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Conserved domains on  [gi|1907067820|ref|XP_036018686|]
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tyrosine-protein phosphatase non-receptor type 18 isoform X1 [Mus musculus]

Protein Classification

protein-tyrosine phosphatase family protein( domain architecture ID 1000023)

cys-based protein-tyrosine phosphatase (PTP) family protein may be a PTP or a dual-specificity phosphatase (DUSP or DSP), and may catalyze the dephosphorylation of target phosphoproteins at tyrosine or tyrosine and serine/threonine residues, respectively

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTP_DSP_cys super family cl28904
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 27-292 5.09e-172

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


The actual alignment was detected with superfamily member cd14603:

Pssm-ID: 475123 [Multi-domain]  Cd Length: 266  Bit Score: 482.40  E-value: 5.09e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  27 AREFSDIKARSVAWKSEGVCSTKAGSRLGNTNKNRYKDVVAYDETRVILSLLQEEGHGDYINANFIRGIDGSQAYIATQG 106
Cdd:cd14603     1 AGEFSEIRACSAAFKADYVCSTVAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 107 PLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWAREQEPLKAGPFCITLTKETTLNADITLRTLQVTFQKEFRS 186
Cdd:cd14603    81 PLSHTVLDFWRMIWQYGVKVILMACREIEMGKKKCERYWAQEQEPLQTGPFTITLVKEKRLNEEVILRTLKVTFQKESRS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 187 VHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPNFSLFQVVLE 266
Cdd:cd14603   161 VSHFQYMAWPDHGIPDSPDCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPDFSIFDVVLE 240

                         250       260
                  ....*....|....*....|....*.
gi 1907067820 267 MRKQRPAAVQTEEQYRFLYHTVAQLF 292
Cdd:cd14603   241 MRKQRPAAVQTEEQYEFLYHTVAQMF 266
PRK12323 super family cl46901
DNA polymerase III subunit gamma/tau;
331-428 5.95e-03

DNA polymerase III subunit gamma/tau;


The actual alignment was detected with superfamily member PRK14951:

Pssm-ID: 481241 [Multi-domain]  Cd Length: 618  Bit Score: 38.93  E-value: 5.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 331 RPPGGVLRSI-SVPAPPTLPMADTYAVVQKRGASAGTGPGPRAPTSTDTPIYSQVA---PRAQRPVAHTEDAQGTTALRR 406
Cdd:PRK14951  365 KPAAAAEAAApAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAappAPVAAPAAAAPAAAPAAAPAA 444

                          90       100
                  ....*....|....*....|..
gi 1907067820 407 VPADQNSSGPDAYEEVTDGAQT 428
Cdd:PRK14951  445 VALAPAPPAQAAPETVAIPVRV 466
 
Name Accession Description Interval E-value
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 27-292 5.09e-172

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: 482.40  E-value: 5.09e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  27 AREFSDIKARSVAWKSEGVCSTKAGSRLGNTNKNRYKDVVAYDETRVILSLLQEEGHGDYINANFIRGIDGSQAYIATQG 106
Cdd:cd14603     1 AGEFSEIRACSAAFKADYVCSTVAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 107 PLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWAREQEPLKAGPFCITLTKETTLNADITLRTLQVTFQKEFRS 186
Cdd:cd14603    81 PLSHTVLDFWRMIWQYGVKVILMACREIEMGKKKCERYWAQEQEPLQTGPFTITLVKEKRLNEEVILRTLKVTFQKESRS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 187 VHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPNFSLFQVVLE 266
Cdd:cd14603   161 VSHFQYMAWPDHGIPDSPDCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPDFSIFDVVLE 240

                         250       260
                  ....*....|....*....|....*.
gi 1907067820 267 MRKQRPAAVQTEEQYRFLYHTVAQLF 292
Cdd:cd14603   241 MRKQRPAAVQTEEQYEFLYHTVAQMF 266
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
56-290 6.31e-108

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 318.03  E-value: 6.31e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  56 NTNKNRYKDVVAYDETRVILSllQEEGHGDYINANFIRGIDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETE 135
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLT--GDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 136 NGRRKCERYWAREQE-PLKAGPFCITLTKETTLNADITLRTLQVTF--QKEFRSVHQLQYMSWPDHGVPSSSDHILTMVE 212
Cdd:pfam00102  79 KGREKCAQYWPEEEGeSLEYGDFTVTLKKEKEDEKDYTVRTLEVSNggSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907067820 213 EARCLQGLGP-GPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFQVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 290
Cdd:pfam00102 159 KVRKSSLDGRsGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGE---VDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
26-290 1.34e-107

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 318.45  E-value: 1.34e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820   26 LAREFSDIKARSVawkseGVCSTKAGSRLGNTNKNRYKDVVAYDETRVILSLLQEEGHgDYINANFIRGIDGSQAYIATQ 105
Cdd:smart00194   2 LEEEFEKLDRLKP-----DDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGS-DYINASYIDGPNGPKAYIATQ 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  106 GPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWAREQ-EPLKAGPFCITLTKETTLnADITLRTLQVTFQKEF 184
Cdd:smart00194  76 GPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEgEPLTYGDITVTLKSVEKV-DDYTIRTLEVTNTGCS 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  185 --RSVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQtipPNFSLFQ 262
Cdd:smart00194 155 etRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAG---KEVDIFE 231

                          250       260
                   ....*....|....*....|....*...
gi 1907067820  263 VVLEMRKQRPAAVQTEEQYRFLYHTVAQ 290
Cdd:smart00194 232 IVKELRSQRPGMVQTEEQYIFLYRAILE 259
PHA02738 PHA02738
hypothetical protein; Provisional
 11-288 1.90e-48

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 168.18  E-value: 1.90e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  11 FLEQLEARDYREgaILAREFSDIkarsVAWKSEGVCStkagSRLGNTNKNRYKDVVAYDETRVILSllQEEGHGDYINAN 90
Cdd:PHA02738   14 FLALMEKSDCEE--VITREHQKV----ISEKVDGTFN----AEKKNRKLNRYLDAVCFDHSRVILP--AERNRGDYINAN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  91 FIRGIDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWAR-EQEPLKAGPFCITLTKETTLNA 169
Cdd:PHA02738   82 YVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDvEQGSIRFGKFKITTTQVETHPH 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 170 DITlRTLQVTFQKE-FRSVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQ-------------GLGPGPLCVHCSAGCGR 235
Cdd:PHA02738  162 YVK-STLLLTDGTSaTQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRQCQkelaqeslqighnRLQPPPIVVHCNAGLGR 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907067820 236 TGVLCAVDY-VRQLLLTQTIppnfSLFQVVLEMRKQRPAAVQTEEQYRFLYHTV 288
Cdd:PHA02738  241 TPCYCVVDIsISRFDACATV----SIPSIVSSIRNQRYYSLFIPFQYFFCYRAV 290
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
54-284 7.16e-44

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 154.86  E-value: 7.16e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  54 LGNTNKNRYKDVVAYDETRVilsllQEEGhgDYINANFIRGIDGSQaYIATQGPLPHTLLDFWRLVWEFGVKVI--LMAC 131
Cdd:COG5599    40 INGSPLNRFRDIQPYKETAL-----RANL--GYLNANYIQVIGNHR-YIATQYPLEEQLEDFFQMLFDNNTPVLvvLASD 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 132 QETENGRRKCERYWaREQEplKAGPFCI--TLTKETTLNADITLRTLQVTFQ---KEFRSVHQLQYMSWPDHGVPSSS-- 204
Cdd:COG5599   112 DEISKPKVKMPVYF-RQDG--EYGKYEVssELTESIQLRDGIEARTYVLTIKgtgQKKIEIPVLHVKNWPDHGAISAEal 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 205 -DHILTMVEEARCLQGLGpGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIpPNFSLFQVVLEMRKQR-PAAVQTEEQYR 282
Cdd:COG5599   189 kNLADLIDKKEKIKDPDK-LLPVVHCRAGVGRTGTLIACLALSKSINALVQ-ITLSVEEIVIDMRTSRnGGMVQTSEQLD 266


                  ..
gi 1907067820 283 FL 284
Cdd:COG5599   267 VL 268
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 331-428 5.95e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 38.93  E-value: 5.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 331 RPPGGVLRSI-SVPAPPTLPMADTYAVVQKRGASAGTGPGPRAPTSTDTPIYSQVA---PRAQRPVAHTEDAQGTTALRR 406
Cdd:PRK14951  365 KPAAAAEAAApAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAappAPVAAPAAAAPAAAPAAAPAA 444

                          90       100
                  ....*....|....*....|..
gi 1907067820 407 VPADQNSSGPDAYEEVTDGAQT 428
Cdd:PRK14951  445 VALAPAPPAQAAPETVAIPVRV 466
 
Name Accession Description Interval E-value
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 27-292 5.09e-172

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: 482.40  E-value: 5.09e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  27 AREFSDIKARSVAWKSEGVCSTKAGSRLGNTNKNRYKDVVAYDETRVILSLLQEEGHGDYINANFIRGIDGSQAYIATQG 106
Cdd:cd14603     1 AGEFSEIRACSAAFKADYVCSTVAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 107 PLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWAREQEPLKAGPFCITLTKETTLNADITLRTLQVTFQKEFRS 186
Cdd:cd14603    81 PLSHTVLDFWRMIWQYGVKVILMACREIEMGKKKCERYWAQEQEPLQTGPFTITLVKEKRLNEEVILRTLKVTFQKESRS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 187 VHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPNFSLFQVVLE 266
Cdd:cd14603   161 VSHFQYMAWPDHGIPDSPDCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPDFSIFDVVLE 240

                         250       260
                  ....*....|....*....|....*.
gi 1907067820 267 MRKQRPAAVQTEEQYRFLYHTVAQLF 292
Cdd:cd14603   241 MRKQRPAAVQTEEQYEFLYHTVAQMF 266
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 86-286 9.41e-124

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: 357.12  E-value: 9.41e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  86 YINANFIRGIDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWAREQEP-LKAGPFCITLTKE 164
Cdd:cd14542     1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEqLQFGPFKISLEKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 165 TTLNADITLRTLQVTFQKEFRSVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDY 244
Cdd:cd14542    81 KRVGPDFLIRTLKVTFQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGCGRTGTICAIDY 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1907067820 245 VRQLLLTQTIPPNFSLFQVVLEMRKQRPAAVQTEEQYRFLYH 286
Cdd:cd14542   161 VWNLLKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVYR 202
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 59-292 5.54e-113

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: 331.03  E-value: 5.54e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  59 KNRYKDVVAYDETRVILSLLQEEGHGDYINANFIRGIDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGR 138
Cdd:cd14602     1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 139 RKCERYWARE-QEPLKAGPFCITLTKETTLNaDITLRTLQVTFQKEFRSVHQLQYMSWPDHGVPSSSDHILTMVEEARCL 217
Cdd:cd14602    81 KKCERYWAEPgEMQLEFGPFSVTCEAEKRKS-DYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCY 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907067820 218 QGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPNFSLFQVVLEMRKQRPAAVQTEEQYRFLYHTVAQLF 292
Cdd:cd14602   160 QEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIELF 234
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 6-296 3.03e-108

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: 321.50  E-value: 3.03e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820   6 DLVRSFLEQLEA---RDYREGAILAREFSDIKARSVAWKSEGVCSTKAGSRLGNTNKNRYKDVVAYDETRVILSLLQEEG 82
Cdd:cd14604     4 EILKKFIERVQAmksTDHNGEDNFASDFMRLRRLSTKYRTEKIYPTATGEKEENVKKNRYKDILPFDHSRVKLTLKTSSQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  83 HGDYINANFIRGIDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWARE-QEPLKAGPFCITL 161
Cdd:cd14604    84 DSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWPLYgEEPMTFGPFRISC 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 162 TKETTLNaDITLRTLQVTFQKEFRSVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGPGPLCVHCSAGCGRTGVLCA 241
Cdd:cd14604   164 EAEQART-DYFIRTLLLEFQNETRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICA 242

