSLLTSDEDSSYINASFIKGVYGPKAYIATQG 104
Cdd:cd14603    1 AGEFSEIRACSAAFKADYVCSTVAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 105 PLSTTLLDFWRMIWEYRILVIVMACMEFEMGKKKCERYWAEPGETqLQFGPFSIS-CEAEKKKSDYKIRTLKAKFNNETR 183
Cdd:cd14603   81 PLSHTVLDFWRMIWQYGVKVILMACREIEMGKKKCERYWAQEQEP-LQTGPFTITlVKEKRLNEEVILRTLKVTFQKESR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 184 IIYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQEDDCVPICIHCSAGCGRTGVICAVDYTWMLLKDGIIPKNFSVFNLIQ 263
Cdd:cd14603  160 SVSHFQYMAWPDHGIPDSPDCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPDFSIFDVVL 239

                        250       260
                 ....*....|....*....|....*..
gi 568922106 264 EMRTQRPSLVQTQEQYELVYSAVLELF 290
Cdd:cd14603  240 EMRKQRPAAVQTEEQYEFLYHTVAQMF 266
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
24-288 2.79e-113

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 344.64  E-value: 2.79e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106    24 FASEFLKLKRQstkykADKIYPTTVAQRPKNIKKNRYKDILPYDHSLVELSLLTsDEDSSYINASFIKGVYGPKAYIATQ 103
Cdd:smart00194   2 LEEEFEKLDRL-----KPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPP-GEGSDYINASYIDGPNGPKAYIATQ 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106   104 GPLSTTLLDFWRMIWEYRILVIVMACMEFEMGKKKCERYWAEPGETQLQFGPFSISCEAEKKKSDYKIRTLKAKF--NNE 181
Cdd:smart00194  76 GPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNtgCSE 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106   182 TRIIYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQEDDCVPICIHCSAGCGRTGVICAVDYTWMLLKDGiipKNFSVFNL 261
Cdd:smart00194 156 TRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAG---KEVDIFEI 232

                          250       260
                   ....*....|....*....|....*..
gi 568922106   262 IQEMRTQRPSLVQTQEQYELVYSAVLE 288
Cdd:smart00194 233 VKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
54-288 4.61e-104

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 319.57  E-value: 4.61e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106   54 NIKKNRYKDILPYDHSLVELSllTSDEDSSYINASFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYRILVIVMACMEFE 133
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLT--GDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  134 MGKKKCERYWAEPGETQLQFGPFSISCEAEKK-KSDYKIRTL--KAKFNNETRIIYQFHYKNWPDHDVPSSIDPILQLIW 210
Cdd:pfam00102  79 KGREKCAQYWPEEEGESLEYGDFTVTLKKEKEdEKDYTVRTLevSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568922106  211 DMRCYQEDDCV-PICIHCSAGCGRTGVICAVDYTWMLLKDGIIpknFSVFNLIQEMRTQRPSLVQTQEQYELVYSAVLE 288
Cdd:pfam00102 159 KVRKSSLDGRSgPIVVHCSAGIGRTGTFIAIDIALQQLEAEGE---VDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 84-283 9.40e-89

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: 278.40  E-value: 9.40e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  84 YINASFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYRILVIVMACMEFEMGKKKCERYWAEPGETQLQFGPFSISCEAE 163
Cdd:cd00047    1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPLEYGDITVTLVSE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 164 KKKSDYKIRTLKAKFNN--ETRIIYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQEDDCVPICIHCSAGCGRTGVICAVD 241
Cdd:cd00047   81 EELSDYTIRTLELSPKGcsESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTGTFIAID 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 568922106 242 YTWMLLKDGiipKNFSVFNLIQEMRTQRPSLVQTQEQYELVY 283
Cdd:cd00047  161 ILLERLEAE---GEVDVFEIVKALRKQRPGMVQTLEQYEFIY 199
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 52-284 1.18e-69

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: 230.33  E-value: 1.18e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  52 PKNIKKNRYKDILPYDHSLVELSLLTSDEDSSYINASFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYRILVIVMACME 131
Cdd:cd14543   27 PANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLVIVMTTRV 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 132 FEMGKKKCERYWAEPGETQLQFGPFSISCEAEKKKSDYKIRTLK--AKFNNETRIIYQFHYKNWPDHDVPSSIDPILQLI 209
Cdd:cd14543  107 VERGRVKCGQYWPLEEGSSLRYGDLTVTNLSVENKEHYKKTTLEihNTETDESRQVTHFQFTSWPDFGVPSSAAALLDFL 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 210 WDMRCYQEDDCV-------------PICIHCSAGCGRTGVICAVDYTWMLLKD-GIIpknfSVFNLIQEMRTQRPSLVQT 275
Cdd:cd14543  187 GEVRQQQALAVKamgdrwkghppgpPIVVHCSAGIGRTGTFCTLDICLSQLEDvGTL----NVMQTVRRMRTQRAFSIQT 262


                 ....*....
gi 568922106 276 QEQYELVYS 284
Cdd:cd14543  263 PDQYYFCYK 271
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 59-279 1.48e-69

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: 228.39  E-value: 1.48e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  59 RYKDILPYDHSLVELSLLTSDEDSSYINASFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYRILVIVMACMEFEMGKKK 138
Cdd:cd14548    1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 139 CERYWAEpGETQLQFGPFSISCEAEKKKSDYKIRTLKAKFNNETRIIYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQED 218
Cdd:cd14548   81 CDHYWPF-DQDPVYYGDITVTMLSESVLPDWTIREFKLERGDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDYIKQ 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568922106 219 DCVPICIHCSAGCGRTGVICAVDYtwmlLKDGIIPKNF-SVFNLIQEMRTQRPSLVQTQEQY 279
Cdd:cd14548  160 EKGPTIVHCSAGVGRTGTFIALDR----LLQQIESEDYvDIFGIVYDLRKHRPLMVQTEAQY 217
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 54-286 5.84e-66

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: 219.64  E-value: 5.84e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  54 NIKKNRYKDILPYDHSLVELSLLTSDED-SSYINASFIK------GVYGP-KAYIATQGPLSTTLLDFWRMIWEYRILVI 125
Cdd:cd14544    1 NKGKNRYKNILPFDHTRVILKDRDPNVPgSDYINANYIRnenegpTTDENaKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 126 VMACMEFEMGKKKCERYWAEPGETQlQFGPFSISCEAEKKKSDYKIRTL---KAKFNNETRIIYQFHYKNWPDHDVPSSI 202
Cdd:cd14544   81 VMTTKEVERGKNKCVRYWPDEGMQK-QYGPYRVQNVSEHDTTDYTLRELqvsKLDQGDPIREIWHYQYLSWPDHGVPSDP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 203 DPILQLIWDMRCYQE--DDCVPICIHCSAGCGRTGVICAVDytwMLLKdgIIPKN-----FSVFNLIQEMRTQRPSLVQT 275
Cdd:cd14544  160 GGVLNFLEDVNQRQEslPHAGPIVVHCSAGIGRTGTFIVID---MLLD--QIKRKgldcdIDIQKTIQMVRSQRSGMVQT 234

                        250
                 ....*....|.
gi 568922106 276 QEQYELVYSAV 286
Cdd:cd14544  235 EAQYKFIYVAV 245
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 84-283 3.03e-64

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: 213.65  E-value: 3.03e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  84 YINASFIK-GVYGPKAYIATQGPLSTTLLDFWRMIWEYRILVIVMACMEFEMGKKKCERYWAEpGETQLQFGPFSISC-- 160
Cdd:cd18533    1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPS-GEYEGEYGDLTVELvs 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 161 EAEKKKSDYKIRTLK-AKFNNETRIIYQFHYKNWPDHDVPSSIDPILQLIwdmRC-----YQEDDCVPICIHCSAGCGRT 234
Cdd:cd18533   80 EEENDDGGFIVREFElSKEDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLI---KLkrelnDSASLDPPIIVHCSAGVGRT 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568922106 235 GVICAVDyTWM-LLKDGIIPKNFS------VFNLIQEMRTQRPSLVQTQEQYELVY 283
Cdd:cd18533  157 GTFIALD-SLLdELKRGLSDSQDLedsedpVYEIVNQLRKQRMSMVQTLRQYIFLY 211
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 58-283 1.16e-61

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: 207.25  E-value: 1.16e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  58 NRYKDILPYDHSLVELSLLTSDEDSSYINASFIKGVYG-PKAYIATQGPLSTTLLDFWRMIWEYRILVIVMACMEFEMgK 136
Cdd:cd14547    1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYDGeEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA-K 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 137 KKCERYWaePGETQLQFGPFSISCEAEKKKSDYKIRTLKAKFNNETRIIYQFHYKNWPDHDVPSSIDPILQLIWDMRCY- 215
Cdd:cd14547   80 EKCAQYW--PEEENETYGDFEVTVQSVKETDGYTVRKLTLKYGGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEEAr 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 216 -QEDDCVPICIHCSAGCGRTGVICAVDY-TWMLLKDGIIpknfSVFNLIQEMRTQRPSLVQTQEQYELVY 283
Cdd:cd14547  158 qTEPHRGPIVVHCSAGIGRTGCFIATSIgCQQLREEGVV----DVLGIVCQLRLDRGGMVQTAEQYEFVH 223
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 54-288 1.79e-60

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: 204.55  E-value: 1.79e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  54 NIKKNRYKDILPYDHSLVELSLLTSDEDSSYINASFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYRILVIVMACMEFE 133
Cdd:cd14553    3 NKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 134 MGKKKCERYWaePGETQLQFGPFSISCEAEKKKSDYKIRTLKAKFN--NETRIIYQFHYKNWPDHDVPSSIDPILQLIWD 211
Cdd:cd14553   83 RSRVKCDQYW--PTRGTETYGLIQVTLLDTVELATYTVRTFALHKNgsSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRR 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568922106 212 MRCYQEDDCVPICIHCSAGCGRTGVICAVDYTWMLLKDGiipKNFSVFNLIQEMRTQRPSLVQTQEQYELVYSAVLE 288
Cdd:cd14553  161 VKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHE---KTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLE 234
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 53-288 8.76e-60

