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Conserved domains on  [gi|1958801479|ref|XP_038939142|]
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tyrosine-protein phosphatase non-receptor type 18 isoform X11 [Rattus norvegicus]

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 ...
 27-298 1.85e-171

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: 476.24  E-value: 1.85e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  27 AREFSDIKARSVAWKTEGVCSTKAGSQQGNSKKNRYKDVVPYDETRVILSLLQEEGHGDYINANFIRGTDGSQAYIATQG 106
Cdd:cd14603     1 AGEFSEIRACSAAFKADYVCSTVAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 107 PLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWAQEREPLQAGPFCITLTKETALTADITLRTLQVTFqkvpkg 186
Cdd:cd14603    81 PLSHTVLDFWRMIWQYGVKVILMACREIEMGKKKCERYWAQEQEPLQTGPFTITLVKEKRLNEEVILRTLKVTF------ 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 187 QKESRPVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPNFSL 266
Cdd:cd14603   155 QKESRSVSHFQYMAWPDHGIPDSPDCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPDFSI 234

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1958801479 267 FEVVLEMRKQRPAAVQTEEQYRFLYHTVAQLF 298
Cdd:cd14603   235 FDVVLEMRKQRPAAVQTEEQYEFLYHTVAQMF 266
 
Name Accession Description Interval E-value
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 27-298 1.85e-171

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: 476.24  E-value: 1.85e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  27 AREFSDIKARSVAWKTEGVCSTKAGSQQGNSKKNRYKDVVPYDETRVILSLLQEEGHGDYINANFIRGTDGSQAYIATQG 106
Cdd:cd14603     1 AGEFSEIRACSAAFKADYVCSTVAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 107 PLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWAQEREPLQAGPFCITLTKETALTADITLRTLQVTFqkvpkg 186
Cdd:cd14603    81 PLSHTVLDFWRMIWQYGVKVILMACREIEMGKKKCERYWAQEQEPLQTGPFTITLVKEKRLNEEVILRTLKVTF------ 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 187 QKESRPVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPNFSL 266
Cdd:cd14603   155 QKESRSVSHFQYMAWPDHGIPDSPDCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPDFSI 234

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1958801479 267 FEVVLEMRKQRPAAVQTEEQYRFLYHTVAQLF 298
Cdd:cd14603   235 FDVVLEMRKQRPAAVQTEEQYEFLYHTVAQMF 266
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
26-296 4.97e-111

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 322.69  E-value: 4.97e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479   26 LAREFSDIKArsvawKTEGVCSTKAGSQQGNSKKNRYKDVVPYDETRVILSLLQEEGHgDYINANFIRGTDGSQAYIATQ 105
Cdd:smart00194   2 LEEEFEKLDR-----LKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGS-DYINASYIDGPNGPKAYIATQ 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  106 GPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWAQE-REPLQAGPFCITLTKETAlTADITLRTLQVTfqkvP 184
Cdd:smart00194  76 GPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEeGEPLTYGDITVTLKSVEK-VDDYTIRTLEVT----N 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  185 KGQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQtipPNF 264
Cdd:smart00194 151 TGCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAG---KEV 227

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1958801479  265 SLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 296
Cdd:smart00194 228 DIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
56-296 6.85e-110

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 319.19  E-value: 6.85e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  56 NSKKNRYKDVVPYDETRVILSllQEEGHGDYINANFIRGTDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETE 135
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLT--GDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 136 NGRRKCERYWAQERE-PLQAGPFCITLTKETALTADITLRTLQVTFqkvpKGQKESRPVHQLQYMSWPDHGVPSSSDHIL 214
Cdd:pfam00102  79 KGREKCAQYWPEEEGeSLEYGDFTVTLKKEKEDEKDYTVRTLEVSN----GGSEETRTVKHFHYTGWPDHGVPESPNSLL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 215 TMVEEARCLQGLGP-GPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLYHT 293
Cdd:pfam00102 155 DLLRKVRKSSLDGRsGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGE---VDIFQIVKELRSQRPGMVQTLEQYIFLYDA 231


                  ...
gi 1958801479 294 VAQ 296
Cdd:pfam00102 232 ILE 234
PHA02738 PHA02738
hypothetical protein; Provisional
 11-323 3.47e-47