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907067820 242 VDYVRQLLLTQTIPPNFSLFQVVLEMRKQRPAAVQTEEQYRFLYHTVAQLFSRTL 296
Cdd:cd14604   243 IDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQLFEKQL 297
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
56-290 6.31e-108

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 318.03  E-value: 6.31e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  56 NTNKNRYKDVVAYDETRVILSllQEEGHGDYINANFIRGIDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETE 135
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLT--GDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 136 NGRRKCERYWAREQE-PLKAGPFCITLTKETTLNADITLRTLQVTF--QKEFRSVHQLQYMSWPDHGVPSSSDHILTMVE 212
Cdd:pfam00102  79 KGREKCAQYWPEEEGeSLEYGDFTVTLKKEKEDEKDYTVRTLEVSNggSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907067820 213 EARCLQGLGP-GPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFQVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 290
Cdd:pfam00102 159 KVRKSSLDGRsGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGE---VDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
26-290 1.34e-107

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 318.45  E-value: 1.34e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820   26 LAREFSDIKARSVawkseGVCSTKAGSRLGNTNKNRYKDVVAYDETRVILSLLQEEGHgDYINANFIRGIDGSQAYIATQ 105
Cdd:smart00194   2 LEEEFEKLDRLKP-----DDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGS-DYINASYIDGPNGPKAYIATQ 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  106 GPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWAREQ-EPLKAGPFCITLTKETTLnADITLRTLQVTFQKEF 184
Cdd:smart00194  76 GPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEgEPLTYGDITVTLKSVEKV-DDYTIRTLEVTNTGCS 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  185 --RSVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQtipPNFSLFQ 262
Cdd:smart00194 155 etRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAG---KEVDIFE 231

                          250       260
                   ....*....|....*....|....*...
gi 1907067820  263 VVLEMRKQRPAAVQTEEQYRFLYHTVAQ 290
Cdd:smart00194 232 IVKELRSQRPGMVQTEEQYIFLYRAILE 259
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 86-286 3.15e-91

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: 274.16  E-value: 3.15e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  86 YINANFIRGIDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWAREQE-PLKAGPFCITLTKE 164
Cdd:cd00047     1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGkPLEYGDITVTLVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 165 TTLNaDITLRTLQVTFQK--EFRSVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGPGPLCVHCSAGCGRTGVLCAV 242
Cdd:cd00047    81 EELS-DYTIRTLELSPKGcsESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTGTFIAI 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1907067820 243 DYVRQLLLTQTIPpnfSLFQVVLEMRKQRPAAVQTEEQYRFLYH 286
Cdd:cd00047   160 DILLERLEAEGEV---DVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 61-285 9.39e-76

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: 235.71  E-value: 9.39e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  61 RYKDVVAYDETRVILSLLQEEGHGDYINANFIRGIDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRK 140
Cdd:cd14548     1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 141 CERYWAREQEPLKAGPFCITLTKETTLnADITLRTLQVTFQKEFRSVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGL 220
Cdd:cd14548    81 CDHYWPFDQDPVYYGDITVTMLSESVL-PDWTIREFKLERGDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDYIKQ 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907067820 221 GPGPLCVHCSAGCGRTGVLCAVDY-VRQLLLTQTIPPnfslFQVVLEMRKQRPAAVQTEEQYRFLY 285
Cdd:cd14548   160 EKGPTIVHCSAGVGRTGTFIALDRlLQQIESEDYVDI----FGIVYDLRKHRPLMVQTEAQYIFLH 221
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 86-286 4.06e-73

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: 228.29  E-value: 4.06e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  86 YINANFIRGIDGSQ-AYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWAREQEPLKAGPFCITLTKE 164
Cdd:cd18533     1 YINASYITLPGTSSkRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGEYGDLTVELVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 165 TTLN-ADITLRTLQVTF-QKEFRSVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGP--GPLCVHCSAGCGRTGVLC 240
Cdd:cd18533    81 EENDdGGFIVREFELSKeDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNDSASldPPIIVHCSAGVGRTGTFI 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907067820 241 AVDYVRQLL---LTQTIPPNFSL---FQVVLEMRKQRPAAVQTEEQYRFLYH 286
Cdd:cd18533   161 ALDSLLDELkrgLSDSQDLEDSEdpvYEIVNQLRKQRMSMVQTLRQYIFLYD 212
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 28-285 3.78e-72

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: 228.02  E-value: 3.78e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  28 REFSDIKARSVAWKSEgvCSTKAGsrlgNTNKNRYKDVVAYDETRVILSLLQEEGHGDYINANFIRGIDGSQAYIATQGP 107
Cdd:cd14543     7 EEYEDIRREPPAGTFL--CSLAPA----NQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 108 LPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWAREQEP-LKAGPFCITlTKETTLNADITLRTLQV----TFQK 182
Cdd:cd14543    81 LPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSsLRYGDLTVT-NLSVENKEHYKKTTLEIhnteTDES 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 183 efRSVHQLQYMSWPDHGVPSSSDHILTMVEE-----ARCLQGLGPG--------PLCVHCSAGCGRTGVLCAVDY-VRQL 248
Cdd:cd14543   160 --RQVTHFQFTSWPDFGVPSSAAALLDFLGEvrqqqALAVKAMGDRwkghppgpPIVVHCSAGIGRTGTFCTLDIcLSQL 237

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1907067820 249 LLTQTIppnfSLFQVVLEMRKQRPAAVQTEEQYRFLY 285
Cdd:cd14543   238 EDVGTL----NVMQTVRRMRTQRAFSIQTPDQYYFCY 270
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 56-290 2.23e-66

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


Pssm-ID: 350392 [Multi-domain]  Cd Length: 251  Bit Score: 212.32  E-value: 2.23e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  56 NTNKNRYKDVVAYDETRVILSLLQEEGHG-DYINANFIR-------GIDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVI 127
Cdd:cd14544     1 NKGKNRYKNILPFDHTRVILKDRDPNVPGsDYINANYIRnenegptTDENAKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 128 LMACQETENGRRKCERYWAREQEPLKAGPFCITLTKETTlNADITLRTLQVTFQKEF---RSVHQLQYMSWPDHGVPSSS 204
Cdd:cd14544    81 VMTTKEVERGKNKCVRYWPDEGMQKQYGPYRVQNVSEHD-TTDYTLRELQVSKLDQGdpiREIWHYQYLSWPDHGVPSDP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 205 DHILTMVEEARCLQG--LGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPNFSLFQVVLEMRKQRPAAVQTEEQYR 282
Cdd:cd14544   160 GGVLNFLEDVNQRQEslPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLDCDIDIQKTIQMVRSQRSGMVQTEAQYK 239


                  ....*...
gi 1907067820 283 FLYHTVAQ 290
Cdd:cd14544   240 FIYVAVAQ 247
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 56-285 5.96e-65

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: 208.40  E-value: 5.96e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  56 NTNKNRYKDVVAYDETRVILSLLQEEGHGDYINANFIRGIDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETE 135
Cdd:cd14553     3 NKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 136 NGRRKCERYW-AREQEplKAGPFCITLTKETTLnADITLRTLQV--TFQKEFRSVHQLQYMSWPDHGVPsssDHILTMVE 212
Cdd:cd14553    83 RSRVKCDQYWpTRGTE--TYGLIQVTLLDTVEL-ATYTVRTFALhkNGSSEKREVRQFQFTAWPDHGVP---EHPTPFLA 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907067820 213 EARCLQGLGP---GPLCVHCSAGCGRTGVLCAVD-YVRQLLLTQTIppnfSLFQVVLEMRKQRPAAVQTEEQYRFLY 285
Cdd:cd14553   157 FLRRVKACNPpdaGPIVVHCSAGVGRTGCFIVIDsMLERIKHEKTV----DIYGHVTCLRAQRNYMVQTEDQYIFIH 229
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 60-288 7.29e-64

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: 205.51  E-value: 7.29e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  60 NRYKDVVAYDETRVILSLLQEEGHGDYINANFIRGIDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRR 139
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 140 KCERYWAREQEPLKAGPFCITLTKETTLNaDITLR--TLQVTFQKEFRSVHQLQYMSWPDHGVPSSSDHILTMVEEAR-- 215
Cdd:cd14619    81 KCEHYWPLDYTPCTYGHLRVTVVSEEVME-NWTVRefLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRqw 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907067820 216 CLQGLGPGPLCVHCSAGCGRTGVLCAVDY-VRQLLLTQTIPPnfslFQVVLEMRKQRPAAVQTEEQYRFLYHTV 288
Cdd:cd14619   160 LDQTMSGGPTVVHCSAGVGRTGTLIALDVlLQQLQSEGLLGP----FSFVQKMRENRPLMVQTESQYVFLHQCI 229
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 60-286 2.34e-63

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: 203.78  E-value: 2.34e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  60 NRYKDVVAYDETRVILSLLQEEGHGDYINANFIRGIDG-SQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENgR 138
Cdd:cd14547     1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYDGeEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA-K 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 139 RKCERYWArEQEPLKAGPFCITL--TKETTlnaDITLRTLQVTFQKEFRSVHQLQYMSWPDHGVPSSSDHILTM---VEE 213
Cdd:cd14547    80 EKCAQYWP-EEENETYGDFEVTVqsVKETD---GYTVRKLTLKYGGEKRYLKHYWYTSWPDHKTPEAAQPLLSLvqeVEE 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907067820 214 ARcLQGLGPGPLCVHCSAGCGRTGVLCAVDY-VRQLLLTQTIppnfSLFQVVLEMRKQRPAAVQTEEQYRFLYH 286
Cdd:cd14547   156 AR-QTEPHRGPIVVHCSAGIGRTGCFIATSIgCQQLREEGVV----DVLGIVCQLRLDRGGMVQTAEQYEFVHR 224
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 60-285 1.61e-61

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: 199.40  E-value: 1.61e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  60 NRYKDVVAYDETRVILSLLQEEGHGDYINANFIRGIDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRR 139
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 140 KCERYWAREQEPLKAGPFCITLTKETTLNaDITLRTLQV---TFQKEfRSVHQLQYMSWPDHGVPSSSDHILTMVEEAR- 215
Cdd:cd14618    81 LCDHYWPSESTPVSYGHITVHLLAQSSED-EWTRREFKLwheDLRKE-RRVKHLHYTAWPDHGIPESTSSLMAFRELVRe 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907067820 216 -CLQGLGPGPLCVHCSAGCGRTGVLCAVD-YVRQLLLTQTIppnfSLFQVVLEMRKQRPAAVQTEEQYRFLY 285
Cdd:cd14618   159 hVQATKGKGPTLVHCSAGVGRSGTFIALDrLLRQLKEEKVV----DVFNTVYILRMHRYLMIQTLSQYIFLH 226
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 86-290 7.03e-61

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: 196.83  E-value: 7.03e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  86 YINANFIR-GIDGSQ-AYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWARE-QEPL-KAGPFCITL 161
Cdd:cd14538     1 YINASHIRiPVGGDTyHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSlNKPLiCGGRLEVSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 162 TKETTLNaDITLRTLQVTFQK--EFRSVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQglGPGPLCVHCSAGCGRTGVL 239
Cdd:cd14538    81 EKYQSLQ-DFVIRRISLRDKEtgEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIH--NSGPIVVHCSAGIGRTGVL 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907067820 240 CAVDYVrQLLLTQTIPpnFSLFQVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 290
Cdd:cd14538   158 ITIDVA-LGLIERDLP--FDIQDIVKDLREQRQGMIQTKDQYIFCYKACLE 205
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 86-285 6.29e-60