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: 202.56  E-value: 8.76e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  53 KNIKKNRYKDILPYDHSLVELSLLTSDEDSSYINASFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYRILVIVMACMEF 132
Cdd:cd14630    2 ENRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 133 EMGKKKCERYWaePGETQLqFGPFSISCEAEKKKSDYKIR--TLKAKFNNETRIIYQFHYKNWPDHDVPSSIDPILQLIW 210
Cdd:cd14630   82 EVGRVKCVRYW--PDDTEV-YGDIKVTLIETEPLAEYVIRtfTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGFVR 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568922106 211 DMRCYQEDDCVPICIHCSAGCGRTGVICAVDYTW-MLLKDGIIpknfSVFNLIQEMRTQRPSLVQTQEQYELVYSAVLE 288
Cdd:cd14630  159 QVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLdMAENEGVV----DIFNCVRELRAQRVNMVQTEEQYVFVHDAILE 233
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 58-289 1.99e-58

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: 198.57  E-value: 1.99e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  58 NRYKDILPYDHSLVELSLLTSDEDSSYINASFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYRILVIVMACMEFEMGKK 137
Cdd:cd14619    1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 138 KCERYWaePGETQ-LQFGPFSISCEAEKKKSDYKIR--TLKAKFNNETRIIYQFHYKNWPDHDVPSSIDPILQLiWDM-R 213
Cdd:cd14619   81 KCEHYW--PLDYTpCTYGHLRVTVVSEEVMENWTVRefLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAF-RRLlR 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568922106 214 CY--QEDDCVPICIHCSAGCGRTGVICAVDYtwmLLKDGIIPKNFSVFNLIQEMRTQRPSLVQTQEQYELVYSAVLEL 289
Cdd:cd14619  158 QWldQTMSGGPTVVHCSAGVGRTGTLIALDV---LLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDF 232
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 49-287 1.06e-57

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: 196.98  E-value: 1.06e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  49 AQRPKNIKKNRYKDILPYDHSLVELSLLTSDEDSSYINASFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYRILVIVMA 128
Cdd:cd14554    1 ANLPCNKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 129 CMEFEMGKKKCERYWaePGETQLQFGPFSISCEAEKKKSDYKIRTLKAKFNN--ETRIIYQFHYKNWPDHDVPSSIDPIL 206
Cdd:cd14554   81 TKLREMGREKCHQYW--PAERSARYQYFVVDPMAEYNMPQYILREFKVTDARdgQSRTVRQFQFTDWPEQGVPKSGEGFI 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 207 QLIWDM-RCYQEDDCV-PICIHCSAGCGRTGVICAVDYTWMLLK-DGIIpknfSVFNLIQEMRTQRPSLVQTQEQYELVY 283
Cdd:cd14554  159 DFIGQVhKTKEQFGQEgPITVHCSAGVGRTGVFITLSIVLERMRyEGVV----DVFQTVKLLRTQRPAMVQTEDQYQFCY 234


                 ....
gi 568922106 284 SAVL 287
Cdd:cd14554  235 RAAL 238
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 50-288 1.47e-57

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: 197.41  E-value: 1.47e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  50 QRPKNIKKNRYKDILPYDHSLVELSLLTSD-EDSSYINASFIKG-VYG----PKAYIATQGPLSTTLLDFWRMIWEYRIL 123
Cdd:cd14606   14 QRPENKSKNRYKNILPFDHSRVILQGRDSNiPGSDYINANYVKNqLLGpdenAKTYIASQGCLEATVNDFWQMAWQENSR 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 124 VIVMACMEFEMGKKKCERYWAEPGeTQLQFGPFSISCEAEKKKSDYKIRTLKAKFNNET---RIIYQFHYKNWPDHDVPS 200
Cdd:cd14606   94 VIVMTTREVEKGRNKCVPYWPEVG-MQRAYGPYSVTNCGEHDTTEYKLRTLQVSPLDNGeliREIWHYQYLSWPDHGVPS 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 201 SIDPILQLIWDMRCYQED--DCVPICIHCSAGCGRTGVICAVDytwMLLkDGIIPK----NFSVFNLIQEMRTQRPSLVQ 274
Cdd:cd14606  173 EPGGVLSFLDQINQRQESlpHAGPIIVHCSAGIGRTGTIIVID---MLM-ENISTKgldcDIDIQKTIQMVRAQRSGMVQ 248

                        250
                 ....*....|....
gi 568922106 275 TQEQYELVYSAVLE 288
Cdd:cd14606  249 TEAQYKFIYVAIAQ 262
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 84-279 5.16e-57

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: 193.72  E-value: 5.16e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  84 YINASFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYRILVIVMACMEFEMGKKKCERYWaePGETQLQFGPFSISCEAE 163
Cdd:cd14549    1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYW--PKEGTETYGNIQVTLLST 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 164 KKKSDYKIRTL--------KAKFNNETRIIYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQEDDCVPICIHCSAGCGRTG 235
Cdd:cd14549   79 EVLATYTVRTFslknlklkKVKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVGRTG 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 568922106 236 VICAVDYTWMLLKDgiiPKNFSVFNLIQEMRTQRPSLVQTQEQY 279
Cdd:cd14549  159 TYIVIDSMLQQIQD---KGTVNVFGFLKHIRTQRNYLVQTEEQY 199
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 24-288 1.29e-56

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: 195.25  E-value: 1.29e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  24 FASEFLKLKRQStkykADKIYPTTVAQRPKNIKKNRYKDILPYDHSLVELSLLTSDED--SSYINASFIKGVYGPKAYIA 101
Cdd:cd17667    1 FSEDFEEVQRCT----ADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSkhSDYINANYVDGYNKAKAYIA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 102 TQGPLSTTLLDFWRMIWEYRILVIVMACMEFEMGKKKCERYWaePGETQLQFGPFSISCEAEKKKSDYKIRTL------- 174
Cdd:cd17667   77 TQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYW--PTENSEEYGNIIVTLKSTKIHACYTVRRFsirntkv 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 175 ------KAKFNNETRIIYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQEDDCVPICIHCSAGCGRTGVICAVDYTWMLLK 248
Cdd:cd17667  155 kkgqkgNPKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIK 234

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 568922106 249 DgiiPKNFSVFNLIQEMRTQRPSLVQTQEQYELVYSAVLE 288
Cdd:cd17667  235 D---KSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 271
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 84-288 1.96e-56

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: 192.20  E-value: 1.96e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  84 YINASFIKGVYGPKA--YIATQGPLSTTLLDFWRMIWEYRILVIVMACMEFEMGKKKCERYWAE-PGETQLQFGPFSISC 160
Cdd:cd14538    1 YINASHIRIPVGGDTyhYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDsLNKPLICGGRLEVSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 161 EAEKKKSDYKIR--TLKAKFNNETRIIYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQEDdcVPICIHCSAGCGRTGVIC 238
Cdd:cd14538   81 EKYQSLQDFVIRriSLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIHNS--GPIVVHCSAGIGRTGVLI 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 568922106 239 AVDYTWMLLKDGIipkNFSVFNLIQEMRTQRPSLVQTQEQYELVYSAVLE 288
Cdd:cd14538  159 TIDVALGLIERDL---PFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLE 205
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 58-279 3.05e-56

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: 192.72  E-value: 3.05e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  58 NRYKDILPYDHSLVELSLLTSDEDSsYINASFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYRILVIVMACMEFEMGKK 137
Cdd:cd14615    1 NRYNNVLPYDISRVKLSVQSHSTDD-YINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 138 KCERYWaePGETQLQFGPFSISCEAEKKKSDYKIR--TLKAKFNNETRIIYQFHYKNWPDHDVPSSIDPIL---QLIWD- 211
Cdd:cd14615   80 KCEEYW--PSKQKKDYGDITVTMTSEIVLPEWTIRdfTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLInfrHLVREy 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568922106 212 MRCYQEDDcvPICIHCSAGCGRTGVICAVDY-TWMLLKDGIIpknfSVFNLIQEMRTQRPSLVQTQEQY 279
Cdd:cd14615  158 MKQNPPNS--PILVHCSAGVGRTGTFIAIDRlIYQIENENVV----DVYGIVYDLRMHRPLMVQTEDQY 220
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 20-288 3.33e-55

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: 191.79  E-value: 3.33e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  20 NSEEFASEFLKLkrqsTKYKADkiyPTT--VAQRPKNIKKNRYKDILPYDHSLVELSLLTSDEDSSYINASFIKGvYGPK 97
Cdd:cd14609   13 NRDRLAKEWQAL----CAYQAE---PNTcsTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPIIE-HDPR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  98 --AYIATQGPLSTTLLDFWRMIWEYRILVIVMACMEFEMGKKKCERYWAEPGET-----QLQFGPFSISCEaekkksDYK 170
Cdd:cd14609   85 mpAYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEGSSlyhiyEVNLVSEHIWCE------DFL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 171 IRT--LKAKFNNETRIIYQFHYKNWPDHDVPSSIDPILQLIWDM-RCYQEDDCvPICIHCSAGCGRTGVICAVDYTWMLL 247
Cdd:cd14609  159 VRSfyLKNVQTQETRTLTQFHFLSWPAEGIPSSTRPLLDFRRKVnKCYRGRSC-PIIVHCSDGAGRTGTYILIDMVLNRM 237

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 568922106 248 KDGIipKNFSVFNLIQEMRTQRPSLVQTQEQYELVYSAVLE 288
Cdd:cd14609  238 AKGV--KEIDIAATLEHVRDQRPGMVRTKDQFEFALTAVAE 276
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 53-287 4.27e-55

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: 189.66  E-value: 4.27e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  53 KNIKKNRYKDILPYDHSLVELSlltsdEDSSYINASFIKGVYGPK--AYIATQGPLSTTLLDFWRMIWEYRILVIVMACM 130
Cdd:cd14597    2 ENRKKNRYKNILPYDTTRVPLG-----DEGGYINASFIKMPVGDEefVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQ 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 131 EFEMGKKKCERYWAE-PGETQLQFGPFSISCEAEKKKSDYKIRTLKAK--FNNETRIIYQFHYKNWPDHDVPSSIDPILQ 207
Cdd:cd14597   77 EVEGGKIKCQRYWPEiLGKTTMVDNRLQLTLVRMQQLKNFVIRVLELEdiQTREVRHITHLNFTAWPDHDTPSQPEQLLT 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 208 LIWDMRCYQEDDcvPICIHCSAGCGRTGVICAVDYtwMLlkdGIIPKN--FSVFNLIQEMRTQRPSLVQTQEQYELVYSA 285
Cdd:cd14597  157 FISYMRHIHKSG--PIITHCSAGIGRSGTLICIDV--VL---GLISKDldFDISDIVRTMRLQRHGMVQTEDQYIFCYQV 229


                 ..
gi 568922106 286 VL 287
Cdd:cd14597  230 IL 231
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 45-287 1.02e-53

