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Conserved domains on  [gi|1831510059|ref|NP_001368044|]
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Tyrosine-protein phosphatase domain-containing protein [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;
272-512 1.05e-44

Protein tyrosine phosphatase, catalytic domain;


:

Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 159.75  E-value: 1.05e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059  272 TAMSAGNPKLCRDPKVQAWDST-----SYLVDDTHFIHASTVTAP--GKEYIgkaiICQAPFddkekghPDTRESFWRMV 344
Cdd:smart00194  21 VAAFPENRDKNRYKDVLPYDHTrvklkPPPGEGSDYINASYIDGPngPKAYI----ATQGPL-------PSTVEDFWRMV 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059  345 WDTRATYVVMCCQIMENGVQKCGRYFPDETGATENYGFAEVQLLEKHEMlnGHLLTRKIELTSGtwkhsdDDPPIRTITH 424
Cdd:smart00194  90 WEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKV--DDYTIRTLEVTNT------GCSETRTVTH 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059  425 FQFLKWKEGEGLEGEMSMDAF-NYVNHRTRNNLDPIIVHSSLGTGRACAFVGAEYMFQMINTKKcgTARFFQV--DFRTK 501
Cdd:smart00194 162 YHYTNWPDHGVPESPESILDLiRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGK--EVDIFEIvkELRSQ 239

                          250
                   ....*....|.
gi 1831510059  502 RLGALQNGKQL 512
Cdd:smart00194 240 RPGMVQTEEQY 250
 
Name Accession Description Interval E-value
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
272-512 1.05e-44

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 159.75  E-value: 1.05e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059  272 TAMSAGNPKLCRDPKVQAWDST-----SYLVDDTHFIHASTVTAP--GKEYIgkaiICQAPFddkekghPDTRESFWRMV 344
Cdd:smart00194  21 VAAFPENRDKNRYKDVLPYDHTrvklkPPPGEGSDYINASYIDGPngPKAYI----ATQGPL-------PSTVEDFWRMV 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059  345 WDTRATYVVMCCQIMENGVQKCGRYFPDETGATENYGFAEVQLLEKHEMlnGHLLTRKIELTSGtwkhsdDDPPIRTITH 424
Cdd:smart00194  90 WEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKV--DDYTIRTLEVTNT------GCSETRTVTH 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059  425 FQFLKWKEGEGLEGEMSMDAF-NYVNHRTRNNLDPIIVHSSLGTGRACAFVGAEYMFQMINTKKcgTARFFQV--DFRTK 501
Cdd:smart00194 162 YHYTNWPDHGVPESPESILDLiRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGK--EVDIFEIvkELRSQ 239

                          250
                   ....*....|.
gi 1831510059  502 RLGALQNGKQL 512
Cdd:smart00194 240 RPGMVQTEEQY 250
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
278-515 1.07e-44

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 158.94  E-value: 1.07e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 278 NPKLCRDPKVQAWDST----SYLVDDTHFIHASTVTAPGKEYigKAIICQAPFddkekghPDTRESFWRMVWDTRATYVV 353
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTrvklTGDPGPSDYINASYIDGYKKPK--KYIATQGPL-------PNTVEDFWRMVWEEKVTIIV 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 354 MCCQIMENGVQKCGRYFPDETGATENYGFAEVQlLEKHEMLNGHLLTRKIELTSGTWKHSdddppiRTITHFQFLKWKEG 433
Cdd:pfam00102  72 MLTELEEKGREKCAQYWPEEEGESLEYGDFTVT-LKKEKEDEKDYTVRTLEVSNGGSEET------RTVKHFHYTGWPDH 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 434 EGLEGEMSM-DAFNYVNHRTRNNLD-PIIVHSSLGTGRACAFVGAEYMFQMIntKKCGTARFFQV--DFRTKRLGALQNG 509
Cdd:pfam00102 145 GVPESPNSLlDLLRKVRKSSLDGRSgPIVVHCSAGIGRTGTFIAIDIALQQL--EAEGEVDIFQIvkELRSQRPGMVQTL 222


                  ....*.
gi 1831510059 510 KQLFWV 515
Cdd:pfam00102 223 EQYIFL 228
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 302-512 2.11e-39

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: 143.19  E-value: 2.11e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 302 FIHASTVTAPGKEYigKAIICQAPfddkekgHPDTRESFWRMVWDTRATYVVMCCQIMENGVQKCGRYFPDETGATENYG 381
Cdd:cd00047     1 YINASYIDGYRGPK--EYIATQGP-------LPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPLEYG 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 382 FAEVQLLEKHEMlnGHLLTRKIELTSGTWKHSdddppiRTITHFQFLKWKEGEGLEGEMSMDAF-NYVNHRTRNNLDPII 460
Cdd:cd00047    72 DITVTLVSEEEL--SDYTIRTLELSPKGCSES------REVTHLHYTGWPDHGVPSSPEDLLALvRRVRKEARKPNGPIV 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1831510059 461 VHSSLGTGRACAFVGAEYMFQMINTKKCgtarffqVDF-------RTKRLGALQNGKQL 512
Cdd:cd00047   144 VHCSAGVGRTGTFIAIDILLERLEAEGE-------VDVfeivkalRKQRPGMVQTLEQY 195
PHA02738 PHA02738
hypothetical protein; Provisional
 302-473 7.03e-12

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 66.87  E-value: 7.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 302 FIHASTVTapGKEYIGKAIICQAPFDDkekghpdTRESFWRMVWDTRATYVVMCCQIMENGVQKCGRYFPDETGATENYG 381
Cdd:PHA02738   77 YINANYVD--GFEYKKKFICGQAPTRQ-------TCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDVEQGSIRFG 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 382 FAEVQL--LEKHEmlngHLLTRKIELTSGTwkhsdddPPIRTITHFQFLKWKEGEGLEGEMSMDAF-------------- 445
Cdd:PHA02738  148 KFKITTtqVETHP----HYVKSTLLLTDGT-------SATQTVTHFNFTAWPDHDVPKNTSEFLNFvlevrqcqkelaqe 216

                         170       180
                  ....*....|....*....|....*...
gi 1831510059 446 NYVNHRTRNNLDPIIVHSSLGTGRACAF 473
Cdd:PHA02738  217 SLQIGHNRLQPPPIVVHCNAGLGRTPCY 244
 
Name Accession Description Interval E-value
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
272-512 1.05e-44

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 159.75  E-value: 1.05e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059  272 TAMSAGNPKLCRDPKVQAWDST-----SYLVDDTHFIHASTVTAP--GKEYIgkaiICQAPFddkekghPDTRESFWRMV 344
Cdd:smart00194  21 VAAFPENRDKNRYKDVLPYDHTrvklkPPPGEGSDYINASYIDGPngPKAYI----ATQGPL-------PSTVEDFWRMV 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059  345 WDTRATYVVMCCQIMENGVQKCGRYFPDETGATENYGFAEVQLLEKHEMlnGHLLTRKIELTSGtwkhsdDDPPIRTITH 424
Cdd:smart00194  90 WEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKV--DDYTIRTLEVTNT------GCSETRTVTH 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059  425 FQFLKWKEGEGLEGEMSMDAF-NYVNHRTRNNLDPIIVHSSLGTGRACAFVGAEYMFQMINTKKcgTARFFQV--DFRTK 501
Cdd:smart00194 162 YHYTNWPDHGVPESPESILDLiRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGK--EVDIFEIvkELRSQ 239

                          250
                   ....*....|.
gi 1831510059  502 RLGALQNGKQL 512
Cdd:smart00194 240 RPGMVQTEEQY 250
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
278-515 1.07e-44

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 158.94  E-value: 1.07e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 278 NPKLCRDPKVQAWDST----SYLVDDTHFIHASTVTAPGKEYigKAIICQAPFddkekghPDTRESFWRMVWDTRATYVV 353
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTrvklTGDPGPSDYINASYIDGYKKPK--KYIATQGPL-------PNTVEDFWRMVWEEKVTIIV 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 354 MCCQIMENGVQKCGRYFPDETGATENYGFAEVQlLEKHEMLNGHLLTRKIELTSGTWKHSdddppiRTITHFQFLKWKEG 433
Cdd:pfam00102  72 MLTELEEKGREKCAQYWPEEEGESLEYGDFTVT-LKKEKEDEKDYTVRTLEVSNGGSEET------RTVKHFHYTGWPDH 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 434 EGLEGEMSM-DAFNYVNHRTRNNLD-PIIVHSSLGTGRACAFVGAEYMFQMIntKKCGTARFFQV--DFRTKRLGALQNG 509
Cdd:pfam00102 145 GVPESPNSLlDLLRKVRKSSLDGRSgPIVVHCSAGIGRTGTFIAIDIALQQL--EAEGEVDIFQIvkELRSQRPGMVQTL 222


                  ....*.
gi 1831510059 510 KQLFWV 515
Cdd:pfam00102 223 EQYIFL 228
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 302-512 2.11e-39

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: 143.19  E-value: 2.11e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 302 FIHASTVTAPGKEYigKAIICQAPfddkekgHPDTRESFWRMVWDTRATYVVMCCQIMENGVQKCGRYFPDETGATENYG 381
Cdd:cd00047     1 YINASYIDGYRGPK--EYIATQGP-------LPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPLEYG 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 382 FAEVQLLEKHEMlnGHLLTRKIELTSGTWKHSdddppiRTITHFQFLKWKEGEGLEGEMSMDAF-NYVNHRTRNNLDPII 460
Cdd:cd00047    72 DITVTLVSEEEL--SDYTIRTLELSPKGCSES------REVTHLHYTGWPDHGVPSSPEDLLALvRRVRKEARKPNGPIV 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1831510059 461 VHSSLGTGRACAFVGAEYMFQMINTKKCgtarffqVDF-------RTKRLGALQNGKQL 512
Cdd:cd00047   144 VHCSAGVGRTGTFIAIDILLERLEAEGE-------VDVfeivkalRKQRPGMVQTLEQY 195
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 303-515 3.12e-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: 98.09  E-value: 3.12e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 303 IHASTVTAPGKEyIGKAIICQAPFddkekghPDTRESFWRMVWDTRATYVVMCCQIMENGVQKCGRYFPDETGaTENYGF 382
Cdd:cd18533     2 INASYITLPGTS-SKRYIATQGPL-------PATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEY-EGEYGD 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 383 AEVQLLEKHEMLNGHLLTRKIELTSgtwkhsdDDPPIRTITHFQFLKWKEGEGLEGEMS----MDAFNYVNhRTRNNLDP 458
Cdd:cd18533    73 LTVELVSEEENDDGGFIVREFELSK-------EDGKVKKVYHIQYKSWPDFGVPDSPEDlltlIKLKRELN-DSASLDPP 144