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 161.63  E-value: 3.47e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  11 FLEQQEARDHREgaILAREFSDIkarsVAWKTEGVCStkagSQQGNSKKNRYKDVVPYDETRVILSllQEEGHGDYINAN 90
Cdd:PHA02738   14 FLALMEKSDCEE--VITREHQKV----ISEKVDGTFN----AEKKNRKLNRYLDAVCFDHSRVILP--AERNRGDYINAN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  91 FIRGTDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWAQ-EREPLQAGPFCITLTKETALTA 169
Cdd:PHA02738   82 YVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDvEQGSIRFGKFKITTTQVETHPH 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 170 DITlRTLQVTfqkvpKGQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQ-------------GLGPGPLCVHCS 236
Cdd:PHA02738  162 YVK-STLLLT-----DGTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRQCQkelaqeslqighnRLQPPPIVVHCN 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 237 AGCGRTGVLCAVDY-VRQLLLTQTIppnfSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAqlfsrtlqnnspLYQNLKEN 315
Cdd:PHA02738  236 AGLGRTPCYCVVDIsISRFDACATV----SIPSIVSSIRNQRYYSLFIPFQYFFCYRAVK------------RYVNLTVN 299


                  ....*...
gi 1958801479 316 SLLPQAVP 323
Cdd:PHA02738  300 KVSKKLIP 307
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
55-290 1.08e-45

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 156.40  E-value: 1.08e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  55 GNSKKNRYKDVVPYDETRVilsllQEEGhgDYINANFIRGTDGSQaYIATQGPLPHTLLDFWRLVWEFGVKVI--LMACQ 132
Cdd:COG5599    41 NGSPLNRFRDIQPYKETAL-----RANL--GYLNANYIQVIGNHR-YIATQYPLEEQLEDFFQMLFDNNTPVLvvLASDD 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 133 ETENGRRKCERYWAQEReplQAGPFCI--TLTKETALTADITLRTLQVTFQKvpKGQKeSRPVHQLQYMSWPDHGVPSSS 210
Cdd:COG5599   113 EISKPKVKMPVYFRQDG---EYGKYEVssELTESIQLRDGIEARTYVLTIKG--TGQK-KIEIPVLHVKNWPDHGAISAE 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 211 ---DHILTMVEEARCLQGLGpGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIpPNFSLFEVVLEMRKQR-PAAVQTEEQ 286
Cdd:COG5599   187 alkNLADLIDKKEKIKDPDK-LLPVVHCRAGVGRTGTLIACLALSKSINALVQ-ITLSVEEIVIDMRTSRnGGMVQTSEQ 264


                  ....
gi 1958801479 287 YRFL 290
Cdd:COG5599   265 LDVL 268
 
Name Accession Description Interval E-value
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 27-298 1.85e-171

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: 476.24  E-value: 1.85e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  27 AREFSDIKARSVAWKTEGVCSTKAGSQQGNSKKNRYKDVVPYDETRVILSLLQEEGHGDYINANFIRGTDGSQAYIATQG 106
Cdd:cd14603     1 AGEFSEIRACSAAFKADYVCSTVAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 107 PLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWAQEREPLQAGPFCITLTKETALTADITLRTLQVTFqkvpkg 186
Cdd:cd14603    81 PLSHTVLDFWRMIWQYGVKVILMACREIEMGKKKCERYWAQEQEPLQTGPFTITLVKEKRLNEEVILRTLKVTF------ 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 187 QKESRPVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPNFSL 266
Cdd:cd14603   155 QKESRSVSHFQYMAWPDHGIPDSPDCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPDFSI 234

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1958801479 267 FEVVLEMRKQRPAAVQTEEQYRFLYHTVAQLF 298
Cdd:cd14603   235 FDVVLEMRKQRPAAVQTEEQYEFLYHTVAQMF 266
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 86-292 1.20e-122