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: 186.25  E-value: 1.02e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  45 PTTVAQRPKNIKKNRYKDILPYDHSLVELSLLTSDEDSSYINASFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYRILV 124
Cdd:cd14614    3 PHFAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 125 IVMACMEFEMGKKKCERYW---AEPgetqLQFGPFSISCEAEKKKSDYKIRTLKAKFNNETRIIYQFHYKNWPDHDVPS- 200
Cdd:cd14614   83 IVMLTQCNEKRRVKCDHYWpftEEP----VAYGDITVEMLSEEEQPDWAIREFRVSYADEVQDVMHFNYTAWPDHGVPTa 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 201 -SIDPILQLIWDMRCYQEDDCVPICIHCSAGCGRTGVICAVDYTWMLLKDGiipKNFSVFNLIQEMRTQRPSLVQTQEQY 279
Cdd:cd14614  159 nAAESILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDH---EFVDILGLVSEMRSYRMSMVQTEEQY 235


                 ....*...
gi 568922106 280 ELVYSAVL 287
Cdd:cd14614  236 IFIHQCVQ 243
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 44-288 2.86e-53

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: 186.38  E-value: 2.86e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  44 YPTTVAQRPKNIKKNRYKDILPYDHSLVELSLltsdEDSSYINASFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYRIL 123
Cdd:cd14608   15 FPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQ----EDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSR 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 124 VIVMACMEFEMGKKKCERYWAEPGETQLQF--GPFSISCEAEKKKSDYKIRTLKAK--FNNETRIIYQFHYKNWPDHDVP 199
Cdd:cd14608   91 GVVMLNRVMEKGSLKCAQYWPQKEEKEMIFedTNLKLTLISEDIKSYYTVRQLELEnlTTQETREILHFHYTTWPDFGVP 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 200 SSIDPILQLIWDMRcyqEDDCV-----PICIHCSAGCGRTGVICAVDYTWMLLKDGIIPKNFSVFNLIQEMRTQRPSLVQ 274
Cdd:cd14608  171 ESPASFLNFLFKVR---ESGSLspehgPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQ 247

                        250
                 ....*....|....
gi 568922106 275 TQEQYELVYSAVLE 288
Cdd:cd14608  248 TADQLRFSYLAVIE 261
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 53-286 7.67e-53

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: 184.07  E-value: 7.67e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  53 KNIKKNRYKDILPYDHSLVELSLLTSDED-SSYINASFIKGVYG--------PKAYIATQGPLSTTLLDFWRMIWEYRIL 123
Cdd:cd14605    1 ENKNKNRYKNILPFDHTRVVLHDGDPNEPvSDYINANIIMPEFEtkcnnskpKKSYIATQGCLQNTVNDFWRMVFQENSR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 124 VIVMACMEFEMGKKKCERYWaePGETQL-QFGPFSISCEAEKKKSDYKIRTLKAKF---NNETRIIYQFHYKNWPDHDVP 199
Cdd:cd14605   81 VIVMTTKEVERGKSKCVKYW--PDEYALkEYGVMRVRNVKESAAHDYILRELKLSKvgqGNTERTVWQYHFRTWPDHGVP 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 200 SSIDPILQLIWDMRCYQED--DCVPICIHCSAGCGRTGVICAVDYTWMLLKDGIIPKNFSVFNLIQEMRTQRPSLVQTQE 277
Cdd:cd14605  159 SDPGGVLDFLEEVHHKQESimDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVDCDIDVPKTIQMVRSQRSGMVQTEA 238


                 ....*....
gi 568922106 278 QYELVYSAV 286
Cdd:cd14605  239 QYRFIYMAV 247
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 84-291 1.39e-52

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: 181.76  E-value: 1.39e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  84 YINASF----IKGVYGPKAYIATQGPLSTTLLDFWRMIWEYRILVIVMACMEFEMGKKKCERYWAEPGETQlQFGPFSIS 159
Cdd:cd14541    2 YINANYvnmeIPGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGETM-QFGNLQIT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 160 CEAEKKKSDYKIR--TLKAKFNNETRIIYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQEDDCVPICIHCSAGCGRTGVI 237
Cdd:cd14541   81 CVSEEVTPSFAFRefILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCSAGIGRTGVL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568922106 238 CAVDyTWMLLkdgiIPKNFSVFNL--IQEMRTQRPSLVQTQEQYELVYSAVLELFK 291
Cdd:cd14541  161 ITME-TAMCL----IEANEPVYPLdiVRTMRDQRAMLIQTPSQYRFVCEAILRVYE 211
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 57-283 2.05e-52

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: 182.21  E-value: 2.05e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  57 KNRYKDILPYDHSLVELSLltSDEDSSYINASFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYRILVIVMACMEFEMGK 136
Cdd:cd14545    1 LNRYRDRDPYDHDRSRVKL--KQGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 137 KKCERYWAePGETQ---LQFGPFSISCEAEKKKSDYKIRTLK--AKFNNETRIIYQFHYKNWPDHDVPSSIDPILQLIWD 211
Cdd:cd14545   79 IKCAQYWP-QGEGNamiFEDTGLKVTLLSEEDKSYYTVRTLEleNLKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQK 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568922106 212 MRCYQ--EDDCVPICIHCSAGCGRTGVICAVDyTWMLLKDGIIPKNFSVFNLIQEMRTQRPSLVQTQEQYELVY 283
Cdd:cd14545  158 VRESGslSSDVGPPVVHCSAGIGRSGTFCLVD-TCLVLIEKGNPSSVDVKKVLLEMRKYRMGLIQTPDQLRFSY 230
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 58-279 2.42e-52

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: 181.64  E-value: 2.42e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  58 NRYKDILPYDHSLVELSLLTSDEDSSYINASFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYRILVIVMACMEFEMGKK 137
Cdd:cd14616    1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 138 KCERYWAEPGETQLQFGPFSISCEAEKKKSDYKIRTLKAKFNNETRIIYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQE 217
Cdd:cd14616   81 RCHQYWPEDNKPVTVFGDIVITKLMEDVQIDWTIRDLKIERHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVRASRA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568922106 218 DDCVPICIHCSAGCGRTGVICAVDYTWMLLKDgiipKNF-SVFNLIQEMRTQRPSLVQTQEQY 279
Cdd:cd14616  161 HDNTPMIVHCSAGVGRTGVFIALDHLTQHIND----HDFvDIYGLVAELRSERMCMVQNLAQY 219
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 45-288 2.99e-52

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: 183.32  E-value: 2.99e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  45 PTTVAQRPKNIKKNRYKDILPYDHSLVELSLLTSDEDSSYINASFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYRILV 124
Cdd:cd14633   31 PWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTAS 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 125 IVMACMEFEMGKKKCERYWaePGETQLqFGPFSISCEAEKKKSDYKIRT--LKAKFNNETRIIYQFHYKNWPDHDVPSSI 202
Cdd:cd14633  111 IIMVTNLVEVGRVKCCKYW--PDDTEI-YKDIKVTLIETELLAEYVIRTfaVEKRGVHEIREIRQFHFTGWPDHGVPYHA 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 203 DPILQLIWDMRCYQEDDCVPICIHCSAGCGRTGVICAVDYTW-MLLKDGIIpknfSVFNLIQEMRTQRPSLVQTQEQYEL 281
Cdd:cd14633  188 TGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLdMAEREGVV----DIYNCVRELRSRRVNMVQTEEQYVF 263


                 ....*..
gi 568922106 282 VYSAVLE 288
Cdd:cd14633  264 IHDAILE 270
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 47-291 1.05e-51

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: 181.59  E-value: 1.05e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  47 TVAQRPKNIKKNRYKDILPYDHSLVelsLLTSDEDssYINASFIK----GVYGPKAYIATQGPLSTTLLDFWRMIWEYRI 122
Cdd:cd14600   33 TCAKLPQNMDKNRYKDVLPYDATRV---VLQGNED--YINASYVNmeipSANIVNKYIATQGPLPHTCAQFWQVVWEQKL 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 123 LVIVMACMEFEMGKKKCERYWAEPGETqLQFGPFSISCEAEKKKSDYKIR--TLKAKFNNETRIIYQFHYKNWPDHDVPS 200
Cdd:cd14600  108 SLIVMLTTLTERGRTKCHQYWPDPPDV-MEYGGFRVQCHSEDCTIAYVFRemLLTNTQTGEERTVTHLQYVAWPDHGVPD 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 201 SIDPILQLIWDMRCYQEDDcVPICIHCSAGCGRTGVICAVDyTWMLLkdgiIPKNFSVFNL--IQEMRTQRPSLVQTQEQ 278
Cdd:cd14600  187 DSSDFLEFVNYVRSKRVEN-EPVLVHCSAGIGRTGVLVTME-TAMCL----TERNQPVYPLdiVRKMRDQRAMMVQTSSQ 260

                        250
                 ....*....|...
gi 568922106 279 YELVYSAVLELFK 291
Cdd:cd14600  261 YKFVCEAILRVYE 273
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 52-284 1.12e-51

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: 180.80  E-value: 1.12e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  52 PKNIKKNRYKDILPYDHSLVEL-SLLTSDEDSSYINASFIKGVYG-PKAYIATQGPLSTTLLDFWRMIWEYRILVIVMaC 129
Cdd:cd14612   13 PGHASKDRYKTILPNPQSRVCLrRAGSQEEEGSYINANYIRGYDGkEKAYIATQGPMLNTVSDFWEMVWQEECPIIVM-I 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 130 MEFEMGKKKCERYWAEPGETqlqFGPFSISCEAEKKKSDYKIRTLKAKFNNETRIIYQFHYKNWPDHDVPSSIDPILQLI 209
Cdd:cd14612   92 TKLKEKKEKCVHYWPEKEGT---YGRFEIRVQDMKECDGYTIRDLTIQLEEESRSVKHYWFSSWPDHQTPESAGPLLRLV 168

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568922106 210 WDMRCYQEDDCV--PICIHCSAGCGRTGVICAVDYTWMLLKDgiiPKNFSVFNLIQEMRTQRPSLVQTQEQYELVYS 284
Cdd:cd14612  169 AEVEESRQTAASpgPIVVHCSAGIGRTGCFIATSIGCQQLKD---TGKVDILGIVCQLRLDRGGMIQTSEQYQFLHH 242
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 84-288 1.35e-51