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1831510059 459 IIVHSSLGTGRACAFVGAEYMFQMINTKKCGTARF-------FQV--DFRTKRLGALQNGKQLFWV 515
Cdd:cd18533   145 IIVHCSAGVGRTGTFIALDSLLDELKRGLSDSQDLedsedpvYEIvnQLRKQRMSMVQTLRQYIFL 210
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 313-502 1.97e-21

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: 92.80  E-value: 1.97e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 313 KEYIGkaiiCQAPFddkekghPDTRESFWRMVWDTRATYVVMCCQIMENGVQKCGRYFPDEtgATENYGFAEVQLLEKHE 392
Cdd:cd14549    14 RAYIA----TQGPL-------PSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKE--GTETYGNIQVTLLSTEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 393 MlnGHLLTRKIELTSGTWKHSDDDPPIRTITHFQFLKWKEgEGLEgEMSMDAFNYVNHRTRNN---LDPIIVHSSLGTGR 469
Cdd:cd14549    81 L--ATYTVRTFSLKNLKLKKVKGRSSERVVYQYHYTQWPD-HGVP-DYTLPVLSFVRKSSAANppgAGPIVVHCSAGVGR 156

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1831510059 470 ACAFVGAEYMFQMINTKKCGTARFFQVDFRTKR 502
Cdd:cd14549   157 TGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQR 189
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 297-511 1.07e-20

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: 91.43  E-value: 1.07e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 297 VDDTHFIHASTVTapGKEYIGKAIICQAPFddkekghPDTRESFWRMVWDTRATYVVMCCQIMENGVQKCGRYFPDETGA 376
Cdd:cd14554    31 VEGSDYINASFID--GYRQRGAYIATQGPL-------AETTEDFWRMLWEHNSTIIVMLTKLREMGREKCHQYWPAERSA 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 377 teNYGFAEVQLLEKHEMLNGHLltRKIELTSGtwkhsdDDPPIRTITHFQFLKWKE-GEGLEGEMSMDAFNYVnHRTRNN 455
Cdd:cd14554   102 --RYQYFVVDPMAEYNMPQYIL--REFKVTDA------RDGQSRTVRQFQFTDWPEqGVPKSGEGFIDFIGQV-HKTKEQ 170

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1831510059 456 LD---PIIVHSSLGTGRACAFV------------GAEYMFQMINTkkcgtarffqvdFRTKRLGALQNGKQ 511
Cdd:cd14554   171 FGqegPITVHCSAGVGRTGVFItlsivlermryeGVVDVFQTVKL------------LRTQRPAMVQTEDQ 229
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 302-483 2.18e-20

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: 89.70  E-value: 2.18e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 302 FIHASTVTA--PGKEYIGKAIICQAPFddkekghPDTRESFWRMVWDTRATYVVMCCQIMENGVQKCGRYFPDEtGATEN 379
Cdd:cd14541     2 YINANYVNMeiPGSGIVNRYIAAQGPL-------PNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDL-GETMQ 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 380 YGFAEVQLLEkhEMLNGHLLTRKIELTSGTWKHSdddppiRTITHFQFLKWKEgEGLEGEmSMDAFNYVnHRTRNN---- 455
Cdd:cd14541    74 FGNLQITCVS--EEVTPSFAFREFILTNTNTGEE------RHITQMQYLAWPD-HGVPDD-SSDFLDFV-KRVRQNrvgm 142

                         170       180
                  ....*....|....*....|....*...
gi 1831510059 456 LDPIIVHSSLGTGRACAFVGAEYMFQMI 483
Cdd:cd14541   143 VEPTVVHCSAGIGRTGVLITMETAMCLI 170
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 302-487 2.70e-20

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: 89.72  E-value: 2.70e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 302 FIHASTVtaPG----KEYIgkaiICQAPFddkekghPDTRESFWRMVWDTRATYVVMCCQIMENGVQKCGRYFPDETGAT 377
Cdd:cd14548    26 YINANYI--PGynspREFI----ATQGPL-------PGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVKCDHYWPFDQDPV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 378 EnYGFAEVQLLEKHEMLNGHLLTRKIELTSGTwkhsdddppiRTITHFQFLKWKEGEGLEGEMSMDAFNY-VNHRTRNNL 456
Cdd:cd14548    93 Y-YGDITVTMLSESVLPDWTIREFKLERGDEV----------RSVRQFHFTAWPDHGVPEAPDSLLRFVRlVRDYIKQEK 161

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1831510059 457 DPIIVHSSLGTGRACAFVGAEYMFQMINTKK 487
Cdd:cd14548   162 GPTIVHCSAGVGRTGTFIALDRLLQQIESED 192
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 298-473 6.32e-20

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: 90.12  E-value: 6.32e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 298 DDTHFIHASTVTA--PGKEYIGKaiicQAPFddkekghPDTRESFWRMVWDTRATYVVMCCQIMENGVQKCGRYFPDETG 375
Cdd:cd14543    55 ERTDYINANFMDGykQKNAYIAT----QGPL-------PKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEG 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 376 ATENYGFAEVQLLEKHEMlnGHLLTRKIELtsgtwkHSDDDPPIRTITHFQFLKWKEGEGLEGEMSMDAF-----NYVNH 450
Cdd:cd14543   124 SSLRYGDLTVTNLSVENK--EHYKKTTLEI------HNTETDESRQVTHFQFTSWPDFGVPSSAAALLDFlgevrQQQAL 195

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1831510059 451 RTRNNLD---------PIIVHSSLGTGRACAF 473
Cdd:cd14543   196 AVKAMGDrwkghppgpPIVVHCSAGIGRTGTF 227
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 334-474 5.11e-19

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: 85.96  E-value: 5.11e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 334 PDTRESFWRMVWDTRATYVVMCCQIMENGVQKCGRYFPDETGatENYGFAEVQLLEKHeMLNGHLLTRKIEL----TSGT 409
Cdd:cd14546    25 PHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGS--EVYHIYEVHLVSEH-IWCDDYLVRSFYLknlqTSET 101

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1831510059 410 wkhsdddppiRTITHFQFLKWKEGEGLEGEMSMDAFNY-VNHRTRNNLDPIIVHSSLGTGRACAFV 474
Cdd:cd14546   102 ----------RTVTQFHFLSWPDEGIPASAKPLLEFRRkVNKSYRGRSCPIVVHCSDGAGRTGTYI 157
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 299-512 5.30e-19

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: 86.29  E-value: 5.30e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 299 DTHFIHASTVTAP--GKEYIgkaiICQAPFddkekghPDTRESFWRMVWDTRATYVVMCCQIMENGVQKCGRYFPDETGA 376
Cdd:cd14545    23 DNDYINASLVEVEeaKRSYI----LTQGPL-------PNTSGHFWQMVWEQNSKAVIMLNKLMEKGQIKCAQYWPQGEGN 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 377 T---ENYGFaEVQLLEkhEMLNGHLLTRKIELTSGTWKHSdddppiRTITHFQFLKWKEGEGLEgemSMDAFNYVNHRTR 453
Cdd:cd14545    92 AmifEDTGL-KVTLLS--EEDKSYYTVRTLELENLKTQET------REVLHFHYTTWPDFGVPE---SPAAFLNFLQKVR 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1831510059 454 N------NLDPIIVHSSLGTGRACAFVGAEYMFQMINTKKCGTARFFQV--DFRTKRLGALQNGKQL 512
Cdd:cd14545   160 EsgslssDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPSSVDVKKVllEMRKYRMGLIQTPDQL 226
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 309-486 8.36e-19

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: 86.36  E-value: 8.36e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 309 TAPGKEYIGKAIIcqaPFDDKEKGHPDTRES--------------FWRMVWDTRATYVVMCCQIMENGVQKCGRYFPDEt 374
Cdd:cd14544    26 NVPGSDYINANYI---RNENEGPTTDENAKTyiatqgclentvsdFWSMVWQENSRVIVMTTKEVERGKNKCVRYWPDE- 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 375 GATENYGFAEVQLLEKHEMLNGHLltRKIELTSGtwkhsDDDPPIRTITHFQFLKWKE-GEGLEGEMSMDAFNYVNHR-- 451
Cdd:cd14544   102 GMQKQYGPYRVQNVSEHDTTDYTL--RELQVSKL-----DQGDPIREIWHYQYLSWPDhGVPSDPGGVLNFLEDVNQRqe 174

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1831510059 452 TRNNLDPIIVHSSLGTGRACAFVGAEYMFQMINTK 486
Cdd:cd14544   175 SLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRK 209
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 302-483 1.34e-18

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: 84.73  E-value: 1.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 302 FIHASTVTAP-GKEYIgKAIICQAPFddkekghPDTRESFWRMVWDTRATYVVMCCQIMENGVQKCGRYFPDETGATE-N 379
Cdd:cd14538     1 YINASHIRIPvGGDTY-HYIACQGPL-------PNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNKPLiC 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 380 YGFAEVQlLEKHEMLNGhLLTRKIELT---SGTwkhsdddppIRTITHFQFLKWKEGEGLEGEMSMDAFNYVNHRTRNNL 456
Cdd:cd14538    73 GGRLEVS-LEKYQSLQD-FVIRRISLRdkeTGE---------VHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIHNSG 141

                         170       180
                  ....*....|....*....|....*..
gi 1831510059 457 dPIIVHSSLGTGRACAFVGAEYMFQMI 483
Cdd:cd14538   142 -PIVVHCSAGIGRTGVLITIDVALGLI 167
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 334-487 2.26e-17

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: 81.67  E-value: 2.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 334 PDTRESFWRMVWDTRATYVVMCCQIMENGVQKCGRYFPdeTGATENYGFAEVQLLEKHEMLNGHLLTRKIeltsgtwkHS 413
Cdd:cd14553    56 PETFGDFWRMVWEQRSATIVMMTKLEERSRVKCDQYWP--TRGTETYGLIQVTLLDTVELATYTVRTFAL--------HK 125

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1831510059 414 DDDPPIRTITHFQFLKWKEGEGLEGEMSMDAF-NYVnhRTRNNLD--PIIVHSSLGTGRACAFVGAEYMFQMINTKK 487
Cdd:cd14553   126 NGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFlRRV--KACNPPDagPIVVHCSAGVGRTGCFIVIDSMLERIKHEK 200
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 257-474 2.35e-17

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: 82.78  E-value: 2.35e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 257 WFEWCQPEFEIPIELTAMSAGNPKLCRDPKVQAWDSTSYLV------DDTHFIHASTVTAPGKEyIGKAIICQAPFddke 330
Cdd:cd14609    21 WQALCAYQAEPNTCSTAQGEANVKKNRNPDFVPYDHARIKLkaesnpSRSDYINASPIIEHDPR-MPAYIATQGPL---- 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 331 kghPDTRESFWRMVWDTRATYVVMCCQIMENGVQKCGRYFPDETGATenYGFAEVQLLEKHeMLNGHLLTRKIELTSGTW 410
Cdd:cd14609    96 ---SHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEGSSL--YHIYEVNLVSEH-IWCEDFLVRSFYLKNVQT 169