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: 350.18  E-value: 1.20e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  86 YINANFIRGTDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWAQEREP-LQAGPFCITLTKE 164
Cdd:cd14542     1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEqLQFGPFKISLEKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 165 TALTADITLRTLQVTFQKvpkgqkESRPVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGPGPLCVHCSAGCGRTGV 244
Cdd:cd14542    81 KRVGPDFLIRTLKVTFQK------ESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGCGRTGT 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1958801479 245 LCAVDYVRQLLLTQTIPPNFSLFEVVLEMRKQRPAAVQTEEQYRFLYH 292
Cdd:cd14542   155 ICAIDYVWNLLKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVYR 202
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 59-298 6.69e-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: 326.80  E-value: 6.69e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  59 KNRYKDVVPYDETRVILSLLQEEGHGDYINANFIRGTDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGR 138
Cdd:cd14602     1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 139 RKCERYWAQE-REPLQAGPFCITLTKETALTaDITLRTLQVTFQKvpkgqkESRPVHQLQYMSWPDHGVPSSSDHILTMV 217
Cdd:cd14602    81 KKCERYWAEPgEMQLEFGPFSVTCEAEKRKS-DYIIRTLKVKFNS------ETRTIYQFHYKNWPDHDVPSSIDPILELI 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 218 EEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPNFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQL 297
Cdd:cd14602   154 WDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIEL 233


                  .
gi 1958801479 298 F 298
Cdd:cd14602   234 F 234
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 4-302 5.00e-112

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: 326.89  E-value: 5.00e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479   4 QSDLVRSFLEQQEA---RDHREGAILAREFSDIKARSVAWKTEGVCSTKAGSQQGNSKKNRYKDVVPYDETRVILSLLQE 80
Cdd:cd14604     2 QVEILKKFIERVQAmksTDHNGEDNFASDFMRLRRLSTKYRTEKIYPTATGEKEENVKKNRYKDILPFDHSRVKLTLKTS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  81 EGHGDYINANFIRGTDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWA-QEREPLQAGPFCI 159
Cdd:cd14604    82 SQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWPlYGEEPMTFGPFRI 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 160 TLTKETALTaDITLRTLQVTFqkvpkgQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGPGPLCVHCSAGC 239
Cdd:cd14604   162 SCEAEQART-DYFIRTLLLEF------QNETRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGC 234

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958801479 240 GRTGVLCAVDYVRQLLLTQTIPPNFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQLFSRTL 302
Cdd:cd14604   235 GRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQLFEKQL 297
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
26-296 4.97e-111

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 322.69  E-value: 4.97e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479   26 LAREFSDIKArsvawKTEGVCSTKAGSQQGNSKKNRYKDVVPYDETRVILSLLQEEGHgDYINANFIRGTDGSQAYIATQ 105
Cdd:smart00194   2 LEEEFEKLDR-----LKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGS-DYINASYIDGPNGPKAYIATQ 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  106 GPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWAQE-REPLQAGPFCITLTKETAlTADITLRTLQVTfqkvP 184
Cdd:smart00194  76 GPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEeGEPLTYGDITVTLKSVEK-VDDYTIRTLEVT----N 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  185 KGQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQtipPNF 264
Cdd:smart00194 151 TGCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAG---KEV 227

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1958801479  265 SLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 296
Cdd:smart00194 228 DIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
56-296 6.85e-110

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 319.19  E-value: 6.85e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  56 NSKKNRYKDVVPYDETRVILSllQEEGHGDYINANFIRGTDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETE 135
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLT--GDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 136 NGRRKCERYWAQERE-PLQAGPFCITLTKETALTADITLRTLQVTFqkvpKGQKESRPVHQLQYMSWPDHGVPSSSDHIL 214
Cdd:pfam00102  79 KGREKCAQYWPEEEGeSLEYGDFTVTLKKEKEDEKDYTVRTLEVSN----GGSEETRTVKHFHYTGWPDHGVPESPNSLL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 215 TMVEEARCLQGLGP-GPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLYHT 293
Cdd:pfam00102 155 DLLRKVRKSSLDGRsGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGE---VDIFQIVKELRSQRPGMVQTLEQYIFLYDA 231