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: 194.11  E-value: 6.29e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  86 YINANFIRGIDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWAREQEPlKAGPFCITLtKET 165
Cdd:cd14549     1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTE-TYGNIQVTL-LST 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 166 TLNADITLRTLQVTFQK--------EFRSVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGPGPLCVHCSAGCGRTG 237
Cdd:cd14549    79 EVLATYTVRTFSLKNLKlkkvkgrsSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVGRTG 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1907067820 238 VLCAVD-YVRQLLLTQTIppnfSLFQVVLEMRKQRPAAVQTEEQYRFLY 285
Cdd:cd14549   159 TYIVIDsMLQQIQDKGTV----NVFGFLKHIRTQRNYLVQTEEQYIFIH 203
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 47-290 1.18e-59

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: 195.48  E-value: 1.18e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  47 STKAGSRLGNTNKNRYKDVVAYDETRVILSLLQEEGHG-DYINANFIR----GIDGSQ-AYIATQGPLPHTLLDFWRLVW 120
Cdd:cd14606     9 QRLEGQRPENKSKNRYKNILPFDHSRVILQGRDSNIPGsDYINANYVKnqllGPDENAkTYIASQGCLEATVNDFWQMAW 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 121 EFGVKVILMACQETENGRRKCERYWAREQEPLKAGPFCITLTKETTlNADITLRTLQVTF---QKEFRSVHQLQYMSWPD 197
Cdd:cd14606    89 QENSRVIVMTTREVEKGRNKCVPYWPEVGMQRAYGPYSVTNCGEHD-TTEYKLRTLQVSPldnGELIREIWHYQYLSWPD 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 198 HGVPSSSDHILTMVEEARCLQGLGP--GPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPNFSLFQVVLEMRKQRPAAV 275
Cdd:cd14606   168 HGVPSEPGGVLSFLDQINQRQESLPhaGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLDCDIDIQKTIQMVRAQRSGMV 247

                         250
                  ....*....|....*
gi 1907067820 276 QTEEQYRFLYHTVAQ 290
Cdd:cd14606   248 QTEAQYKFIYVAIAQ 262
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 60-284 3.83e-59

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: 193.11  E-value: 3.83e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  60 NRYKDVVAYDETRVILSLlQEEGHGDYINANFIRGIDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRR 139
Cdd:cd14615     1 NRYNNVLPYDISRVKLSV-QSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 140 KCERYWAREQePLKAGPFCITLTKETTLnADITLRTLQVTFQK--EFRSVHQLQYMSWPDHGVPSSSDHILTMVEEAR-- 215
Cdd:cd14615    80 KCEEYWPSKQ-KKDYGDITVTMTSEIVL-PEWTIRDFTVKNAQtnESRTVRHFHFTSWPDHGVPETTDLLINFRHLVRey 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 216 CLQGLGPGPLCVHCSAGCGRTGVLCAVDY-VRQLLLTQTIppnfSLFQVVLEMRKQRPAAVQTEEQYRFL 284
Cdd:cd14615   158 MKQNPPNSPILVHCSAGVGRTGTFIAIDRlIYQIENENVV----DVYGIVYDLRMHRPLMVQTEDQYVFL 223
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 41-284 6.83e-59

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: 193.91  E-value: 6.83e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  41 KSEGVCSTKAgsRLG-NTNKNRYKDVVAYDETRVILsllqeEGHGDYINANF----IRGIDGSQAYIATQGPLPHTLLDF 115
Cdd:cd14600    26 KKPGLAITCA--KLPqNMDKNRYKDVLPYDATRVVL-----QGNEDYINASYvnmeIPSANIVNKYIATQGPLPHTCAQF 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 116 WRLVWEFGVKVILMACQETENGRRKCERYWAREQEPLKAGPFCITLTKETTLNADITlRTLQVTFQK--EFRSVHQLQYM 193
Cdd:cd14600    99 WQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDPPDVMEYGGFRVQCHSEDCTIAYVF-REMLLTNTQtgEERTVTHLQYV 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 194 SWPDHGVPSSSDHILTMVEEARCLQgLGPGPLCVHCSAGCGRTGVLCAVDYVrqLLLTQTIPPNFSLfQVVLEMRKQRPA 273
Cdd:cd14600   178 AWPDHGVPDDSSDFLEFVNYVRSKR-VENEPVLVHCSAGIGRTGVLVTMETA--MCLTERNQPVYPL-DIVRKMRDQRAM 253

                         250
                  ....*....|.
gi 1907067820 274 AVQTEEQYRFL 284
Cdd:cd14600   254 MVQTSSQYKFV 264
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 56-288 1.27e-58

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: 192.41  E-value: 1.27e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  56 NTNKNRYKDVVAYDETRVILSLLQEEGHGDYINANFIRGIDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETE 135
Cdd:cd14614    12 NRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 136 NGRRKCERYWAREQEPLKAGPFCITLTKETTLNaDITLRTLQVTFQKEFRSVHQLQYMSWPDHGVPS--SSDHILTMVEE 213
Cdd:cd14614    92 KRRVKCDHYWPFTEEPVAYGDITVEMLSEEEQP-DWAIREFRVSYADEVQDVMHFNYTAWPDHGVPTanAAESILQFVQM 170

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907067820 214 ARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFQVVLEMRKQRPAAVQTEEQYRFLYHTV 288
Cdd:cd14614   171 VRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEF---VDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 242
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 60-285 1.95e-58

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: 191.29  E-value: 1.95e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  60 NRYKDVVAYDETRVILSLLQEEGHGDYINANFIRGIDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRR 139
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 140 KCERYWAREQEPLKAGPFCITLTKETTLnADITLRTLQVTFQKEFRS---VHQLQYMSWPDHGVPSSSDHILTMVEEARC 216
Cdd:cd14617    81 KCDHYWPADQDSLYYGDLIVQMLSESVL-PEWTIREFKICSEEQLDAprlVRHFHYTVWPDHGVPETTQSLIQFVRTVRD 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907067820 217 L--QGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTippNFSLFQVVLEMRKQRPAAVQTEEQYRFLY 285
Cdd:cd14617   160 YinRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKD---SVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 56-290 1.71e-57

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: 189.08  E-value: 1.71e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  56 NTNKNRYKDVVAYDETRVILSLLQEEGHGDYINANFIRGIDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETE 135
Cdd:cd14630     3 NRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 136 NGRRKCERYWAREQEPLkaGPFCITLTkETTLNADITLRTLqvTFQK----EFRSVHQLQYMSWPDHGVPSSSDHILTMV 211
Cdd:cd14630    83 VGRVKCVRYWPDDTEVY--GDIKVTLI-ETEPLAEYVIRTF--TVQKkgyhEIREIRQFHFTSWPDHGVPCYATGLLGFV 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907067820 212 EEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFQVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 290
Cdd:cd14630   158 RQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGV---VDIFNCVRELRAQRVNMVQTEEQYVFVHDAILE 233
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 56-288 5.47e-57

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: 187.73  E-value: 5.47e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  56 NTNKNRYKDVVAYDETRVilsLLQEEGhgDYINANFIRGIDGSQ--AYIATQGPLPHTLLDFWRLVWEFGVKVILMACQE 133
Cdd:cd14597     3 NRKKNRYKNILPYDTTRV---PLGDEG--GYINASFIKMPVGDEefVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 134 TENGRRKCERYWARE-------QEPLKagpfcITLTKETTL-NADITLRTLQVTFQKEFRSVHQLQYMSWPDHGVPSSSD 205
Cdd:cd14597    78 VEGGKIKCQRYWPEIlgkttmvDNRLQ-----LTLVRMQQLkNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPE 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 206 HILTMVEEARCLQGLgpGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTippNFSLFQVVLEMRKQRPAAVQTEEQYRFLY 285
Cdd:cd14597   153 QLLTFISYMRHIHKS--GPIITHCSAGIGRSGTLICIDVVLGLISKDL---DFDISDIVRTMRLQRHGMVQTEDQYIFCY 227


                  ...
gi 1907067820 286 HTV 288
Cdd:cd14597   228 QVI 230
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 5-290 4.27e-56

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: 186.78  E-value: 4.27e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820   5 TDLVRSfLEQLEARDyreGAILAREFSDIK-ARSVAWKSEGVCSTKAgsrlgntnKNRYKDVVAYDETRVILSLLQEEGH 83
Cdd:cd14626     1 SDLADN-IERLKAND---GLKFSQEYESIDpGQQFTWENSNLEVNKP--------KNRYANVIAYDHSRVILTSVDGVPG 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  84 GDYINANFIRGIDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYW-AREQEplKAGPFCITLT 162
Cdd:cd14626    69 SDYINANYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWpIRGTE--TYGMIQVTLL 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 163 KETTLnADITLRTLQV--TFQKEFRSVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGPGPLCVHCSAGCGRTGVLC 240
Cdd:cd14626   147 DTVEL-ATYSVRTFALykNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFI 225

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907067820 241 AVD-YVRQLLLTQTIppnfSLFQVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 290
Cdd:cd14626   226 VIDaMLERMKHEKTV----DIYGHVTCMRSQRNYMVQTEDQYIFIHEALLE 272
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 56-287 1.27e-55

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


Pssm-ID: 350402 [Multi-domain]  Cd Length: 238  Bit Score: 184.26  E-value: 1.27e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  56 NTNKNRYKDVVAYDETRVILSLLQEEGHGDYINANFIRGIDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETE 135
Cdd:cd14554     6 NKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKLRE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 136 NGRRKCERYWAREQEpLKAGPFCITLTKETTLNADItLRTLQVTFQK--EFRSVHQLQYMSWPDHGVPSSSDHIL---TM 210
Cdd:cd14554    86 MGREKCHQYWPAERS-ARYQYFVVDPMAEYNMPQYI-LREFKVTDARdgQSRTVRQFQFTDWPEQGVPKSGEGFIdfiGQ 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907067820 211 VEEARCLQGlGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFQVVLEMRKQRPAAVQTEEQYRFLYHT 287
Cdd:cd14554   164 VHKTKEQFG-QEGPITVHCSAGVGRTGVFITLSIVLERMRYEGV---VDVFQTVKLLRTQRPAMVQTEDQYQFCYRA 236
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 56-290 3.88e-55

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: 184.08  E-value: 3.88e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  56 NTNKNRYKDVVAYDETRVILSLL--QEEGHGDYINANFIRGIDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQE 133
Cdd:cd17667    27 NKHKNRYINILAYDHSRVKLRPLpgKDSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 134 TENGRRKCERYWAREQEPlKAGPFCITLtKETTLNADITLRTLQVTFQK-------------EFRSVHQLQYMSWPDHGV 200
Cdd:cd17667   107 VEKGRRKCDQYWPTENSE-EYGNIIVTL-KSTKIHACYTVRRFSIRNTKvkkgqkgnpkgrqNERTVIQYHYTQWPDMGV 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 201 PSSSDHILTMVEEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTippNFSLFQVVLEMRKQRPAAVQTEEQ 280
Cdd:cd17667   185 PEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKS---TVNVLGFLKHIRTQRNYLVQTEEQ 261

                         250
                  ....*....|
gi 1907067820 281 YRFLYHTVAQ 290
Cdd:cd17667   262 YIFIHDALLE 271
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 59-285 5.71e-55

