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Conserved domains on  [gi|1845972907|ref|NP_001369855|]
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Protein tyrosine phosphatase-like protein egg-3 [Caenorhabditis elegans]

Protein Classification

protein tyrosine phosphatase family protein( domain architecture ID 12193126)

cys-based protein tyrosine phosphatase (PTP) family protein, such as tyrosine-protein phosphatase that catalyzes the dephosphorylation of phosphotyrosine groups in phosphoproteins

CATH:  3.90.190.10
EC:  3.1.3.-
Gene Ontology:  GO:0004721|GO:0006470
PubMed:  27514797|17057753

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
207-513 9.91e-72

Protein tyrosine phosphatase, catalytic domain;


:

Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 230.24  E-value: 9.91e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907  207 FVQEFNRLDRMFVSnelsDEESLQTAFNANyLTKARSKMVPCAEFSRVKLNDGLGrlddrnelrngmfsdeheflqeegy 286
Cdd:smart00194   2 LEEEFEKLDRLKPD----DESCTVAAFPEN-RDKNRYKDVLPYDHTRVKLKPPPG------------------------- 51
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907  287 takstyGTTDFIHANYVKGGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSavdsstlgpLDSANRNHCPYYWP 366
Cdd:smart00194  52 ------EGSDYINASYIDGPNGPKAYIATQGPLPSTVEDFWRMVWEQKVTVIVMLTE---------LVEKGREKCAQYWP 116
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907  367 RAENESLRFGSFHITCMKVDSKADplFTITKLKVQKVGGnlldaefDEELFLEHWQW-DWQYLG---DVHWPFRVLRKAR 442
Cdd:smart00194 117 DEEGEPLTYGDITVTLKSVEKVDD--YTIRTLEVTNTGC-------SETRTVTHYHYtNWPDHGvpeSPESILDLIRAVR 187
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1845972907  443 Q----LSTPTIVQCIDGCSKSGTLVSIETALMHFIRGSPItksLILQSCVFVRLQRRLSVSSVLLYLFIYRVILR 513
Cdd:smart00194 188 KsqstSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEV---DIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
 
Name Accession Description Interval E-value
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
207-513 9.91e-72

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 230.24  E-value: 9.91e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907  207 FVQEFNRLDRMFVSnelsDEESLQTAFNANyLTKARSKMVPCAEFSRVKLNDGLGrlddrnelrngmfsdeheflqeegy 286
Cdd:smart00194   2 LEEEFEKLDRLKPD----DESCTVAAFPEN-RDKNRYKDVLPYDHTRVKLKPPPG------------------------- 51
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907  287 takstyGTTDFIHANYVKGGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSavdsstlgpLDSANRNHCPYYWP 366
Cdd:smart00194  52 ------EGSDYINASYIDGPNGPKAYIATQGPLPSTVEDFWRMVWEQKVTVIVMLTE---------LVEKGREKCAQYWP 116
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907  367 RAENESLRFGSFHITCMKVDSKADplFTITKLKVQKVGGnlldaefDEELFLEHWQW-DWQYLG---DVHWPFRVLRKAR 442
Cdd:smart00194 117 DEEGEPLTYGDITVTLKSVEKVDD--YTIRTLEVTNTGC-------SETRTVTHYHYtNWPDHGvpeSPESILDLIRAVR 187
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1845972907  443 Q----LSTPTIVQCIDGCSKSGTLVSIETALMHFIRGSPItksLILQSCVFVRLQRRLSVSSVLLYLFIYRVILR 513
Cdd:smart00194 188 KsqstSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEV---DIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
238-512 1.08e-64

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 210.95  E-value: 1.08e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 238 LTKARSKMVPCAEFSRVKLndglgrlddrnelrngmfsdeheflqeegytaKSTYGTTDFIHANYVKGGPLLNTFICAQA 317
Cdd:pfam00102   2 LEKNRYKDVLPYDHTRVKL--------------------------------TGDPGPSDYINASYIDGYKKPKKYIATQG 49
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 318 PLKNTQEDFWRMVFQEKCQFIVMLNSavdsstlgpLDSANRNHCPYYWPRAENESLRFGSFHITCMKVdSKADPLFTITK 397
Cdd:pfam00102  50 PLPNTVEDFWRMVWEEKVTIIVMLTE---------LEEKGREKCAQYWPEEEGESLEYGDFTVTLKKE-KEDEKDYTVRT 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 398 LKVQKVGGNlldaefdEELFLEHWQW-DWQYLG---DVHWPFRVLRKARQLS-----TPTIVQCIDGCSKSGTLVSIETA 468
Cdd:pfam00102 120 LEVSNGGSE-------ETRTVKHFHYtGWPDHGvpeSPNSLLDLLRKVRKSSldgrsGPIVVHCSAGIGRTGTFIAIDIA 192
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1845972907 469 LMHFIRGSPItksLILQSCVFVRLQRRLSVSSVLLYLFIYRVIL 512
Cdd:pfam00102 193 LQQLEAEGEV---DIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
297-509 5.04e-51

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: 173.63  E-value: 5.04e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 297 FIHANYVKGGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSAVDSstlgpldsaNRNHCPYYWPRAENESLRFG 376
Cdd:cd00047     1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEK---------GREKCERYWPEEGGKPLEYG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 377 SFHITCMKVDSKADplFTITKLKVQKVGGnlldaefDEELFLEHWQWDwqylgdvHWP---------------FRVLRKA 441
Cdd:cd00047    72 DITVTLVSEEELSD--YTIRTLELSPKGC-------SESREVTHLHYT-------GWPdhgvpsspedllalvRRVRKEA 135
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1845972907 442 RQLSTPTIVQCIDGCSKSGTLVSIETALMHFIRGSPITkslILQSCVFVRLQRRLSVSSVLLYLFIYR 509
Cdd:cd00047   136 RKPNGPIVVHCSAGVGRTGTFIAIDILLERLEAEGEVD---VFEIVKALRKQRPGMVQTLEQYEFIYE 200
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
240-512 2.54e-19

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 88.91  E-value: 2.54e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 240 KARSKMVPCAEFSRVKLNDGLGrlddrnelrngmfsdeheflqeegytakstyGTTDFIHANYVKGGPLLNTFICAQAPL 319
Cdd:PHA02747   54 KNRYWDIPCWDHNRVILDSGGG-------------------------------STSDYIHANWIDGFEDDKKFIATQGPF 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 320 KNTQEDFWRMVFQEKCQFIVMLNSAVDSStlgpldsaNRNHCPYYWPRAENESLRFGSFHITCMKVDSKadPLFTITKLK 399
Cdd:PHA02747  103 AETCADFWKAVWQEHCSIIVMLTPTKGTN--------GEEKCYQYWCLNEDGNIDMEDFRIETLKTSVR--AKYILTLIE 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 400 VQkvggnllDAEFDEELFLEHWQW-DW---QYLGDVHWPFRVLR--------------KARQLSTPTIVQCIDGCSKSGT 461
Cdd:PHA02747  173 IT-------DKILKDSRKISHFQCsEWfedETPSDHPDFIKFIKiidinrkksgklfnPKDALLCPIVVHCSDGVGKTGI 245
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1845972907 462 LVSIETALMHFIRgspiTKSLILQSCVF-VRLQRRLSVSSVLLYLFI---YRVIL 512
Cdd:PHA02747  246 FCAVDICLNQLVK----RKAICLAKTAEkIREQRHAGIMNFDDYLFIqpgYEVLH 296
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
298-366 3.45e-11

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 63.96  E-value: 3.45e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1845972907 298 IHANYVKGGPLlNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSAVDsstlgplDSANRNHCPYYWP 366
Cdd:COG5599    66 LNANYIQVIGN-HRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDE-------ISKPKVKMPVYFR 126
 
Name Accession Description Interval E-value
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
207-513 9.91e-72

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 230.24  E-value: 9.91e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907  207 FVQEFNRLDRMFVSnelsDEESLQTAFNANyLTKARSKMVPCAEFSRVKLNDGLGrlddrnelrngmfsdeheflqeegy 286
Cdd:smart00194   2 LEEEFEKLDRLKPD----DESCTVAAFPEN-RDKNRYKDVLPYDHTRVKLKPPPG------------------------- 51
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907  287 takstyGTTDFIHANYVKGGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSavdsstlgpLDSANRNHCPYYWP 366
Cdd:smart00194  52 ------EGSDYINASYIDGPNGPKAYIATQGPLPSTVEDFWRMVWEQKVTVIVMLTE---------LVEKGREKCAQYWP 116
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907  367 RAENESLRFGSFHITCMKVDSKADplFTITKLKVQKVGGnlldaefDEELFLEHWQW-DWQYLG---DVHWPFRVLRKAR 442
Cdd:smart00194 117 DEEGEPLTYGDITVTLKSVEKVDD--YTIRTLEVTNTGC-------SETRTVTHYHYtNWPDHGvpeSPESILDLIRAVR 187
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1845972907  443 Q----LSTPTIVQCIDGCSKSGTLVSIETALMHFIRGSPItksLILQSCVFVRLQRRLSVSSVLLYLFIYRVILR 513
Cdd:smart00194 188 KsqstSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEV---DIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
238-512 1.08e-64

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 210.95  E-value: 1.08e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 238 LTKARSKMVPCAEFSRVKLndglgrlddrnelrngmfsdeheflqeegytaKSTYGTTDFIHANYVKGGPLLNTFICAQA 317
Cdd:pfam00102   2 LEKNRYKDVLPYDHTRVKL--------------------------------TGDPGPSDYINASYIDGYKKPKKYIATQG 49
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 318 PLKNTQEDFWRMVFQEKCQFIVMLNSavdsstlgpLDSANRNHCPYYWPRAENESLRFGSFHITCMKVdSKADPLFTITK 397
Cdd:pfam00102  50 PLPNTVEDFWRMVWEEKVTIIVMLTE---------LEEKGREKCAQYWPEEEGESLEYGDFTVTLKKE-KEDEKDYTVRT 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 398 LKVQKVGGNlldaefdEELFLEHWQW-DWQYLG---DVHWPFRVLRKARQLS-----TPTIVQCIDGCSKSGTLVSIETA 468
Cdd:pfam00102 120 LEVSNGGSE-------ETRTVKHFHYtGWPDHGvpeSPNSLLDLLRKVRKSSldgrsGPIVVHCSAGIGRTGTFIAIDIA 192
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1845972907 469 LMHFIRGSPItksLILQSCVFVRLQRRLSVSSVLLYLFIYRVIL 512
Cdd:pfam00102 193 LQQLEAEGEV---DIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
297-509 5.04e-51