                  ...
gi 1958801479 294 VAQ 296
Cdd:pfam00102 232 ILE 234
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 86-292 3.31e-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: 270.31  E-value: 3.31e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  86 YINANFIRGTDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWAQERE-PLQAGPFCITLTKE 164
Cdd:cd00047     1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGkPLEYGDITVTLVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 165 TALtADITLRTLQVTfqkvPKGQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGPGPLCVHCSAGCGRTGV 244
Cdd:cd00047    81 EEL-SDYTIRTLELS----PKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTGT 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1958801479 245 LCAVDYVRQLLLTQTIPpnfSLFEVVLEMRKQRPAAVQTEEQYRFLYH 292
Cdd:cd00047   156 FIAIDILLERLEAEGEV---DVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 61-291 7.40e-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: 231.86  E-value: 7.40e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  61 RYKDVVPYDETRVILSLLQEEGHGDYINANFIRGTDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRK 140
Cdd:cd14548     1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 141 CERYWAQEREPLQAGPFCITLTKETALTaDITLRTLQVTfqkvpkGQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEEA 220
Cdd:cd14548    81 CDHYWPFDQDPVYYGDITVTMLSESVLP-DWTIREFKLE------RGDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLV 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958801479 221 RCLQGLGPGPLCVHCSAGCGRTGVLCAVDY-VRQLLLTQTIPPnfslFEVVLEMRKQRPAAVQTEEQYRFLY 291
Cdd:cd14548   154 RDYIKQEKGPTIVHCSAGVGRTGTFIALDRlLQQIESEDYVDI----FGIVYDLRKHRPLMVQTEAQYIFLH 221
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 86-292 2.72e-74

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: 227.52  E-value: 2.72e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  86 YINANFIR-GTDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWAQEREPLQAGPFCITLTKE 164
Cdd:cd18533     1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGEYGDLTVELVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 165 TALT-ADITLRTLQVTfqkvpKGQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGP--GPLCVHCSAGCGR 241
Cdd:cd18533    81 EENDdGGFIVREFELS-----KEDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNDSASldPPIIVHCSAGVGR 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958801479 242 TGVLCAVDYVRQLL---LTQTIPPNFSL---FEVVLEMRKQRPAAVQTEEQYRFLYH 292
Cdd:cd18533   156 TGTFIALDSLLDELkrgLSDSQDLEDSEdpvYEIVNQLRKQRMSMVQTLRQYIFLYD 212
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 28-291 1.36e-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: 225.32  E-value: 1.36e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  28 REFSDIKARSVAwkTEGVCSTKAGsqqgNSKKNRYKDVVPYDETRVILSLLQEEGHGDYINANFIRGTDGSQAYIATQGP 107
Cdd:cd14543     7 EEYEDIRREPPA--GTFLCSLAPA----NQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 108 LPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWAQEREPLQAGPFCITLTKETALTADITLRTLQVTFQKvpkgQ 187
Cdd:cd14543    81 LPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTE----T 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 188 KESRPVHQLQYMSWPDHGVPSSSDHILTMVEE-----ARCLQGLGPG--------PLCVHCSAGCGRTGVLCAVDY-VRQ 253
Cdd:cd14543   157 DESRQVTHFQFTSWPDFGVPSSAAALLDFLGEvrqqqALAVKAMGDRwkghppgpPIVVHCSAGIGRTGTFCTLDIcLSQ 236

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1958801479 254 LLLTQTIppnfSLFEVVLEMRKQRPAAVQTEEQYRFLY 291
Cdd:cd14543   237 LEDVGTL----NVMQTVRRMRTQRAFSIQTPDQYYFCY 270
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 56-296 2.01e-68

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: 214.25  E-value: 2.01e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  56 NSKKNRYKDVVPYDETRVILSLLQEEGHG-DYINANFIR------GTDG-SQAYIATQGPLPHTLLDFWRLVWEFGVKVI 127
Cdd:cd14544     1 NKGKNRYKNILPFDHTRVILKDRDPNVPGsDYINANYIRnenegpTTDEnAKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 128 LMACQETENGRRKCERYWAQEREPLQAGPFCITLTKETAlTADITLRTLQVTfqkvPKGQKES-RPVHQLQYMSWPDHGV 206
Cdd:cd14544    81 VMTTKEVERGKNKCVRYWPDEGMQKQYGPYRVQNVSEHD-TTDYTLRELQVS----KLDQGDPiREIWHYQYLSWPDHGV 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 207 PSSSDHILTMVEEARCLQG--LGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPNFSLFEVVLEMRKQRPAAVQTE 284
Cdd:cd14544   156 PSDPGGVLNFLEDVNQRQEslPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLDCDIDIQKTIQMVRSQRSGMVQTE 235