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1831510059 411 KHSdddppiRTITHFQFLKW-KEGEGLEGEMSMDAFNYVNHRTRNNLDPIIVHSSLGTGRACAFV 474
Cdd:cd14609   170 QET------RTLTQFHFLSWpAEGIPSSTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYI 228
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 257-512 4.19e-17

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: 82.03  E-value: 4.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 257 WFEWCQPEFEIPIELTAMSAGNPKLCRDPKVQAWDSTSYLV------DDTHFIHASTVT---APGKEYIGKaiicQAPFd 327
Cdd:cd14610    23 WEALCAYQAEPNATNVAQREENVQKNRSLAVLPYDHSRIILkaenshSHSDYINASPIMdhdPRNPAYIAT----QGPL- 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 328 dkekghPDTRESFWRMVWDTRATYVVMCCQIMENGVQKCGRYFPDEtgATENYGFAEVQLLEKHeMLNGHLLTRKIELTS 407
Cdd:cd14610    98 ------PATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDE--GSNLYHIYEVNLVSEH-IWCEDFLVRSFYLKN 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 408 GTWKHSdddppiRTITHFQFLKWKEGEGLEGEMSMDAFNY-VNHRTRNNLDPIIVHSSLGTGRACAFVgaeyMFQMINTK 486
Cdd:cd14610   169 LQTNET------RTVTQFHFLSWNDQGVPASTRSLLDFRRkVNKCYRGRSCPIIVHCSDGAGRSGTYI----LIDMVLNK 238

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1831510059 487 KCGTARFFQV-----DFRTKRLGALQNGKQL 512
Cdd:cd14610   239 MAKGAKEIDIaatleHLRDQRPGMVQTKEQF 269
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 302-523 1.18e-16

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: 79.02  E-value: 1.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 302 FIHASTVTAP--GKEYIgkAIICQAPFddkekghPDTRESFWRMVWDTRATYVVMCCQIMENGVQKCGRYFPD---ETGA 376
Cdd:cd14596     1 YINASYITMPvgEEELF--YIATQGPL-------PSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPEtlqEPME 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 377 TENYgfaevQL-LEKHEMLnGHLLTRKIELTSgtwKHSDDDppiRTITHFQFLKWKE-GEGLEGEMSMDAFNYVnhRTRN 454
Cdd:cd14596    72 LENY-----QLrLENYQAL-QYFIIRIIKLVE---KETGEN---RLIKHLQFTTWPDhGTPQSSDQLVKFICYM--RKVH 137

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1831510059 455 NLDPIIVHSSLGTGRACAFVGAEYMFQMINTKKCGTARFFQVDFRTKRLGALQNGKQLFWVQNMAFELL 523
Cdd:cd14596   138 NTGPIVVHCSAGIGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVL 206
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 290-486 1.56e-16

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: 79.19  E-value: 1.56e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 290 WDST----SYLVDD--THFIHASTVtaPGKEYIGKAIICQAPFddkekghPDTRESFWRMVWDTRATYVVMCCQIMENGV 363
Cdd:cd14617     9 YDSTrvklSNVDDDpcSDYINASYI--PGNNFRREYIATQGPL-------PGTKDDFWKMVWEQNVHNIVMVTQCVEKGR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 364 QKCGRYFPDETGATeNYGFAEVQLLEkhEMLNGHLLTRKIELTSgtwkHSDDDPPiRTITHFQFLKWKEGEGLEGEMSMD 443
Cdd:cd14617    80 VKCDHYWPADQDSL-YYGDLIVQMLS--ESVLPEWTIREFKICS----EEQLDAP-RLVRHFHYTVWPDHGVPETTQSLI 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1831510059 444 AF-----NYVNhRTrNNLDPIIVHSSLGTGRACAFVGAEYMFQMINTK 486
Cdd:cd14617   152 QFvrtvrDYIN-RT-PGSGPTVVHCSAGVGRTGTFIALDRILQQLDSK 197
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 311-502 2.09e-16

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: 78.45  E-value: 2.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 311 PGKEYIGKAIICQAPFddkekghPDTRESFWRMVWDTRATYVVMCCQIMENGVQKCGRYFPDETGATENYGFaevQLLEK 390
Cdd:cd14601    13 PSSSIINRYIACQGPL-------PNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSSSYGGF---QVTCH 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 391 HEMLNGHLLTRKIELTSGTWKHSdddppiRTITHFQFLKWKEgEGLEGEmSMDAFNYVNH---RTRNNLDPIIVHSSLGT 467
Cdd:cd14601    83 SEEGNPAYVFREMTLTNLEKNES------RPLTQIQYIAWPD-HGVPDD-SSDFLDFVCLvrnKRAGKDEPVVVHCSAGI 154

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1831510059 468 GRACAFVGAEYMFQMIntkKCGTARFFQVDFRTKR 502
Cdd:cd14601   155 GRTGVLITMETAMCLI---ECNQPVYPLDIVRTMR 186
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 311-508 2.50e-16

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: 78.41  E-value: 2.50e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 311 PGKEYIGKAII----CQAPFDDKEKGHPDTRESFWRMVWDTRATYVVMCCQIMENGVQKCGRYFPDETGATENYGFAEVQ 386
Cdd:cd14616    23 PGSDYINASYIsgylCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRIRCHQYWPEDNKPVTVFGDIVIT 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 387 LLEKHEMLNGHLLTRKIEltsgtwKHSDddppIRTITHFQFLKWKEgEGLEgEMSMDAFNYVN----HRTRNNlDPIIVH 462
Cdd:cd14616   103 KLMEDVQIDWTIRDLKIE------RHGD----YMMVRQCNFTSWPE-HGVP-ESSAPLIHFVKlvraSRAHDN-TPMIVH 169

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1831510059 463 SSLGTGRACAFVGAEYMFQMINTKKCGTARFFQVDFRTKRLGALQN 508
Cdd:cd14616   170 CSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQN 215
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 320-487 4.20e-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: 77.06  E-value: 4.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 320 IICQAPFddkekghPDTRESFWRMVWDTRATYVVMCCQiMENGVQKCGRYFPDETGATenYGFAEVQLLEkhEMLNGHLL 399
Cdd:cd14556    17 IVTQHPL-------PNTVTDFWRLVYDYGCTSIVMLNQ-LDPKDQSCPQYWPDEGSGT--YGPIQVEFVS--TTIDEDVI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 400 TRKIELTSGTwkhsDDDPPIRTITHFQFLKWKEGEglEGEMSMDAFNYVNHRT-----RNNLDPIIVHSSLGTGRACAFV 474
Cdd:cd14556    85 SRIFRLQNTT----RPQEGYRMVQQFQFLGWPRDR--DTPPSKRALLKLLSEVekwqeQSGEGPIVVHCLNGVGRSGVFC 158

                         170
                  ....*....|...
gi 1831510059 475 GAEYMFQMINTKK 487
Cdd:cd14556   159 AISSVCERIKVEN 171
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 287-477 5.09e-16

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: 78.74  E-value: 5.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 287 VQAWDSTSYLVD-DTHFIHASTVTA--PGKEYIGKAIICQAPFddkekghPDTRESFWRMVWDTRATYVVMCCQIMENGV 363
Cdd:cd14600    49 VLPYDATRVVLQgNEDYINASYVNMeiPSANIVNKYIATQGPL-------PHTCAQFWQVVWEQKLSLIVMLTTLTERGR 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 364 QKCGRYFPDETGATEnYGFAEVQLleKHEMLNGHLLTRKIELTSgtwKHSDDDppiRTITHFQFLKWKEgEGLEgEMSMD 443
Cdd:cd14600   122 TKCHQYWPDPPDVME-YGGFRVQC--HSEDCTIAYVFREMLLTN---TQTGEE---RTVTHLQYVAWPD-HGVP-DDSSD 190

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1831510059 444 AFNYVNH--RTRNNLDPIIVHSSLGTGRACAFVGAE 477
Cdd:cd14600   191 FLEFVNYvrSKRVENEPVLVHCSAGIGRTGVLVTME 226
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 298-540 5.22e-16

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: 78.53  E-value: 5.22e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 298 DDTHFIHASTVTApgKEYIGKAIICQAPFddkekghPDTRESFWRMVWDTRATYVVMCCQIMENGVQKCGRYFPDETGAT 377
Cdd:cd14608    47 EDNDYINASLIKM--EEAQRSYILTQGPL-------PNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKE 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 378 ENYGFAEVQLLEKHEMLNGHLLTRKIELTSGTWKHSdddppiRTITHFQFLKWKEGEGLEGEMSMDAFNYvNHRTRNNLD 457
Cdd:cd14608   118 MIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQET------REILHFHYTTWPDFGVPESPASFLNFLF-KVRESGSLS 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 458 ----PIIVHSSLGTGRACAFVGAEYMFQMINTKK-CGTARFFQV--DFRTKRLGALQNGKQLfwvqNMAFELLIKKLKMH 530
Cdd:cd14608   191 pehgPVVVHCSAGIGRSGTFCLADTCLLLMDKRKdPSSVDIKKVllEMRKFRMGLIQTADQL----RFSYLAVIEGAKFI 266

                         250
                  ....*....|
gi 1831510059 531 HLKFEMEEQW 540
Cdd:cd14608   267 MGDSSVQDQW 276
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 320-473 6.80e-16

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: 76.65  E-value: 6.80e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 320 IICQAPFddkekghPDTRESFWRMVWDTRATYVVMCCQIMENGVQKCGRYFPDETGATENYGFAEVQLLEKHEMLNGhlL 399
Cdd:cd14539    18 IATQAPL-------PGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERGQALVYGAITVSLQSVRTTPTH--V 88

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1831510059 400 TRKIELTSGTWKHSdddppiRTITHFQFLKWKEGEGLEGEMSMDAF-----NYVNHRtRNNLDPIIVHSSLGTGRACAF 473
Cdd:cd14539    89 ERIISIQHKDTRLS------RSVVHLQFTTWPELGLPDSPNPLLRFieevhSHYLQQ-RSLQTPIVVHCSSGVGRTGAF 160
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 300-511 1.17e-15