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: 179.18  E-value: 1.35e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  84 YINASFIKGvYGPK--AYIATQGPLSTTLLDFWRMIWEYRILVIVMACMEFEMGKKKCERYWAEPGETqlQFGPFSISCE 161
Cdd:cd14546    1 YINASTIYD-HDPRnpAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSE--VYHIYEVHLV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 162 AEKKKS-DYKIRT--LKAKFNNETRIIYQFHYKNWPDHDVPSSIDPILQLIWDM-RCYQEDDCvPICIHCSAGCGRTGVI 237
Cdd:cd14546   78 SEHIWCdDYLVRSfyLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVnKSYRGRSC-PIVVHCSDGAGRTGTY 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568922106 238 CAVDYTWMLLKDGIipKNFSVFNLIQEMRTQRPSLVQTQEQYELVYSAVLE 288
Cdd:cd14546  157 ILIDMVLNRMAKGA--KEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAE 205
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 46-288 1.54e-51

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: 181.79  E-value: 1.54e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  46 TTVAQRPKNIKKNRYKDILPYDHSLVELSLLTSDEDSSYINASFIKGvYGPK--AYIATQGPLSTTLLDFWRMIWEYRIL 123
Cdd:cd14610   36 TNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPIMD-HDPRnpAYIATQGPLPATVADFWQMVWESGCV 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 124 VIVMACMEFEMGKKKCERYWAEPGET-----QLQFGPFSISCEaekkksDYKIRT--LKAKFNNETRIIYQFHYKNWPDH 196
Cdd:cd14610  115 VIVMLTPLAENGVKQCYHYWPDEGSNlyhiyEVNLVSEHIWCE------DFLVRSfyLKNLQTNETRTVTQFHFLSWNDQ 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 197 DVPSSIDPILQLIWDM-RCYQEDDCvPICIHCSAGCGRTGVICAVDYTWMLLKDGiiPKNFSVFNLIQEMRTQRPSLVQT 275
Cdd:cd14610  189 GVPASTRSLLDFRRKVnKCYRGRSC-PIIVHCSDGAGRSGTYILIDMVLNKMAKG--AKEIDIAATLEHLRDQRPGMVQT 265

                        250
                 ....*....|...
gi 568922106 276 QEQYELVYSAVLE 288
Cdd:cd14610  266 KEQFEFALTAVAE 278
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 58-287 1.03e-50

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: 177.44  E-value: 1.03e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  58 NRYKDILPYDHSLVELSLLTSDEDSSYINASFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYRILVIVMACMEFEMGKK 137
Cdd:cd14618    1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 138 KCERYWaePGE-TQLQFGPFSISCEAEKKKSDYKIRTLKAKFNNE--TRIIYQFHYKNWPDHDVPSSIDPILQLIWDMRC 214
Cdd:cd14618   81 LCDHYW--PSEsTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLrkERRVKHLHYTAWPDHGIPESTSSLMAFRELVRE 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568922106 215 YQE--DDCVPICIHCSAGCGRTGVICAVDYTWMLLKDgiiPKNFSVFNLIQEMRTQRPSLVQTQEQYELVYSAVL 287
Cdd:cd14618  159 HVQatKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKE---EKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 49-288 1.08e-50

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: 179.54  E-value: 1.08e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  49 AQRPKNIKKNRYKDILPYDHSLVELSLLTSDEDSSYINASFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYRILVIVMA 128
Cdd:cd14628   47 ANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVML 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 129 CMEFEMGKKKCERYWaePGETQLQFGPFSISCEAEKKKSDYKIRTLKAK--FNNETRIIYQFHYKNWPDHDVPSS----I 202
Cdd:cd14628  127 TKLREMGREKCHQYW--PAERSARYQYFVVDPMAEYNMPQYILREFKVTdaRDGQSRTVRQFQFTDWPEQGVPKSgegfI 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 203 DPILQLIWDMRCYQEDDcvPICIHCSAGCGRTGVICAVDYTWMLLK-DGIIpknfSVFNLIQEMRTQRPSLVQTQEQYEL 281
Cdd:cd14628  205 DFIGQVHKTKEQFGQDG--PISVHCSAGVGRTGVFITLSIVLERMRyEGVV----DIFQTVKMLRTQRPAMVQTEDQYQF 278


                 ....*..
gi 568922106 282 VYSAVLE 288
Cdd:cd14628  279 CYRAALE 285
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 54-288 3.20e-50

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: 177.54  E-value: 3.20e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  54 NIKKNRYKDILPYDHSLVELSLLTSDEDSSYINASFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYRILVIVMACMEFE 133
Cdd:cd14626   41 NKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEE 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 134 MGKKKCERYWaePGETQLQFGPFSISCEAEKKKSDYKIRTLKAKFN--NETRIIYQFHYKNWPDHDVPSSIDPILQLIWD 211
Cdd:cd14626  121 KSRVKCDQYW--PIRGTETYGMIQVTLLDTVELATYSVRTFALYKNgsSEKREVRQFQFMAWPDHGVPEYPTPILAFLRR 198

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568922106 212 MRCYQEDDCVPICIHCSAGCGRTGVICAVDytwMLLKDGIIPKNFSVFNLIQEMRTQRPSLVQTQEQYELVYSAVLE 288
Cdd:cd14626  199 VKACNPPDAGPMVVHCSAGVGRTGCFIVID---AMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLE 272
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 84-286 5.31e-50

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: 174.38  E-value: 5.31e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  84 YINASFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYRILVIVMACMEFEMGKKKCERYWaePGETQLQFGPFSISCEAE 163
Cdd:cd14552    1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYW--PEDGSVSSGDITVELKDQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 164 KKKSDYKIRTLKAKFN--NETRIIYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQEDDCV-PICIHCSAGCGRTGVICAV 240
Cdd:cd14552   79 TDYEDYTLRDFLVTKGkgGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSGNhPITVHCSAGAGRTGTFCAL 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 568922106 241 DYTWMLLK-DGIIpknfSVFNLIQEMRTQRPSLVQTQEQYELVYSAV 286
Cdd:cd14552  159 STVLERVKaEGVL----DVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 49-288 8.68e-50

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: 176.84  E-value: 8.68e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  49 AQRPKNIKKNRYKDILPYDHSLVELSLLTSDEDSSYINASFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYRILVIVMA 128
Cdd:cd14629   48 ANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVML 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 129 CMEFEMGKKKCERYWaePGETQLQFGPFSISCEAEKKKSDYKIRTLKAK--FNNETRIIYQFHYKNWPDHDVPSS----I 202
Cdd:cd14629  128 TKLREMGREKCHQYW--PAERSARYQYFVVDPMAEYNMPQYILREFKVTdaRDGQSRTIRQFQFTDWPEQGVPKTgegfI 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 203 DPILQLIWDMRCYQEDDcvPICIHCSAGCGRTGVICAVDYTWMLLK-DGIIpknfSVFNLIQEMRTQRPSLVQTQEQYEL 281
Cdd:cd14629  206 DFIGQVHKTKEQFGQDG--PITVHCSAGVGRTGVFITLSIVLERMRyEGVV----DMFQTVKTLRTQRPAMVQTEDQYQL 279


                 ....*..
gi 568922106 282 VYSAVLE 288
Cdd:cd14629  280 CYRAALE 286
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 49-288 1.02e-49

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: 176.85  E-value: 1.02e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  49 AQRPKNIKKNRYKDILPYDHSLVELSLLTSDEDSSYINASFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYRILVIVMA 128
Cdd:cd14627   48 ANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVML 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 129 CMEFEMGKKKCERYWaePGETQLQFGPFSISCEAEKKKSDYKIRTLKAK--FNNETRIIYQFHYKNWPDHDVPSS----I 202
Cdd:cd14627  128 TKLREMGREKCHQYW--PAERSARYQYFVVDPMAEYNMPQYILREFKVTdaRDGQSRTVRQFQFTDWPEQGVPKSgegfI 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 203 DPILQLIWDMRCYQEDDcvPICIHCSAGCGRTGVICAVDYTWMLLK-DGIIpknfSVFNLIQEMRTQRPSLVQTQEQYEL 281
Cdd:cd14627  206 DFIGQVHKTKEQFGQDG--PISVHCSAGVGRTGVFITLSIVLERMRyEGVV----DIFQTVKMLRTQRPAMVQTEDEYQF 279


                 ....*..
gi 568922106 282 VYSAVLE 288
Cdd:cd14627  280 CYQAALE 286
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 59-288 1.54e-49

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: 174.08  E-value: 1.54e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  59 RYKDILPYDHSLVELSLLTSDEDSSYINASFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYRILVIVMACMEFEMGKKK 138
Cdd:cd14623    1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 139 CERYWaePGETQLQFGPFSISCEAEKKKSDYKIRTLKAKFN--NETRIIYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQ 216
Cdd:cd14623   81 CAQYW--PSDGSVSYGDITIELKKEEECESYTVRDLLVTNTreNKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQ 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568922106 217 EDDCV-PICIHCSAGCGRTGVICAVDYTWMLLK-DGIIpknfSVFNLIQEMRTQRPSLVQTQEQYELVYSAVLE 288
Cdd:cd14623  159 QQSGNhPITVHCSAGAGRTGTFCALSTVLERVKaEGIL----DVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 52-290 1.10e-48

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: 172.74  E-value: 1.10e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  52 PKNIKKNRYKDILPYDHSLVelSLLTSDED---SSYINASFIKGvYG--PKAYIATQGPLSTTLLDFWRMIWEYRILVIV 126
Cdd:cd14613   23 PGLVRKNRYKTILPNPHSRV--CLTSPDQDdplSSYINANYIRG-YGgeEKVYIATQGPTVNTVGDFWRMVWQERSPIIV 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 127 MACMEFEMgKKKCERYWAepgETQLQFGPFSISCEAEKKKSDYKIRTLKAKFNNETRIIYQFHYKNWPDHDVPSSIDPIL 206
Cdd:cd14613  100 MITNIEEM-NEKCTEYWP---EEQVTYEGIEITVKQVIHADDYRLRLITLKSGGEERGLKHYWYTSWPDQKTPDNAPPLL 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 207 QLIWDM---RCYQEDDCVPICIHCSAGCGRTGVICAVDYTWMLLKDGIIpknFSVFNLIQEMRTQRPSLVQTQEQYELVY 283
Cdd:cd14613  176 QLVQEVeeaRQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGV---VDILRTTCQLRLDRGGMIQTCEQYQFVH 252


                 ....*..
gi 568922106 284 SaVLELF 290
Cdd:cd14613  253 H-VLSLY 258
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 84-288 1.64e-48