                         250
                  ....*....|..
gi 1958801479 285 EQYRFLYHTVAQ 296
Cdd:cd14544   236 AQYKFIYVAVAQ 247
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 56-291 5.73e-67

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: 209.95  E-value: 5.73e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  56 NSKKNRYKDVVPYDETRVILSLLQEEGHGDYINANFIRGTDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETE 135
Cdd:cd14553     3 NKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 136 NGRRKCERYWAQeREPLQAGPFCITLTKETALtADITLRTLQVTFQkvpkGQKESRPVHQLQYMSWPDHGVPsssDHILT 215
Cdd:cd14553    83 RSRVKCDQYWPT-RGTETYGLIQVTLLDTVEL-ATYTVRTFALHKN----GSSEKREVRQFQFTAWPDHGVP---EHPTP 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 216 MVEEARCLQGLGP---GPLCVHCSAGCGRTGVLCAVD-YVRQLLLTQTIppnfSLFEVVLEMRKQRPAAVQTEEQYRFLY 291
Cdd:cd14553   154 FLAFLRRVKACNPpdaGPIVVHCSAGVGRTGCFIVIDsMLERIKHEKTV----DIYGHVTCLRAQRNYMVQTEDQYIFIH 229
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 86-291 3.81e-65

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: 204.12  E-value: 3.81e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  86 YINANFIRGTDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWAQEREPlQAGPFCITLTKET 165
Cdd:cd14549     1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTE-TYGNIQVTLLSTE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 166 ALtADITLRTLQVTFQKV--PKGQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGPGPLCVHCSAGCGRTG 243
Cdd:cd14549    80 VL-ATYTVRTFSLKNLKLkkVKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVGRTG 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1958801479 244 VLCAVD-YVRQLLLTQTIppnfSLFEVVLEMRKQRPAAVQTEEQYRFLY 291
Cdd:cd14549   159 TYIVIDsMLQQIQDKGTV----NVFGFLKHIRTQRNYLVQTEEQYIFIH 203
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 60-291 6.48e-65

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: 204.35  E-value: 6.48e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  60 NRYKDVVPYDETRVILSLLQEEGHGDYINANFIRGTDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRR 139
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 140 KCERYWAQEREPLQAGPFCITLTKETALtADITLRTLQVTFQKvpkgQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEE 219
Cdd:cd14619    81 KCEHYWPLDYTPCTYGHLRVTVVSEEVM-ENWTVREFLLKQVE----EQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRL 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958801479 220 AR--CLQGLGPGPLCVHCSAGCGRTGVLCAVDY-VRQLLLTQTIPPnfslFEVVLEMRKQRPAAVQTEEQYRFLY 291
Cdd:cd14619   156 LRqwLDQTMSGGPTVVHCSAGVGRTGTLIALDVlLQQLQSEGLLGP----FSFVQKMRENRPLMVQTESQYVFLH 226
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 60-292 1.14e-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: 201.09  E-value: 1.14e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  60 NRYKDVVPYDETRVILSLLQEEGHGDYINANFIRGTDG-SQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENgR 138
Cdd:cd14547     1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYDGeEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA-K 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 139 RKCERYWAQErEPLQAGPFCITLTKeTALTADITLRTLQVTFqkvpkgQKESRPVHQLQYMSWPDHGVPSSSDHILTM-- 216
Cdd:cd14547    80 EKCAQYWPEE-ENETYGDFEVTVQS-VKETDGYTVRKLTLKY------GGEKRYLKHYWYTSWPDHKTPEAAQPLLSLvq 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958801479 217 -VEEARcLQGLGPGPLCVHCSAGCGRTGVLCAVDY-VRQLLLTQTIppnfSLFEVVLEMRKQRPAAVQTEEQYRFLYH 292
Cdd:cd14547   152 eVEEAR-QTEPHRGPIVVHCSAGIGRTGCFIATSIgCQQLREEGVV----DVLGIVCQLRLDRGGMVQTAEQYEFVHR 224
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 60-291 5.35e-63