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: 77.56  E-value: 1.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 300 THFIHASTVTAPGKE--YIGKaiicQAPFddkekghPDTRESFWRMVWDTRATYVVMCCQIMENGVQKCGRYFPDETgAT 377
Cdd:cd14603    58 SDYINANFIKGVDGSraYIAT----QGPL-------SHTVLDFWRMIWQYGVKVILMACREIEMGKKKCERYWAQEQ-EP 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 378 ENYGFAEVQLLEKHEmLNGHLLTRKIELTsgtwkHSDDDppiRTITHFQFLKWKEgEGLEGEMS--MDAFNYVNHRTRNN 455
Cdd:cd14603   126 LQTGPFTITLVKEKR-LNEEVILRTLKVT-----FQKES---RSVSHFQYMAWPD-HGIPDSPDcmLAMIELARRLQGSG 195

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1831510059 456 LDPIIVHSSLGTGRACAFVGAEYMFQMINTKKcgtarfFQVDF---------RTKRLGALQNGKQ 511
Cdd:cd14603   196 PEPLCVHCSAGCGRTGVICTVDYVRQLLLTQR------IPPDFsifdvvlemRKQRPAAVQTEEQ 254
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 312-523 1.36e-15

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: 77.85  E-value: 1.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 312 GKEYIGKAII----CQAPFDDKEKGHPDTRESFWRMVWDTRATYVVMCCQIMENGVQKCGRYFPDETGAteNYGFAEVQL 387
Cdd:cd14628    79 GSDYINASFIdgyrQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSA--RYQYFVVDP 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 388 LEKHEMlnGHLLTRKIELTSGTwkhsddDPPIRTITHFQFLKWKE-GEGLEGEMSMDAFNYVnHRTRNNL---DPIIVHS 463
Cdd:cd14628   157 MAEYNM--PQYILREFKVTDAR------DGQSRTVRQFQFTDWPEqGVPKSGEGFIDFIGQV-HKTKEQFgqdGPISVHC 227

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1831510059 464 SLGTGRACAFVGAEYMFQMINTKkcGTARFFQV--DFRTKRLGALQNGKQLFWVQNMAFELL 523
Cdd:cd14628   228 SAGVGRTGVFITLSIVLERMRYE--GVVDIFQTvkMLRTQRPAMVQTEDQYQFCYRAALEYL 287
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 312-523 1.57e-15

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: 77.47  E-value: 1.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 312 GKEYIGKAII----CQAPFDDKEKGHPDTRESFWRMVWDTRATYVVMCCQIMENGVQKCGRYFPDETGAteNYGFAEVQL 387
Cdd:cd14627    80 GSDYINASFIdgyrQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQYWPAERSA--RYQYFVVDP 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 388 LEKHEMlnGHLLTRKIELTSGTwkhsddDPPIRTITHFQFLKWKE-GEGLEGEMSMDAFNYVnHRTRNNL---DPIIVHS 463
Cdd:cd14627   158 MAEYNM--PQYILREFKVTDAR------DGQSRTVRQFQFTDWPEqGVPKSGEGFIDFIGQV-HKTKEQFgqdGPISVHC 228

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1831510059 464 SLGTGRACAFVGAEYMFQMINTKkcGTARFFQV--DFRTKRLGALQNGKQLFWVQNMAFELL 523
Cdd:cd14627   229 SAGVGRTGVFITLSIVLERMRYE--GVVDIFQTvkMLRTQRPAMVQTEDEYQFCYQAALEYL 288
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 302-479 2.43e-15

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: 75.57  E-value: 2.43e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 302 FIHASTVTAP--GKE--YIGkaiiCQAPFddkekghPDTRESFWRMVWDTRATYVVMCCQIMENGVQKCGRYFPDETGAT 377
Cdd:cd14540     1 YINASHITATvgGKQrfYIA----AQGPL-------QNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGEH 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 378 ENYGFAEVQLLEKHEMLNGHLLTRKIELtsgtwKHSDDDpPIRTITHFQFLKWKEgEGLEGEMS-----MDAFNYVNHRT 452
Cdd:cd14540    70 DALTFGEYKVSTKFSVSSGCYTTTGLRV-----KHTLSG-QSRTVWHLQYTDWPD-HGCPEDVSgfldfLEEINSVRRHT 142

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1831510059 453 RNNLD------PIIVHSSLGTGRACAFVGAEYM 479
Cdd:cd14540   143 NQDVAghnrnpPTLVHCSAGVGRTGVVILADLM 175
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 335-523 2.47e-15

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: 77.07  E-value: 2.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 335 DTRESFWRMVWDTRATYVVMCCQIMENGVQKCGRYFPDETGAteNYGFAEVQLLEKHEMlnGHLLTRKIELTSGTwkhsd 414
Cdd:cd14629   107 ETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSA--RYQYFVVDPMAEYNM--PQYILREFKVTDAR----- 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 415 dDPPIRTITHFQFLKWKE-GEGLEGEMSMDAFNYVnHRTRNNL---DPIIVHSSLGTGRACAFVGAEYMFQMINTKkcGT 490
Cdd:cd14629   178 -DGQSRTIRQFQFTDWPEqGVPKTGEGFIDFIGQV-HKTKEQFgqdGPITVHCSAGVGRTGVFITLSIVLERMRYE--GV 253

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1831510059 491 ARFFQV--DFRTKRLGALQNGKQLFWVQNMAFELL 523
Cdd:cd14629   254 VDMFQTvkTLRTQRPAMVQTEDQYQLCYRAALEYL 288
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 278-484 3.33e-15

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: 75.25  E-value: 3.33e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 278 NPKLCRDPKVQAWDSTSYLVDDTH-FIHASTVTAP--GKEYIgkAIICQAPFddkekghPDTRESFWRMVWDTRATYVVM 354
Cdd:cd14597     3 NRKKNRYKNILPYDTTRVPLGDEGgYINASFIKMPvgDEEFV--YIACQGPL-------PTTVADFWQMVWEQKSTVIAM 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 355 CCQIMENGVQKCGRYFPDETGATENYGfAEVQL-LEKHEMLNGHLLtRKIELtsgtwkHSDDDPPIRTITHFQFLKWKE- 432
Cdd:cd14597    74 MTQEVEGGKIKCQRYWPEILGKTTMVD-NRLQLtLVRMQQLKNFVI-RVLEL------EDIQTREVRHITHLNFTAWPDh 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1831510059 433 GEGLEGEMSMDAFNYVNHRTRnnLDPIIVHSSLGTGRACAFVGAEYMFQMIN 484
Cdd:cd14597   146 DTPSQPEQLLTFISYMRHIHK--SGPIITHCSAGIGRSGTLICIDVVLGLIS 195
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 336-517 4.14e-15

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: 74.63  E-value: 4.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 336 TRESFWRMVWDTRATYVVMCCQIMENGVQKCGRYFPDEtgATENYG-----FAEVQLLEKHEMLNGHLLTRKIELTSGTW 410
Cdd:cd17668    26 TAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPAD--GSEEYGnflvtQKSVQVLAYYTVRNFTLRNTKIKKGSQKG 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 411 KHSDddppiRTITHFQFLKWKEgEGLEgEMSMDAFNYV---NHRTRNNLDPIIVHSSLGTGRACAFVGAEYMFQMINTKK 487
Cdd:cd17668   104 RPSG-----RVVTQYHYTQWPD-MGVP-EYTLPVLTFVrkaSYAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEG 176

                         170       180       190
                  ....*....|....*....|....*....|
gi 1831510059 488 CGTARFFQVDFRTKRLGALQNGKQLFWVQN 517
Cdd:cd17668   177 TVNIFGFLKHIRSQRNYLVQTEEQYVFIHD 206
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 302-515 4.25e-15

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: 74.42  E-value: 4.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 302 FIHASTVTAPGKEYIGKAIICQAPFddkekghPDTRESFWRMVWDTRATYVVMCCQIMEN-GVQKCGRYFPDETGATENY 380
Cdd:cd17658     1 YINASLVETPASESLPKFIATQGPL-------PHTFEDFWEMVIQQRCPVIIMLTRLVDNySTAKCADYFPAEENESREF 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 381 GfaEVQLLEKHEMLNGHLLT-RKIELtsgtwKHSDDDPPIRTITHFQFLKWKEgeglegemsmdafNYVNHRTR------ 453
Cdd:cd17658    74 G--RISVTNKKLKHSQHSITlRVLEV-----QYIESEEPPLSVLHIQYPEWPD-------------HGVPKDTRsvrell 133

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1831510059 454 -------NNLDPIIVHSSLGTGRACAFVGAEYMFQMI--------NTKKcgTARffqvDFRTKRLGALQNGKQ-LFWV 515
Cdd:cd17658   134 krlygipPSAGPIVVHCSAGIGRTGAYCTIHNTIRRIlegdmsavDLSK--TVR----KFRSQRIGMVQTQDQyIFCY 205
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 285-487 4.34e-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: 75.84  E-value: 4.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 285 PKVQAWDSTSYlvDDTHFIHASTVTAPGKEYIGKAII----CQAPFDDKEKGHPDTRESFWRMVWDTRATYVVMCCQIME 360
Cdd:cd14626    43 PKNRYANVIAY--DHSRVILTSVDGVPGSDYINANYIdgyrKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEE 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 361 NGVQKCGRYFPDEtgATENYGFAEVQLLEKHEMLNGHLLTRKIeltsgtwkHSDDDPPIRTITHFQFLKWKEGEGLEGEM 440
Cdd:cd14626   121 KSRVKCDQYWPIR--GTETYGMIQVTLLDTVELATYSVRTFAL--------YKNGSSEKREVRQFQFMAWPDHGVPEYPT 190

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1831510059 441 SMDAF-NYVNHRTRNNLDPIIVHSSLGTGRACAFVGAEYMFQMINTKK 487
Cdd:cd14626   191 PILAFlRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEK 238
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 334-511 4.79e-15

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: 74.00  E-value: 4.79e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 334 PDTRESFWRMVWDTRATYVVMCCQIMENGVQKCGRYFPDETGATENYGFAEVqLLEKHEMLNGHLLTRKIELTSGTWKhs 413
Cdd:cd14542    24 PNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQLQFGPFKI-SLEKEKRVGPDFLIRTLKVTFQKES-- 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 414 dddppiRTITHFQFLKWKEgEGLEG------EMSMDAFNYVNHRTrnnlDPIIVHSSLGTGRACAFVGAEYMFQMINTKK 487
Cdd:cd14542   101 ------RTVYQFHYTAWPD-HGVPSsvdpilDLVRLVRDYQGSED----VPICVHCSAGCGRTGTICAIDYVWNLLKTGK 169

                         170       180
                  ....*....|....*....|....*...
gi 1831510059 488 CgTARF--FQV--DFRTKRLGALQNGKQ 511
Cdd:cd14542   170 I-PEEFslFDLvrEMRKQRPAMVQTKEQ 196
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 334-521 7.43e-15