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: 170.48  E-value: 1.64e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  84 YINASFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYRILVIVMACMEFEMGKKKCERYWAEPGETqlqFGPFSISCEAE 163
Cdd:cd14555    1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTEV---YGDIKVTLVET 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 164 KKKSDYKIRT--LKAKFNNETRIIYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQEDDCVPICIHCSAGCGRTGVICAVD 241
Cdd:cd14555   78 EPLAEYVVRTfaLERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTGCYIVID 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 568922106 242 YTW-MLLKDGIIpknfSVFNLIQEMRTQRPSLVQTQEQYELVYSAVLE 288
Cdd:cd14555  158 IMLdMAEREGVV----DIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 44-286 1.64e-48

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: 172.46  E-value: 1.64e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  44 YPTTVAQRPKNIKKNRYKDILPYDHSLVELSlltsDEDSSYINASFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYRIL 123
Cdd:cd14607   14 YPHRVAKYPENRNRNRYRDVSPYDHSRVKLQ----NTENDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTK 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 124 VIVMACMEFEMGKKKCERYWAEPGETQLQFGP--FSISCEAEKKKSDYKIRTLKAKFNN--ETRIIYQFHYKNWPDHDVP 199
Cdd:cd14607   90 AVVMLNRIVEKDSVKCAQYWPTDEEEVLSFKEtgFSVKLLSEDVKSYYTVHLLQLENINsgETRTISHFHYTTWPDFGVP 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 200 SSIDPILQLIWDMRcyqEDDCV-----PICIHCSAGCGRTGVICAVDyTWMLLKDGIIPKNFSVFNLIQEMRTQRPSLVQ 274
Cdd:cd14607  170 ESPASFLNFLFKVR---ESGSLspehgPAVVHCSAGIGRSGTFSLVD-TCLVLMEKKDPDSVDIKQVLLDMRKYRMGLIQ 245

                        250
                 ....*....|..
gi 568922106 275 TQEQYELVYSAV 286
Cdd:cd14607  246 TPDQLRFSYMAV 257
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 84-291 4.76e-48

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: 169.16  E-value: 4.76e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  84 YINASFIKGVYGPKA--YIATQGPLSTTLLDFWRMIWEYRILVIVMACMEFEMGKKKCERYWAEPGETQLQFGPFSISCE 161
Cdd:cd14596    1 YINASYITMPVGEEElfYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELENYQLRLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 162 AEKKKSDYKIRTLKAkFNNET---RIIYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQEDDcvPICIHCSAGCGRTGVIC 238
Cdd:cd14596   81 NYQALQYFIIRIIKL-VEKETgenRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNTG--PIVVHCSAGIGRAGVLI 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568922106 239 AVDYTWMLLKDGIipkNFSVFNLIQEMRTQRPSLVQTQEQYELVYSAVLELFK 291
Cdd:cd14596  158 CVDVLLSLIEKDL---SFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVLQ 207
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 58-283 6.32e-48

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: 169.71  E-value: 6.32e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  58 NRYKDILPYDHSLVELSLLTSDEDSSYINASFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYRILVIVMACMEFEMGKK 137
Cdd:cd14617    1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 138 KCERYWAEPGETqLQFGPFSISCEAEKKKSDYKIRTLKAKFNNE---TRIIYQFHYKNWPDHDVPSSIDPILQLIWDMRC 214
Cdd:cd14617   81 KCDHYWPADQDS-LYYGDLIVQMLSESVLPEWTIREFKICSEEQldaPRLVRHFHYTVWPDHGVPETTQSLIQFVRTVRD 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568922106 215 Y--QEDDCVPICIHCSAGCGRTGVICAVDYTWMLL--KDGIipknfSVFNLIQEMRTQRPSLVQTQEQYELVY 283
Cdd:cd14617  160 YinRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLdsKDSV-----DIYGAVHDLRLHRVHMVQTECQYVYLH 227
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 84-287 1.08e-47

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: 168.23  E-value: 1.08e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  84 YINASFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYRILVIVMACMEFEMGKKKCERYWaePGETQLQFGPFSISCEAE 163
Cdd:cd17668    1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYW--PADGSEEYGNFLVTQKSV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 164 KKKSDYKIRTL----------KAKFNNETRIIYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQEDDCVPICIHCSAGCGR 233
Cdd:cd17668   79 QVLAYYTVRNFtlrntkikkgSQKGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSAGVGR 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568922106 234 TGVICAVDytwMLLKDGIIPKNFSVFNLIQEMRTQRPSLVQTQEQYELVYSAVL 287
Cdd:cd17668  159 TGTYIVLD---SMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 71-288 1.24e-47

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: 168.28  E-value: 1.24e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  71 VELSLLTSDEDSSYINASFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYRILVIVMACMEFEMGKKKCERYWaePGETQ 150
Cdd:cd14631    2 VILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYW--PDDTE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 151 LqFGPFSISCEAEKKKSDYKIR--TLKAKFNNETRIIYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQEDDCVPICIHCS 228
Cdd:cd14631   80 V-YGDFKVTCVEMEPLAEYVVRtfTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCS 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568922106 229 AGCGRTGVICAVDYTW-MLLKDGIIpknfSVFNLIQEMRTQRPSLVQTQEQYELVYSAVLE 288
Cdd:cd14631  159 AGAGRTGCYIVIDIMLdMAEREGVV----DIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 16-291 5.18e-46

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: 166.33  E-value: 5.18e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  16 KKKLNSEEFASEFlklkRQSTKYKADKIYptTVAQRPKNIKKNRYKDILPYDHSLVELsLLTSDEDSSYINASFIKGVYG 95
Cdd:cd14599    6 ERKLEEGMVFTEY----EQIPKKKADGVF--TTATLPENAERNRIREVVPYEENRVEL-VPTKENNTGYINASHIKVTVG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  96 PKA--YIATQGPLSTTLLDFWRMIWEYRILVIVMACMEFEMGKKKCERYWAEPG--ETQLQFGPFSISCEAEKKKSDYKI 171
Cdd:cd14599   79 GEEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKLGskHSSATYGKFKVTTKFRTDSGCYAT 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 172 RTLKAK--FNNETRIIYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQE---------DDCV-PICIHCSAGCGRTGVICA 239
Cdd:cd14599  159 TGLKVKhlLSGQERTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVRRhtnsmldstKNCNpPIVVHCSAGVGRTGVVIL 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568922106 240 VDYTWMLLKDGiipKNFSVFNLIQEMRTQRPSLVQTQEQYELVYSAVLELFK 291
Cdd:cd14599  239 TELMIGCLEHN---EKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQFLK 287
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 84-288 5.56e-46

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: 163.78  E-value: 5.56e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  84 YINASFIKGVYGPKA--YIATQGPLSTTLLDFWRMIWEYRILVIVMACMEFEMGKKKCERYW--AEPGETQLQFGPFSIS 159
Cdd:cd14540    1 YINASHITATVGGKQrfYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWptLGGEHDALTFGEYKVS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 160 CEAEKKKSDYKIRTLKAKFNNE--TRIIYQFHYKNWPDHDVPSSIDPILQLIWDM-----RCYQEDDC----VPICIHCS 228
Cdd:cd14540   81 TKFSVSSGCYTTTGLRVKHTLSgqSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEInsvrrHTNQDVAGhnrnPPTLVHCS 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568922106 229 AGCGRTGVICAVDYTWMLLKDGI---IPKnfsvfnLIQEMRTQRPSLVQTQEQYELVYSAVLE 288
Cdd:cd14540  161 AGVGRTGVVILADLMLYCLDHNEeldIPR------VLALLRHQRMLLVQTLAQYKFVYNVLIQ 217
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 25-288 1.39e-45

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: 164.88  E-value: 1.39e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  25 ASEFLKLKRQSTKYKADKIYPTTVAQRPKNIKKNRYKDILPYDHSLVELSLLTSDEDSSYINASFIKGVYGPKAYIATQG 104
Cdd:cd14625   18 ANDNLKLSQEYESIDPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINANYIDGYRKQNAYIATQG 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 105 PLSTTLLDFWRMIWEYRILVIVMACMEFEMGKKKCERYWaePGETQLQFGPFSISCEAEKKKSDYKIRTLKAKFN--NET 182
Cdd:cd14625   98 PLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYW--PSRGTETYGMIQVTLLDTIELATFCVRTFSLHKNgsSEK 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 183 RIIYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQEDDCVPICIHCSAGCGRTGVICAVDYTWMLLKDgiiPKNFSVFNLI 262
Cdd:cd14625  176 REVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVIDAMLERIKH---EKTVDIYGHV 252

                        250       260
                 ....*....|....*....|....*.
gi 568922106 263 QEMRTQRPSLVQTQEQYELVYSAVLE 288
Cdd:cd14625  253 TLMRSQRNYMVQTEDQYSFIHDALLE 278
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 57-283 2.24e-45

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: 162.39  E-value: 2.24e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  57 KNRYKDILPYDHSLVELSLLTSDED-SSYINASFIKGVYG-PKAYIATQGPLSTTLLDFWRMIWEYRILVIVMaCMEFEM 134
Cdd:cd14611    2 KNRYKTILPNPHSRVCLKPKNSNDSlSTYINANYIRGYGGkEKAFIATQGPMINTVNDFWQMVWQEDSPVIVM-ITKLKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 135 GKKKCERYWAEpgeTQLQFGPFSISCEAEKKKSDYKIRTLKAKFNNETRIIYQFHYKNWPDHDVPSSIDPILQLIWDMrc 214
Cdd:cd14611   81 KNEKCVLYWPE---KRGIYGKVEVLVNSVKECDNYTIRNLTLKQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLDV-- 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568922106 215 yQEDDCV-----PICIHCSAGCGRTGVICAVDYTWMLLK-DGIIpknfSVFNLIQEMRTQRPSLVQTQEQYELVY 283
Cdd:cd14611  156 -EEDRLAspgrgPVVVHCSAGIGRTGCFIATTIGCQQLKeEGVV----DVLSIVCQLRVDRGGMVQTSEQYEFVH 225
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 84-283 5.34e-45

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: 160.64  E-value: 5.34e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  84 YINASFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYRILVIVMACMEFEMGKKKCERYWAEPGETqlqFGPFSISCEAE 163
Cdd:cd14558    1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKT---YGDIEVELKDT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 164 KKKSDYKIRTLKAKFNN--ETRIIYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQEDDC------VPICIHCSAGCGRTG 235
Cdd:cd14558   78 EKSPTYTVRVFEITHLKrkDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKNskhgrsVPIVVHCSDGSSRTG 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 568922106 236 VICAVdytWMLLKDGIIPKNFSVFNLIQEMRTQRPSLVQTQEQYELVY 283
Cdd:cd14558  158 IFCAL---WNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 60-288 9.57e-45