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: 5.35e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  60 NRYKDVVPYDETRVILSLLQEEGHGDYINANFIRGTDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRR 139
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 140 KCERYWAQEREPLQAGPFCITLTKETAlTADITLRtlqvTFQKVPKGQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEE 219
Cdd:cd14618    81 LCDHYWPSESTPVSYGHITVHLLAQSS-EDEWTRR----EFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFREL 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958801479 220 AR--CLQGLGPGPLCVHCSAGCGRTGVLCAVD-YVRQLLLTQTIppnfSLFEVVLEMRKQRPAAVQTEEQYRFLY 291
Cdd:cd14618   156 VRehVQATKGKGPTLVHCSAGVGRSGTFIALDrLLRQLKEEKVV----DVFNTVYILRMHRYLMIQTLSQYIFLH 226
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 47-296 1.70e-62

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: 199.34  E-value: 1.70e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  47 STKAGSQQGNSKKNRYKDVVPYDETRVILSLLQEEGHG-DYINANFIRG-----TDGSQAYIATQGPLPHTLLDFWRLVW 120
Cdd:cd14606     9 QRLEGQRPENKSKNRYKNILPFDHSRVILQGRDSNIPGsDYINANYVKNqllgpDENAKTYIASQGCLEATVNDFWQMAW 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 121 EFGVKVILMACQETENGRRKCERYWAQEREPLQAGPFCITLTKETAlTADITLRTLQVTfqkVPKGQKESRPVHQLQYMS 200
Cdd:cd14606    89 QENSRVIVMTTREVEKGRNKCVPYWPEVGMQRAYGPYSVTNCGEHD-TTEYKLRTLQVS---PLDNGELIREIWHYQYLS 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 201 WPDHGVPSSSDHILTMVEEARCLQGLGP--GPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPNFSLFEVVLEMRKQRP 278
Cdd:cd14606   165 WPDHGVPSEPGGVLSFLDQINQRQESLPhaGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLDCDIDIQKTIQMVRAQRS 244

                         250
                  ....*....|....*...
gi 1958801479 279 AAVQTEEQYRFLYHTVAQ 296
Cdd:cd14606   245 GMVQTEAQYKFIYVAIAQ 262
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 41-290 2.26e-62

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: 199.31  E-value: 2.26e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  41 KTEGVCSTKAGSQQgNSKKNRYKDVVPYDETRVILsllqeEGHGDYINANF----IRGTDGSQAYIATQGPLPHTLLDFW 116
Cdd:cd14600    26 KKPGLAITCAKLPQ-NMDKNRYKDVLPYDATRVVL-----QGNEDYINASYvnmeIPSANIVNKYIATQGPLPHTCAQFW 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 117 RLVWEFGVKVILMACQETENGRRKCERYWAQEREPLQAGPFCITLTKETALTADITlRTLQVTfqKVPKGQKesRPVHQL 196
Cdd:cd14600   100 QVVWEQKLSLIVMLTTLTERGRTKCHQYWPDPPDVMEYGGFRVQCHSEDCTIAYVF-REMLLT--NTQTGEE--RTVTHL 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 197 QYMSWPDHGVPSSSDHILTMVEEARCLQgLGPGPLCVHCSAGCGRTGVLCAVDYVrqLLLTQTIPPNFSLfEVVLEMRKQ 276
Cdd:cd14600   175 QYVAWPDHGVPDDSSDFLEFVNYVRSKR-VENEPVLVHCSAGIGRTGVLVTMETA--MCLTERNQPVYPL-DIVRKMRDQ 250

                         250
                  ....*....|....
gi 1958801479 277 RPAAVQTEEQYRFL 290
Cdd:cd14600   251 RAMMVQTSSQYKFV 264
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 60-290 1.14e-61