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: 173.63  E-value: 5.04e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 297 FIHANYVKGGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSAVDSstlgpldsaNRNHCPYYWPRAENESLRFG 376
Cdd:cd00047     1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEK---------GREKCERYWPEEGGKPLEYG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 377 SFHITCMKVDSKADplFTITKLKVQKVGGnlldaefDEELFLEHWQWDwqylgdvHWP---------------FRVLRKA 441
Cdd:cd00047    72 DITVTLVSEEELSD--YTIRTLELSPKGC-------SESREVTHLHYT-------GWPdhgvpsspedllalvRRVRKEA 135
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1845972907 442 RQLSTPTIVQCIDGCSKSGTLVSIETALMHFIRGSPITkslILQSCVFVRLQRRLSVSSVLLYLFIYR 509
Cdd:cd00047   136 RKPNGPIVVHCSAGVGRTGTFIAIDILLERLEAEGEVD---VFEIVKALRKQRPGMVQTLEQYEFIYE 200
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
296-513 1.28e-28

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: 113.19  E-value: 1.28e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 296 DFIHANYVK----GGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSAVDSStlgpldsanRNHCPYYWPRaENE 371
Cdd:cd14541     1 DYINANYVNmeipGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERG---------RVKCHQYWPD-LGE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 372 SLRFGSFHITCMKvdSKADPLFTITKLKvqkvggnLLDAEFDEELFLEHwqwdWQYLGdvhWP---------------FR 436
Cdd:cd14541    71 TMQFGNLQITCVS--EEVTPSFAFREFI-------LTNTNTGEERHITQ----MQYLA---WPdhgvpddssdfldfvKR 134
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1845972907 437 VlRKARQ-LSTPTIVQCIDGCSKSGTLVSIETAlMHFIRGS-PITKSLILQScvfVRLQRRLSVSSVLLYLFIYRVILR 513
Cdd:cd14541   135 V-RQNRVgMVEPTVVHCSAGIGRTGVLITMETA-MCLIEANePVYPLDIVRT---MRDQRAMLIQTPSQYRFVCEAILR 208
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
238-508 8.79e-25

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: 103.98  E-value: 8.79e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 238 LTKARSKMVPCAEFSRVKLNdglgrLDDRNElrngmfsdeheflqeegytakstygTTDFIHANYVKGGPLLNTFICAQA 317
Cdd:cd14543    30 QEKNRYGDVLCLDQSRVKLP-----KRNGDE-------------------------RTDYINANFMDGYKQKNAYIATQG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 318 PLKNTQEDFWRMVFQEKCQFIVMLNSavdsstlgpLDSANRNHCPYYWPRAENESLRFGSFHITCMKVDSKADplFTITK 397
Cdd:cd14543    80 PLPKTYSDFWRMVWEQKVLVIVMTTR---------VVERGRVKCGQYWPLEEGSSLRYGDLTVTNLSVENKEH--YKKTT 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 398 LKVQkvggnllDAEFDEELFLEHWQWdwqylgdVHWP-FRV----------LRKARQ-----------------LSTPTI 449
Cdd:cd14543   149 LEIH-------NTETDESRQVTHFQF-------TSWPdFGVpssaaalldfLGEVRQqqalavkamgdrwkghpPGPPIV 214
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1845972907 450 VQCIDGCSKSGTLVSIETALMHFirgSPITKSLILQSCVFVRLQRRLSVSSVLLYLFIY 508
Cdd:cd14543   215 VHCSAGIGRTGTFCTLDICLSQL---EDVGTLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
298-508 1.45e-23

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: 98.86  E-value: 1.45e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 298 IHANYVK-GGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNsavdsstlgPLDSANRNHCPYYWPRAENESlRFG 376
Cdd:cd18533     2 INASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLT---------PLVENGREKCDQYWPSGEYEG-EYG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 377 SFHITCMKVDSKADPLFTITKLKVQKVGGNlldaefdeelflEHWQWDWQYLGdvhWP-FRV----------------LR 439
Cdd:cd18533    72 DLTVELVSEEENDDGGFIVREFELSKEDGK------------VKKVYHIQYKS---WPdFGVpdspedlltliklkreLN 136
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1845972907 440 KARQLSTPTIVQCIDGCSKSGTLVSIETALMHFIRGSPITKS------LILQSCVFVRLQRRLSVSSVLLYLFIY 508
Cdd:cd18533   137 DSASLDPPIIVHCSAGVGRTGTFIALDSLLDELKRGLSDSQDledsedPVYEIVNQLRKQRMSMVQTLRQYIFLY 211
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
293-513 1.17e-21

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


Pssm-ID: 350448 [Multi-domain]  Cd Length: 274  Bit Score: 94.92  E-value: 1.17e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 293 GTTDFIHANYVK----GGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSavdsstlgpLDSANRNHCPYYWPRA 368
Cdd:cd14600    61 GNEDYINASYVNmeipSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSLIVMLTT---------LTERGRTKCHQYWPDP 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 369 EnESLRFGSFHITCMKVDskadplFTITKLKVQKVggnLLDAEFDEELFLEHWQWdwqylgdVHWP-------------- 434
Cdd:cd14600   132 P-DVMEYGGFRVQCHSED------CTIAYVFREML---LTNTQTGEERTVTHLQY-------VAWPdhgvpddssdflef 194
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1845972907 435 FRVLRKARQLSTPTIVQCIDGCSKSGTLVSIETALMHFIRGSPITKSLILQScvfVRLQRRLSVSSVLLYLFIYRVILR 513
Cdd:cd14600   195 VNYVRSKRVENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRK---MRDQRAMMVQTSSQYKFVCEAILR 270
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
295-515 3.24e-21

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: 93.56  E-value: 3.24e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 295 TDFIHANYVKGGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSAVDSStlgpldsanRNHCPYYWPRAENEslR 374
Cdd:cd17667    57 SDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKG---------RRKCDQYWPTENSE--E 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 375 FGSFHITCMKVDSKA---DPLFTITKLKVQKVGGNLLDAEFDEELFLEHWQWDWQYLGDVHWPFRVLRKARQLST----- 446
Cdd:cd17667   126 YGNIIVTLKSTKIHAcytVRRFSIRNTKVKKGQKGNPKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAartpe 205
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1845972907 447 --PTIVQCIDGCSKSGTLVSIETALMHFIRGSPITkslILQSCVFVRLQRRLSVSSVLLYLFIYRVILRWI 515
Cdd:cd17667   206 mgPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVN---VLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAI 273
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
295-516 2.96e-20

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: 90.21  E-value: 2.96e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 295 TDFIHANYVK---GGPLL----NTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSAVDSStlgpldsanRNHCPYYWPr 367
Cdd:cd14544    30 SDYINANYIRnenEGPTTdenaKTYIATQGCLENTVSDFWSMVWQENSRVIVMTTKEVERG---------KNKCVRYWP- 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 368 AENESLRFGSFHITCMKVDSKADplFTITKLKVQKVGgnlldaEFDEELFLEHWQW-DWQYLGDVHWPFRVL-------- 438
Cdd:cd14544   100 DEGMQKQYGPYRVQNVSEHDTTD--YTLRELQVSKLD------QGDPIREIWHYQYlSWPDHGVPSDPGGVLnfledvnq 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 439 -RKARQLSTPTIVQCIDGCSKSGTLVSIEtALMHFIRGSPITKSLILQSCV-FVRLQRRLSVSSVLLYLFIYRVILRWIE 516
Cdd:cd14544   172 rQESLPHAGPIVVHCSAGIGRTGTFIVID-MLLDQIKRKGLDCDIDIQKTIqMVRSQRSGMVQTEAQYKFIYVAVAQYIE 250
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
297-509 1.12e-19

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: 87.19  E-value: 1.12e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 297 FIHANYVKGGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSAvdsstlgplDSANRNHCPYYWPRAENESLRFG 376
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRC---------EEGNRNKCAQYWPSMEEGSRAFG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 377 SFHITCMkvDSKADPLFTITKLKVQKvggnlldaefDEELFLEHWQWDWQYL--------GDVHWPFRVLRKARQL---- 444
Cdd:cd14557    72 DVVVKIN--EEKICPDYIIRKLNINN----------KKEKGSGREVTHIQFTswpdhgvpEDPHLLLKLRRRVNAFnnff 139
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1845972907 445 STPTIVQCIDGCSKSGTLVSIETalmhFIRGSPITKSLILQSCVF-VRLQRRLSVSSVLLYLFIYR 509
Cdd:cd14557   140 SGPIVVHCSAGVGRTGTYIGIDA----MLEGLEAEGRVDVYGYVVkLRRQRCLMVQVEAQYILIHQ 201
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
240-512 2.54e-19

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 88.91  E-value: 2.54e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 240 KARSKMVPCAEFSRVKLNDGLGrlddrnelrngmfsdeheflqeegytakstyGTTDFIHANYVKGGPLLNTFICAQAPL 319
Cdd:PHA02747   54 KNRYWDIPCWDHNRVILDSGGG-------------------------------STSDYIHANWIDGFEDDKKFIATQGPF 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 320 KNTQEDFWRMVFQEKCQFIVMLNSAVDSStlgpldsaNRNHCPYYWPRAENESLRFGSFHITCMKVDSKadPLFTITKLK 399
Cdd:PHA02747  103 AETCADFWKAVWQEHCSIIVMLTPTKGTN--------GEEKCYQYWCLNEDGNIDMEDFRIETLKTSVR--AKYILTLIE 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 400 VQkvggnllDAEFDEELFLEHWQW-DW---QYLGDVHWPFRVLR--------------KARQLSTPTIVQCIDGCSKSGT 461
Cdd:PHA02747  173 IT-------DKILKDSRKISHFQCsEWfedETPSDHPDFIKFIKiidinrkksgklfnPKDALLCPIVVHCSDGVGKTGI 245
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1845972907 462 LVSIETALMHFIRgspiTKSLILQSCVF-VRLQRRLSVSSVLLYLFI---YRVIL 512
Cdd:PHA02747  246 FCAVDICLNQLVK----RKAICLAKTAEkIREQRHAGIMNFDDYLFIqpgYEVLH 296
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
297-515 5.36e-19

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: 85.97  E-value: 5.36e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 297 FIHANYVK---GGPLLNtFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSAVDSStlgpldsanRNHCPYYWPRA--ENE 371
Cdd:cd14540     1 YINASHITatvGGKQRF-YIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGG---------REKCFRYWPTLggEHD 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 372 SLRFGSFHITcmKVDSKADPLFTITKLKVQKVGGNlldaefdeelfLEHWQWDWQYLGdvhWP--------------FRV 437
Cdd:cd14540    71 ALTFGEYKVS--TKFSVSSGCYTTTGLRVKHTLSG-----------QSRTVWHLQYTD---WPdhgcpedvsgfldfLEE 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 438 LRKARQLST----------PTIVQCIDGCSKSGTLVSIETALMHFIRGSPITkslILQSCVFVRLQRRLSVSSVLLYLFI 507
Cdd:cd14540   135 INSVRRHTNqdvaghnrnpPTLVHCSAGVGRTGVVILADLMLYCLDHNEELD---IPRVLALLRHQRMLLVQTLAQYKFV 211