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: 160.88  E-value: 9.57e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  60 YKDILPYDHSLVELSLLTSDEDSSYINASFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYRILVIVMACMEFEMGKKKC 139
Cdd:cd14620    1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 140 ERYWAEPGetQLQFGPFSISCEAEKKKSDYKIRTLKAKFN-----NETRIIYQFHYKNWPDHDVPSSIDPILQLIWDMRC 214
Cdd:cd14620   81 YQYWPDQG--CWTYGNIRVAVEDCVVLVDYTIRKFCIQPQlpdgcKAPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVKS 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568922106 215 YQEDDCVPICIHCSAGCGRTGVICAVDYTWMLLKDgiiPKNFSVFNLIQEMRTQRPSLVQTQEQYELVYSAVLE 288
Cdd:cd14620  159 VNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHA---EQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 49-288 5.06e-44

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: 160.96  E-value: 5.06e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  49 AQRPKNIKKNRYKDILPYDHSLVELSLLTSDEDSSYINASFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYRILVIVMA 128
Cdd:cd14621   47 ASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMV 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 129 CMEFEMGKKKCERYWaePGETQLQFGPFSISCEAEKKKSDYKIRTL------KAKFNNETRIIYQFHYKNWPDHDVPSSI 202
Cdd:cd14621  127 TNLKERKECKCAQYW--PDQGCWTYGNIRVSVEDVTVLVDYTVRKFciqqvgDVTNKKPQRLITQFHFTSWPDFGVPFTP 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 203 DPILQLIWDMRCYQEDDCVPICIHCSAGCGRTGVICAVDYTWMLLKDgiiPKNFSVFNLIQEMRTQRPSLVQTQEQYELV 282
Cdd:cd14621  205 IGMLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVIDAMLDMMHA---ERKVDVYGFVSRIRAQRCQMVQTDMQYVFI 281


                 ....*.
gi 568922106 283 YSAVLE 288
Cdd:cd14621  282 YQALLE 287
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 54-288 5.52e-44

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: 160.67  E-value: 5.52e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  54 NIKKNRYKDILPYDHSLVELSLLTSDEDSSYINASFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYRILVIVMACMEFE 133
Cdd:cd14624   47 NKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEE 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 134 MGKKKCERYWAEPG-ETQlqfGPFSISCEAEKKKSDYKIRTLKAKFN--NETRIIYQFHYKNWPDHDVPSSIDPILQLIW 210
Cdd:cd14624  127 RSRVKCDQYWPSRGtETY---GLIQVTLLDTVELATYCVRTFALYKNgsSEKREVRQFQFTAWPDHGVPEHPTPFLAFLR 203

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568922106 211 DMRCYQEDDCVPICIHCSAGCGRTGVICAVDYTWMLLKDgiiPKNFSVFNLIQEMRTQRPSLVQTQEQYELVYSAVLE 288
Cdd:cd14624  204 RVKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERIKH---EKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLE 278
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
22-280 4.60e-43

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 157.95  E-value: 4.60e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  22 EEFASEFLKLKRQSTKYKADKIYPTTVAQRPKNikknRYKDILPYDHSLVElslltsdEDSSYINASFIKgVYGPKAYIA 101
Cdd:COG5599   14 EKINSRLSTLTNELAPSHNDPQYLQNINGSPLN----RFRDIQPYKETALR-------ANLGYLNANYIQ-VIGNHRYIA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 102 TQGPLSTTLLDFWRMIWEYRILVIVM--ACMEFEMGKKKCERYWaepgETQLQFGPFSISCEAEKK---KSDYKIRTLKA 176
Cdd:COG5599   82 TQYPLEEQLEDFFQMLFDNNTPVLVVlaSDDEISKPKVKMPVYF----RQDGEYGKYEVSSELTESiqlRDGIEARTYVL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 177 KFNN---ETRIIYQFHYKNWPDHDVPSS--IDPILQLIWDMRCYQEDDCVPICIHCSAGCGRTGVICAVDYTWMLLKDGI 251
Cdd:COG5599  158 TIKGtgqKKIEIPVLHVKNWPDHGAISAeaLKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALV 237

                        250       260       270
                 ....*....|....*....|....*....|
gi 568922106 252 IpKNFSVFNLIQEMRTQR-PSLVQTQEQYE 280
Cdd:COG5599  238 Q-ITLSVEEIVIDMRTSRnGGMVQTSEQLD 266
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 84-286 1.19e-42

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: 154.01  E-value: 1.19e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  84 YINASFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYRILVIVMACMEFEMGKKKCERYWaePGETQLQFGPFSISCEAE 163
Cdd:cd14622    2 YINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYW--PSEGSVTHGEITIEIKND 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 164 KKKSDYKIRTLKAKFNNE--TRIIYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQEDDCV-PICIHCSAGCGRTGVICAV 240
Cdd:cd14622   80 TLLETISIRDFLVTYNQEkqTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQTGNhPIVVHCSAGAGRTGTFIAL 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 568922106 241 DYTWMLLK-DGIIpknfSVFNLIQEMRTQRPSLVQTQEQYELVYSAV 286
Cdd:cd14622  160 SNILERVKaEGLL----DVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 84-283 8.50e-42

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: 151.38  E-value: 8.50e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  84 YINASFIKGV--YGPKaYIATQGPLSTTLLDFWRMIWEYRILVIVMACMEFEMGKKKCERYWAEPGETQLQFGPFSISCE 161
Cdd:cd14539    1 YINASLIEDLtpYCPR-FIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERGQALVYGAITVSLQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 162 AEKKKSDYKIRTLKAKFNN--ETRIIYQFHYKNWPDHDVPSSIDPILQLIWDMRCY---QEDDCVPICIHCSAGCGRTGV 236
Cdd:cd14539   80 SVRTTPTHVERIISIQHKDtrLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHylqQRSLQTPIVVHCSSGVGRTGA 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568922106 237 ICAVdYTWML---LKDGI--IPKnfsvfnLIQEMRTQRPSLVQTQEQYELVY 283
Cdd:cd14539  160 FCLL-YAAVQeieAGNGIpdLPQ------LVRKMRQQRKYMLQEKEHLKFCY 204
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 84-283 2.93e-41

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: 149.98  E-value: 2.93e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  84 YINASFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYRILVIVMACMEFEMGKKKCERYWAEPGETQLQFGPFSISCEAE 163
Cdd:cd14557    1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRAFGDVVVKINEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 164 KKKSDYKIRTL---KAKFNNETRIIYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQEDDCVPICIHCSAGCGRTGVICAV 240
Cdd:cd14557   81 KICPDYIIRKLninNKKEKGSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGTYIGI 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 568922106 241 DytwmLLKDGIIPKN-FSVFNLIQEMRTQRPSLVQTQEQYELVY 283
Cdd:cd14557  161 D----AMLEGLEAEGrVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 84-291 3.12e-41

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: 150.10  E-value: 3.12e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  84 YINASFIKGVYGPKA----YIATQGPLSTTLLDFWRMIWEYRILVIVMACMEFEMGKKKCERYWAEPGETQlQFGPFSIS 159
Cdd:cd14601    2 YINANYINMEIPSSSiinrYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSS-SYGGFQVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 160 CEAEKKKSDYKIR--TLKAKFNNETRIIYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQEDDCVPICIHCSAGCGRTGVI 237
Cdd:cd14601   81 CHSEEGNPAYVFRemTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVHCSAGIGRTGVL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568922106 238 CAVDyTWMLLKDGiipkNFSVFNL--IQEMRTQRPSLVQTQEQYELVYSAVLELFK 291
Cdd:cd14601  161 ITME-TAMCLIEC----NQPVYPLdiVRTMRDQRAMMIQTPSQYRFVCEAILKVYE 211
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 84-288 1.76e-40

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: 147.89  E-value: 1.76e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  84 YINASFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYRILVIVMACMEFEMGKKKCERYWAEPGETqlqFGPFSISCEAE 163
Cdd:cd14632    1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSDT---YGDIKITLLKT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 164 KKKSDYKIRT--LKAKFNNETRIIYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQEDDCVPICIHCSAGCGRTGVICAVD 241
Cdd:cd14632   78 ETLAEYSVRTfaLERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYIVLD 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 568922106 242 YTW-MLLKDGIIpknfSVFNLIQEMRTQRPSLVQTQEQYELVYSAVLE 288
Cdd:cd14632  158 VMLdMAECEGVV----DIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 84-283 3.15e-40

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: 146.78  E-value: 3.15e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  84 YINASFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYRILVIVMaCMEFEMGKKKCERYWAEPGetQLQFGPFSISCEAE 163
Cdd:cd14556    1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVM-LNQLDPKDQSCPQYWPDEG--SGTYGPIQVEFVST 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 164 KKKSDYKIRTLK----AKFNNETRIIYQFHYKNWPDH-DVPSSIDPILQLIWDMRCYQED-DCVPICIHCSAGCGRTGVI 237
Cdd:cd14556   78 TIDEDVISRIFRlqntTRPQEGYRMVQQFQFLGWPRDrDTPPSKRALLKLLSEVEKWQEQsGEGPIVVHCLNGVGRSGVF 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 568922106 238 CAVDYTWMLLKdgiIPKNFSVFNLIQEMRTQRPSLVQTQEQYELVY 283
Cdd:cd14556  158 CAISSVCERIK---VENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 84-283 2.91e-38

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: 141.59  E-value: 2.91e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  84 YINASFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYRILVIVMACMEFEMGKKKCERYWAEPGETqlQFGPFSISCEAE 163
Cdd:cd14551    1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCW--TYGNLRVRVEDT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 164 KKKSDYKIRTLKAKFNNE------TRIIYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQEDDCVPICIHCSAGCGRTGVI 237
Cdd:cd14551   79 VVLVDYTTRKFCIQKVNRgigekrVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGRTGTF 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 568922106 238 CAVDYTWMLLKDgiiPKNFSVFNLIQEMRTQRPSLVQTQEQYELVY 283
Cdd:cd14551  159 IVIDAMLDMMHA---EGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
PHA02738 PHA02738
hypothetical protein; Provisional
 26-286 2.74e-37