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: 196.19  E-value: 1.14e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  60 NRYKDVVPYDETRVILSLlQEEGHGDYINANFIRGTDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRR 139
Cdd:cd14615     1 NRYNNVLPYDISRVKLSV-QSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 140 KCERYWAQErEPLQAGPFCITLTKETALTaDITLRTLQVTFQKvpkgQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEE 219
Cdd:cd14615    80 KCEEYWPSK-QKKDYGDITVTMTSEIVLP-EWTIRDFTVKNAQ----TNESRTVRHFHFTSWPDHGVPETTDLLINFRHL 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958801479 220 AR--CLQGLGPGPLCVHCSAGCGRTGVLCAVDY-VRQLLLTQTIppnfSLFEVVLEMRKQRPAAVQTEEQYRFL 290
Cdd:cd14615   154 VReyMKQNPPNSPILVHCSAGVGRTGTFIAIDRlIYQIENENVV----DVYGIVYDLRMHRPLMVQTEDQYVFL 223
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 86-296 8.10e-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: 192.97  E-value: 8.10e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  86 YINANFIRGTDGSQA--YIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWA-QEREPL-QAGPFCITL 161
Cdd:cd14538     1 YINASHIRIPVGGDTyhYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPdSLNKPLiCGGRLEVSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 162 TKETALtADITLRTLQVTfqkvPKGQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQglGPGPLCVHCSAGCGR 241
Cdd:cd14538    81 EKYQSL-QDFVIRRISLR----DKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIH--NSGPIVVHCSAGIGR 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958801479 242 TGVLCAVDYVrQLLLTQTIPpnFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 296
Cdd:cd14538   154 TGVLITIDVA-LGLIERDLP--FDIQDIVKDLREQRQGMIQTKDQYIFCYKACLE 205
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 54-294 5.80e-60

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


Pssm-ID: 350445 [Multi-domain]  Cd Length: 234  Bit Score: 191.97  E-value: 5.80e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  54 QGNSKKNRYKDVVPYDETRVilsLLQEEGhgDYINANFIRGTDGSQ--AYIATQGPLPHTLLDFWRLVWEFGVKVILMAC 131
Cdd:cd14597     1 KENRKKNRYKNILPYDTTRV---PLGDEG--GYINASFIKMPVGDEefVYIACQGPLPTTVADFWQMVWEQKSTVIAMMT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 132 QETENGRRKCERYWAQE-------REPLQagpfcITLTKETALTADItLRTLQVtfQKVPKGqkESRPVHQLQYMSWPDH 204
Cdd:cd14597    76 QEVEGGKIKCQRYWPEIlgkttmvDNRLQ-----LTLVRMQQLKNFV-IRVLEL--EDIQTR--EVRHITHLNFTAWPDH 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 205 GVPSSSDHILTMVEEARCLQGLgpGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTippNFSLFEVVLEMRKQRPAAVQTE 284
Cdd:cd14597   146 DTPSQPEQLLTFISYMRHIHKS--GPIITHCSAGIGRSGTLICIDVVLGLISKDL---DFDISDIVRTMRLQRHGMVQTE 220

                         250
                  ....*....|
gi 1958801479 285 EQYRFLYHTV 294
Cdd:cd14597   221 DQYIFCYQVI 230
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 56-296 6.77e-60

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: 192.94  E-value: 6.77e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  56 NSKKNRYKDVVPYDETRVILSLL--QEEGHGDYINANFIRGTDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQE 133
Cdd:cd17667    27 NKHKNRYINILAYDHSRVKLRPLpgKDSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 134 TENGRRKCERYWAQEREPlQAGPFCITLtKETALTADITLRTLQVTFQKV-------PKGQKESRPVHQLQYMSWPDHGV 206
Cdd:cd17667   107 VEKGRRKCDQYWPTENSE-EYGNIIVTL-KSTKIHACYTVRRFSIRNTKVkkgqkgnPKGRQNERTVIQYHYTQWPDMGV 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 207 PSSSDHILTMVEEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTippNFSLFEVVLEMRKQRPAAVQTEEQ 286
Cdd:cd17667   185 PEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKS---TVNVLGFLKHIRTQRNYLVQTEEQ 261

                         250
                  ....*....|
gi 1958801479 287 YRFLYHTVAQ 296
Cdd:cd17667   262 YIFIHDALLE 271
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 60-291 4.06e-59