                  ....*...
gi 1845972907 508 YRVILRWI 515
Cdd:cd14540   212 YNVLIQYL 219
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
287-516 5.82e-19

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: 87.68  E-value: 5.82e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 287 TAKSTYGTTDFIHANYVKG--GPllNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMlnsAVDSSTLGpldsanRNHCPYY 364
Cdd:cd14604    77 TLKTSSQDSDYINANFIKGvyGP--KAYIATQGPLANTVIDFWRMIWEYNVAIIVM---ACREFEMG------RKKCERY 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 365 WPRAENESLRFGSFHITCMKVDSKADplFTITKLKVqkvggnlldaEFDEElflEHWQWDWQYlgdVHWP---------- 434
Cdd:cd14604   146 WPLYGEEPMTFGPFRISCEAEQARTD--YFIRTLLL----------EFQNE---TRRLYQFHY---VNWPdhdvpssfds 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 435 ----FRVLRKARQL-STPTIVQCIDGCSKSGTLVSIETAlMHFIRGSPITKSLILQSCVF-VRLQRRLSVSSVLLYLFIY 508
Cdd:cd14604   208 ildmISLMRKYQEHeDVPICIHCSAGCGRTGAICAIDYT-WNLLKAGKIPEEFNVFNLIQeMRTQRHSAVQTKEQYELVH 286

                  ....*...
gi 1845972907 509 RVILRWIE 516
Cdd:cd14604   287 RAIAQLFE 294
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
294-508 9.59e-19

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: 85.10  E-value: 9.59e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 294 TTDFIHANYVKGGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSAVDsstlgpldsANRNHCPYYWPrAENESL 373
Cdd:cd14548    23 GSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCME---------KGRVKCDHYWP-FDQDPV 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 374 RFGSFHITCMKVDSKADplFTITKLKVQKVggnlldaefDEELFLEHWQWdwqylgdVHWP-----------FRVLRKAR 442
Cdd:cd14548    93 YYGDITVTMLSESVLPD--WTIREFKLERG---------DEVRSVRQFHF-------TAWPdhgvpeapdslLRFVRLVR 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1845972907 443 QLS----TPTIVQCIDGCSKSGTLVSIETALMHfirgspitksliLQSCVFV---------RLQRRLSVSSVLLYLFIY 508
Cdd:cd14548   155 DYIkqekGPTIVHCSAGVGRTGTFIALDRLLQQ------------IESEDYVdifgivydlRKHRPLMVQTEAQYIFLH 221
PHA02738 PHA02738
hypothetical protein; Provisional
296-521 1.34e-18

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 86.90  E-value: 1.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 296 DFIHANYVKGGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSAVDSStlgpldsanRNHCPYYWPRAENESLRF 375
Cdd:PHA02738   76 DYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENG---------REKCFPYWSDVEQGSIRF 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 376 GSFHITCMKVDS-----KADPLFTITKLKVQKVGGNLLDAEFDEEL------FLEHWQWDWQYLGDVHWPFRVLRKARQL 444
Cdd:PHA02738  147 GKFKITTTQVEThphyvKSTLLLTDGTSATQTVTHFNFTAWPDHDVpkntseFLNFVLEVRQCQKELAQESLQIGHNRLQ 226
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1845972907 445 STPTIVQCIDGCSKSGTLVSIETALMHFIRGSPITKSLILQScvfVRLQRRLSVSSVLLYLFIYRVILRWIEPYVNK 521
Cdd:PHA02738  227 PPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSS---IRNQRYYSLFIPFQYFFCYRAVKRYVNLTVNK 300
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
238-511 1.57e-18

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 86.62  E-value: 1.57e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 238 LTKARSKMVPCAEFSRVKLNDglgrlddRNELRNGMFSDEHEFLQEegytAKSTYGTTDFIHANYVKGGPLLNTFICAQA 317
Cdd:PHA02746   52 LKKNRFHDIPCWDHSRVVINA-------HESLKMFDVGDSDGKKIE----VTSEDNAENYIHANFVDGFKEANKFICAQG 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 318 PLKNTQEDFWRMVFQEKCQFIVMLNSAVDSSTLgpldsanrnhCPYYWPRAENESLRFGSFHITCMKVDSKADplFTITK 397
Cdd:PHA02746  121 PKEDTSEDFFKLISEHESQVIVSLTDIDDDDEK----------CFELWTKEEDSELAFGRFVAKILDIIEELS--FTKTR 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 398 LKVQKVggnllDAEFDEELFlEHWQWDWQYLGDVHWPFRVL--------RKARQLST---------PTIVQCIDGCSKSG 460
Cdd:PHA02746  189 LMITDK-----ISDTSREIH-HFWFPDWPDNGIPTGMAEFLelinkvneEQAELIKQadndpqtlgPIVVHCSAGIGRAG 262
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1845972907 461 TLVSIETALMHFIRGSPITkslILQSCVFVRLQRRLSVSSVLLYLFIYRVI 511
Cdd:PHA02746  263 TFCAIDNALEQLEKEKEVC---LGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
295-516 2.32e-18

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: 85.32  E-value: 2.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 295 TDFIHANYVKG---GPLLN--TFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSAVDSStlgpldsanRNHCPYYWPRAE 369
Cdd:cd14606    47 SDYINANYVKNqllGPDENakTYIASQGCLEATVNDFWQMAWQENSRVIVMTTREVEKG---------RNKCVPYWPEVG 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 370 NESlRFGSFHIT-CMKVDSKadplftitKLKVQKVGGNLLDaefDEELFLEHWQwdWQYLGdvhWP-------------F 435
Cdd:cd14606   118 MQR-AYGPYSVTnCGEHDTT--------EYKLRTLQVSPLD---NGELIREIWH--YQYLS---WPdhgvpsepggvlsF 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 436 --RVLRKARQL--STPTIVQCIDGCSKSGTLVSIETaLMHFIRGSPITKSLILQSCV-FVRLQRRLSVSSVLLYLFIYRV 510
Cdd:cd14606   181 ldQINQRQESLphAGPIIVHCSAGIGRTGTIIVIDM-LMENISTKGLDCDIDIQKTIqMVRAQRSGMVQTEAQYKFIYVA 259

                  ....*.
gi 1845972907 511 ILRWIE 516
Cdd:cd14606   260 IAQFIE 265
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
297-509 2.69e-18

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: 83.24  E-value: 2.69e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 297 FIHANYVKG--GPLlnTFICAQAPLKNTQEDFWRMVFQEKCQFIVMlnsAVDSSTLGpldsanRNHCPYYWPRAENESLR 374
Cdd:cd14542     1 YINANFIKGvsGSK--AYIATQGPLPNTVLDFWRMIWEYNVQVIVM---ACREFEMG------KKKCERYWPEEGEEQLQ 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 375 FGSFHITCMKvDSKADPLFTITKLKVQkvggnlldaeFDEElflEHWQWDWQYlgdVHWPFR-----------VLRKARQ 443
Cdd:cd14542    70 FGPFKISLEK-EKRVGPDFLIRTLKVT----------FQKE---SRTVYQFHY---TAWPDHgvpssvdpildLVRLVRD 132
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1845972907 444 L----STPTIVQCIDGCSKSGTLVSIETALMhFIRGSPITKSLILQSCVF-VRLQRRLSVSSVLLYLFIYR 509
Cdd:cd14542   133 YqgseDVPICVHCSAGCGRTGTICAIDYVWN-LLKTGKIPEEFSLFDLVReMRKQRPAMVQTKEQYELVYR 202
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
295-468 3.36e-18

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: 83.60  E-value: 3.36e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 295 TDFIHANYVKGGPLLN-TFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSAVDsstlgpldsaNRNHCPYYWPRAENEsl 373
Cdd:cd14547    25 SSYINANYIRGYDGEEkAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTE----------AKEKCAQYWPEEENE-- 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 374 RFGSFHITCMKVDSKADplFTITKLKVQKVGgnlldaefdEELFLEH-WQWDWQylgDVHWPFRV------------LRK 440
Cdd:cd14547    93 TYGDFEVTVQSVKETDG--YTVRKLTLKYGG---------EKRYLKHyWYTSWP---DHKTPEAAqpllslvqeveeARQ 158
                         170       180
                  ....*....|....*....|....*...
gi 1845972907 441 ARQLSTPTIVQCIDGCSKSGTLVSIETA 468
Cdd:cd14547   159 TEPHRGPIVVHCSAGIGRTGCFIATSIG 186
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
297-508 6.12e-18

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: 82.72  E-value: 6.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 297 FIHANYVKGGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSAVDSStlgpldsanRNHCPYYWPrAENeSLRFG 376
Cdd:cd17668     1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKG---------RRKCDQYWP-ADG-SEEYG 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 377 SFHITCMKVDSKADPL---FTITKLKVQKvGGNllDAEFDEELFLEHWQWDWQYLGDVHWPFRVL---RKARQLST---- 446
Cdd:cd17668    70 NFLVTQKSVQVLAYYTvrnFTLRNTKIKK-GSQ--KGRPSGRVVTQYHYTQWPDMGVPEYTLPVLtfvRKASYAKRhavg 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1845972907 447 PTIVQCIDGCSKSGTLVSIETALMHFIRGSPITkslILQSCVFVRLQRRLSVSSVLLYLFIY 508
Cdd:cd17668   147 PVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVN---IFGFLKHIRSQRNYLVQTEEQYVFIH 205
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
293-514 6.41e-18

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 84.67  E-value: 6.41e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 293 GTTDFIHANYVKGGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSAVDSstlgpldsaNRNHCPYYWPRAENES 372
Cdd:PHA02742   76 GGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIMED---------GKEACYPYWMPHERGK 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 373 LRFGSFHITCMKVDSKADplFTITKLKVQKVG-GNLLDaefdeelfLEHWQW-DWQYLGDVHWPFRVL------------ 438
Cdd:PHA02742  147 ATHGEFKIKTKKIKSFRN--YAVTNLCLTDTNtGASLD--------IKHFAYeDWPHGGLPRDPNKFLdfvlavreadlk 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 439 ------RKARQLSTPTIVQCIDGCSKSGTLVSIETALMHFIRGSPITKSLILQScvfVRLQRRLSVSSVLLYLFIYRVIL 512
Cdd:PHA02742  217 advdikGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRD---LRKQRHNCLSLPQQYIFCYFIVL 293

                  ..
gi 1845972907 513 RW 514
Cdd:PHA02742  294 IF 295
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
280-511 2.28e-17