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: 73.55  E-value: 7.43e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 334 PDTRESFWRMVWDTRATYVVMCCQIMENGVQKCGRYFPDEtgaTENYGFAEVQLLEKHEMLNGHLLTRKIELTSGTWKHS 413
Cdd:cd14632    24 QEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDD---SDTYGDIKITLLKTETLAEYSVRTFALERRGYSARHE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 414 dddppirtITHFQFLKWKEGEGLEGEMSMDAF-NYVNHRTRNNLDPIIVHSSLGTGRACAFVGAEYMFQMINTKkcGTAR 492
Cdd:cd14632   101 --------VKQFHFTSWPEHGVPYHATGLLAFiRRVKASTPPDAGPVVVHCSAGAGRTGCYIVLDVMLDMAECE--GVVD 170

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1831510059 493 FFQV--DFRTKRLGALQNGKQLFWVQNMAFE 521
Cdd:cd14632   171 IYNCvkTLCSRRINMIQTEEQYIFIHDAILE 201
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 302-481 9.60e-15

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: 73.32  E-value: 9.60e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 302 FIHASTVTapGKEYIGKAIICQAPFDDkekghpdTRESFWRMVWDTRATYVVMCCQIMENGVQKCGRYFPDETGATENYG 381
Cdd:cd14557     1 YINASYID--GFKEPRKYIAAQGPKDE-------TVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRAFG 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 382 FAEVQLLEkhEMLNGHLLTRKIELTSGTWKHSDddppiRTITHFQFLKWKEgEGLEGEMSMdafnYVNHRTR----NNL- 456
Cdd:cd14557    72 DVVVKINE--EKICPDYIIRKLNINNKKEKGSG-----REVTHIQFTSWPD-HGVPEDPHL----LLKLRRRvnafNNFf 139

                         170       180
                  ....*....|....*....|....*.
gi 1831510059 457 -DPIIVHSSLGTGRACAFVGAEYMFQ 481
Cdd:cd14557   140 sGPIVVHCSAGVGRTGTYIGIDAMLE 165
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 334-521 1.10e-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: 74.74  E-value: 1.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 334 PDTRESFWRMVWDTRATYVVMCCQIMENGVQKCGRYFPDEtgATENYGFAEVQLLEKHEMLNghLLTRKIELtsgtwkHS 413
Cdd:cd14625   100 PETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSR--GTETYGMIQVTLLDTIELAT--FCVRTFSL------HK 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 414 DDDPPIRTITHFQFLKWKEGEGLEGEMSMDAFnYVNHRTRNNLD--PIIVHSSLGTGRACAFVGAEYMFQMINTKKCGTA 491
Cdd:cd14625   170 NGSSEKREVRQFQFTAWPDHGVPEYPTPFLAF-LRRVKTCNPPDagPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDI 248

                         170       180       190
                  ....*....|....*....|....*....|
gi 1831510059 492 RFFQVDFRTKRLGALQNGKQLFWVQNMAFE 521
Cdd:cd14625   249 YGHVTLMRSQRNYMVQTEDQYSFIHDALLE 278
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 302-487 2.04e-14

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: 72.25  E-value: 2.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 302 FIHASTVTapGKEYIGKAIICQAPFDDkekghpdTRESFWRMVWDTRATYVVMCCQIMENGVQKCGRYFPDETGATenYG 381
Cdd:cd14551     1 YINASYID--GYQEKNKFIAAQGPKDE-------TVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCWT--YG 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 382 FAEVQLLEKHEMLNghLLTRKIELTsgtwKHSDD--DPPIRTITHFQFLKWKEGEGLEGEMSMDAFnyvnHRTRNNLD-- 457
Cdd:cd14551    70 NLRVRVEDTVVLVD--YTTRKFCIQ----KVNRGigEKRVRLVTQFHFTSWPDFGVPFTPIGMLKF----LKKVKSANpp 139

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1831510059 458 ---PIIVHSSLGTGRACAFVGAEYMFQMINTKK 487
Cdd:cd14551   140 ragPIVVHCSAGVGRTGTFIVIDAMLDMMHAEG 172
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 335-521 2.90e-14

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: 72.75  E-value: 2.90e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 335 DTRESFWRMVWDTRATYVVMCCQIMENGVQKCGRYFPDEtgaTENYGFAEVQLLEKHEMLNGHLLTRKIEltsgtwKHSD 414
Cdd:cd14630    57 ETVKDFWRMIWQENSASVVMVTNLVEVGRVKCVRYWPDD---TEVYGDIKVTLIETEPLAEYVIRTFTVQ------KKGY 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 415 DDppIRTITHFQFLKWKE------GEGLEGEMSMdafnyVNHRTRNNLDPIIVHSSLGTGRACAFVGAEYMFQMINTKkc 488
Cdd:cd14630   128 HE--IREIRQFHFTSWPDhgvpcyATGLLGFVRQ-----VKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENE-- 198

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1831510059 489 GTARFFQV--DFRTKRLGALQNGKQLFWVQNMAFE 521
Cdd:cd14630   199 GVVDIFNCvrELRAQRVNMVQTEEQYVFVHDAILE 233
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 302-511 5.35e-14

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: 71.19  E-value: 5.35e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 302 FIHASTVTA-PGKEYIgkaIICQAPFddkekghPDTRESFWRMVWDTRATYVVMCCQIMENGVQKCGRYFPDETGATeny 380
Cdd:cd14622     2 YINASFIDGyRQKDYF---IATQGPL-------AHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGSVT--- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 381 gFAEVQLLEKHEMLNGHLLTRKIELTSGTWKHSdddppiRTITHFQFLKWKE-GEGLEGEMSMD---AFNYVNHRTRNNl 456
Cdd:cd14622    69 -HGEITIEIKNDTLLETISIRDFLVTYNQEKQT------RLVRQFHFHGWPEiGIPAEGKGMIDliaAVQKQQQQTGNH- 140

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1831510059 457 dPIIVHSSLGTGRACAFVGAEYMFQMIntKKCGTARFFQV--DFRTKRLGALQNGKQ 511
Cdd:cd14622   141 -PIVVHCSAGAGRTGTFIALSNILERV--KAEGLLDVFQTvkSLRLQRPHMVQTLEQ 194
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 258-521 5.69e-14

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: 72.84  E-value: 5.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 258 FEWCQPEFEIPIELTAMSAGNPKlCRDPKVQAWDSTSYLVDDTHFIhastvtaPGKEYIGKAII----CQAPFDDKEKGH 333
Cdd:cd14624    28 YESIDPGQQFTWEHSNLEVNKPK-NRYANVIAYDHSRVLLSAIEGI-------PGSDYINANYIdgyrKQNAYIATQGAL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 334 PDTRESFWRMVWDTRATYVVMCCQIMENGVQKCGRYFPDEtgATENYGFAEVQLLEKHEMLNGHLLTRKIELTSGTWKhs 413
Cdd:cd14624   100 PETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSR--GTETYGLIQVTLLDTVELATYCVRTFALYKNGSSEK-- 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 414 dddppiRTITHFQFLKWKEGEGLEGEMSMDAFnYVNHRTRNNLD--PIIVHSSLGTGRACAFVGAEYMFQMINTKKCGTA 491
Cdd:cd14624   176 ------REVRQFQFTAWPDHGVPEHPTPFLAF-LRRVKTCNPPDagPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDI 248

                         250       260       270
                  ....*....|....*....|....*....|
gi 1831510059 492 RFFQVDFRTKRLGALQNGKQLFWVQNMAFE 521
Cdd:cd14624   249 YGHVTLMRAQRNYMVQTEDQYIFIHDALLE 278
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 326-474 8.83e-14

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: 70.89  E-value: 8.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 326 FDDKEKGH-------PDTRESFWRMVWDTRATYVVMCCQIMENGvQKCGRYFPDETGatENYGFAEVQLLEKHEMLNGHL 398
Cdd:cd14547    36 YDGEEKAYiatqgplPNTVADFWRMVWQEKTPIIVMITNLTEAK-EKCAQYWPEEEN--ETYGDFEVTVQSVKETDGYTV 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 399 ltRKIELTSGTWKHSdddppirtITHFQFLKWKEGE------GLEgEMSMDAFNYVnhRTRNNLDPIIVHSSLGTGRACA 472
Cdd:cd14547   113 --RKLTLKYGGEKRY--------LKHYWYTSWPDHKtpeaaqPLL-SLVQEVEEAR--QTEPHRGPIVVHCSAGIGRTGC 179


                  ..
gi 1831510059 473 FV 474
Cdd:cd14547   180 FI 181
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 298-524 1.64e-13

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: 71.22  E-value: 1.64e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 298 DDTH--FIHASTVTAPGKeyiGKAIIC-QAPFDDkekghpdTRESFWRMVWDTRATYVVMCCQIMENGVQKCGRYFPDET 374
Cdd:cd17667    53 DSKHsdYINANYVDGYNK---AKAYIAtQGPLKS-------TFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTEN 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 375 gaTENYGFAEVQLleKHEMLNGHLLTRKIELTSGTWKHSDDDPPI-----RTITHFQFLKWKEgEGLEgEMSMDAFNYVN 449
Cdd:cd17667   123 --SEEYGNIIVTL--KSTKIHACYTVRRFSIRNTKVKKGQKGNPKgrqneRTVIQYHYTQWPD-MGVP-EYALPVLTFVR 196

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1831510059 450 HRT---RNNLDPIIVHSSLGTGRACAFVGAEYMFQMINTKKCGTARFFQVDFRTKRLGALQNGKQLFWVQNMAFELLI 524
Cdd:cd17667   197 RSSaarTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 274
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 282-486 2.77e-13

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: 70.29  E-value: 2.77e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 282 CRDPKVQAWDstsylvddthFIHASTV-------TAPGKEYIGkaiiCQAPFDDkekghpdTRESFWRMVWDTRATYVVM 354
Cdd:cd14606    39 GRDSNIPGSD----------YINANYVknqllgpDENAKTYIA----SQGCLEA-------TVNDFWQMAWQENSRVIVM 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 355 CCQIMENGVQKCGRYFPdETGATENYGFAEVQLLEKHEMLNGHLltRKIELTSgtwkhSDDDPPIRTITHFQFLKWKE-G 433
Cdd:cd14606    98 TTREVEKGRNKCVPYWP-EVGMQRAYGPYSVTNCGEHDTTEYKL--RTLQVSP-----LDNGELIREIWHYQYLSWPDhG 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1831510059 434 EGLEGEMSMDAFNYVNHRTRN--NLDPIIVHSSLGTGRACAFVGAEYMFQMINTK 486
Cdd:cd14606   170 VPSEPGGVLSFLDQINQRQESlpHAGPIIVHCSAGIGRTGTIIVIDMLMENISTK 224
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 334-521 4.31e-13