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


Pssm-ID: 350393 [Multi-domain]  Cd Length: 231  Bit Score: 182.21  E-value: 5.71e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  59 KNRYKDVVAYDETRVILSLLQEEGhgDYINANFIRGIDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGR 138
Cdd:cd14545     1 LNRYRDRDPYDHDRSRVKLKQGDN--DYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 139 RKCERYWAREQEP---LKAGPFCITLTKETTlNADITLRTLQVTFQK--EFRSVHQLQYMSWPDHGVPSSSD---HILTM 210
Cdd:cd14545    79 IKCAQYWPQGEGNamiFEDTGLKVTLLSEED-KSYYTVRTLELENLKtqETREVLHFHYTTWPDFGVPESPAaflNFLQK 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907067820 211 VEEARCLQGlGPGPLCVHCSAGCGRTGVLCAVDYVrQLLLTQTIPPNFSLFQVVLEMRKQRPAAVQTEEQYRFLY 285
Cdd:cd14545   158 VRESGSLSS-DVGPPVVHCSAGIGRSGTFCLVDTC-LVLIEKGNPSSVDVKKVLLEMRKYRMGLIQTPDQLRFSY 230
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 55-290 1.43e-54

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: 181.57  E-value: 1.43e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  55 GNTNKNRYKDVVAYDETRVILSLLQ-EEGHGDYINANFIRGIDGS-QAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQ 132
Cdd:cd14612    14 GHASKDRYKTILPNPQSRVCLRRAGsQEEEGSYINANYIRGYDGKeKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITK 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 133 ETEnGRRKCERYWAREQEPLkaGPFCITLT--KETtlnADITLRTLQVTFQKEFRSVHQLQYMSWPDHGVPSSSD---HI 207
Cdd:cd14612    94 LKE-KKEKCVHYWPEKEGTY--GRFEIRVQdmKEC---DGYTIRDLTIQLEEESRSVKHYWFSSWPDHQTPESAGpllRL 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 208 LTMVEEARCLQGlGPGPLCVHCSAGCGRTGVLCAVDY-VRQLLLTQTIppnfSLFQVVLEMRKQRPAAVQTEEQYRFLYH 286
Cdd:cd14612   168 VAEVEESRQTAA-SPGPIVVHCSAGIGRTGCFIATSIgCQQLKDTGKV----DILGIVCQLRLDRGGMIQTSEQYQFLHH 242


                  ....
gi 1907067820 287 TVAQ 290
Cdd:cd14612   243 TLAL 246
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 85-283 2.72e-54

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: 179.83  E-value: 2.72e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  85 DYINANFIR-GIDGSQA---YIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWAREQEPLKAGPFCIT 160
Cdd:cd14541     1 DYINANYVNmEIPGSGIvnrYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGETMQFGNLQIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 161 LTKETTlNADITLRTLQVTFQK--EFRSVHQLQYMSWPDHGVPSSSDHILTMVEEAR-CLQGLGPgPLCVHCSAGCGRTG 237
Cdd:cd14541    81 CVSEEV-TPSFAFREFILTNTNtgEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRqNRVGMVE-PTVVHCSAGIGRTG 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1907067820 238 VLCAVDYVrqLLLTQTIPPNFSLfQVVLEMRKQRPAAVQTEEQYRF 283
Cdd:cd14541   159 VLITMETA--MCLIEANEPVYPL-DIVRTMRDQRAMLIQTPSQYRF 201
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 56-288 6.07e-53

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


Pssm-ID: 350453 [Multi-domain]  Cd Length: 253  Bit Score: 177.90  E-value: 6.07e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  56 NTNKNRYKDVVAYDETRVILSL--LQEEGhGDYINANFI--------RGIDGSQAYIATQGPLPHTLLDFWRLVWEFGVK 125
Cdd:cd14605     2 NKNKNRYKNILPFDHTRVVLHDgdPNEPV-SDYINANIImpefetkcNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 126 VILMACQETENGRRKCERYWAREQEPLKAGPFCITLTKETTLNaDITLRTL---QVTFQKEFRSVHQLQYMSWPDHGVPS 202
Cdd:cd14605    81 VIVMTTKEVERGKSKCVKYWPDEYALKEYGVMRVRNVKESAAH-DYILRELklsKVGQGNTERTVWQYHFRTWPDHGVPS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 203 SSDHILTMVEEARCLQG--LGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPNFSLFQVVLEMRKQRPAAVQTEEQ 280
Cdd:cd14605   160 DPGGVLDFLEEVHHKQEsiMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVDCDIDVPKTIQMVRSQRSGMVQTEAQ 239


                  ....*...
gi 1907067820 281 YRFLYHTV 288
Cdd:cd14605   240 YRFIYMAV 247
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 56-304 1.56e-51

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: 174.83  E-value: 1.56e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  56 NTNKNRYKDVVAYDETRVILsllqEEGHGDYINANFIRGIDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETE 135
Cdd:cd14608    25 NKNRNRYRDVSPFDHSRIKL----HQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVME 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 136 NGRRKCERYWAREQEplKAGPFCITLTKETTLNADI----TLRTLQVT--FQKEFRSVHQLQYMSWPDHGVPSSSDHILT 209
Cdd:cd14608   101 KGSLKCAQYWPQKEE--KEMIFEDTNLKLTLISEDIksyyTVRQLELEnlTTQETREILHFHYTTWPDFGVPESPASFLN 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 210 MVEEARCLQGLGP--GPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPNFSLFQVVLEMRKQRPAAVQTEEQYRFLYHT 287
Cdd:cd14608   179 FLFKVRESGSLSPehGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLA 258

                         250
                  ....*....|....*..
gi 1907067820 288 VAQLFSRTLQDTSPHYQ 304
Cdd:cd14608   259 VIEGAKFIMGDSSVQDQ 275
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 86-288 2.75e-51

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: 171.68  E-value: 2.75e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  86 YINANFIRGIDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWAREQEpLKAGPFCITLTKEt 165
Cdd:cd14552     1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGS-VSSGDITVELKDQ- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 166 TLNADITLRTLQVTFQKE--FRSVHQLQYMSWPDHGVPSSSDHILTMVEEA-RCLQGLGPGPLCVHCSAGCGRTGVLCAV 242
Cdd:cd14552    79 TDYEDYTLRDFLVTKGKGgsTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVqKQQQQSGNHPITVHCSAGAGRTGTFCAL 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1907067820 243 DYVRQLLLTQTIppnFSLFQVVLEMRKQRPAAVQTEEQYRFLYHTV 288
Cdd:cd14552   159 STVLERVKAEGV---LDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 86-288 3.01e-51

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: 171.85  E-value: 3.01e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  86 YINANFIRGIDGSQA--YIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWARE-QEPLKAGPFCITLT 162
Cdd:cd14596     1 YINASYITMPVGEEElfYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETlQEPMELENYQLRLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 163 KETTLNaDITLRTLQVTFQK--EFRSVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLgpGPLCVHCSAGCGRTGVLC 240
Cdd:cd14596    81 NYQALQ-YFIIRIIKLVEKEtgENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNT--GPIVVHCSAGIGRAGVLI 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1907067820 241 AVDYVRQLLLTQTippNFSLFQVVLEMRKQRPAAVQTEEQYRFLYHTV 288
Cdd:cd14596   158 CVDVLLSLIEKDL---SFNIKDIVREMRQQRYGMIQTKDQYLFCYKVV 202
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 86-290 1.47e-50

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


Pssm-ID: 350388 [Multi-domain]  Cd Length: 219  Bit Score: 170.33  E-value: 1.47e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  86 YINANFIR-GIDGSQA-YIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWAR---EQEPLKAGPFCIT 160
Cdd:cd14540     1 YINASHITaTVGGKQRfYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTlggEHDALTFGEYKVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 161 LTKETTlNADITLRTLQV--TFQKEFRSVHQLQYMSWPDHGVPSSSDHILTMVEEA-----RCLQGLG----PGPLCVHC 229
Cdd:cd14540    81 TKFSVS-SGCYTTTGLRVkhTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEInsvrrHTNQDVAghnrNPPTLVHC 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907067820 230 SAGCGRTGVLCAVDYVrQLLLTQTIPPNfsLFQVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 290
Cdd:cd14540   160 SAGVGRTGVVILADLM-LYCLDHNEELD--IPRVLALLRHQRMLLVQTLAQYKFVYNVLIQ 217
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 56-290 1.89e-49

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: 169.07  E-value: 1.89e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  56 NTNKNRYKDVVAYDETRVILSLLQEEGHGDYINANFIRGIDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETE 135
Cdd:cd14633    40 NRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVE 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 136 NGRRKCERYWAREQEPLKagPFCITLTkETTLNADITLRTLQVTFQ--KEFRSVHQLQYMSWPDHGVPSSSDHILTMVEE 213
Cdd:cd14633   120 VGRVKCCKYWPDDTEIYK--DIKVTLI-ETELLAEYVIRTFAVEKRgvHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQ 196

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907067820 214 ARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFQVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 290
Cdd:cd14633   197 VKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGV---VDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 270
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 60-285 3.83e-49

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: 167.01  E-value: 3.83e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  60 NRYKDVVAYDETRVilSLLQEEG--HGDYINANFIRGIDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENG 137
Cdd:cd14616     1 NRFPNIKPYNNNRV--KLIADAGvpGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 138 RRKCERYWAREQEPLKA-GPFCITLTKETTlNADITLRTLQVTFQKEFRSVHQLQYMSWPDHGVPSSSDHILTMVEEARC 216
Cdd:cd14616    79 RIRCHQYWPEDNKPVTVfGDIVITKLMEDV-QIDWTIRDLKIERHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVRA 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907067820 217 LQGLGPGPLCVHCSAGCGRTGVLCAVDYvrqllLTQTIPPN--FSLFQVVLEMRKQRPAAVQTEEQYRFLY 285
Cdd:cd14616   158 SRAHDNTPMIVHCSAGVGRTGVFIALDH-----LTQHINDHdfVDIYGLVAELRSERMCMVQNLAQYIFLH 223
PHA02738 PHA02738
hypothetical protein; Provisional
 11-288 1.90e-48

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 168.18  E-value: 1.90e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  11 FLEQLEARDYREgaILAREFSDIkarsVAWKSEGVCStkagSRLGNTNKNRYKDVVAYDETRVILSllQEEGHGDYINAN 90
Cdd:PHA02738   14 FLALMEKSDCEE--VITREHQKV----ISEKVDGTFN----AEKKNRKLNRYLDAVCFDHSRVILP--AERNRGDYINAN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  91 FIRGIDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWAR-EQEPLKAGPFCITLTKETTLNA 169
Cdd:PHA02738   82 YVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDvEQGSIRFGKFKITTTQVETHPH 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 170 DITlRTLQVTFQKE-FRSVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQ-------------GLGPGPLCVHCSAGCGR 235
Cdd:PHA02738  162 YVK-STLLLTDGTSaTQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRQCQkelaqeslqighnRLQPPPIVVHCNAGLGR 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907067820 236 TGVLCAVDY-VRQLLLTQTIppnfSLFQVVLEMRKQRPAAVQTEEQYRFLYHTV 288
Cdd:PHA02738  241 TPCYCVVDIsISRFDACATV----SIPSIVSSIRNQRYYSLFIPFQYFFCYRAV 290
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 56-288 2.39e-48