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: 82.18  E-value: 2.28e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 280 FLQEEGYTakstygttDFIHANYVKGGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSAVDSStlgpldsanRN 359
Cdd:cd14603    51 LLQEEGHS--------DYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVILMACREIEMG---------KK 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 360 HCPYYWPRAEnESLRFGSFHITCMKvDSKADPLFTITKLKVQKVggnlldaefDEELFLEHWQWdwqylgdVHWPFR--- 436
Cdd:cd14603   114 KCERYWAQEQ-EPLQTGPFTITLVK-EKRLNEEVILRTLKVTFQ---------KESRSVSHFQY-------MAWPDHgip 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 437 --------VLRKARQL----STPTIVQCIDGCSKSGTLVSIEtalmhFIRGSPITKSL-----ILQSCVFVRLQRRLSVS 499
Cdd:cd14603   176 dspdcmlaMIELARRLqgsgPEPLCVHCSAGCGRTGVICTVD-----YVRQLLLTQRIppdfsIFDVVLEMRKQRPAAVQ 250
                         250
                  ....*....|..
gi 1845972907 500 SVLLYLFIYRVI 511
Cdd:cd14603   251 TEEQYEFLYHTV 262
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
296-513 4.34e-17

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: 79.99  E-value: 4.34e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 296 DFIHANYVK----GGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSAVDSStlgpldsanRNHCPYYWPRAENE 371
Cdd:cd14601     1 DYINANYINmeipSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERG---------RVKCHQYWPEPSGS 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 372 SlRFGSFHITCmkVDSKADPLFTITKLkvqkvggNLLDAEFDEELFLEHWQWdwqylgdVHWP-------------FRVL 438
Cdd:cd14601    72 S-SYGGFQVTC--HSEEGNPAYVFREM-------TLTNLEKNESRPLTQIQY-------IAWPdhgvpddssdfldFVCL 134
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1845972907 439 RKARQL--STPTIVQCIDGCSKSGTLVSIETALMHFIRGSPITKSLILQScvfVRLQRRLSVSSVLLYLFIYRVILR 513
Cdd:cd14601   135 VRNKRAgkDEPVVVHCSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRT---MRDQRAMMIQTPSQYRFVCEAILK 208
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
297-469 2.14e-16

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: 77.83  E-value: 2.14e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 297 FIHANYVKGGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSaVDSSTLGpldsanrnhCPYYWPraENESLRFG 376
Cdd:cd14556     1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQ-LDPKDQS---------CPQYWP--DEGSGTYG 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 377 SFHITCMKVDskADPLFTITKLKVQKvggnllDAEFDEELFLEHwqwDWQYLGdvhWP---------------FRVLRKA 441
Cdd:cd14556    69 PIQVEFVSTT--IDEDVISRIFRLQN------TTRPQEGYRMVQ---QFQFLG---WPrdrdtppskrallklLSEVEKW 134
                         170       180       190
                  ....*....|....*....|....*....|
gi 1845972907 442 RQLST--PTIVQCIDGCSKSGTLVSIETAL 469
Cdd:cd14556   135 QEQSGegPIVVHCLNGVGRSGVFCAISSVC 164
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
297-508 2.58e-16

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: 77.89  E-value: 2.58e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 297 FIHANYVK--GGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSAVDSSTLgpldsanrNHCPYYWPRAENESLR 374
Cdd:cd17658     1 YINASLVEtpASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYST--------AKCADYFPAEENESRE 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 375 FGSFHITCMKVdSKADPLFTITKLKVQKVggnlldaEFDEE-LFLEHWQW-DWQYLGDVHWPFRVLRKARQLST------ 446
Cdd:cd17658    73 FGRISVTNKKL-KHSQHSITLRVLEVQYI-------ESEEPpLSVLHIQYpEWPDHGVPKDTRSVRELLKRLYGippsag 144
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1845972907 447 PTIVQCIDGCSKSGTLVSIETALMHFIRGSpiTKSLILQSCV-FVRLQRRLSVSSVLLYLFIY 508
Cdd:cd17658   145 PIVVHCSAGIGRTGAYCTIHNTIRRILEGD--MSAVDLSKTVrKFRSQRIGMVQTQDQYIFCY 205
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
293-515 5.07e-16

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: 77.62  E-value: 5.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 293 GTTDFIHANYVKGGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSAVDsstlgpldsANRNHCPYYWPrAENES 372
Cdd:cd14619    23 PGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCME---------AGRVKCEHYWP-LDYTP 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 373 LRFGsfHITCMKVDSKADPLFTITKLkvqkvggNLLDAEFDEELFLEHWQWD-WQYLG-----DVHWPFR-VLRKARQL- 444
Cdd:cd14619    93 CTYG--HLRVTVVSEEVMENWTVREF-------LLKQVEEQKTLSVRHFHFTaWPDHGvpsstDTLLAFRrLLRQWLDQt 163
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1845972907 445 --STPTIVQCIDGCSKSGTLVSIETALMHFIRGSPITKSLILQScvfVRLQRRLSVSSVLLYLFIYRVILRWI 515
Cdd:cd14619   164 msGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQK---MRENRPLMVQTESQYVFLHQCILDFL 233
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
297-508 7.96e-16

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: 76.24  E-value: 7.96e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 297 FIHANYVKGGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSAVDSStlgpldsanRNHCPYYWPraENESLRFG 376
Cdd:cd14549     1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERG---------RRKCDQYWP--KEGTETYG 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 377 SFHITCMKVDSKAD---PLFTITKLKVQKVGGnlldaEFDEELFLEHWQWDWQYLGDVHWPFRVLRKARQLST------- 446
Cdd:cd14549    70 NIQVTLLSTEVLATytvRTFSLKNLKLKKVKG-----RSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAanppgag 144
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1845972907 447 PTIVQCIDGCSKSGTLVSIETALmhfirgspitKSLILQSCVFV-------RLQRRLSVSSVLLYLFIY 508
Cdd:cd14549   145 PIVVHCSAGVGRTGTYIVIDSML----------QQIQDKGTVNVfgflkhiRTQRNYLVQTEEQYIFIH 203
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
418-512 8.00e-16

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 73.16  E-value: 8.00e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907  418 LEHWQWDWQYLGDVHWPFRVLRKA-------RQLSTPTIVQCIDGCSKSGTLVSIETALMHFIRGSPitKSLILQSCVFV 490
Cdd:smart00404   5 YHYTGWPDHGVPESPDSILELLRAvkknlnqSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAG--EVDIFDTVKEL 82
                           90       100
                   ....*....|....*....|..
gi 1845972907  491 RLQRRLSVSSVLLYLFIYRVIL 512
Cdd:smart00404  83 RSQRPGMVQTEEQYLFLYRALL 104
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
418-512 8.00e-16

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: 73.16  E-value: 8.00e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907  418 LEHWQWDWQYLGDVHWPFRVLRKA-------RQLSTPTIVQCIDGCSKSGTLVSIETALMHFIRGSPitKSLILQSCVFV 490
Cdd:smart00012   5 YHYTGWPDHGVPESPDSILELLRAvkknlnqSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAG--EVDIFDTVKEL 82
                           90       100
                   ....*....|....*....|..
gi 1845972907  491 RLQRRLSVSSVLLYLFIYRVIL 512
Cdd:smart00012  83 RSQRPGMVQTEEQYLFLYRALL 104
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
295-471 1.04e-15

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: 76.48  E-value: 1.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 295 TDFIHANYVKGGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSAVDSStlgpldsanRNHCPYYWPRAENESLR 374
Cdd:cd14616    25 SDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKG---------RIRCHQYWPEDNKPVTV 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 375 FGSFHITCMKVDSKADplFTITKLKVQKVGGNLLDAEFDEELFLEHWQWDwQYLGDVHWpFRVLRKAR-QLSTPTIVQCI 453
Cdd:cd14616    96 FGDIVITKLMEDVQID--WTIRDLKIERHGDYMMVRQCNFTSWPEHGVPE-SSAPLIHF-VKLVRASRaHDNTPMIVHCS 171
                         170
                  ....*....|....*...
gi 1845972907 454 DGCSKSGTLVSIETALMH 471
Cdd:cd14616   172 AGVGRTGVFIALDHLTQH 189
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
293-509 1.07e-15

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: 76.50  E-value: 1.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 293 GTTDFIHANYVKGGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSAVDSStlgpldsanRNHCPYYWPrAENES 372
Cdd:cd14617    23 PCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKG---------RVKCDHYWP-ADQDS 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 373 LRFGSfhITCMKVDSKADPLFTITKLKVQKvggnllDAEFDEELFLEHWQWdwqylgdVHWP-----------FRVLRKA 441
Cdd:cd14617    93 LYYGD--LIVQMLSESVLPEWTIREFKICS------EEQLDAPRLVRHFHY-------TVWPdhgvpettqslIQFVRTV 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1845972907 442 RQL------STPTIVQCIDGCSKSGTLVSIETALMHFIRgspiTKSLILQSCVF-VRLQRRLSVSSVLLYLFIYR 509
Cdd:cd14617   158 RDYinrtpgSGPTVVHCSAGVGRTGTFIALDRILQQLDS----KDSVDIYGAVHdLRLHRVHMVQTECQYVYLHQ 228
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
295-512 1.72e-15

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: 76.08  E-value: 1.72e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 295 TDFIHANYVKGGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSAvdsstlgplDSANRNHCPYYWPRAEnESLR 374
Cdd:cd14614    40 SDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQC---------NEKRRVKCDHYWPFTE-EPVA 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 375 FGSfhITCMKVDSKADPLFTITKLKVqkvggnlldAEFDEELFLEHWQWdwqylgdVHWP-------------FRVLRKA 441
Cdd:cd14614   110 YGD--ITVEMLSEEEQPDWAIREFRV---------SYADEVQDVMHFNY-------TAWPdhgvptanaaesiLQFVQMV 171
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1845972907 442 RQLST----PTIVQCIDGCSKSGTLVSIETaLMHFIRGSPITKSLILQScvFVRLQRRLSVSSVLLYLFIYRVIL 512
Cdd:cd14614   172 RQQAVkskgPMIIHCSAGVGRTGTFIALDR-LLQHIRDHEFVDILGLVS--EMRSYRMSMVQTEEQYIFIHQCVQ 243
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
295-516 2.01e-15

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: 76.21  E-value: 2.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 295 TDFIHANYV--------KGGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSAVDSStlgpldsanRNHCPYYWP 366
Cdd:cd14605    31 SDYINANIImpefetkcNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSRVIVMTTKEVERG---------KSKCVKYWP 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 367 raENESLR-FGSFHITCMKVDSKADplFTITKLKVQKVG-GNLLDAEfdeelflehWQWDWQYLGDVHWP--------FR 436
Cdd:cd14605   102 --DEYALKeYGVMRVRNVKESAAHD--YILRELKLSKVGqGNTERTV---------WQYHFRTWPDHGVPsdpggvldFL 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 437 VLRKARQLST----PTIVQCIDGCSKSGTLVSIETaLMHFIRGSPITKSL-ILQSCVFVRLQRRLSVSSVLLYLFIYRVI 511
Cdd:cd14605   169 EEVHHKQESImdagPVVVHCSAGIGRTGTFIVIDI-LIDIIREKGVDCDIdVPKTIQMVRSQRSGMVQTEAQYRFIYMAV 247

                  ....*
gi 1845972907 512 LRWIE 516
Cdd:cd14605   248 QHYIE 252
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
295-512 2.02e-15