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: 68.40  E-value: 4.31e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 334 PDTRESFWRMVWDTRATYVVMCCQIMENGVQKCGRYFPDEtgaTENYGFAEVQLLEKHEMlnGHLLTRKIELTSGTWKHs 413
Cdd:cd14555    24 QETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDD---TEVYGDIKVTLVETEPL--AEYVVRTFALERRGYHE- 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 414 dddppIRTITHFQFLKWKE-GEGLEGEMSMDAFNYVNHRTRNNLDPIIVHSSLGTGRACAFVGAEYMFQMINTKkcGTAR 492
Cdd:cd14555    98 -----IREVRQFHFTGWPDhGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAERE--GVVD 170

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1831510059 493 FFQV--DFRTKRLGALQNGKQLFWVQNMAFE 521
Cdd:cd14555   171 IYNCvkELRSRRVNMVQTEEQYIFIHDAILE 201
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 320-511 4.51e-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: 68.45  E-value: 4.51e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 320 IICQAPFDDkekghpdTRESFWRMVWDTRATYVVMCCQIMENGVQKCGRYFPDETGATenYGFAEVQLleKHEMLNGHLL 399
Cdd:cd14552    17 IATQGPLDH-------TVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGSVS--SGDITVEL--KDQTDYEDYT 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 400 TRKIELTSGTWKHSdddppiRTITHFQFLKWKE-GEGLEGEMSMDAFNYVNHRTRNNLD-PIIVHSSLGTGRACAFVGAE 477
Cdd:cd14552    86 LRDFLVTKGKGGST------RTVRQFHFHGWPEvGIPDNGKGMIDLIAAVQKQQQQSGNhPITVHCSAGAGRTGTFCALS 159

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1831510059 478 YMFQMIntKKCGTARFFQV--DFRTKRLGALQNGKQ 511
Cdd:cd14552   160 TVLERV--KAEGVLDVFQVvkSLRLQRPHMVQTLEQ 193
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 283-487 5.07e-13

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: 68.82  E-value: 5.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 283 RDPKVQAWDST----SYLVDDTH--FIHASTVtaPGKEYIGKAIICQAPFDDkekghpdTRESFWRMVWDTRATYVVMCC 356
Cdd:cd14618     2 RYPHVLPYDHSrvrlSQLGGEPHsdYINANFI--PGYTSPQEFIATQGPLKK-------TIEDFWRLVWEQQVCNIIMLT 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 357 QIMENGVQKCGRYFPDETgATENYGFAEVQLLEKHEmlNGHLLTRKIELTSGTWKHSdddppiRTITHFQFLKWKEGEGL 436
Cdd:cd14618    73 VGMENGRVLCDHYWPSES-TPVSYGHITVHLLAQSS--EDEWTRREFKLWHEDLRKE------RRVKHLHYTAWPDHGIP 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1831510059 437 EGEMSMDAFNYVNH---RTRNNLDPIIVHSSLGTGRACAFVGAEYMFQMINTKK 487
Cdd:cd14618   144 ESTSSLMAFRELVRehvQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEK 197
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 299-495 9.19e-13

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: 68.38  E-value: 9.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 299 DTHFIHASTVtaPG----KEYIGKaiicQAPFddkekghPDTRESFWRMVWDTRATYVVMCCQIMENGVQKCGRYFP-DE 373
Cdd:cd14619    24 GSDYINANYM--PGywssQEFIAT----QGPL-------PQTVGDFWRMIWEQQSSTIVMLTNCMEAGRVKCEHYWPlDY 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 374 TGATenYGFAEVQLLEKHEMLNGHL--LTRKIELTSGTwkhsdddppiRTITHFQFLKWKEGEGLEGEMSMDAFNYVnhr 451
Cdd:cd14619    91 TPCT--YGHLRVTVVSEEVMENWTVreFLLKQVEEQKT----------LSVRHFHFTAWPDHGVPSSTDTLLAFRRL--- 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1831510059 452 TRNNLD------PIIVHSSLGTGRACAFVGAEYMFQMINTKK-CGTARFFQ 495
Cdd:cd14619   156 LRQWLDqtmsggPTVVHCSAGVGRTGTLIALDVLLQQLQSEGlLGPFSFVQ 206
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 303-511 1.93e-12

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: 67.74  E-value: 1.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 303 IHASTVTAPGKEYIGKAIIcqAPFDDKEKGHPDTRES--------------FWRMVWDTRATYVVMCCQIMENGVQKCGR 368
Cdd:cd14605    21 LHDGDPNEPVSDYINANII--MPEFETKCNNSKPKKSyiatqgclqntvndFWRMVFQENSRVIVMTTKEVERGKSKCVK 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 369 YFPDETGATEnYGFAEVQLLeKHEMLNGHLLtRKIELTSGTWKHSDddppiRTITHFQFLKWKEgEGLEGEMS--MDAFN 446
Cdd:cd14605    99 YWPDEYALKE-YGVMRVRNV-KESAAHDYIL-RELKLSKVGQGNTE-----RTVWQYHFRTWPD-HGVPSDPGgvLDFLE 169

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1831510059 447 YVNHRTRNNLD--PIIVHSSLGTGRACAFVGAEYMFQMINTK--KC--GTARFFQVdFRTKRLGALQNGKQ 511
Cdd:cd14605   170 EVHHKQESIMDagPVVVHCSAGIGRTGTFIVIDILIDIIREKgvDCdiDVPKTIQM-VRSQRSGMVQTEAQ 239
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 299-512 5.84e-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: 66.14  E-value: 5.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 299 DTHFIHASTVTApgKEYIGKAIICQAPFddkekghPDTRESFWRMVWDTRATYVVMCCQIMENGVQKCGRYFPdeTGATE 378
Cdd:cd14607    47 ENDYINASLVVI--EEAQRSYILTQGPL-------PNTCCHFWLMVWQQKTKAVVMLNRIVEKDSVKCAQYWP--TDEEE 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 379 NYGFAEVQLLEK--HEMLNGHLLTRKIELTSGTWKHSdddppiRTITHFQFLKWKEGEGLEGEMSMDAFNYVNHRTRN-N 455
Cdd:cd14607   116 VLSFKETGFSVKllSEDVKSYYTVHLLQLENINSGET------RTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSlS 189

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1831510059 456 LD--PIIVHSSLGTGRACAFVGAEYMFQMINTKKCGTARFFQV--DFRTKRLGALQNGKQL 512
Cdd:cd14607   190 PEhgPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDPDSVDIKQVllDMRKYRMGLIQTPDQL 250
PHA02738 PHA02738
hypothetical protein; Provisional
 302-473 7.03e-12

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 66.87  E-value: 7.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 302 FIHASTVTapGKEYIGKAIICQAPFDDkekghpdTRESFWRMVWDTRATYVVMCCQIMENGVQKCGRYFPDETGATENYG 381
Cdd:PHA02738   77 YINANYVD--GFEYKKKFICGQAPTRQ-------TCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDVEQGSIRFG 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 382 FAEVQL--LEKHEmlngHLLTRKIELTSGTwkhsdddPPIRTITHFQFLKWKEGEGLEGEMSMDAF-------------- 445
Cdd:PHA02738  148 KFKITTtqVETHP----HYVKSTLLLTDGT-------SATQTVTHFNFTAWPDHDVPKNTSEFLNFvlevrqcqkelaqe 216

                         170       180
                  ....*....|....*....|....*...
gi 1831510059 446 NYVNHRTRNNLDPIIVHSSLGTGRACAF 473
Cdd:PHA02738  217 SLQIGHNRLQPPPIVVHCNAGLGRTPCY 244
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 294-483 7.46e-12

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: 65.61  E-value: 7.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 294 SYLVDDthFIHASTVtaPG----KEYIGkaiiCQAPFddkekghPDTRESFWRMVWDTRATYVVMCCQIMENGVQKCGRY 369
Cdd:cd14615    20 SHSTDD--YINANYM--PGynskKEFIA----AQGPL-------PNTVKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEY 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 370 FPDEtgATENYGFAEVQLLEkhEMLNGHLLTRKIELTSGTWKHSdddppiRTITHFQFLKWKE-GEGLEGEMSMDAFNYV 448
Cdd:cd14615    85 WPSK--QKKDYGDITVTMTS--EIVLPEWTIRDFTVKNAQTNES------RTVRHFHFTSWPDhGVPETTDLLINFRHLV 154

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1831510059 449 NHRTRNNL--DPIIVHSSLGTGRACAFVGAEYMFQMI 483
Cdd:cd14615   155 REYMKQNPpnSPILVHCSAGVGRTGTFIAIDRLIYQI 191
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 290-473 2.03e-11

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 65.44  E-value: 2.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 290 WDSTSYLV----DDTHFIHASTVTapGKEYIGKAIICQAPFDDkekghpdTRESFWRMVWDTRATYVVMCCQImENGVQK 365
Cdd:PHA02746   84 SDGKKIEVtsedNAENYIHANFVD--GFKEANKFICAQGPKED-------TSEDFFKLISEHESQVIVSLTDI-DDDDEK 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 366 CGRYFPDETGATENYGFAEVQLLEKHEMLNGH----LLTRKIELTSgtwkhsdddppiRTITHFQFLKWKEGEGLEG-EM 440
Cdd:PHA02746  154 CFELWTKEEDSELAFGRFVAKILDIIEELSFTktrlMITDKISDTS------------REIHHFWFPDWPDNGIPTGmAE 221

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1831510059 441 SMDAFNYVNHRTR----------NNLDPIIVHSSLGTGRACAF 473
Cdd:PHA02746  222 FLELINKVNEEQAelikqadndpQTLGPIVVHCSAGIGRAGTF 264
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 299-527 2.09e-11

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: 65.34  E-value: 2.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 299 DTHFIHAS---TVTAPgKEYIGKaiicQAPFddkekghPDTRESFWRMVWDTRATYVVMCCQIMENGVQKCGRYFPDETG 375
Cdd:cd14604    84 DSDYINANfikGVYGP-KAYIAT----QGPL-------ANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWPLYGE 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 376 ATENYGFAEVQLLEKHEMLNGHLLTRKIELTSGTwkhsdddppiRTITHFQFLKWKEGEGLEGEMS-MDAFNYVNHRTRN 454
Cdd:cd14604   152 EPMTFGPFRISCEAEQARTDYFIRTLLLEFQNET----------RRLYQFHYVNWPDHDVPSSFDSiLDMISLMRKYQEH 221

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1831510059 455 NLDPIIVHSSLGTGRACAFVGAEYMFQMINTKKcgTARFFQV-----DFRTKRLGALQNGKQLFWVQNMAFELLIKKL 527
Cdd:cd14604   222 EDVPICIHCSAGCGRTGAICAIDYTWNLLKAGK--IPEEFNVfnliqEMRTQRHSAVQTKEQYELVHRAIAQLFEKQL 297
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 335-521 2.52e-11