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 142.37  E-value: 2.74e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  26 SEFLKL----------KRQSTKYKADKIYPTTVAQRpKNIKKNRYKDILPYDHSLVELSllTSDEDSSYINASFIKGVYG 95
Cdd:PHA02738  12 AEFLALmeksdceeviTREHQKVISEKVDGTFNAEK-KNRKLNRYLDAVCFDHSRVILP--AERNRGDYINANYVDGFEY 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  96 PKAYIATQGPLSTTLLDFWRMIWEYRILVIVMACMEFEMGKKKCERYWAEPGETQLQFGPFSISCEAEKKKSDYKIRTLK 175
Cdd:PHA02738  89 KKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDVEQGSIRFGKFKITTTQVETHPHYVKSTLL 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 176 AKFNNE-TRIIYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQED-------------DCVPICIHCSAGCGRTGVICAVD 241
Cdd:PHA02738 169 LTDGTSaTQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRQCQKElaqeslqighnrlQPPPIVVHCNAGLGRTPCYCVVD 248

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 568922106 242 YTWMLLKDGiipKNFSVFNLIQEMRTQRPSLVQTQEQYELVYSAV 286
Cdd:PHA02738 249 ISISRFDAC---ATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAV 290
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 50-303 9.01e-37

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 140.91  E-value: 9.01e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  50 QRPKNIKKNRYKDILPYDHSLVELSLlTSDEDSSYINASFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYRILVIVMAC 129
Cdd:PHA02747  47 EKPENQPKNRYWDIPCWDHNRVILDS-GGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLT 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 130 -MEFEMGKKKCERYWAEPGETQLQFGPFSISCEAEKKKSDYKIRTLKA--KFNNETRIIYQFHYKNWPDHDVPSSIDPIL 206
Cdd:PHA02747 126 pTKGTNGEEKCYQYWCLNEDGNIDMEDFRIETLKTSVRAKYILTLIEItdKILKDSRKISHFQCSEWFEDETPSDHPDFI 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 207 QLI--------WDMRCYQEDDCV--PICIHCSAGCGRTGVICAVDytwMLLKDGIIPKNFSVFNLIQEMRTQRPSLVQTQ 276
Cdd:PHA02747 206 KFIkiidinrkKSGKLFNPKDALlcPIVVHCSDGVGKTGIFCAVD---ICLNQLVKRKAICLAKTAEKIREQRHAGIMNF 282

                        250       260       270
                 ....*....|....*....|....*....|
gi 568922106 277 EQYELV---YSAVLELFKRHMDVISDNHLG 303
Cdd:PHA02747 283 DDYLFIqpgYEVLHYFLSKIKAIDKIKFCG 312
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 47-286 2.01e-36

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 140.16  E-value: 2.01e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  47 TVAQ--RPKNIKKNRYKDILPYDHSLVELS------------------LLTS-DEDSSYINASFIKGVYGPKAYIATQGP 105
Cdd:PHA02746  42 TTNHflKKENLKKNRFHDIPCWDHSRVVINaheslkmfdvgdsdgkkiEVTSeDNAENYIHANFVDGFKEANKFICAQGP 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 106 LSTTLLDFWRMIWEYRILVIVmACMEFEMGKKKCERYWAEPGETQLQFGPFSI-SCEAEKKKSDYKIRT-LKAKFNNETR 183
Cdd:PHA02746 122 KEDTSEDFFKLISEHESQVIV-SLTDIDDDDEKCFELWTKEEDSELAFGRFVAkILDIIEELSFTKTRLmITDKISDTSR 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 184 IIYQFHYKNWPDHDVPSSIDPILQLI-------WDMRCYQEDDCV---PICIHCSAGCGRTGVICAVDYTWMLLKDgiiP 253
Cdd:PHA02746 201 EIHHFWFPDWPDNGIPTGMAEFLELInkvneeqAELIKQADNDPQtlgPIVVHCSAGIGRAGTFCAIDNALEQLEK---E 277

                        250       260       270
                 ....*....|....*....|....*....|...
gi 568922106 254 KNFSVFNLIQEMRTQRPSLVQTQEQYELVYSAV 286
Cdd:PHA02746 278 KEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 53-291 3.80e-36

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 138.60  E-value: 3.80e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  53 KNIKKNRYKDILPYDHSLVELSllTSDEDSSYINASFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYRILVIVMACMEF 132
Cdd:PHA02742  51 KNMKKCRYPDAPCFDRNRVILK--IEDGGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIM 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 133 EMGKKKCERYWAEPGETQLQFGPFSISCEAEKKKSDYKIRTLKAKFNNETRI--IYQFHYKNWPDHDVPSSIDPILQLIW 210
Cdd:PHA02742 129 EDGKEACYPYWMPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASldIKHFAYEDWPHGGLPRDPNKFLDFVL 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 211 DMRCYQEDDCV-----------PICIHCSAGCGRTGVICAVDYTWMLLKDGIIpknFSVFNLIQEMRTQRPSLVQTQEQY 279
Cdd:PHA02742 209 AVREADLKADVdikgenivkepPILVHCSAGLDRAGAFCAIDICISKYNERAI---IPLLSIVRDLRKQRHNCLSLPQQY 285

                        250
                 ....*....|..
gi 568922106 280 ELVYSAVLELFK 291
Cdd:PHA02742 286 IFCYFIVLIFAK 297
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 84-291 1.12e-35

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: 134.72  E-value: 1.12e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  84 YINASFIKGVYGPKA--YIATQGPLSTTLLDFWRMIWEYRILVIVMACMEFEMGKKKCERYWAEPG--ETQLQFGPFSIS 159
Cdd:cd14598    1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLGsrHNTVTYGRFKIT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 160 CEAEKKKSDYKIRTLKAK--FNNETRIIYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQ---------EDDCVPICIHCS 228
Cdd:cd14598   81 TRFRTDSGCYATTGLKIKhlLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRrhtnstidpKSPNPPVLVHCS 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568922106 229 AGCGRTGVICAVDYTWMLLKDGIIPKNFSVFNLiqeMRTQRPSLVQTQEQYELVYSAVLELFK 291
Cdd:cd14598  161 AGVGRTGVVILSEIMIACLEHNEMLDIPRVLDM---LRQQRMMMVQTLSQYTFVYKVLIQFLK 220
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
184-288 5.61e-35

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 128.25  E-value: 5.61e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106   184 IIYQFHYKNWPDHDVPSSIDPILQLIWDMR--CYQEDDCVPICIHCSAGCGRTGVICAVDYTWMLLKDGIipKNFSVFNL 261
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKknLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEA--GEVDIFDT 78

                           90       100
                   ....*....|....*....|....*..
gi 568922106   262 IQEMRTQRPSLVQTQEQYELVYSAVLE 288
Cdd:smart00404  79 VKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 184-288 5.61e-35

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: 128.25  E-value: 5.61e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106   184 IIYQFHYKNWPDHDVPSSIDPILQLIWDMR--CYQEDDCVPICIHCSAGCGRTGVICAVDYTWMLLKDGIipKNFSVFNL 261
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKknLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEA--GEVDIFDT 78

                           90       100
                   ....*....|....*....|....*..
gi 568922106   262 IQEMRTQRPSLVQTQEQYELVYSAVLE 288
Cdd:smart00012  79 VKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 84-284 2.22e-33

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: 127.58  E-value: 2.22e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  84 YINASFIKG---VYGPKaYIATQGPLSTTLLDFWRMIWEYRILVIVMACMEFEMGKK-KCERYWAEPGETQLQFGPFSIS 159
Cdd:cd17658    1 YINASLVETpasESLPK-FIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTaKCADYFPAEENESREFGRISVT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 160 CEAEkKKSDYKI--RTLKAKFN---NETRIIYQFHYKNWPDHDVPSSIDPILQLIwdMRCYQ-EDDCVPICIHCSAGCGR 233
Cdd:cd17658   80 NKKL-KHSQHSItlRVLEVQYIeseEPPLSVLHIQYPEWPDHGVPKDTRSVRELL--KRLYGiPPSAGPIVVHCSAGIGR 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568922106 234 TGVICAVDYTWmllkDGIIPKNFSVFNL---IQEMRTQRPSLVQTQEQYELVYS 284
Cdd:cd17658  157 TGAYCTIHNTI----RRILEGDMSAVDLsktVRKFRSQRIGMVQTQDQYIFCYA 206
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 84-288 5.65e-29

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: 115.12  E-value: 5.65e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  84 YINASFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYRILVIVMaCMEFEMgKKKCERYWaePGETQLQFGPFSISCEAE 163
Cdd:cd14636    1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVM-LNEVDL-AQGCPQYW--PEEGMLRYGPIQVECMSC 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 164 KKKSDYKIRTLkaKFNNETR------IIYQFHYKNWPDH-DVPSSIDPILQLIWDMRCYQEdDCVP----ICIHCSAGCG 232
Cdd:cd14636   77 SMDCDVISRIF--RICNLTRpqegylMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQE-ECDEgegrTIIHCLNGGG 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568922106 233 RTGVICAVDYTWMLLKDGIIpknFSVFNLIQEMRTQRPSLVQTQEQYELVYSAVLE 288
Cdd:cd14636  154 RSGMFCAISIVCEMIKRQNV---VDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 84-288 1.03e-26

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: 108.57  E-value: 1.03e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  84 YINASFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYRILVIVMACmefEMGKKK-CERYWaePGETQLQFGPFSISCEA 162
Cdd:cd14634    1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLN---EMDAAQlCMQYW--PEKTSCCYGPIQVEFVS 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 163 EKKKSDYKIRTLK----AKFNNETRIIYQFHYKNWPDH-DVPSSIDPILQLIWDMRCYQED----DCVPIcIHCSAGCGR 233
Cdd:cd14634   76 ADIDEDIISRIFRicnmARPQDGYRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEQydgrEGRTV-VHCLNGGGR 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568922106 234 TGVICAV-DYTWMLLKDGIIpknfSVFNLIQEMRTQRPSLVQTQEQYELVYSAVLE 288
Cdd:cd14634  155 SGTFCAIcSVCEMIQQQNII----DVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 84-288 1.29e-22

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: 96.68  E-value: 1.29e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  84 YINASFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYRILVIVMacMEFEMGKKKCERYWAEPGETqlQFGPFSISCEAE 163
Cdd:cd14635    1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVM--LNDVDPAQLCPQYWPENGVH--RHGPIQVEFVSA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 164 KKKSDYKIRTLK----AKFNNETRIIYQFHYKNWPDH-DVPSSIDPILQLIWDMRCYQED---DCVPICIHCSAGCGRTG 235
Cdd:cd14635   77 DLEEDIISRIFRiynaARPQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEyngGEGRTVVHCLNGGGRSG 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568922106 236 VICAVDYTWMLLKDgiiPKNFSVFNLIQEMRTQRPSLVQTQEQYELVYSAVLE 288
Cdd:cd14635  157 TFCAISIVCEMLRH---QRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 84-288 1.49e-21