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


Pssm-ID: 350455 [Multi-domain]  Cd Length: 257  Bit Score: 165.91  E-value: 2.39e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  56 NTNKNRYKDVVAYDETRVILsllqEEGHGDYINANFIRGIDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETE 135
Cdd:cd14607    24 NRNRNRYRDVSPYDHSRVKL----QNTENDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVE 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 136 NGRRKCERYW-AREQEPL--KAGPFCITLTKEtTLNADITLRTLQVTFQK--EFRSVHQLQYMSWPDHGVPSSSDHILTM 210
Cdd:cd14607   100 KDSVKCAQYWpTDEEEVLsfKETGFSVKLLSE-DVKSYYTVHLLQLENINsgETRTISHFHYTTWPDFGVPESPASFLNF 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 211 ---VEEARCLqGLGPGPLCVHCSAGCGRTGVLCAVDYVrQLLLTQTIPPNFSLFQVVLEMRKQRPAAVQTEEQYRFLYHT 287
Cdd:cd14607   179 lfkVRESGSL-SPEHGPAVVHCSAGIGRSGTFSLVDTC-LVLMEKKDPDSVDIKQVLLDMRKYRMGLIQTPDQLRFSYMA 256


                  .
gi 1907067820 288 V 288
Cdd:cd14607   257 V 257
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 56-290 6.82e-48

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: 165.27  E-value: 6.82e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  56 NTNKNRYKDVVAYDETRVILSLLQEEGHGDYINANFIRGIDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETE 135
Cdd:cd14625    47 NKPKNRYANVIAYDHSRVILQPIEGIMGSDYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEE 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 136 NGRRKCERYW-AREQEPLkaGPFCITLTKETTLnADITLRT--LQVTFQKEFRSVHQLQYMSWPDHGVPSSSDHILTMVE 212
Cdd:cd14625   127 KSRIKCDQYWpSRGTETY--GMIQVTLLDTIEL-ATFCVRTfsLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLR 203

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907067820 213 EARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTippNFSLFQVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 290
Cdd:cd14625   204 RVKTCNPPDAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEK---TVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLE 278
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 56-285 1.76e-47

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: 164.52  E-value: 1.76e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  56 NTNKNRYKDVVAYDETRVILSLLQEEGHGDYINANFIRGIDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETE 135
Cdd:cd14628    52 NKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLRE 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 136 NGRRKCERYWAREQEPlKAGPFCITLTKETTLNADItLRTLQVTFQK--EFRSVHQLQYMSWPDHGVPSSSDHILTMVEE 213
Cdd:cd14628   132 MGREKCHQYWPAERSA-RYQYFVVDPMAEYNMPQYI-LREFKVTDARdgQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQ 209

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907067820 214 A-RCLQGLGP-GPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFQVVLEMRKQRPAAVQTEEQYRFLY 285
Cdd:cd14628   210 VhKTKEQFGQdGPISVHCSAGVGRTGVFITLSIVLERMRYEGV---VDIFQTVKMLRTQRPAMVQTEDQYQFCY 280
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 61-290 2.69e-47

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: 162.14  E-value: 2.69e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  61 RYKDVVAYDETRVILSLLQEEGHGDYINANFIRGIDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRK 140
Cdd:cd14623     1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 141 CERYWAREQEpLKAGPFCITLTKETTLNAdITLRTLQVTFQKE--FRSVHQLQYMSWPDHGVPSSSDHILTMVEEA-RCL 217
Cdd:cd14623    81 CAQYWPSDGS-VSYGDITIELKKEEECES-YTVRDLLVTNTREnkSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVqKQQ 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907067820 218 QGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFQVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 290
Cdd:cd14623   159 QQSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGI---LDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 43-290 3.24e-47

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: 163.69  E-value: 3.24e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  43 EGVCSTKA-------GSRLGNTNKNRYKDVVAYDETRVILSLLQEEGHGDYINANFIRGIDG-SQAYIATQGPLPHTLLD 114
Cdd:cd14610    24 EALCAYQAepnatnvAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPIMDHDPrNPAYIATQGPLPATVAD 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 115 FWRLVWEFGVKVILMACQETENGRRKCERYWAREQEPLKAgPFCITLTKETTLNADITLRT--LQVTFQKEFRSVHQLQY 192
Cdd:cd14610   104 FWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSNLYH-IYEVNLVSEHIWCEDFLVRSfyLKNLQTNETRTVTQFHF 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 193 MSWPDHGVPSSSDHILTMVEEA-RCLQGLGpGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTipPNFSLFQVVLEMRKQR 271
Cdd:cd14610   183 LSWNDQGVPASTRSLLDFRRKVnKCYRGRS-CPIIVHCSDGAGRSGTYILIDMVLNKMAKGA--KEIDIAATLEHLRDQR 259

                         250
                  ....*....|....*....
gi 1907067820 272 PAAVQTEEQYRFLYHTVAQ 290
Cdd:cd14610   260 PGMVQTKEQFEFALTAVAE 278
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 86-288 4.45e-47

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


Pssm-ID: 350506 [Multi-domain]  Cd Length: 209  Bit Score: 160.91  E-value: 4.45e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  86 YINANFIRGIDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWAREQEPlKAGPFCITLTKET 165
Cdd:cd17668     1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSE-EYGNFLVTQKSVQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 166 TLnADITLRTLQVTFQK----------EFRSVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGPGPLCVHCSAGCGR 235
Cdd:cd17668    80 VL-AYYTVRNFTLRNTKikkgsqkgrpSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSAGVGR 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907067820 236 TGVLCAVD-YVRQLLLTQTIppnfSLFQVVLEMRKQRPAAVQTEEQYRFLYHTV 288
Cdd:cd17668   159 TGTYIVLDsMLQQIQHEGTV----NIFGFLKHIRSQRNYLVQTEEQYVFIHDAL 208
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 56-290 6.68e-47

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: 162.98  E-value: 6.68e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  56 NTNKNRYKDVVAYDETRVILSLLQEEGHGDYINANFIRGIDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETE 135
Cdd:cd14627    53 NKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLRE 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 136 NGRRKCERYWAREQEPlKAGPFCITLTKETTLNADItLRTLQVTFQK--EFRSVHQLQYMSWPDHGVPSSSDHILTMVEE 213
Cdd:cd14627   133 MGREKCHQYWPAERSA-RYQYFVVDPMAEYNMPQYI-LREFKVTDARdgQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQ 210

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907067820 214 A-RCLQGLGP-GPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFQVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 290
Cdd:cd14627   211 VhKTKEQFGQdGPISVHCSAGVGRTGVFITLSIVLERMRYEGV---VDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALE 286
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 43-290 9.29e-47

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: 162.51  E-value: 9.29e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  43 EGVCSTKA-------GSRLGNTNKNRYKDVVAYDETRVILSLLQEEGHGDYINANFIRGIDGSQ-AYIATQGPLPHTLLD 114
Cdd:cd14609    22 QALCAYQAepntcstAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPIIEHDPRMpAYIATQGPLSHTIAD 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 115 FWRLVWEFGVKVILMACQETENGRRKCERYWAREQEPLkAGPFCITLTKETTLNADITLRT--LQVTFQKEFRSVHQLQY 192
Cdd:cd14609   102 FWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEGSSL-YHIYEVNLVSEHIWCEDFLVRSfyLKNVQTQETRTLTQFHF 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 193 MSWPDHGVPSSSDHILTMVEEA-RCLQGLGpGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTipPNFSLFQVVLEMRKQR 271
Cdd:cd14609   181 LSWPAEGIPSSTRPLLDFRRKVnKCYRGRS-CPIIVHCSDGAGRTGTYILIDMVLNRMAKGV--KEIDIAATLEHVRDQR 257

                         250
                  ....*....|....*....
gi 1907067820 272 PAAVQTEEQYRFLYHTVAQ 290
Cdd:cd14609   258 PGMVRTKDQFEFALTAVAE 276
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 56-285 1.08e-46

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: 162.21  E-value: 1.08e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  56 NTNKNRYKDVVAYDETRVILSLLQEEGHGDYINANFIRGIDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETE 135
Cdd:cd14624    47 NKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEE 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 136 NGRRKCERYW-AREQEplKAGPFCITLTKETTLnADITLRTLQV--TFQKEFRSVHQLQYMSWPDHGVPSSSDHILTMVE 212
Cdd:cd14624   127 RSRVKCDQYWpSRGTE--TYGLIQVTLLDTVEL-ATYCVRTFALykNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLR 203

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907067820 213 EARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTippNFSLFQVVLEMRKQRPAAVQTEEQYRFLY 285
Cdd:cd14624   204 RVKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEK---TVDIYGHVTLMRAQRNYMVQTEDQYIFIH 273
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 41-292 1.67e-46

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


Pssm-ID: 350447 [Multi-domain]  Cd Length: 287  Bit Score: 162.09  E-value: 1.67e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  41 KSEGVCSTKAGSRlgNTNKNRYKDVVAYDETRVILSLLQEEGHGdYINANFIRGIDGSQA--YIATQGPLPHTLLDFWRL 118
Cdd:cd14599    25 KADGVFTTATLPE--NAERNRIREVVPYEENRVELVPTKENNTG-YINASHIKVTVGGEEwhYIATQGPLPHTCHDFWQM 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 119 VWEFGVKVILMACQETENGRRKCERYWAR---EQEPLKAGPFCITlTKETTLNADITLRTLQVT--FQKEFRSVHQLQYM 193
Cdd:cd14599   102 VWEQGVNVIAMVTAEEEGGRSKSHRYWPKlgsKHSSATYGKFKVT-TKFRTDSGCYATTGLKVKhlLSGQERTVWHLQYT 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 194 SWPDHGVPSSSDHILTMVEEARCLQ-----------GLGPgPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTippNFSLFQ 262
Cdd:cd14599   181 DWPDHGCPEEVQGFLSYLEEIQSVRrhtnsmldstkNCNP-PIVVHCSAGVGRTGVVILTELMIGCLEHNE---KVEVPV 256

                         250       260       270
                  ....*....|....*....|....*....|
gi 1907067820 263 VVLEMRKQRPAAVQTEEQYRFLYHTVAQLF 292
Cdd:cd14599   257 MLRHLREQRMFMIQTIAQYKFVYQVLIQFL 286
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 85-292 5.08e-46

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: 158.18  E-value: 5.08e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  85 DYINANFIRGIDGSQA----YIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWAREQEPLKAGPFCIT 160
Cdd:cd14601     1 DYINANYINMEIPSSSiinrYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSSSYGGFQVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 161 LTKETTlNADITLRTLQVTFQ--KEFRSVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGPGPLCVHCSAGCGRTGV 238
Cdd:cd14601    81 CHSEEG-NPAYVFREMTLTNLekNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVHCSAGIGRTGV 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907067820 239 LCAVDYVrqLLLTQTIPPNFSLfQVVLEMRKQRPAAVQTEEQYRFLYHTVAQLF 292
Cdd:cd14601   160 LITMETA--MCLIECNQPVYPL-DIVRTMRDQRAMMIQTPSQYRFVCEAILKVY 210
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 86-290 6.12e-46

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: 157.99  E-value: 6.12e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  86 YINANFIRGIDGSQ-AYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWAREQEPLKaGPFCITLTKE 164
Cdd:cd14546     1 YINASTIYDHDPRNpAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEVY-HIYEVHLVSE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 165 TTLNADITLRT--LQVTFQKEFRSVHQLQYMSWPDHGVPSSSDHILTMVEEA-RCLQGLGpGPLCVHCSAGCGRTGVLCA 241
Cdd:cd14546    80 HIWCDDYLVRSfyLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVnKSYRGRS-CPIVVHCSDGAGRTGTYIL 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1907067820 242 VDYVRQLLLTQTipPNFSLFQVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 290
Cdd:cd14546   159 IDMVLNRMAKGA--KEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAE 205
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 86-288 6.86e-45