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: 64.68  E-value: 2.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 335 DTRESFWRMVWDTRATYVVMCCQIMENGVQKCGRYFPDEtgaTENYGFAEVQLLEKhemlngHLLTRKIELTSGTWKHSD 414
Cdd:cd14633    94 ETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDD---TEIYKDIKVTLIET------ELLAEYVIRTFAVEKRGV 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 415 DDppIRTITHFQFLKWKE-GEGLEGEMSMDAFNYVNHRTRNNLDPIIVHSSLGTGRACAFVGAEYMFQMinTKKCGTARF 493
Cdd:cd14633   165 HE--IREIRQFHFTGWPDhGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDM--AEREGVVDI 240

                         170       180       190
                  ....*....|....*....|....*....|
gi 1831510059 494 FQV--DFRTKRLGALQNGKQLFWVQNMAFE 521
Cdd:cd14633   241 YNCvrELRSRRVNMVQTEEQYVFIHDAILE 270
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 335-521 3.75e-11

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: 63.12  E-value: 3.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 335 DTRESFWRMVWDTRATYVVMCCQIMENGVQKCGRYFPDEtgaTENYGFAEVQLLEKHEMlnGHLLTRKIELTSGTWKHsd 414
Cdd:cd14631    39 ETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDD---TEVYGDFKVTCVEMEPL--AEYVVRTFTLERRGYNE-- 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 415 ddppIRTITHFQFLKWKE-GEGLEGEMSMDAFNYVNHRTRNNLDPIIVHSSLGTGRACAFVGAEYMFQMinTKKCGTARF 493
Cdd:cd14631   112 ----IREVKQFHFTGWPDhGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDM--AEREGVVDI 185

                         170       180       190
                  ....*....|....*....|....*....|
gi 1831510059 494 FQV--DFRTKRLGALQNGKQLFWVQNMAFE 521
Cdd:cd14631   186 YNCvkALRSRRINMVQTEEQYIFIHDAILE 215
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 298-511 6.13e-11

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: 62.93  E-value: 6.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 298 DDTHFIHASTVTAPG---KEYIGKaiicQAPFddkekghPDTRESFWRMVWDTRATYVVMCCQIMEnGVQKCGRYFPDET 374
Cdd:cd14612    42 EEGSYINANYIRGYDgkeKAYIAT----QGPM-------LNTVSDFWEMVWQEECPIIVMITKLKE-KKEKCVHYWPEKE 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 375 GAtenYGFAEVQLLEKHEMlnGHLLTRKIeltsgTWKHSDDDppiRTITHFQFLKWKEGEGLE-GEMSMDAFNYVNHR-- 451
Cdd:cd14612   110 GT---YGRFEIRVQDMKEC--DGYTIRDL-----TIQLEEES---RSVKHYWFSSWPDHQTPEsAGPLLRLVAEVEESrq 176

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1831510059 452 TRNNLDPIIVHSSLGTGRACAFVGAEYMFQMIntKKCGTARFFQV--DFRTKRLGALQNGKQ 511
Cdd:cd14612   177 TAASPGPIVVHCSAGIGRTGCFIATSIGCQQL--KDTGKVDILGIvcQLRLDRGGMIQTSEQ 236
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 334-511 9.33e-11

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: 61.64  E-value: 9.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 334 PDTRESFWRMVWDTRATYVVMCCQIMENGVQKCGRYFPDEtgaTENYGFAEVQLleKHEMLNGHLLTRKIELTSGTWKHS 413
Cdd:cd14558    24 PDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDE---KKTYGDIEVEL--KDTEKSPTYTVRVFEITHLKRKDS 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 414 dddppiRTITHFQFLKWKE---GEGLEGEMSM-----DAFNYVNHRTRNNLdPIIVHSSLG---TGRACAFvgaeyMFQM 482
Cdd:cd14558    99 ------RTVYQYQYHKWKGeelPEKPKDLVDMiksikQKLPYKNSKHGRSV-PIVVHCSDGssrTGIFCAL-----WNLL 166

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1831510059 483 INTKKCGTARFFQV--DFRTKRLGALQNGKQ 511
Cdd:cd14558   167 ESAETEKVVDVFQVvkALRKQRPGMVSTLEQ 197
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 421-508 1.25e-10

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: 58.52  E-value: 1.25e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059  421 TITHFQFLKWKE-GEGLEGEMSMDAFNYVNHRT--RNNLDPIIVHSSLGTGRACAFVGAEYMFQMINTKKcGTARFFQV- 496
Cdd:smart00012   1 TVKHYHYTGWPDhGVPESPDSILELLRAVKKNLnqSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEA-GEVDIFDTv 79

                           90
                   ....*....|...
gi 1831510059  497 -DFRTKRLGALQN 508
Cdd:smart00012  80 kELRSQRPGMVQT 92
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
421-508 1.25e-10

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 58.52  E-value: 1.25e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059  421 TITHFQFLKWKE-GEGLEGEMSMDAFNYVNHRT--RNNLDPIIVHSSLGTGRACAFVGAEYMFQMINTKKcGTARFFQV- 496
Cdd:smart00404   1 TVKHYHYTGWPDhGVPESPDSILELLRAVKKNLnqSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEA-GEVDIFDTv 79

                           90
                   ....*....|...
gi 1831510059  497 -DFRTKRLGALQN 508
Cdd:smart00404  80 kELRSQRPGMVQT 92
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 298-511 1.34e-10

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: 61.60  E-value: 1.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 298 DDTHFIHASTVTapGKEYIGKAIICQAPFDDkekghpdTRESFWRMVWDTRATYVVMCCQIMENGVQKCGRYFPdeTGAT 377
Cdd:cd14623    22 ENTDYVNASFID--GYRQKDSYIASQGPLQH-------TIEDFWRMIWEWKSCSIVMLTELEERGQEKCAQYWP--SDGS 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 378 ENYGFAEVQLleKHEMLNGHLLTRKIELTSGTWKHSdddppiRTITHFQFLKWKE-GEGLEGEMSMDAFNYVNHRTRNNL 456
Cdd:cd14623    91 VSYGDITIEL--KKEEECESYTVRDLLVTNTRENKS------RQIRQFHFHGWPEvGIPSDGKGMINIIAAVQKQQQQSG 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1831510059 457 D-PIIVHSSLGTGRACAFVGAEYMFQMINTKkcGTARFFQV--DFRTKRLGALQNGKQ 511
Cdd:cd14623   163 NhPITVHCSAGAGRTGTFCALSTVLERVKAE--GILDVFQTvkSLRLQRPHMVQTLEQ 218
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 311-511 2.65e-10

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: 60.72  E-value: 2.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 311 PGKEYIGKAII----CQAPFDDKEKGHPDTRESFWRMVWDTRATYVVMCCQIMENGVQKCGRYFPDETGATenYGFAEVQ 386
Cdd:cd14620    21 PCSDYINASYIdgykEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKCYQYWPDQGCWT--YGNIRVA 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 387 lLEKHEMLNGHLLtRKIELTSgtwKHSDDDPPIRTITHFQFLKWKEGEGLEGEMSMDAF-NYVNHRTRNNLDPIIVHSSL 465
Cdd:cd14620    99 -VEDCVVLVDYTI-RKFCIQP---QLPDGCKAPRLVTQLHFTSWPDFGVPFTPIGMLKFlKKVKSVNPVHAGPIVVHCSA 173

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1831510059 466 GTGRACAFVGAEYMFQMINTKKCGTARFFQVDFRTKRLGALQNGKQ 511
Cdd:cd14620   174 GVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQ 219
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 297-521 2.75e-10

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: 61.96  E-value: 2.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 297 VDDTHFIHASTVTapGKEYIGKAIICQAPfddKEkghpDTRESFWRMVWDTRATYVVMCCQIMENGVQKCGRYFPDETGA 376
Cdd:cd14621    77 VPDSDYINASFIN--GYQEKNKFIAAQGP---KE----ETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGCW 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 377 TenYGFAEVQLLEKHEMLNGHLLTRKIELTSGTwkhsDDDPPIRTITHFQFLKWKEGEGLEGEMSMDAF-NYVNHRTRNN 455
Cdd:cd14621   148 T--YGNIRVSVEDVTVLVDYTVRKFCIQQVGDV----TNKKPQRLITQFHFTSWPDFGVPFTPIGMLKFlKKVKNCNPQY 221

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1831510059 456 LDPIIVHSSLGTGRACAFVGAEYMFQMINTKKCGTARFFQVDFRTKRLGALQNGKQLFWVQNMAFE 521
Cdd:cd14621   222 AGAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLE 287
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 302-516 6.78e-10

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: 59.90  E-value: 6.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 302 FIHASTVtaPGKEYIGKAIICQAPFddkekghPDTRESFWRMVWDTRATYVVMCCQIMENGVQKCGRYFPdETGATENYG 381
Cdd:cd14614    42 YINANYI--PGYNSPQEYIATQGPL-------PETRNDFWKMVLQQKSQIIVMLTQCNEKRRVKCDHYWP-FTEEPVAYG 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 382 FAEVQLLEKHEMLNghLLTRKIELTsgtwkHSDDdppIRTITHFQFLKWKEgEGL----EGEMSMDAFNYVNHRTRNNLD 457
Cdd:cd14614   112 DITVEMLSEEEQPD--WAIREFRVS-----YADE---VQDVMHFNYTAWPD-HGVptanAAESILQFVQMVRQQAVKSKG 180

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1831510059 458 PIIVHSSLGTGRACAFVGAEYMFQMINTKKCGTARFFQVDFRTKRLGALQNGKQLFWVQ 516
Cdd:cd14614   181 PMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIH 239
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 278-473 1.79e-09

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 59.25  E-value: 1.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 278 NPKLCRDPKVQAWDSTSYLV------DDthFIHASTVTapGKEYIGKAIICQAPFDDkekghpdTRESFWRMVWDTRATY 351
Cdd:PHA02742   52 NMKKCRYPDAPCFDRNRVILkiedggDD--FINASYVD--GHNAKGRFICTQAPLEE-------TALDFWQAIFQDQVRV 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 352 VVMCCQIMENGVQKCGRYFPDETGATENYGFAEVQLLEKHEMLNGHLLTrkIELTSGTWKHSDDdppirtITHFQFLKWK 431
Cdd:PHA02742  121 IVMITKIMEDGKEACYPYWMPHERGKATHGEFKIKTKKIKSFRNYAVTN--LCLTDTNTGASLD------IKHFAYEDWP 192