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: 75.75  E-value: 2.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 295 TDFIHANYVKGGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSavdsstlgpLDSANRNHCPYYWPraENESLR 374
Cdd:cd14620    23 SDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTN---------LKERKEEKCYQYWP--DQGCWT 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 375 FGSFHITCMKVDSKADplFTITKLKVQKVGGNLLDA-EFDEELFLEHWQwdwqylgDVHWPF------RVLRKARQL--- 444
Cdd:cd14620    92 YGNIRVAVEDCVVLVD--YTIRKFCIQPQLPDGCKApRLVTQLHFTSWP-------DFGVPFtpigmlKFLKKVKSVnpv 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1845972907 445 -STPTIVQCIDGCSKSGTLVSIET--ALMHFIRgspitKSLILQSCVFVRLQRRLSVSSVLLYLFIYRVIL 512
Cdd:cd14620   163 hAGPIVVHCSAGVGRTGTFIVIDAmiDMMHAEQ-----KVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALL 228
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
297-512 2.35e-15

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: 75.10  E-value: 2.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 297 FIHANYVK---GGPLLNtFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSAVDSStlgpldsanRNHCPYYWPRAENESL 373
Cdd:cd14538     1 YINASHIRipvGGDTYH-YIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGG---------KVKCHRYWPDSLNKPL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 374 RF-GSFHITCMKVDSKADplFTITKLkvqkvggNLLDAEFDEELFLEHWQWdwqylgdVHWP-----------FRVLRKA 441
Cdd:cd14538    71 ICgGRLEVSLEKYQSLQD--FVIRRI-------SLRDKETGEVHHITHLNF-------TTWPdhgtpqsadplLRFIRYM 134
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1845972907 442 RQL--STPTIVQCIDGCSKSGTLVSIETALMHFIRGSPITKSLILQScvfVRLQRRLSVSSVLLYLFIYRVIL 512
Cdd:cd14538   135 RRIhnSGPIVVHCSAGIGRTGVLITIDVALGLIERDLPFDIQDIVKD---LREQRQGMIQTKDQYIFCYKACL 204
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
295-512 2.52e-15

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: 76.23  E-value: 2.52e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 295 TDFIHANYVKGGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSavdsstlgpLDSANRNHCPYYWPRAENESlr 374
Cdd:cd14626    69 SDYINANYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTR---------LEEKSRVKCDQYWPIRGTET-- 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 375 FGSFHITCMkvDSKADPLFTITKLKVQKVGGNlldaefdEELFLEHWQW-DWQYLGDVHWPFRVLRKARQLST------- 446
Cdd:cd14626   138 YGMIQVTLL--DTVELATYSVRTFALYKNGSS-------EKREVRQFQFmAWPDHGVPEYPTPILAFLRRVKAcnppdag 208
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1845972907 447 PTIVQCIDGCSKSGTLVSIETALMHFIRGSPITkslILQSCVFVRLQRRLSVSSVLLYLFIYRVIL 512
Cdd:cd14626   209 PMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVD---IYGHVTCMRSQRNYMVQTEDQYIFIHEALL 271
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
295-512 2.88e-15

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: 75.36  E-value: 2.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 295 TDFIHANYVKGGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSAVDSStlgpldsanRNHCPYYWPrAENESLR 374
Cdd:cd14618    25 SDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENG---------RVLCDHYWP-SESTPVS 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 375 FGsfHITCMKVDSKADPLFTITKLKVQKVGgnlldaeFDEELFLEHWQWdwqylgdVHWP-------------FRVLR-- 439
Cdd:cd14618    95 YG--HITVHLLAQSSEDEWTRREFKLWHED-------LRKERRVKHLHY-------TAWPdhgipestsslmaFRELVre 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1845972907 440 --KARQLSTPTIVQCIDGCSKSGTLVsietALMHFIRGSPITKSLILQSCVFV-RLQRRLSVSSVLLYLFIYRVIL 512
Cdd:cd14618   159 hvQATKGKGPTLVHCSAGVGRSGTFI----ALDRLLRQLKEEKVVDVFNTVYIlRMHRYLMIQTLSQYIFLHSCIL 230
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
289-469 5.12e-15

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: 74.74  E-value: 5.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 289 KSTYGTTDFIHANYVKGGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSAVDSSTLgpldsanrnHCPYYWPRA 368
Cdd:cd14545    18 KLKQGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQI---------KCAQYWPQG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 369 ENES--LRFGSFHITCMKVDSKADplFTITKLKvqkvggnLLDAEFDEELFLEHWQW-DWQYLGDVHWP---FRVLRKAR 442
Cdd:cd14545    89 EGNAmiFEDTGLKVTLLSEEDKSY--YTVRTLE-------LENLKTQETREVLHFHYtTWPDFGVPESPaafLNFLQKVR 159
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1845972907 443 Q---LST---PTIVQCIDGCSKSGTLVSIETAL 469
Cdd:cd14545   160 EsgsLSSdvgPPVVHCSAGIGRSGTFCLVDTCL 192
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
295-512 9.22e-15

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: 73.72  E-value: 9.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 295 TDFIHANYVKG--GPllNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMlnsAVDSSTLGpldsanRNHCPYYWPRAENES 372
Cdd:cd14602    26 SDYINANFIKGvyGP--RAYIATQGPLSTTLLDFWRMIWEYSVLIIVM---ACMEFEMG------KKKCERYWAEPGEMQ 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 373 LRFGSFHITCMKVDSKADplFTITKLKVQKVGGNLLDAEFdeelfleHWQwDW---------QYLGDVHWPFRVLRKARq 443
Cdd:cd14602    95 LEFGPFSVTCEAEKRKSD--YIIRTLKVKFNSETRTIYQF-------HYK-NWpdhdvpssiDPILELIWDVRCYQEDD- 163
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1845972907 444 lSTPTIVQCIDGCSKSGTLVSIETALMHFIRG-SPITKSL--ILQScvfVRLQRRLSVSSVLLYLFIYRVIL 512
Cdd:cd14602   164 -SVPICIHCSAGCGRTGVICAIDYTWMLLKDGiIPENFSVfsLIQE---MRTQRPSLVQTKEQYELVYNAVI 231
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
294-466 1.22e-14

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: 73.31  E-value: 1.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 294 TTDFIHANYVKGGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSAVDSStlgpldsanRNHCPYYWPraENESL 373
Cdd:cd14615    23 TDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQG---------RTKCEEYWP--SKQKK 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 374 RFGsfHITCMKVDSKADPLFTITKLKVQKVGGNlldaefdEELFLEHWQW-DWQYLG-----DVHWPFRVL----RKARQ 443
Cdd:cd14615    92 DYG--DITVTMTSEIVLPEWTIRDFTVKNAQTN-------ESRTVRHFHFtSWPDHGvpettDLLINFRHLvreyMKQNP 162
                         170       180
                  ....*....|....*....|...
gi 1845972907 444 LSTPTIVQCIDGCSKSGTLVSIE 466
Cdd:cd14615   163 PNSPILVHCSAGVGRTGTFIAID 185
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
297-512 1.42e-14

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: 72.64  E-value: 1.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 297 FIHANYVKGGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSAVDsstlgpldsANRNHCPYYWPraeNESLRFG 376
Cdd:cd14555     1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVE---------VGRVKCSRYWP---DDTEVYG 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 377 SFHITCMKVDSKADplFTITKLKVQKVGGNLLdaefdEELFLEHWQwDWQYLGDVHWPFRVLRKARQLST-------PTI 449
Cdd:cd14555    69 DIKVTLVETEPLAE--YVVRTFALERRGYHEI-----REVRQFHFT-GWPDHGVPYHATGLLGFIRRVKAsnppsagPIV 140
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1845972907 450 VQCIDGCSKSGTLVSIETALMHFIRGSPITksliLQSCVFVRLQRRLS-VSSVLLYLFIYRVIL 512
Cdd:cd14555   141 VHCSAGAGRTGCYIVIDIMLDMAEREGVVD----IYNCVKELRSRRVNmVQTEEQYIFIHDAIL 200
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
293-470 1.64e-14

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: 73.91  E-value: 1.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 293 GTTDFIHANYVKGGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSAVDSSTLgpldsanrnHCPYYWPRAENES 372
Cdd:cd14608    47 EDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSL---------KCAQYWPQKEEKE 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 373 LRF--GSFHITCMKVDSKAdpLFTITKLKVQkvggNLLDAEFDEELfleHWQW-DWQYLGDVHWP-------FRVlRKAR 442
Cdd:cd14608   118 MIFedTNLKLTLISEDIKS--YYTVRQLELE----NLTTQETREIL---HFHYtTWPDFGVPESPasflnflFKV-RESG 187
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1845972907 443 QLST---PTIVQCIDGCSKSGTLVSIETALM 470
Cdd:cd14608   188 SLSPehgPVVVHCSAGIGRSGTFCLADTCLL 218
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
295-512 1.93e-14

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: 74.29  E-value: 1.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 295 TDFIHANYVKGGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSavdsstlgpLDSANRNHCPYYWPraENESLR 374
Cdd:cd14621    80 SDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTN---------LKERKECKCAQYWP--DQGCWT 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 375 FGSFHITCMKVDSKADplFTITKLKVQKVGGnlLDAEFDEELFLEHWQWDWQYLGDVHWP---FRVLRKAR----QLSTP 447
Cdd:cd14621   149 YGNIRVSVEDVTVLVD--YTVRKFCIQQVGD--VTNKKPQRLITQFHFTSWPDFGVPFTPigmLKFLKKVKncnpQYAGA 224
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1845972907 448 TIVQCIDGCSKSGTLVSIETAL--MHFIRgspitKSLILQSCVFVRLQRRLSVSSVLLYLFIYRVIL 512
Cdd:cd14621   225 IVVHCSAGVGRTGTFIVIDAMLdmMHAER-----KVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALL 286
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
297-512 2.34e-14

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: 72.01  E-value: 2.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 297 FIHANYVKGGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSAVDsstlgpldsANRNHCPYYWPraeNESLRFG 376
Cdd:cd14632     1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVE---------VGRVKCSKYWP---DDSDTYG 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 377 SFHITCMKVDSKADplFTITKLKVQKVGGNLLD--AEFDEELFLEHwQWDWQYLGDVHWPFRVLRKARQLSTPTIVQCID 454
Cdd:cd14632    69 DIKITLLKTETLAE--YSVRTFALERRGYSARHevKQFHFTSWPEH-GVPYHATGLLAFIRRVKASTPPDAGPVVVHCSA 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 455 GCSKSGTLVSIETAL-MHFIRGspitkSLILQSCVFVRLQRRLS-VSSVLLYLFIYRVIL 512
Cdd:cd14632   146 GAGRTGCYIVLDVMLdMAECEG-----VVDIYNCVKTLCSRRINmIQTEEQYIFIHDAIL 200
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
295-512 2.81e-14