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: 155.07  E-value: 6.86e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  86 YINANFIRGIDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWAREQEPLkaGPFCITLTKET 165
Cdd:cd14555     1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTEVY--GDIKVTLVETE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 166 TLnADITLRTLQVTFQ--KEFRSVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGPGPLCVHCSAGCGRTGVLCAVD 243
Cdd:cd14555    79 PL-AEYVVRTFALERRgyHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTGCYIVID 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1907067820 244 YVRQLLLTQTIppnFSLFQVVLEMRKQRPAAVQTEEQYRFLYHTV 288
Cdd:cd14555   158 IMLDMAEREGV---VDIYNCVKELRSRRVNMVQTEEQYIFIHDAI 199
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 56-285 8.25e-45

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: 157.58  E-value: 8.25e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  56 NTNKNRYKDVVAYDETRVILSLLQEEGHGDYINANFIRGIDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETE 135
Cdd:cd14629    53 NKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLRE 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 136 NGRRKCERYWAREQEPlKAGPFCITLTKETTLNADItLRTLQVTFQK--EFRSVHQLQYMSWPDHGVPSSSDHILTMVEE 213
Cdd:cd14629   133 MGREKCHQYWPAERSA-RYQYFVVDPMAEYNMPQYI-LREFKVTDARdgQSRTIRQFQFTDWPEQGVPKTGEGFIDFIGQ 210

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907067820 214 A-RCLQGLGP-GPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFQVVLEMRKQRPAAVQTEEQYRFLY 285
Cdd:cd14629   211 VhKTKEQFGQdGPITVHCSAGVGRTGVFITLSIVLERMRYEGV---VDMFQTVKTLRTQRPAMVQTEDQYQLCY 281
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 85-288 1.39e-44

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


Pssm-ID: 350470 [Multi-domain]  Cd Length: 205  Bit Score: 154.39  E-value: 1.39e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  85 DYINANFIRGIDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWAREQEpLKAGPFCITLTKE 164
Cdd:cd14622     1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGS-VTHGEITIEIKND 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 165 TTLNAdITLRTLQVTF--QKEFRSVHQLQYMSWPDHGVPSSSDHILTMVEEA-RCLQGLGPGPLCVHCSAGCGRTGVLCA 241
Cdd:cd14622    80 TLLET-ISIRDFLVTYnqEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVqKQQQQTGNHPIVVHCSAGAGRTGTFIA 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1907067820 242 VDYVRQLLLTQTIppnFSLFQVVLEMRKQRPAAVQTEEQYRFLYHTV 288
Cdd:cd14622   159 LSNILERVKAEGL---LDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 62-288 1.83e-44

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: 154.71  E-value: 1.83e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  62 YKDVVAYDETRVILSLLQEEGHGDYINANFIRGIDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKC 141
Cdd:cd14620     1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 142 ERYWArEQEPLKAGPFCITLTKETTLnADITLRTLQVTFQ-----KEFRSVHQLQYMSWPDHGVPSSSDHILTMVEEARC 216
Cdd:cd14620    81 YQYWP-DQGCWTYGNIRVAVEDCVVL-VDYTIRKFCIQPQlpdgcKAPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVKS 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907067820 217 LQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTippNFSLFQVVLEMRKQRPAAVQTEEQYRFLYHTV 288
Cdd:cd14620   159 VNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQ---KVDVFEFVSRIRNQRPQMVQTDMQYSFIYQAL 227
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 86-285 2.39e-44

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: 153.44  E-value: 2.39e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  86 YINANFIRGIDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWAREQEPLKA-GPFCITLTKE 164
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRAfGDVVVKINEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 165 TTLnADITLRTLQVTFQKEFRS---VHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGPGPLCVHCSAGCGRTGVLCA 241
Cdd:cd14557    81 KIC-PDYIIRKLNINNKKEKGSgreVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGTYIG 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1907067820 242 VDYVRQLLLTQTippNFSLFQVVLEMRKQRPAAVQTEEQYRFLY 285
Cdd:cd14557   160 IDAMLEGLEAEG---RVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
54-284 7.16e-44

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 154.86  E-value: 7.16e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  54 LGNTNKNRYKDVVAYDETRVilsllQEEGhgDYINANFIRGIDGSQaYIATQGPLPHTLLDFWRLVWEFGVKVI--LMAC 131
Cdd:COG5599    40 INGSPLNRFRDIQPYKETAL-----RANL--GYLNANYIQVIGNHR-YIATQYPLEEQLEDFFQMLFDNNTPVLvvLASD 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 132 QETENGRRKCERYWaREQEplKAGPFCI--TLTKETTLNADITLRTLQVTFQ---KEFRSVHQLQYMSWPDHGVPSSS-- 204
Cdd:COG5599   112 DEISKPKVKMPVYF-RQDG--EYGKYEVssELTESIQLRDGIEARTYVLTIKgtgQKKIEIPVLHVKNWPDHGAISAEal 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 205 -DHILTMVEEARCLQGLGpGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIpPNFSLFQVVLEMRKQR-PAAVQTEEQYR 282
Cdd:COG5599   189 kNLADLIDKKEKIKDPDK-LLPVVHCRAGVGRTGTLIACLALSKSINALVQ-ITLSVEEIVIDMRTSRnGGMVQTSEQLD 266


                  ..
gi 1907067820 283 FL 284
Cdd:COG5599   267 VL 268
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 86-285 1.01e-43

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


Pssm-ID: 350387 [Multi-domain]  Cd Length: 205  Bit Score: 151.77  E-value: 1.01e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  86 YINANFIRGIDGSQA-YIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWAREQ-EPLKAGPFCITLTK 163
Cdd:cd14539     1 YINASLIEDLTPYCPrFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERgQALVYGAITVSLQS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 164 ETTLNADITlRTLQVTF--QKEFRSVHQLQYMSWPDHGVPSSSDHILTMVEEA-------RCLQglgpGPLCVHCSAGCG 234
Cdd:cd14539    81 VRTTPTHVE-RIISIQHkdTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVhshylqqRSLQ----TPIVVHCSSGVG 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907067820 235 RTGVLCAVdY--VRQLLLTQTIPpnfSLFQVVLEMRKQRPAAVQTEEQYRFLY 285
Cdd:cd14539   156 RTGAFCLL-YaaVQEIEAGNGIP---DLPQLVRKMRQQRKYMLQEKEHLKFCY 204
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 86-285 1.45e-43

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: 151.39  E-value: 1.45e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  86 YINANFIRGIDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWarEQEPLKAGPFCITLTKET 165
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYW--GDEKKTYGDIEVELKDTE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 166 TLNaDITLRTLQVTF--QKEFRSVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGPG------PLCVHCSAGCGRTG 237
Cdd:cd14558    79 KSP-TYTVRVFEITHlkRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKNSkhgrsvPIVVHCSDGSSRTG 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1907067820 238 VLCAvdyVRQLLLTQTIPPNFSLFQVVLEMRKQRPAAVQTEEQYRFLY 285
Cdd:cd14558   158 IFCA---LWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 86-285 8.36e-43

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


Pssm-ID: 350496 [Multi-domain]  Cd Length: 206  Bit Score: 149.54  E-value: 8.36e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  86 YINANFIRG---IDGSQaYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRR-KCERYW-AREQEPLKAGPFCIT 160
Cdd:cd17658     1 YINASLVETpasESLPK-FIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTaKCADYFpAEENESREFGRISVT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 161 LTKETTLNADITLRTLQVTF---QKEFRSVHQLQYMSWPDHGVPSSSDHILTMVeeaRCLQGLGP--GPLCVHCSAGCGR 235
Cdd:cd17658    80 NKKLKHSQHSITLRVLEVQYiesEEPPLSVLHIQYPEWPDHGVPKDTRSVRELL---KRLYGIPPsaGPIVVHCSAGIGR 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907067820 236 TGVLCAVDYVRQLLLTQTIPPnFSLFQVVLEMRKQRPAAVQTEEQYRFLY 285
Cdd:cd17658   157 TGAYCTIHNTIRRILEGDMSA-VDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 72-290 9.14e-43

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: 149.79  E-value: 9.14e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  72 RVILSLLQEEGHGDYINANFIRGIDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWAREQEP 151
Cdd:cd14631     1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 152 LkaGPFCITLTKETTLnADITLRTLQVTFQ--KEFRSVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGPGPLCVHC 229
Cdd:cd14631    81 Y--GDFKVTCVEMEPL-AEYVVRTFTLERRgyNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHC 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907067820 230 SAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFQVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 290
Cdd:cd14631   158 SAGAGRTGCYIVIDIMLDMAEREGV---VDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 86-285 1.43e-42

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: 148.71  E-value: 1.43e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  86 YINANFIRGIDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMaCQETENGRRKCERYWArEQEPLKAGPFCITLTKeT 165
Cdd:cd14556     1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVM-LNQLDPKDQSCPQYWP-DEGSGTYGPIQVEFVS-T 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 166 TLNADITLRTLQVT----FQKEFRSVHQLQYMSWPDHG-VPSSSDHILTMVEEA-RCLQGLGPGPLCVHCSAGCGRTGVL 239
Cdd:cd14556    78 TIDEDVISRIFRLQnttrPQEGYRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVeKWQEQSGEGPIVVHCLNGVGRSGVF 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1907067820 240 CAVDYVRQLLLTQTIppnFSLFQVVLEMRKQRPAAVQTEEQYRFLY 285
Cdd:cd14556   158 CAISSVCERIKVENV---VDVFQAVKTLRNHRPNMVETEEQYKFCY 200
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 54-289 3.57e-41

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: 146.93  E-value: 3.57e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  54 LGNTNKNRYKDVVAYDETRVIL-SLLQEEGHGDYINANFIRGIDGSQ-AYIATQGPLPHTLLDFWRLVWEFGVKVILMaC 131
Cdd:cd14613    23 PGLVRKNRYKTILPNPHSRVCLtSPDQDDPLSSYINANYIRGYGGEEkVYIATQGPTVNTVGDFWRMVWQERSPIIVM-I 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 132 QETENGRRKCERYWAREQepLKAGPFCITLTKETTLNaDITLRTLQVTFQKEFRSVHQLQYMSWPDHGVPSSSDHILTM- 210
Cdd:cd14613   102 TNIEEMNEKCTEYWPEEQ--VTYEGIEITVKQVIHAD-DYRLRLITLKSGGEERGLKHYWYTSWPDQKTPDNAPPLLQLv 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 211 --VEEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFQVVLEMRKQRPAAVQTEEQYRFLYHTV 288
Cdd:cd14613   179 qeVEEARQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGV---VDILRTTCQLRLDRGGMIQTCEQYQFVHHVL 255


                  .
gi 1907067820 289 A 289
Cdd:cd14613   256 S 256
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 86-290 4.32e-41

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: 145.19  E-value: 4.32e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  86 YINANFIRGIDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWAREQEPLkaGPFCITLTKET 165
Cdd:cd14632     1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSDTY--GDIKITLLKTE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 166 TLnADITLRTLQVTfQKEFRSVH---QLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGPGPLCVHCSAGCGRTGVLCAV 242
Cdd:cd14632    79 TL-AEYSVRTFALE-RRGYSARHevkQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYIVL 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1907067820 243 DYVRQLLLTQTIppnFSLFQVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 290
Cdd:cd14632   157 DVMLDMAECEGV---VDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 47-292 2.03e-40

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: 145.94  E-value: 2.03e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  47 STKAGSRLGNTNKNRYKDVVAYDETRVILSLLQEEGHGDYINANFIRGIDGSQAYIATQGPLPHTLLDFWRLVWEFGVKV 126
Cdd:cd14621    43 TCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTAT 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 127 ILMACQETENGRRKCERYWArEQEPLKAGPFCITLtKETTLNADITLRTL------QVTFQKEFRSVHQLQYMSWPDHGV 200
Cdd:cd14621   123 IVMVTNLKERKECKCAQYWP-DQGCWTYGNIRVSV-EDVTVLVDYTVRKFciqqvgDVTNKKPQRLITQFHFTSWPDFGV 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 201 PSSSDHILTMVEEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTippNFSLFQVVLEMRKQRPAAVQTEEQ 280
Cdd:cd14621   201 PFTPIGMLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAER---KVDVYGFVSRIRAQRCQMVQTDMQ 277