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: 93.43  E-value: 1.49e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  84 YINASFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYRILVIVMACMEFEMGKK-KCERYWAEPGETqlQFGPFSISCEA 162
Cdd:cd14637    1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEPGLQ--QYGPMEVEFVS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 163 EKKKSDYKIRTLK----AKFNNETRIIYQFHYKNW-PDHDVPSSIDPILQLIWDMRCYQEDDCV-PICIHCSAGCGRTGV 236
Cdd:cd14637   79 GSADEDIVTRLFRvqniTRLQEGHLMVRHFQFLRWsAYRDTPDSKKAFLHLLASVEKWQRESGEgRTVVHCLNGGGRSGT 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568922106 237 ICAVDytwmLLKDGIIPKNF-SVFNLIQEMRTQRPSLVQTQEQYELVYSAVLE 288
Cdd:cd14637  159 YCASA----MILEMIRCHNIvDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 84-283 2.05e-18

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: 84.29  E-value: 2.05e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  84 YINASFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYRILVIVMaCMEFEMgKKKCERYWAEPGETqLQFGPFSISCEAE 163
Cdd:cd14550    1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVM-LTDNEL-NEDEPIYWPTKEKP-LECETFKVTLSGE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 164 KKKS-----DYKIR--TLKAKFNNETRIIYQFHYKNWPDHDVPssIDPILQLIWDMRCYQEDDCVPICIHCSAGCGRTGV 236
Cdd:cd14550   78 DHSClsneiRLIVRdfILESTQDDYVLEVRQFQCPSWPNPCSP--IHTVFELINTVQEWAQQRDGPIVVHDRYGGVQAAT 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568922106 237 ICAvdytWMLLKDGIIPKN----FSVFNLIQEMrtqRPSLVQTQEQYELVY 283
Cdd:cd14550  156 FCA----LTTLHQQLEHESsvdvYQVAKLYHLM---RPGVFTSKEDYQFLY 199
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 84-287 4.63e-18

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: 83.50  E-value: 4.63e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  84 YINASFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYRILVIVMACMEFEMGKKKCErYWAEPGETqLQFGPFSISCEAE 163
Cdd:cd17669    1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWPNKDEP-INCETFKVTLIAE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 164 KKK----------SDYKIRTLKAKFNNETRiiyQFHYKNWPDHDVPssIDPILQLIWDMRCYQEDDCVPICIHCSAGCGR 233
Cdd:cd17669   79 EHKclsneekliiQDFILEATQDDYVLEVR---HFQCPKWPNPDSP--ISKTFELISIIKEEAANRDGPMIVHDEHGGVT 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568922106 234 TGVICAVdYTWM--LLKDGIIpknfSVFNLIQEMRTQRPSLVQTQEQYELVYSAVL 287
Cdd:cd17669  154 AGTFCAL-TTLMhqLEKENSV----DVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 84-287 9.97e-17

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: 79.72  E-value: 9.97e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  84 YINASFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYRILVIVMacMEFEMGKKKCER-YWAEPGE---------TQLQF 153
Cdd:cd17670    1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVM--LPDNQGLAEDEFvYWPSREEsmnceaftvTLISK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 154 GPFSISCEAEKKKSDYKIRTLKAKFNNETRiiyQFHYKNWPDHDVP-SSIDPILQLIWDMRCYQEDdcvPICIHCSAGCG 232
Cdd:cd17670   79 DRLCLSNEEQIIIHDFILEATQDDYVLEVR---HFQCPKWPNPDAPiSSTFELINVIKEEALTRDG---PTIVHDEFGAV 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568922106 233 RTGVICAVDYTWMLLKDGIIPKNFSVFNLIQEMrtqRPSLVQTQEQYELVYSAVL 287
Cdd:cd17670  153 SAGTLCALTTLSQQLENENAVDVYQVAKMINLM---RPGVFTDIEQYQFLYKAML 204
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 85-281 1.50e-14

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: 73.59  E-value: 1.50e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  85 INASFIKgVYGPKAYIATQGPLSTTLLDFWRMIWEYRILVIVMACMEFEMGKKKCERYWAEPGetqlQFGpfSISCEAEK 164
Cdd:cd14559   18 LNANRVQ-IGNKNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPPYFRQSG----TYG--SVTVKSKK 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 165 KKSDYKIR-------TLKAKFNNETRIIYQFHYKNWPDHDVPSSID----------------PILQLIWDMRCYQEDDCV 221
Cdd:cd14559   91 TGKDELVDglkadmyNLKITDGNKTITIPVVHVTNWPDHTAISSEGlkeladlvnksaeekrNFYKSKGSSAINDKNKLL 170

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568922106 222 PIcIHCSAGCGRTGVICAVdytwMLLKDGiiPKNFSVFNLIQEMRTQRPS-LVQTQEQYEL 281
Cdd:cd14559  171 PV-IHCRAGVGRTGQLAAA----MELNKS--PNNLSVEDIVSDMRTSRNGkMVQKDEQLDT 224
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 222-283 2.22e-08

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: 52.74  E-value: 2.22e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568922106 222 PICIHCSAGCGRTGVICAVdytWMLLKDGiipknFSVFNLIQEMRTQRPS-LVQTQEQYELVY 283
Cdd:cd14494   58 PVLVHCKAGVGRTGTLVAC---YLVLLGG-----MSAEEAVRIVRLIRPGgIPQTIEQLDFLI 112
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 49-297 9.19e-08

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 54.59  E-value: 9.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106  49 AQRPKNIKKNRYKD------ILPYDHSLVELSlltsdEDSSYINASFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYRI 122
Cdd:PHA02740  42 ANKACAQAENKAKDenlalhITRLLHRRIKLF-----NDEKVLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKV 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 123 LVIVMACmefEMGKKKC-ERYWAEPGETQLQFGPFSISCEAEKKKSDYKIR--TLKAKFNNEtRIIYQFHYKNWP----D 195
Cdd:PHA02740 117 QIIVLIS---RHADKKCfNQFWSLKEGCVITSDKFQIETLEIIIKPHFNLTllSLTDKFGQA-QKISHFQYTAWPadgfS 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 196 HDVPSSID---PILQLIWDMRCYQEDDCV-PICIHCSAGCGRTGVICAVDYTWMLL-KDGIIpknfSVFNLIQEMRTQRP 270
Cdd:PHA02740 193 HDPDAFIDffcNIDDLCADLEKHKADGKIaPIIIDCIDGISSSAVFCVFDICATEFdKTGML----SIANALKKVRQKKY 268

                        250       260
                 ....*....|....*....|....*..
gi 568922106 271 SLVQTQEQYELVYSAVLELFKRHMDVI 297
Cdd:PHA02740 269 GCMNCLDDYVFCYHLIAAYLKEKFDIL 295
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
193-283 7.76e-07

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 49.20  E-value: 7.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 193 WPDHDVPS--SIDPILQLIWdmRCYQEDDcvPICIHCSAGCGRTGVICAvdyTWMLLKDgiipknFSVFNLIQEMRTQRP 270
Cdd:COG2453   55 IPDFGAPDdeQLQEAVDFID--EALREGK--KVLVHCRGGIGRTGTVAA---AYLVLLG------LSAEEALARVRAARP 121

                         90
                 ....*....|...
gi 568922106 271 SLVQTQEQYELVY 283
Cdd:COG2453  122 GAVETPAQRAFLE 134
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 194-283 6.34e-06

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: 46.87  E-value: 6.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 194 PDHDVPSSIDPILQLIWDMR-CYQEDDCVpiCIHCSAGCGRTGVICAVdyTWMLLKDGIIPKnfsvfNLIQEMRTQRPSL 272
Cdd:cd14505   81 PDGGVPSDIAQWQELLEELLsALENGKKV--LIHCKGGLGRTGLIAAC--LLLELGDTLDPE-----QAIAAVRALRPGA 151

                         90
                 ....*....|.
gi 568922106 273 VQTQEQYELVY 283
Cdd:cd14505  152 IQTPKQENFLH 162
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 163-239 2.76e-05

protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar proteins; Phosphatase and tensin homolog (PTEN) is a tumor suppressor that acts as a dual-specificity protein phosphatase and as a lipid phosphatase. It dephosphorylates phosphoinositide trisphosphate. In addition to PTEN, this family includes tensins, voltage-sensitive phosphatases (VSPs), and auxilins. They all contain a protein tyrosine phosphatase-like domain although not all are active phosphatases. Tensins are intracellular proteins that act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility, and they may or may not have phosphatase activity. VSPs are phosphoinositide phosphatases with substrates that include phosphatidylinositol-4,5-diphosphate and phosphatidylinositol-3,4,5-trisphosphate. Auxilins are J domain-containing proteins that facilitate Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles, and they do not exhibit phosphatase activity.


Pssm-ID: 350347 [Multi-domain]  Cd Length: 160  Bit Score: 45.26  E-value: 2.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 163 EKKKSDYKIRTLKA-------KFNNetriiyQFHYKNWPDHDVPSsIDPILQLIWDMRCY-QEDDCVPICIHCSAGCGRT 234
Cdd:cd14497   37 THHPDHYMIFNLSEeeydddsKFEG------RVLHYGFPDHHPPP-LGLLLEIVDDIDSWlSEDPNNVAVVHCKAGKGRT 109


                 ....*
gi 568922106 235 GVICA 239
Cdd:cd14497  110 GTVIC 114
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 185-282 1.81e-04

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: 43.49  E-value: 1.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922106 185 IYQFHYkNWPDHDVPSsidpiLQLIWDM-----RCYQEDdcVPICIHCSAGCGRTGVICAvdyTWMLLKDGIIPKnfsvf 259
Cdd:cd14506   77 IYFYNF-GWKDYGVPS-----LTTILDIvkvmaFALQEG--GKVAVHCHAGLGRTGVLIA---CYLVYALRMSAD----- 140

                         90       100
                 ....*....|....*....|...
gi 568922106 260 NLIQEMRTQRPSLVQTQEQYELV 282
Cdd:cd14506  141 QAIRLVRSKRPNSIQTRGQVLCV 163
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 222-282 2.10e-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: 42.26  E-value: 2.10e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568922106 222 PICIHCSAGCGRTGVICAVdYtwmLLKDGiipkNFSVFNLIQEMRTQRPSLVQTQEQYELV 282
Cdd:cd14504   84 AVLVHCLAGKGRTGTMLAC-Y---LVKTG----KISAVDAINEIRRIRPGSIETSEQEKFV 136
 
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.
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