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: 72.43  E-value: 2.81e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 295 TDFIHANYVKGGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSavdsstlgpLDSANRNHCPYYWPRAENESlr 374
Cdd:cd14553    31 SDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTK---------LEERSRVKCDQYWPTRGTET-- 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 375 FGSFHITCmkVDSKADPLFTITKLKVQKVGGNlldaefdEELFLEHWQ---WDWQYLGDVHWPF-RVLRKARQL----ST 446
Cdd:cd14553   100 YGLIQVTL--LDTVELATYTVRTFALHKNGSS-------EKREVRQFQftaWPDHGVPEHPTPFlAFLRRVKACnppdAG 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1845972907 447 PTIVQCIDGCSKSGTLVSIEtALMHFIRGSpitKSLILQSCVFV-RLQRRLSVSSVLLYLFIYRVIL 512
Cdd:cd14553   171 PIVVHCSAGVGRTGCFIVID-SMLERIKHE---KTVDIYGHVTClRAQRNYMVQTEDQYIFIHDALL 233
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
295-512 3.96e-14

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: 72.82  E-value: 3.96e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 295 TDFIHANYVKGGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSavdsstlgpLDSANRNHCPYYWPRAENESlr 374
Cdd:cd14625    75 SDYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTK---------LEEKSRIKCDQYWPSRGTET-- 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 375 FGSFHITCMkvDSKADPLFTITKLKVQKVGGNlldaefdEELFLEHWQWD-WQYLGDVHWPFRVLRKARQLST------- 446
Cdd:cd14625   144 YGMIQVTLL--DTIELATFCVRTFSLHKNGSS-------EKREVRQFQFTaWPDHGVPEYPTPFLAFLRRVKTcnppdag 214
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1845972907 447 PTIVQCIDGCSKSGTLVSIETALMhfiRGSPITKSLILQSCVFVRLQRRLSVSSVLLYLFIYRVIL 512
Cdd:cd14625   215 PIVVHCSAGVGRTGCFIVIDAMLE---RIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALL 277
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
297-508 4.24e-14

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: 71.27  E-value: 4.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 297 FIHANYVKGGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMlnsavdsstLGPLDSANRNHCPYYWPraeNESLRFG 376
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVM---------LTELKEGDQEQCAQYWG---DEKKTYG 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 377 SFHITCMKVDSKadPLFTITKLKVQKvggnlldAEFDEELFLEHwqwdWQYLgdvHWPFRVL-----------RKARQ-- 443
Cdd:cd14558    69 DIEVELKDTEKS--PTYTVRVFEITH-------LKRKDSRTVYQ----YQYH---KWKGEELpekpkdlvdmiKSIKQkl 132
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1845972907 444 --------LSTPTIVQCIDGCSKSGTLVsietALMHFIRGSPITKSL-ILQSCVFVRLQRRLSVSSVLLYLFIY 508
Cdd:cd14558   133 pyknskhgRSVPIVVHCSDGSSRTGIFC----ALWNLLESAETEKVVdVFQVVKALRKQRPGMVSTLEQYQFLY 202
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
294-512 1.00e-13

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: 70.43  E-value: 1.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 294 TTDFIHANYVKGGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSAVDsstlgpldsANRNHCPYYWPraeNESL 373
Cdd:cd14631    12 SSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVE---------VGRVKCYKYWP---DDTE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 374 RFGSFHITCMKVDSKADplFTITKLKVQKVGGNlldaEFDEELFLEHWQW-----DWQYLGDVHWPFRVLRKARQLSTPT 448
Cdd:cd14631    80 VYGDFKVTCVEMEPLAE--YVVRTFTLERRGYN----EIREVKQFHFTGWpdhgvPYHATGLLSFIRRVKLSNPPSAGPI 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1845972907 449 IVQCIDGCSKSGTLVSIETALMHFIRGSPITksliLQSCVFVRLQRRLS-VSSVLLYLFIYRVIL 512
Cdd:cd14631   154 VVHCSAGAGRTGCYIVIDIMLDMAEREGVVD----IYNCVKALRSRRINmVQTEEQYIFIHDAIL 214
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
297-509 1.18e-13

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: 69.94  E-value: 1.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 297 FIHANYVKGGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSavdsstlgpLDSANRNHCPYYWPRAENESlrFG 376
Cdd:cd14551     1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTN---------LKERKEKKCSQYWPDQGCWT--YG 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 377 SFHITCMKVDSKADplFTITKLKVQKVGGNLldAEFDEELFLEHWQWDWQYLGDVHWP---FRVLRKARQLST----PTI 449
Cdd:cd14551    70 NLRVRVEDTVVLVD--YTTRKFCIQKVNRGI--GEKRVRLVTQFHFTSWPDFGVPFTPigmLKFLKKVKSANPpragPIV 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 450 VQCIDGCSKSGTLVSIEtALMHFIRGSpiTKSLILQSCVFVRLQRRLSVSSVLLYLFIYR 509
Cdd:cd14551   146 VHCSAGVGRTGTFIVID-AMLDMMHAE--GKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
297-516 1.41e-13

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: 70.00  E-value: 1.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 297 FIHANYVK---GGPLLNtFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSAvdsstlgplDSANRNHCPYYWPR--AENE 371
Cdd:cd14598     1 YINASHIKvtvGGKEWD-YIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAE---------EEGGREKSFRYWPRlgSRHN 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 372 SLRFGSFHITC-MKVDSKAdplFTITKLKVQkvggNLLDAefdEELFLEHWQW-DW-------------QYLGDVHwpfR 436
Cdd:cd14598    71 TVTYGRFKITTrFRTDSGC---YATTGLKIK----HLLTG---QERTVWHLQYtDWpehgcpedlkgflSYLEEIQ---S 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 437 VLRKARQLS------TPTIVQCIDGCSKSGTLVSIETALMHFIRGSPITKSLILQscvFVRLQRRLSVSSVLLYLFIYRV 510
Cdd:cd14598   138 VRRHTNSTIdpkspnPPVLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLD---MLRQQRMMMVQTLSQYTFVYKV 214

                  ....*.
gi 1845972907 511 ILRWIE 516
Cdd:cd14598   215 LIQFLK 220
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
296-511 1.90e-13

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: 69.26  E-value: 1.90e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 296 DFIHANYVKGGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSavdsstlgpLDSANRNHCPYYWPrAENeSLRF 375
Cdd:cd14622     1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTE---------LQEREQEKCVQYWP-SEG-SVTH 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 376 GSFHITcMKVDSKADPlFTITKLKVQkvggnlLDAEFDEELFLEHWQWDWQYLG---------DVhwpFRVLRKARQLS- 445
Cdd:cd14622    70 GEITIE-IKNDTLLET-ISIRDFLVT------YNQEKQTRLVRQFHFHGWPEIGipaegkgmiDL---IAAVQKQQQQTg 138
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1845972907 446 -TPTIVQCIDGCSKSGTLVSIETALMHfIRGSPITKslILQSCVFVRLQRRLSVSSVLLYLFIYRVI 511
Cdd:cd14622   139 nHPIVVHCSAGAGRTGTFIALSNILER-VKAEGLLD--VFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
295-511 1.98e-13

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: 70.28  E-value: 1.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 295 TDFIHANYVKG-GPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSavdsstlgpLDSANRNhCPYYWPRaenESL 373
Cdd:cd14613    54 SSYINANYIRGyGGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITN---------IEEMNEK-CTEYWPE---EQV 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 374 RFGSFHITCMKVDSKADPLFTITKLkvqKVGGnlldaefdEELFLEH-WQWDW--QYLGDVHWPFRVL--------RKAR 442
Cdd:cd14613   121 TYEGIEITVKQVIHADDYRLRLITL---KSGG--------EERGLKHyWYTSWpdQKTPDNAPPLLQLvqeveearQQAE 189
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1845972907 443 QLSTPTIVQCIDGCSKSGTLVSIETALMHFIRGSPITkslILQSCVFVRLQRRLSVSSVLLYLFIYRVI 511
Cdd:cd14613   190 PNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVD---ILRTTCQLRLDRGGMIQTCEQYQFVHHVL 255
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
288-401 3.70e-13

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: 69.48  E-value: 3.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 288 AKSTYGTTDFIHANYVKG-GPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSAVDsstlgpldsaNRNHCPYYWP 366
Cdd:cd14612    37 AGSQEEEGSYINANYIRGyDGKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITKLKE----------KKEKCVHYWP 106
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1845972907 367 RAENEslrFGSFHITCMKVdsKADPLFTITKLKVQ 401
Cdd:cd14612   107 EKEGT---YGRFEIRVQDM--KECDGYTIRDLTIQ 136
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
295-512 4.38e-13

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: 69.09  E-value: 4.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 295 TDFIHANYVKGGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSavdsstlgpLDSANRNHCPYYWPraENESLR 374
Cdd:cd14554    34 SDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTK---------LREMGREKCHQYWP--AERSAR 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 375 FGSFhitcmKVDSKAD---PLFTITKLKVQkvggnllDAEFDEELFLEHWQW-DW-------------QYLGDVHwpfrv 437
Cdd:cd14554   103 YQYF-----VVDPMAEynmPQYILREFKVT-------DARDGQSRTVRQFQFtDWpeqgvpksgegfiDFIGQVH----- 165
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1845972907 438 lRKARQLST--PTIVQCIDGCSKSGTLVSIETALMHfIRGSPITKslILQSCVFVRLQRRLSVSSVLLYLFIYRVIL 512
Cdd:cd14554   166 -KTKEQFGQegPITVHCSAGVGRTGVFITLSIVLER-MRYEGVVD--VFQTVKLLRTQRPAMVQTEDQYQFCYRAAL 238
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
295-469 5.00e-13

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: 68.90  E-value: 5.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 295 TDFIHANYVKGGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSAVDsstlgpldsANRNHCPYYWPraeNESLR 374
Cdd:cd14630    31 SDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVE---------VGRVKCVRYWP---DDTEV 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 375 FGSFHITCMKVDSKADplFTITKLKVQKVGGNLLdaefdEELFLEHWQwDWQYLGDVHWPFRVLRKARQL-------STP 447
Cdd:cd14630    99 YGDIKVTLIETEPLAE--YVIRTFTVQKKGYHEI-----REIRQFHFT-SWPDHGVPCYATGLLGFVRQVkflnppdAGP 170
                         170       180
                  ....*....|....*....|..
gi 1845972907 448 TIVQCIDGCSKSGTLVSIETAL 469
Cdd:cd14630   171 IVVHCSAGAGRTGCFIAIDIML 192
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
295-516 5.00e-13