                         250
                  ....*....|..
gi 1907067820 281 YRFLYHTVAQLF 292
Cdd:cd14621   278 YVFIYQALLEHY 289
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 59-286 2.30e-40

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: 143.91  E-value: 2.30e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  59 KNRYKDVVAYDETRVILSLLQ-EEGHGDYINANFIRGIDGSQ-AYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETEN 136
Cdd:cd14611     2 KNRYKTILPNPHSRVCLKPKNsNDSLSTYINANYIRGYGGKEkAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 137 GrRKCERYWareqePLKAGpfcITLTKETTLNA-----DITLRTLQVTFQKEFRSVHQLQYMSWPDHGVPSSSDHILTM- 210
Cdd:cd14611    82 N-EKCVLYW-----PEKRG---IYGKVEVLVNSvkecdNYTIRNLTLKQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLm 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907067820 211 --VEEARcLQGLGPGPLCVHCSAGCGRTGVLCAVDY-VRQLLLTQTIppnfSLFQVVLEMRKQRPAAVQTEEQYRFLYH 286
Cdd:cd14611   153 ldVEEDR-LASPGRGPVVVHCSAGIGRTGCFIATTIgCQQLKEEGVV----DVLSIVCQLRVDRGGMVQTSEQYEFVHH 226
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
186-290 4.81e-40

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 138.65  E-value: 4.81e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  186 SVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGP--GPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPNFslFQV 263
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSEssGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGEVDI--FDT 78

                           90       100
                   ....*....|....*....|....*..
gi 1907067820  264 VLEMRKQRPAAVQTEEQYRFLYHTVAQ 290
Cdd:smart00404  79 VKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 186-290 4.81e-40

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


Pssm-ID: 214469 [Multi-domain]  Cd Length: 105  Bit Score: 138.65  E-value: 4.81e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  186 SVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGP--GPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPNFslFQV 263
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSEssGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGEVDI--FDT 78

                           90       100
                   ....*....|....*....|....*..
gi 1907067820  264 VLEMRKQRPAAVQTEEQYRFLYHTVAQ 290
Cdd:smart00012  79 VKELRSQRPGMVQTEEQYLFLYRALLE 105
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 56-284 1.11e-39

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 144.37  E-value: 1.11e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  56 NTNKNRYKDVVAYDETRVILsllqEEGHG---DYINANFIRGIDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMAC- 131
Cdd:PHA02747   51 NQPKNRYWDIPCWDHNRVIL----DSGGGstsDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTp 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 132 QETENGRRKCERYWA-REQEPLKAGPFCITlTKETTLNADITLRTLQVTFQ--KEFRSVHQLQYMSWPDHGVPssSDHI- 207
Cdd:PHA02747  127 TKGTNGEEKCYQYWClNEDGNIDMEDFRIE-TLKTSVRAKYILTLIEITDKilKDSRKISHFQCSEWFEDETP--SDHPd 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 208 ----LTMVEEARCLQG--LGP-----GPLCVHCSAGCGRTGVLCAVDY-VRQLLLTQTIppnfSLFQVVLEMRKQRPAAV 275
Cdd:PHA02747  204 fikfIKIIDINRKKSGklFNPkdallCPIVVHCSDGVGKTGIFCAVDIcLNQLVKRKAI----CLAKTAEKIREQRHAGI 279


                  ....*....
gi 1907067820 276 QTEEQYRFL 284
Cdd:PHA02747  280 MNFDDYLFI 288
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 86-285 1.13e-39

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


Pssm-ID: 350399 [Multi-domain]  Cd Length: 202  Bit Score: 141.20  E-value: 1.13e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  86 YINANFIRGIDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWAREQEpLKAGPFCITLtKET 165
Cdd:cd14551     1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGC-WTYGNLRVRV-EDT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 166 TLNADITLRTL------QVTFQKEFRSVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGPGPLCVHCSAGCGRTGVL 239
Cdd:cd14551    79 VVLVDYTTRKFciqkvnRGIGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGRTGTF 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1907067820 240 CAVDYVRQLLLTQTippNFSLFQVVLEMRKQRPAAVQTEEQYRFLY 285
Cdd:cd14551   159 IVIDAMLDMMHAEG---KVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 1-290 3.00e-39

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 143.22  E-value: 3.00e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820   1 MSRHTDLVRSFLEQLEARDYREgaILAREFSDIKARSVAWKSEGVCSTKagsrlgNTNKNRYKDVVAYDETRVILSLlqE 80
Cdd:PHA02742    5 CSKKNSFAKNCEQLIEESNLAE--ILKEEHEHIMQEIVAFSCNESLELK------NMKKCRYPDAPCFDRNRVILKI--E 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  81 EGHGDYINANFIRGIDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYW-AREQEPLKAGPFCI 159
Cdd:PHA02742   75 DGGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIMEDGKEACYPYWmPHERGKATHGEFKI 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 160 -TLTKETTLNADITlrTLQVTFQKEFRS--VHQLQYMSWPDHGVPSSSDHILTMVEEARCLQG-----------LGPGPL 225
Cdd:PHA02742  155 kTKKIKSFRNYAVT--NLCLTDTNTGASldIKHFAYEDWPHGGLPRDPNKFLDFVLAVREADLkadvdikgeniVKEPPI 232

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907067820 226 CVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPnfsLFQVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 290
Cdd:PHA02742  233 LVHCSAGLDRAGAFCAIDICISKYNERAIIP---LLSIVRDLRKQRHNCLSLPQQYIFCYFIVLI 294
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 56-288 4.69e-37

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 137.85  E-value: 4.69e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  56 NTNKNRYKDVVAYDETRVILS-------------------LLQEEGHGDYINANFIRGIDGSQAYIATQGPLPHTLLDFW 116
Cdd:PHA02746   51 NLKKNRFHDIPCWDHSRVVINaheslkmfdvgdsdgkkieVTSEDNAENYIHANFVDGFKEANKFICAQGPKEDTSEDFF 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 117 RLVWEFGVKVILmACQETENGRRKCERYWAREQE-PLKAGPFcITLTKETTLNADITLRTLQVT--FQKEFRSVHQLQYM 193
Cdd:PHA02746  131 KLISEHESQVIV-SLTDIDDDDEKCFELWTKEEDsELAFGRF-VAKILDIIEELSFTKTRLMITdkISDTSREIHHFWFP 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 194 SWPDHGVPSSSDHILTMV-----EEARCL-----QGLGPGPLCVHCSAGCGRTGVLCAVD-YVRQLLLTQTIppnfSLFQ 262
Cdd:PHA02746  209 DWPDNGIPTGMAEFLELInkvneEQAELIkqadnDPQTLGPIVVHCSAGIGRAGTFCAIDnALEQLEKEKEV----CLGE 284

                         250       260
                  ....*....|....*....|....*.
gi 1907067820 263 VVLEMRKQRPAAVQTEEQYRFLYHTV 288
Cdd:PHA02746  285 IVLKIRKQRHSSVFLPEQYAFCYKAL 310
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 86-292 7.44e-36

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: 131.64  E-value: 7.44e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  86 YINANFIRGIDGSQA--YIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWAR---EQEPLKAGPFCIT 160
Cdd:cd14598     1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRlgsRHNTVTYGRFKIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 161 --LTKETTLNADITLRTLQVTFQKEfRSVHQLQYMSWPDHGVPSSSDHILTMVEEARCL----------QGLGPgPLCVH 228
Cdd:cd14598    81 trFRTDSGCYATTGLKIKHLLTGQE-RTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVrrhtnstidpKSPNP-PVLVH 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907067820 229 CSAGCGRTGVLcavdyVRQLLLTQTIPPNFSL-FQVVLEM-RKQRPAAVQTEEQYRFLYHTVAQLF 292
Cdd:cd14598   159 CSAGVGRTGVV-----ILSEIMIACLEHNEMLdIPRVLDMlRQQRMMMVQTLSQYTFVYKVLIQFL 219
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 86-285 1.79e-28

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: 111.27  E-value: 1.79e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  86 YINANFIRGIDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQ-ETENGrrkCERYWArEQEPLKAGPF---CITl 161
Cdd:cd14636     1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEvDLAQG---CPQYWP-EEGMLRYGPIqveCMS- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 162 tkeTTLNADITLRTLQVTF----QKEFRSVHQLQYMSWPDH-GVPSSSDHILTMVEEARCLQ---GLGPGPLCVHCSAGC 233
Cdd:cd14636    76 ---CSMDCDVISRIFRICNltrpQEGYLMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQeecDEGEGRTIIHCLNGG 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907067820 234 GRTGVLCAVDYVRQLLLTQTIppnFSLFQVVLEMRKQRPAAVQTEEQYRFLY 285
Cdd:cd14636   153 GRSGMFCAISIVCEMIKRQNV---VDVFHAVKTLRNSKPNMVETPEQYRFCY 201
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 86-285 3.61e-26

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


Pssm-ID: 350482 [Multi-domain]  Cd Length: 206  Bit Score: 105.10  E-value: 3.61e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  86 YINANFIRGIDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQetENGRRKCERYWArEQEPLKAGPFCITLTkET 165
Cdd:cd14634     1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNE--MDAAQLCMQYWP-EKTSCCYGPIQVEFV-SA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 166 TLNADITLRTLQVTF----QKEFRSVHQLQYMSWPDH-GVPSSSDHILTMVEEARCLQGL---GPGPLCVHCSAGCGRTG 237
Cdd:cd14634    77 DIDEDIISRIFRICNmarpQDGYRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEQydgREGRTVVHCLNGGGRSG 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1907067820 238 VLCAVDYVRQLLLTQTIppnFSLFQVVLEMRKQRPAAVQTEEQYRFLY 285
Cdd:cd14634   157 TFCAICSVCEMIQQQNI---IDVFHTVKTLRNNKSNMVETLEQYKFVY 201
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 86-285 2.65e-24

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


Pssm-ID: 350508 [Multi-domain]  Cd Length: 205  Bit Score: 99.75  E-value: 2.65e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  86 YINANFIRGIDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMAcqETENGRRKCER-YWAREQEPLKAGPFCITL--- 161
Cdd:cd17670     1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVML--PDNQGLAEDEFvYWPSREESMNCEAFTVTLisk 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 162 ------TKETTLNADITLRTLQVTFQKEFRsvhQLQYMSWPDHGVPSSSDHILTMV--EEARCLQglgpGPLCVHCSAGC 233
Cdd:cd17670    79 drlclsNEEQIIIHDFILEATQDDYVLEVR---HFQCPKWPNPDAPISSTFELINVikEEALTRD----GPTIVHDEFGA 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907067820 234 GRTGVLCAVDYVRQLLLTQTIppnFSLFQVVLEMRKQRPAAVQTEEQYRFLY 285
Cdd:cd17670   152 VSAGTLCALTTLSQQLENENA---VDVYQVAKMINLMRPGVFTDIEQYQFLY 200
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 86-285 2.04e-22

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


Pssm-ID: 350483 [Multi-domain]  Cd Length: 206  Bit Score: 94.37  E-value: 2.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  86 YINANFIRGIDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMAcqETENGRRKCERYWArEQEPLKAGPFCITLTkET 165
Cdd:cd14635     1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVML--NDVDPAQLCPQYWP-ENGVHRHGPIQVEFV-SA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 166 TLNADITLRTLQVTF----QKEFRSVHQLQYMSWPDH-GVPSSSDHILTMVEEARCLQ---GLGPGPLCVHCSAGCGRTG 237
Cdd:cd14635    77 DLEEDIISRIFRIYNaarpQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQeeyNGGEGRTVVHCLNGGGRSG 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1907067820 238 VLCAVDYVRQLLLTQTippNFSLFQVVLEMRKQRPAAVQTEEQYRFLY 285
Cdd:cd14635   157 TFCAISIVCEMLRHQR---AVDVFHAVKTLRNNKPNMVDLLDQYKFCY 201
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 86-288 2.46e-22