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1831510059 432 EGeGLEGEMS--MDAFNYVNH-----------RTRNNLDPIIVHSSLGTGRACAF 473
Cdd:PHA02742  193 HG-GLPRDPNkfLDFVLAVREadlkadvdikgENIVKEPPILVHCSAGLDRAGAF 246
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 302-479 3.14e-09

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: 57.68  E-value: 3.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 302 FIHAS--TVTAPGKEYigKAIICQAPFDDkekghpdTRESFWRMVWDTRATYVVMCCQIMENGVQKCGRYFPDETGATEN 379
Cdd:cd14598     1 YINAShiKVTVGGKEW--DYIATQGPLQN-------TCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLGSRHNT 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 380 YGFAEVQLLEKHEMLNGHLLTRKIELtsgtwKH--SDDDppiRTITHFQFLKWKEG---EGLEGEMS-MDAFNYVNHRTR 453
Cdd:cd14598    72 VTYGRFKITTRFRTDSGCYATTGLKI-----KHllTGQE---RTVWHLQYTDWPEHgcpEDLKGFLSyLEEIQSVRRHTN 143

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1831510059 454 NNLD------PIIVHSSLGTGRACAFVGAEYM 479
Cdd:cd14598   144 STIDpkspnpPVLVHCSAGVGRTGVVILSEIM 175
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 243-523 7.59e-09

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 57.70  E-value: 7.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 243 PGKERDPSKTVIANWFEWCQPEFEIPieltamsaGNPKLCRDPKVQAWDSTSYLVD-----DTHFIHASTVTapGKEYIG 317
Cdd:PHA02747   24 FGIIRDEHHQIILKPFDGLIANFEKP--------ENQPKNRYWDIPCWDHNRVILDsgggsTSDYIHANWID--GFEDDK 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 318 KAIICQAPFDDkekghpdTRESFWRMVWDTRATYVVMCCQIME-NGVQKCGRYF-PDETGATENYGFAEVQLleKHEMLN 395
Cdd:PHA02747   94 KFIATQGPFAE-------TCADFWKAVWQEHCSIIVMLTPTKGtNGEEKCYQYWcLNEDGNIDMEDFRIETL--KTSVRA 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 396 GHLLTrKIELTSGTWKHSdddppiRTITHFQFLKWKEGEGLEGEMSMDAFNYVNHRTRNN-----------LDPIIVHSS 464
Cdd:PHA02747  165 KYILT-LIEITDKILKDS------RKISHFQCSEWFEDETPSDHPDFIKFIKIIDINRKKsgklfnpkdalLCPIVVHCS 237

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 465 LGTGRACAFVGAEY-MFQMINTKKCGTARFFQvDFRTKRLGALQNGKQLFWVQNMAFELL 523
Cdd:PHA02747  238 DGVGKTGIFCAVDIcLNQLVKRKAICLAKTAE-KIREQRHAGIMNFDDYLFIQPGYEVLH 296
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 298-528 7.60e-09

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: 57.31  E-value: 7.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 298 DDTHFIHAS--TVTAPGKEYigKAIICQAPFddkekghPDTRESFWRMVWDTRATYVVMCCQIMENGVQKCGRYFPD--E 373
Cdd:cd14599    63 NNTGYINAShiKVTVGGEEW--HYIATQGPL-------PHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKlgS 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 374 TGATENYGFAEVqllekhemlnghllTRKIELTSGTW-------KH--SDDDppiRTITHFQFLKWKEG---EGLEGEMS 441
Cdd:cd14599   134 KHSSATYGKFKV--------------TTKFRTDSGCYattglkvKHllSGQE---RTVWHLQYTDWPDHgcpEEVQGFLS 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 442 -MDAFNYVNHRTRNNLD-------PIIVHSSLGTGRACAFVGAEYMFQMINTKKCGTARFFQVDFRTKRLGALQNGKQLF 513
Cdd:cd14599   197 yLEEIQSVRRHTNSMLDstkncnpPIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYK 276

                         250
                  ....*....|....*
gi 1831510059 514 WVqnmaFELLIKKLK 528
Cdd:cd14599   277 FV----YQVLIQFLK 287
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 298-522 1.24e-08

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: 56.00  E-value: 1.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 298 DDTHFIHASTVTapGKEYIGKAIICQAPFddkekghPDTRESFWRMVWDTRATYVVMCCQIMENGVQKCGRYFPdETGaT 377
Cdd:cd14602    24 EDSDYINANFIK--GVYGPRAYIATQGPL-------STTLLDFWRMIWEYSVLIIVMACMEFEMGKKKCERYWA-EPG-E 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 378 ENYGFAEVQLLEKHEMLNGHLLTRKIELTSGTwkhsdddpPIRTITHFQFLKWKEGEGLEG-EMSMDAFNYVNHRTRNNL 456
Cdd:cd14602    93 MQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNS--------ETRTIYQFHYKNWPDHDVPSSiDPILELIWDVRCYQEDDS 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1831510059 457 DPIIVHSSLGTGRACAFVGAEYMFQMINTK---KCGTARFFQVDFRTKRLGALQNGKQLFWVQNMAFEL 522
Cdd:cd14602   165 VPICIHCSAGCGRTGVICAIDYTWMLLKDGiipENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIEL 233
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 320-475 3.10e-08

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: 54.25  E-value: 3.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 320 IICQAPFddkekghPDTRESFWRMVWDTRATYVVMCCQIMENGVQKCgrYFPDETGATENYGFaEVQLLEKHEMLNG--- 396
Cdd:cd14550    17 IITQHPL-------EHTIKDFWQMIWDHNSQTIVMLTDNELNEDEPI--YWPTKEKPLECETF-KVTLSGEDHSCLSnei 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 397 HLLTRKIELTSgtwKHSDDDPPIRtitHFQFLKWKEgeglEGEMSMDAFNYVNH---RTRNNLDPIIVHSSLGTGRACAF 473
Cdd:cd14550    87 RLIVRDFILES---TQDDYVLEVR---QFQCPSWPN----PCSPIHTVFELINTvqeWAQQRDGPIVVHDRYGGVQAATF 156


                  ..
gi 1831510059 474 VG 475
Cdd:cd14550   157 CA 158
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 335-474 1.12e-06

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: 50.25  E-value: 1.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 335 DTRESFWRMVWDTRATYVVMCCQIMENGvQKCGRYFPDETGATENygfaeVQLLEKHEMLNGHLLTRKIELTSGTWKhsd 414
Cdd:cd14613    81 NTVGDFWRMVWQERSPIIVMITNIEEMN-EKCTEYWPEEQVTYEG-----IEITVKQVIHADDYRLRLITLKSGGEE--- 151

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1831510059 415 ddppiRTITHFQFLKWKEGEG-----------LEGEMSMdafnyvnHRTRNNLDPIIVHSSLGTGRACAFV 474
Cdd:cd14613   152 -----RGLKHYWYTSWPDQKTpdnappllqlvQEVEEAR-------QQAEPNCGPVIVHCSAGIGRTGCFI 210
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 335-517 1.51e-05

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: 46.45  E-value: 1.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 335 DTRESFWRMVWDTRATYVVMCCQIMENGvQKCGRYFPDETGAtenYGFAEVQLLEKHEMlnGHLLTRKIELTSGTwkHSd 414
Cdd:cd14611    55 NTVNDFWQMVWQEDSPVIVMITKLKEKN-EKCVLYWPEKRGI---YGKVEVLVNSVKEC--DNYTIRNLTLKQGS--QS- 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 415 ddppiRTITHFQFLKWKEGEGLEGEMSMDAFNYVNHRTRNNL---DPIIVHSSLGTGRACAFVGAEYMFQMINTKKCGTA 491
Cdd:cd14611   126 -----RSVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRLASpgrGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDV 200

                         170       180
                  ....*....|....*....|....*.
gi 1831510059 492 RFFQVDFRTKRLGALQNGKQLFWVQN 517
Cdd:cd14611   201 LSIVCQLRVDRGGMVQTSEQYEFVHH 226
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 333-473 3.91e-05

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: 44.98  E-value: 3.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 333 HP--DTRESFWRMVWDTRATYVVMCCQiMENGVQKCGRYFPDETGATENYGFAEVQLLEKHEMLNGHlltRKIELTSGTW 410
Cdd:cd17669    21 HPllHTIKDFWRMIWDHNAQLIVMLPD-GQNMAEDEFVYWPNKDEPINCETFKVTLIAEEHKCLSNE---EKLIIQDFIL 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1831510059 411 KHSDDDpPIRTITHFQFLKWKEGEGLEGEmSMDAFNYVNHRTRNNLDPIIVHSSLG---TGRACAF 473
Cdd:cd17669    97 EATQDD-YVLEVRHFQCPKWPNPDSPISK-TFELISIIKEEAANRDGPMIVHDEHGgvtAGTFCAL 160
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 334-483 1.44e-04

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: 43.36  E-value: 1.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 334 PDTRESFWRMVWDTRATYVVMCCQIME-NGVQKCGRYFPDEtgATENYGFAEVQLLEKheMLNGHLLTRKIELTSGTwKH 412
Cdd:cd14637    24 QNTTTDFWRLVYDYGCTSVVMLNQLNQsNSAWPCLQYWPEP--GLQQYGPMEVEFVSG--SADEDIVTRLFRVQNIT-RL 98

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1831510059 413 SDDDPPIRtitHFQFLKWKEGEglEGEMSMDAF----NYVNHRTRNNLD-PIIVHSSLGTGRACAFVGAEYMFQMI 483
Cdd:cd14637    99 QEGHLMVR---HFQFLRWSAYR--DTPDSKKAFlhllASVEKWQRESGEgRTVVHCLNGGGRSGTYCASAMILEMI 169
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 320-430 9.19e-04

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: 41.16  E-value: 9.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510059 320 IICQAPFddkekghPDTRESFWRMVWDTRATYVVMCCQImeNGVQKCGRYFPDETGATenYGFAEVQLLEKHemLNGHLL 399
Cdd:cd14634    17 IVTQHPL-------PNTVADFWRLVFDYNCSSVVMLNEM--DAAQLCMQYWPEKTSCC--YGPIQVEFVSAD--IDEDII 83

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1831510059 400 TRKIELTSgtwkHSDDDPPIRTITHFQFLKW 430
Cdd:cd14634    84 SRIFRICN----MARPQDGYRIVQHLQYIGW 110
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 320-388 3.63e-03

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: 39.24  E-value: 3.63e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1831510059 320 IICQAPFddkekghPDTRESFWRMVWDTRATYVVMCCQImeNGVQKCGRYFPDEtgATENYGFAEVQLL 388
Cdd:cd14636    17 IVTQHPL-------PNTVKDFWRLVYDYGCTSIVMLNEV--DLAQGCPQYWPEE--GMLRYGPIQVECM 74
 
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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