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: 69.64  E-value: 5.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 295 TDFIHANYVK---GGPLLNtFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSAvdsstlgplDSANRNHCPYYWPR--AE 369
Cdd:cd14599    65 TGYINASHIKvtvGGEEWH-YIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAE---------EEGGRSKSHRYWPKlgSK 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 370 NESLRFGSFHITC-MKVDSKAdplFTITKLKVQkvggNLLDAefdEELFLEHWQW-DW-------------QYLGDVHWP 434
Cdd:cd14599   135 HSSATYGKFKVTTkFRTDSGC---YATTGLKVK----HLLSG---QERTVWHLQYtDWpdhgcpeevqgflSYLEEIQSV 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 435 FR----VLRKARQLSTPTIVQCIDGCSKSGTLVSIETALMHFIRGSPITKSLILQscvFVRLQRRLSVSSVLLYLFIYRV 510
Cdd:cd14599   205 RRhtnsMLDSTKNCNPPIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVPVMLR---HLREQRMFMIQTIAQYKFVYQV 281

                  ....*.
gi 1845972907 511 ILRWIE 516
Cdd:cd14599   282 LIQFLK 287
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
295-511 6.98e-13

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: 68.15  E-value: 6.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 295 TDFIHANYVKGGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSavdsstlgpLDSANRNHCPYYWPraENESLR 374
Cdd:cd14623    24 TDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTE---------LEERGQEKCAQYWP--SDGSVS 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 375 FGSFHITcMKVDSKADPlFTITKLKVQKVGGNllDAEFDEELFLEHWQwdwqylgDVHWP---------FRVLRKARQLS 445
Cdd:cd14623    93 YGDITIE-LKKEEECES-YTVRDLLVTNTREN--KSRQIRQFHFHGWP-------EVGIPsdgkgminiIAAVQKQQQQS 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1845972907 446 T--PTIVQCIDGCSKSGTLVSIETALMHfIRGSPITKslILQSCVFVRLQRRLSVSSVLLYLFIYRVI 511
Cdd:cd14623   162 GnhPITVHCSAGAGRTGTFCALSTVLER-VKAEGILD--VFQTVKSLRLQRPHMVQTLEQYEFCYKVV 226
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
297-511 9.08e-13

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: 67.29  E-value: 9.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 297 FIHANYVKGGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSavdsstlgpLDSANRNHCPYYWPraENESLRFG 376
Cdd:cd14552     1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTE---------IKERSQNKCAQYWP--EDGSVSSG 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 377 SFHITCMKVDSKADplFTITKLKVQKVGGNllDAEFDEELFLEHWQwdwqylgDVHWP---------FRVLRKARQLST- 446
Cdd:cd14552    70 DITVELKDQTDYED--YTLRDFLVTKGKGG--STRTVRQFHFHGWP-------EVGIPdngkgmidlIAAVQKQQQQSGn 138
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1845972907 447 -PTIVQCIDGCSKSGTLVSIETALMHfIRGSPITKslILQSCVFVRLQRRLSVSSVLLYLFIYRVI 511
Cdd:cd14552   139 hPITVHCSAGAGRTGTFCALSTVLER-VKAEGVLD--VFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
297-508 9.48e-13

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: 67.41  E-value: 9.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 297 FIHANYVKG-GPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLnsavdsstLGPLDSANRN-HCpyYWPRAENESLR 374
Cdd:cd14539     1 YINASLIEDlTPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVML--------VSEQENEKQKvHR--YWPTERGQALV 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 375 FGsfHITCMKVDSKADPLFTITKLKVQKvggnlldAEFDEELFLEHWQW-DW-------------QYLGDVHWPFRVLRK 440
Cdd:cd14539    71 YG--AITVSLQSVRTTPTHVERIISIQH-------KDTRLSRSVVHLQFtTWpelglpdspnpllRFIEEVHSHYLQQRS 141
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1845972907 441 arqLSTPTIVQCIDGCSKSGTLVSIETALMHFIRGSPITKslILQSCVFVRLQRRLSVSSVLLYLFIY 508
Cdd:cd14539   142 ---LQTPIVVHCSSGVGRTGAFCLLYAAVQEIEAGNGIPD--LPQLVRKMRQQRKYMLQEKEHLKFCY 204
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
295-518 2.23e-12

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: 67.83  E-value: 2.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 295 TDFIHANYVKGGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSavdsstlgpLDSANRNHCPYYWPraENESLR 374
Cdd:cd14628    80 SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTK---------LREMGREKCHQYWP--AERSAR 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 375 FGSFhitcmKVDSKAD---PLFTITKLKVQkvggnllDAEFDEELFLEHWQW-DW-------------QYLGDVHwpfrv 437
Cdd:cd14628   149 YQYF-----VVDPMAEynmPQYILREFKVT-------DARDGQSRTVRQFQFtDWpeqgvpksgegfiDFIGQVH----- 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 438 lRKARQLST--PTIVQCIDGCSKSGTLVSIETALMHfIRGSPITKslILQSCVFVRLQRRLSVSSVLLYLFIYRVILRWI 515
Cdd:cd14628   212 -KTKEQFGQdgPISVHCSAGVGRTGVFITLSIVLER-MRYEGVVD--IFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYL 287

                  ...
gi 1845972907 516 EPY 518
Cdd:cd14628   288 GSF 290
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
296-470 3.07e-12

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: 66.91  E-value: 3.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 296 DFIHANYVKGGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSAVDSSTLgpldsanrnHCPYYWPRAENESLRF 375
Cdd:cd14607    49 DYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKDSV---------KCAQYWPTDEEEVLSF 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 376 GS--FHITCMKVDSKAdpLFTITKLKVQkvggnllDAEFDEELFLEHWQW-DWQYLGDVHWP-------FRVlRKARQLS 445
Cdd:cd14607   120 KEtgFSVKLLSEDVKS--YYTVHLLQLE-------NINSGETRTISHFHYtTWPDFGVPESPasflnflFKV-RESGSLS 189
                         170       180
                  ....*....|....*....|....*...
gi 1845972907 446 T---PTIVQCIDGCSKSGTLVSIETALM 470
Cdd:cd14607   190 PehgPAVVHCSAGIGRSGTFSLVDTCLV 217
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
296-512 4.88e-12

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: 66.01  E-value: 4.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 296 DFIHANYVKGgPLLNT---FICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSAVDSSTLgpldsanrnHCPYYWPRAENES 372
Cdd:cd14597    27 GYINASFIKM-PVGDEefvYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQEVEGGKI---------KCQRYWPEILGKT 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 373 LRFGS-FHITCMKVDSKADplFTITKLKVQkvggnllDAEFDEELFLEHWQWD-WQYLGDVHWPFRVLR-----KARQLS 445
Cdd:cd14597    97 TMVDNrLQLTLVRMQQLKN--FVIRVLELE-------DIQTREVRHITHLNFTaWPDHDTPSQPEQLLTfisymRHIHKS 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1845972907 446 TPTIVQCIDGCSKSGTLVSIETALMHFIRGSPITKSLILQScvfVRLQRRLSVSSVLLYLFIYRVIL 512
Cdd:cd14597   168 GPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRT---MRLQRHGMVQTEDQYIFCYQVIL 231
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
295-515 7.08e-12

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: 66.29  E-value: 7.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 295 TDFIHANYVKGGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSavdsstlgpLDSANRNHCPYYWPraENESLR 374
Cdd:cd14627    81 SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTK---------LREMGREKCHQYWP--AERSAR 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 375 FGSFhitcmKVDSKAD---PLFTITKLKVQkvggnllDAEFDEELFLEHWQW-DW-------------QYLGDVHwpfrv 437
Cdd:cd14627   150 YQYF-----VVDPMAEynmPQYILREFKVT-------DARDGQSRTVRQFQFtDWpeqgvpksgegfiDFIGQVH----- 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 438 lRKARQLST--PTIVQCIDGCSKSGTLVSIETALMHfIRGSPITKslILQSCVFVRLQRRLSVSSVLLYLFIYRVILRWI 515
Cdd:cd14627   213 -KTKEQFGQdgPISVHCSAGVGRTGVFITLSIVLER-MRYEGVVD--IFQTVKMLRTQRPAMVQTEDEYQFCYQAALEYL 288
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
312-512 7.33e-12

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: 64.66  E-value: 7.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 312 FICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSaVDSSTLgpldsanrnhCPYYWPraENESLRFGSFHITCMKVDSKADP 391
Cdd:cd14634    16 FIVTQHPLPNTVADFWRLVFDYNCSSVVMLNE-MDAAQL----------CMQYWP--EKTSCCYGPIQVEFVSADIDEDI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 392 LFTITKLkvqkvgGNLLDAEfDEELFLEHwqwdWQYLGdvhWP-FR--------VLRKARQLST----------PTIVQC 452
Cdd:cd14634    83 ISRIFRI------CNMARPQ-DGYRIVQH----LQYIG---WPaYRdtppskrsILKVVRRLEKwqeqydgregRTVVHC 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 453 IDGCSKSGTLVSIeTALMHFIRGSPITKslILQSCVFVRLQRRLSVSSVLLYLFIYRVIL 512
Cdd:cd14634   149 LNGGGRSGTFCAI-CSVCEMIQQQNIID--VFHTVKTLRNNKSNMVETLEQYKFVYEVAL 205
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
297-512 1.07e-11

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: 64.38  E-value: 1.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 297 FIHANYV--KGGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSAVDSStlgpldsanRNHCPYYWPRAENESLR 374
Cdd:cd14596     1 YINASYItmPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERG---------KVKCHRYWPETLQEPME 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 375 FGSFHI---TCMKVDSkadplFTITKLKVqkvggnlLDAEFDEELFLEHWQW-DWQYLGDVHWP---FRVLRKARQ--LS 445
Cdd:cd14596    72 LENYQLrleNYQALQY-----FIIRIIKL-------VEKETGENRLIKHLQFtTWPDHGTPQSSdqlVKFICYMRKvhNT 139
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1845972907 446 TPTIVQCIDGCSKSGTLVSIETALmhfirgspitkSLILQSCVF--------VRLQRRLSVSSVLLYLFIYRVIL 512
Cdd:cd14596   140 GPIVVHCSAGIGRAGVLICVDVLL-----------SLIEKDLSFnikdivreMRQQRYGMIQTKDQYLFCYKVVL 203
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
297-512 1.69e-11

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: 63.86  E-value: 1.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 297 FIHANYVKGGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNsavDSSTLGpldsanRNHCpYYWPRAEnESLRFG 376
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLP---DGQNMA------EDEF-VYWPNKD-EPINCE 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 377 SFHITCMKVDSKAdpLFTITKLKVQKVggnLLDAEFDEE-LFLEHWQWDwqylgdvHWP---------FRVLRKARQLST 446
Cdd:cd17669    70 TFKVTLIAEEHKC--LSNEEKLIIQDF---ILEATQDDYvLEVRHFQCP-------KWPnpdspisktFELISIIKEEAA 137
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1845972907 447 ----PTIVQCIDGCSKSGTLVSIeTALMHFIRGSpitKSL-ILQSCVFVRLQRRLSVSSVLLYLFIYRVIL 512
Cdd:cd17669   138 nrdgPMIVHDEHGGVTAGTFCAL-TTLMHQLEKE---NSVdVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
297-386 2.49e-11