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: 94.20  E-value: 2.46e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  86 YINANFIRGIDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETE-NGRRKCERYWArEQEPLKAGPFCITLTkE 164
Cdd:cd14637     1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQsNSAWPCLQYWP-EPGLQQYGPMEVEFV-S 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 165 TTLNADITLRTLQVT----FQKEFRSVHQLQYMSW-PDHGVPSSSD---HILTMVE--EARClqglGPGPLCVHCSAGCG 234
Cdd:cd14637    79 GSADEDIVTRLFRVQnitrLQEGHLMVRHFQFLRWsAYRDTPDSKKaflHLLASVEkwQRES----GEGRTVVHCLNGGG 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907067820 235 RTGVLCAVDYVRQLLLTQTIppnFSLFQVVLEMRKQRPAAVQTEEQYRFLYHTV 288
Cdd:cd14637   155 RSGTYCASAMILEMIRCHNI---VDVFYAVKTLRNYKPNMVETLEQYRFCYEIA 205
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 86-285 5.78e-22

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: 93.15  E-value: 5.78e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  86 YINANFIRGIDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGrrKCERYWAREQEPLKAGPFCITLTKET 165
Cdd:cd14550     1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWPTKEKPLECETFKVTLSGED 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 166 T--LNADITLRT----LQVTFQKEFRSVHQLQYMSWPDHGVP-SSSDHILTMVEEaRCLQglGPGPLCVHCSAGCGRTGV 238
Cdd:cd14550    79 HscLSNEIRLIVrdfiLESTQDDYVLEVRQFQCPSWPNPCSPiHTVFELINTVQE-WAQQ--RDGPIVVHDRYGGVQAAT 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1907067820 239 LCAVdyvrQLLLTQTIPPN-FSLFQVVLEMRKQRPAAVQTEEQYRFLY 285
Cdd:cd14550   156 FCAL----TTLHQQLEHESsVDVYQVAKLYHLMRPGVFTSKEDYQFLY 199
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 86-288 1.34e-21

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: 92.36  E-value: 1.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  86 YINANFIRGIDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCErYWAREQEPLKAGPFCITL---- 161
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWPNKDEPINCETFKVTLiaee 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 162 -----TKETTLNADITLRTLQVTFQKEFRsvhQLQYMSWPDHGVP-SSSDHILTMVEEARCLQGlgpGPLCVHCSAGCGR 235
Cdd:cd17669    80 hkclsNEEKLIIQDFILEATQDDYVLEVR---HFQCPKWPNPDSPiSKTFELISIIKEEAANRD---GPMIVHDEHGGVT 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907067820 236 TGVLCAVDYVRQLLLTQTippNFSLFQVVLEMRKQRPAAVQTEEQYRFLYHTV 288
Cdd:cd17669   154 AGTFCALTTLMHQLEKEN---SVDVYQVAKMINLMRPGVFTDIEQYQFLYKAI 203
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 205-286 3.57e-14

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


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 68.53  E-value: 3.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 205 DHILTMVEEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLlltqtippNFSLFQVVLEMRKQRPA-AVQTEEQYRF 283
Cdd:cd14494    39 LAMVDRFLEVLDQAEKPGEPVLVHCKAGVGRTGTLVACYLVLLG--------GMSAEEAVRIVRLIRPGgIPQTIEQLDF 110


                  ...
gi 1907067820 284 LYH 286
Cdd:cd14494   111 LIK 113
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 51-296 1.39e-11

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 64.99  E-value: 1.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  51 GSRLGNTNKNRYKD-VVAYDETRVILSLLQEEGHGDYINANFIRGIDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILM 129
Cdd:PHA02740   42 ANKACAQAENKAKDeNLALHITRLLHRRIKLFNDEKVLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVL 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 130 ACQETEngrRKC-ERYWAREQEPLK-AGPFCI-TLTKETTLNADITLRTLQVTFQKEfRSVHQLQYMSWPDHGVPSSSD- 205
Cdd:PHA02740  122 ISRHAD---KKCfNQFWSLKEGCVItSDKFQIeTLEIIIKPHFNLTLLSLTDKFGQA-QKISHFQYTAWPADGFSHDPDa 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 206 ------HILTMVEEARCLQGLGP-GPLCVHCSAGCGRTGVLCAVDyvrqLLLTQTIPPN-FSLFQVVLEMRKQRPAAVQT 277
Cdd:PHA02740  198 fidffcNIDDLCADLEKHKADGKiAPIIIDCIDGISSSAVFCVFD----ICATEFDKTGmLSIANALKKVRQKKYGCMNC 273

                         250
                  ....*....|....*....
gi 1907067820 278 EEQYRFLYHTVAQLFSRTL 296
Cdd:PHA02740  274 LDDYVFCYHLIAAYLKEKF 292
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 194-284 6.03e-10

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


Pssm-ID: 350356 [Multi-domain]  Cd Length: 206  Bit Score: 58.90  E-value: 6.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 194 SWPDHGVPSSsDHILTMVE-EARCLQGlgPGPLCVHCSAGCGRTGVLCAVdyvrQLLLTQTIPPNfslfQVVLEMRKQRP 272
Cdd:cd14506    83 GWKDYGVPSL-TTILDIVKvMAFALQE--GGKVAVHCHAGLGRTGVLIAC----YLVYALRMSAD----QAIRLVRSKRP 151

                          90
                  ....*....|..
gi 1907067820 273 AAVQTEEQYRFL 284
Cdd:cd14506   152 NSIQTRGQVLCV 163
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 60-284 1.05e-08

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


Pssm-ID: 350407 [Multi-domain]  Cd Length: 227  Bit Score: 55.48  E-value: 1.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820  60 NRYKDVvaydETRVilsllqEEGHGDYINANFIRgIDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRR 139
Cdd:cd14559     1 NRFTNI----QTRV------STPVGKNLNANRVQ-IGNKNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRK 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 140 KCERYWAREQEPLKagpfcITLTKETTLNADITLRT------LQVTFQKEFRSVHQLQYMSWPDHGVPSS------SDHI 207
Cdd:cd14559    70 GLPPYFRQSGTYGS-----VTVKSKKTGKDELVDGLkadmynLKITDGNKTITIPVVHVTNWPDHTAISSeglkelADLV 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 208 -------LTMVEEARCLQGLGPGPL--CVHCSAGCGRTGVLCAVDYVRQllltqtiPPN-FSLFQVVLEMRKQRPA-AVQ 276
Cdd:cd14559   145 nksaeekRNFYKSKGSSAINDKNKLlpVIHCRAGVGRTGQLAAAMELNK-------SPNnLSVEDIVSDMRTSRNGkMVQ 217


                  ....*...
gi 1907067820 277 TEEQYRFL 284
Cdd:cd14559   218 KDEQLDTL 225
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
195-286 1.43e-08

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 53.05  E-value: 1.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 195 WPDHGVPSSsDHILTMVEEARCLQGLGpGPLCVHCSAGCGRTGVLCAvdyvrQLLLTQTIPPNfslfQVVLEMRKQRPAA 274
Cdd:COG2453    55 IPDFGAPDD-EQLQEAVDFIDEALREG-KKVLVHCRGGIGRTGTVAA-----AYLVLLGLSAE----EALARVRAARPGA 123

                          90
                  ....*....|..
gi 1907067820 275 VQTEEQYRFLYH 286
Cdd:COG2453   124 VETPAQRAFLER 135
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 189-285 9.89e-08

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


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 51.50  E-value: 9.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 189 QLQYMSW-----PDHGVPSSSDHILTMVEEAR-CLQGlGPGPLcVHCSAGCGRTGVLCAvdyVRQLLLTQTIPPNfslfQ 262
Cdd:cd14505    69 QQAGITWhhlpiPDGGVPSDIAQWQELLEELLsALEN-GKKVL-IHCKGGLGRTGLIAA---CLLLELGDTLDPE----Q 139

                          90       100
                  ....*....|....*....|...
gi 1907067820 263 VVLEMRKQRPAAVQTEEQYRFLY 285
Cdd:cd14505   140 AIAAVRALRPGAIQTPKQENFLH 162
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 186-284 1.41e-06

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


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 47.66  E-value: 1.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 186 SVHQLQY--MSWPDHGVPSSS--DHILTMVEEARCLqglgPGPLCVHCSAGCGRTGVLCAVdYvrqLLLTQTIPPNfslf 261
Cdd:cd14504    46 TCPGLRYhhIPIEDYTPPTLEqiDEFLDIVEEANAK----NEAVLVHCLAGKGRTGTMLAC-Y---LVKTGKISAV---- 113

                          90       100
                  ....*....|....*....|...
gi 1907067820 262 QVVLEMRKQRPAAVQTEEQYRFL 284
Cdd:cd14504   114 DAINEIRRIRPGSIETSEQEKFV 136
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 196-239 2.28e-03

C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division control protein 14 (CDC14) family is highly conserved in all eukaryotes, although the roles of its members seem to have diverged during evolution. Yeast Cdc14, the best characterized member of this family, is a dual-specificity phosphatase that plays key roles in cell cycle control. It preferentially dephosphorylates cyclin-dependent kinase (CDK) targets, which makes it the main antagonist of CDK in the cell. Cdc14 functions at the end of mitosis and it triggers the events that completely eliminates the activity of CDK and other mitotic kinases. It is also involved in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint, and in chromosome segregation. Cdc14 phosphatases also function in DNA replication, DNA damage checkpoint, and DNA repair. Vertebrates may contain more than one Cdc14 homolog; humans have three (CDC14A, CDC14B, and CDC14C). CDC14 family proteins contain a highly conserved N-terminal pseudophosphatase domain that contributes to substrate specificity and a C-terminal catalytic dual-specificity phosphatase domain with the PTP signature motif.


Pssm-ID: 350349 [Multi-domain]  Cd Length: 174  Bit Score: 38.59  E-value: 2.28e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1907067820 196 PDHGVPSssDHI----LTMVEEArclqglgPGPLCVHCSAGCGRTGVL 239
Cdd:cd14499    88 PDGSTPS--DDIvkkfLDICENE-------KGAIAVHCKAGLGRTGTL 126
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 331-428 5.95e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 38.93  E-value: 5.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067820 331 RPPGGVLRSI-SVPAPPTLPMADTYAVVQKRGASAGTGPGPRAPTSTDTPIYSQVA---PRAQRPVAHTEDAQGTTALRR 406
Cdd:PRK14951  365 KPAAAAEAAApAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAappAPVAAPAAAAPAAAPAAAPAA 444

                          90       100
                  ....*....|....*....|..
gi 1907067820 407 VPADQNSSGPDAYEEVTDGAQT 428
Cdd:PRK14951  445 VALAPAPPAQAAPETVAIPVRV 466
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 188-241 6.14e-03

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


Pssm-ID: 350347 [Multi-domain]  Cd Length: 160  Bit Score: 37.17  E-value: 6.14e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907067820 188 HQLQYMSWPDHGVPSSsDHILTMVEEARCLQGLGPGPLCV-HCSAGCGRTGVLCA 241
Cdd:cd14497    61 GRVLHYGFPDHHPPPL-GLLLEIVDDIDSWLSEDPNNVAVvHCKAGKGRTGTVIC 114
 
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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