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: 63.11  E-value: 2.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 297 FIHANYVKGGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLnsavdsstlgpLDSANRNHCPYYWPrAENESLRFG 376
Cdd:cd14550     1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVML-----------TDNELNEDEPIYWP-TKEKPLECE 68
                          90
                  ....*....|
gi 1845972907 377 SFHITCMKVD 386
Cdd:cd14550    69 TFKVTLSGED 78
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
298-366 3.45e-11

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 63.96  E-value: 3.45e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1845972907 298 IHANYVKGGPLlNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSAVDsstlgplDSANRNHCPYYWP 366
Cdd:COG5599    66 LNANYIQVIGN-HRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDE-------ISKPKVKMPVYFR 126
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
295-512 4.51e-11

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: 63.98  E-value: 4.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 295 TDFIHANYVKGGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSavdsstlgpLDSANRNHCPYYWPRAENESlr 374
Cdd:cd14624    75 SDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTK---------LEERSRVKCDQYWPSRGTET-- 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 375 FGSFHITCMkvDSKADPLFTITKLKVQKVGGNlldaefdEELFLEHWQWD-WQYLGDVHWPFRVLRKARQLST------- 446
Cdd:cd14624   144 YGLIQVTLL--DTVELATYCVRTFALYKNGSS-------EKREVRQFQFTaWPDHGVPEHPTPFLAFLRRVKTcnppdag 214
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1845972907 447 PTIVQCIDGCSKSGTLVSIEtALMHFIRGSPITKslILQSCVFVRLQRRLSVSSVLLYLFIYRVIL 512
Cdd:cd14624   215 PMVVHCSAGVGRTGCFIVID-AMLERIKHEKTVD--IYGHVTLMRAQRNYMVQTEDQYIFIHDALL 277
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
299-476 4.97e-11

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: 63.54  E-value: 4.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 299 HANYVKGGPLLN------TFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNsavdsstlgPLDSANRNHCPYYWPRAENE- 371
Cdd:cd14610    71 HSDYINASPIMDhdprnpAYIATQGPLPATVADFWQMVWESGCVVIVMLT---------PLAENGVKQCYHYWPDEGSNl 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 372 ----SLRFGSFHITCmkvdskADPLFTITKLKvqkvggNLLDAEFDEELFLEHWQWDWQYLGDVHWPFRVLRKA-----R 442
Cdd:cd14610   142 yhiyEVNLVSEHIWC------EDFLVRSFYLK------NLQTNETRTVTQFHFLSWNDQGVPASTRSLLDFRRKvnkcyR 209
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1845972907 443 QLSTPTIVQCIDGCSKSGTLVSIETALMHFIRGS 476
Cdd:cd14610   210 GRSCPIIVHCSDGAGRSGTYILIDMVLNKMAKGA 243
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
295-518 6.94e-11

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: 63.21  E-value: 6.94e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 295 TDFIHANYVKGGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSavdsstlgpLDSANRNHCPYYWPraENESLR 374
Cdd:cd14629    81 SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTK---------LREMGREKCHQYWP--AERSAR 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 375 FGSFhitcmKVDSKAD---PLFTITKLKVQkvggnllDAEFDEELFLEHWQW-DW-------------QYLGDVHwpfrv 437
Cdd:cd14629   150 YQYF-----VVDPMAEynmPQYILREFKVT-------DARDGQSRTIRQFQFtDWpeqgvpktgegfiDFIGQVH----- 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 438 lRKARQLST--PTIVQCIDGCSKSGTLVSIETALMHfIRGSPITKslILQSCVFVRLQRRLSVSSVLLYLFIYRVILRWI 515
Cdd:cd14629   213 -KTKEQFGQdgPITVHCSAGVGRTGVFITLSIVLER-MRYEGVVD--MFQTVKTLRTQRPAMVQTEDQYQLCYRAALEYL 288

                  ...
gi 1845972907 516 EPY 518
Cdd:cd14629   289 GSF 291
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
295-475 1.90e-10

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: 61.98  E-value: 1.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 295 TDFIHAN-YVKGGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNsavdsstlgPLDSANRNHCPYYWPRaENESL 373
Cdd:cd14609    70 SDYINASpIIEHDPRMPAYIATQGPLSHTIADFWQMVWENGCTVIVMLT---------PLVEDGVKQCDRYWPD-EGSSL 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 374 ------RFGSFHITCMKVDSKAdplFTITKLKVQKVggnlldAEFDEELFLehwQWDWQYLGDVHWPFRVLRKA-----R 442
Cdd:cd14609   140 yhiyevNLVSEHIWCEDFLVRS---FYLKNVQTQET------RTLTQFHFL---SWPAEGIPSSTRPLLDFRRKvnkcyR 207
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1845972907 443 QLSTPTIVQCIDGCSKSGTLVSIETALMHFIRG 475
Cdd:cd14609   208 GRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKG 240
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
312-398 5.99e-10

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: 59.27  E-value: 5.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 312 FICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSavdsstlgpLDSAnrNHCPYYWPraENESLRFGSFHITCMKVDSKADP 391
Cdd:cd14636    16 FIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNE---------VDLA--QGCPQYWP--EEGMLRYGPIQVECMSCSMDCDV 82

                  ....*..
gi 1845972907 392 LFTITKL 398
Cdd:cd14636    83 ISRIFRI 89
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
295-512 7.69e-10

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: 60.06  E-value: 7.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 295 TDFIHANYVKGGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSAVDsstlgpldsANRNHCPYYWPraeNESLR 374
Cdd:cd14633    68 SDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVE---------VGRVKCCKYWP---DDTEI 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 375 FGSFHITCMKVDSKADplFTITKLKVQKVGGNlldaEFDEELFLEHWQW-----DWQYLGDVHWPFRVLRKARQLSTPTI 449
Cdd:cd14633   136 YKDIKVTLIETELLAE--YVIRTFAVEKRGVH----EIREIRQFHFTGWpdhgvPYHATGLLGFVRQVKSKSPPNAGPLV 209
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1845972907 450 VQCIDGCSKSGTLVSIETALMHFIRGSPITksliLQSCVFVRLQRRLS-VSSVLLYLFIYRVIL 512
Cdd:cd14633   210 VHCSAGAGRTGCFIVIDIMLDMAEREGVVD----IYNCVRELRSRRVNmVQTEEQYVFIHDAIL 269
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
310-465 8.29e-10

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: 58.93  E-value: 8.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 310 NTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSaVDSSTLgpldsanrnhCPYYWPraENESLRFGSFHITCMKVDSKA 389
Cdd:cd14635    14 SAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLND-VDPAQL----------CPQYWP--ENGVHRHGPIQVEFVSADLEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 390 DPLFTITKL--KVQKVGGNLLDAEFdeelflehwqwdwQYLGdvhWPF---------RVLRKARQLST----------PT 448
Cdd:cd14635    81 DIISRIFRIynAARPQDGYRMVQQF-------------QFLG---WPMyrdtpvskrSFLKLIRQVDKwqeeynggegRT 144
                         170
                  ....*....|....*..
gi 1845972907 449 IVQCIDGCSKSGTLVSI 465
Cdd:cd14635   145 VVHCLNGGGRSGTFCAI 161
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
312-475 3.46e-09

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: 57.07  E-value: 3.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 312 FICAQAPLKNTQEDFWRMVFQEKCQFIVMLNsavdsstlgPLDSANRNHCPYYWPraENESLRFGSF-------HITCmk 384
Cdd:cd14546    17 YIATQGPLPHTIADFWQMIWEQGCVVIVMLT---------RLQENGVKQCARYWP--EEGSEVYHIYevhlvseHIWC-- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 385 vdskADPLFTITKLKVQKVGGNLLDAEFDeelFLEhwqwdWQYLGDVHWP-----FR--VLRKARQLSTPTIVQCIDGCS 457
Cdd:cd14546    84 ----DDYLVRSFYLKNLQTSETRTVTQFH---FLS-----WPDEGIPASAkplleFRrkVNKSYRGRSCPIVVHCSDGAG 151
                         170
                  ....*....|....*...
gi 1845972907 458 KSGTLVSIETALMHFIRG 475
Cdd:cd14546   152 RTGTYILIDMVLNRMAKG 169
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
297-386 3.51e-09

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: 57.00  E-value: 3.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 297 FIHANYVKGGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNsavDSSTLGPLDSAnrnhcpyYWPRAEnESLRFG 376
Cdd:cd17670     1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLP---DNQGLAEDEFV-------YWPSRE-ESMNCE 69
                          90
                  ....*....|
gi 1845972907 377 SFHITCMKVD 386
Cdd:cd17670    70 AFTVTLISKD 79
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
287-366 3.68e-09

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: 57.24  E-value: 3.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 287 TAKSTYGTTDFIHANYVKG-GPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSavdsstlgpLDSANRNhCPYYW 365
Cdd:cd14611    20 PKNSNDSLSTYINANYIRGyGGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITK---------LKEKNEK-CVLYW 89

                  .
gi 1845972907 366 P 366
Cdd:cd14611    90 P 90
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
312-474 2.92e-08

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: 54.14  E-value: 2.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 312 FICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSAVDSSTLGPldsanrnhCPYYWPraENESLRFGSFHITCMKVDSKADp 391
Cdd:cd14637    16 FIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAWP--------CLQYWP--EPGLQQYGPMEVEFVSGSADED- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 392 lfTITKL-KVQKVGgnlldAEFDEELFLEHWQW-DWQYLGDV--------HWPFRVLRKARQLST-PTIVQCIDGCSKSG 460
Cdd:cd14637    85 --IVTRLfRVQNIT-----RLQEGHLMVRHFQFlRWSAYRDTpdskkaflHLLASVEKWQRESGEgRTVVHCLNGGGRSG 157
                         170
                  ....*....|....
gi 1845972907 461 TLVSiETALMHFIR 474
Cdd:cd14637   158 TYCA-SAMILEMIR 170
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
300-511 4.64e-07

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 51.89  E-value: 4.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 300 ANYVKGGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSAVDsstlgpldsanRNHCPYYWPRAENESLRFGSFH 379
Cdd:PHA02740   81 ARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHAD-----------KKCFNQFWSLKEGCVITSDKFQ 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845972907 380 ITCMKVDSKadPLFTITKLkvqkvggnLLDAEFDEELFLEHWQWD-WQYLGDVHWP-------FRV------LRKARQLS 445
Cdd:PHA02740  150 IETLEIIIK--PHFNLTLL--------SLTDKFGQAQKISHFQYTaWPADGFSHDPdafidffCNIddlcadLEKHKADG 219
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1845972907 446 T--PTIVQCIDGCSKSGTLVSIETALMHFIRgspiTKSLILQSCV-FVRLQRRLSVSSVLLYLFIYRVI 511
Cdd:PHA02740  220 KiaPIIIDCIDGISSSAVFCVFDICATEFDK----TGMLSIANALkKVRQKKYGCMNCLDDYVFCYHLI 284
 
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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