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: 189.36  E-value: 4.06e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  60 NRYKDVVPYDETRVILSLLQEEGHGDYINANFIRGTDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRR 139
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 140 KCERYWAQEREPLQAGPFCITLTKETALtADITLRTLQVTFQKvpkgQKES-RPVHQLQYMSWPDHGVPSSSDHILTMVE 218
Cdd:cd14617    81 KCDHYWPADQDSLYYGDLIVQMLSESVL-PEWTIREFKICSEE----QLDApRLVRHFHYTVWPDHGVPETTQSLIQFVR 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958801479 219 EARCL--QGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTippNFSLFEVVLEMRKQRPAAVQTEEQYRFLY 291
Cdd:cd14617   156 TVRDYinRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKD---SVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 56-296 1.15e-58

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: 188.70  E-value: 1.15e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  56 NSKKNRYKDVVPYDETRVILSLLQEEGHGDYINANFIRGTDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETE 135
Cdd:cd14630     3 NRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 136 NGRRKCERYWAQEREPLqaGPFCITLTkETALTADITLRTLqvTFQKvpKGQKESRPVHQLQYMSWPDHGVPSSSDHILT 215
Cdd:cd14630    83 VGRVKCVRYWPDDTEVY--GDIKVTLI-ETEPLAEYVIRTF--TVQK--KGYHEIREIRQFHFTSWPDHGVPCYATGLLG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 216 MVEEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVA 295
Cdd:cd14630   156 FVRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGV---VDIFNCVRELRAQRVNMVQTEEQYVFVHDAIL 232


                  .
gi 1958801479 296 Q 296
Cdd:cd14630   233 E 233
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 56-294 1.72e-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: 188.56  E-value: 1.72e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  56 NSKKNRYKDVVPYDETRVILSLLQEEGHGDYINANFIRGTDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETE 135
Cdd:cd14614    12 NRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 136 NGRRKCERYWAQEREPLQAGPFCITLTKETALTaDITLRTLQVTFqkvpkgQKESRPVHQLQYMSWPDHGVPS--SSDHI 213
Cdd:cd14614    92 KRRVKCDHYWPFTEEPVAYGDITVEMLSEEEQP-DWAIREFRVSY------ADEVQDVMHFNYTAWPDHGVPTanAAESI 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 214 LTMVEEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLYHT 293
Cdd:cd14614   165 LQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEF---VDILGLVSEMRSYRMSMVQTEEQYIFIHQC 241


                  .
gi 1958801479 294 V 294
Cdd:cd14614   242 V 242
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 56-293 3.22e-58

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: 187.35  E-value: 3.22e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  56 NSKKNRYKDVVPYDETRVILSLLQEEGHGDYINANFIRGTDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETE 135
Cdd:cd14554     6 NKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKLRE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 136 NGRRKCERYWAQEREpLQAGPFCITLTKETALTADItLRTLQVTFQKvpkgQKESRPVHQLQYMSWPDHGVPSSSDHIL- 214
Cdd:cd14554    86 MGREKCHQYWPAERS-ARYQYFVVDPMAEYNMPQYI-LREFKVTDAR----DGQSRTVRQFQFTDWPEQGVPKSGEGFId 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 215 --TMVEEARCLQGlGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLYH 292
Cdd:cd14554   160 fiGQVHKTKEQFG-QEGPITVHCSAGVGRTGVFITLSIVLERMRYEGV---VDVFQTVKLLRTQRPAMVQTEDQYQFCYR 235


                  .
gi 1958801479 293 T 293
Cdd:cd14554   236 A 236
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 56-294 5.76e-58

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: 187.53  E-value: 5.76e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  56 NSKKNRYKDVVPYDETRVILSL--LQEEGhGDYINANFI--------RGTDGSQAYIATQGPLPHTLLDFWRLVWEFGVK 125
Cdd:cd14605     2 NKNKNRYKNILPFDHTRVVLHDgdPNEPV-SDYINANIImpefetkcNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 126 VILMACQETENGRRKCERYWAQEREPLQAGPFCITLTKETAlTADITLRTLQVTfqKVPKGQKEsRPVHQLQYMSWPDHG 205
Cdd:cd14605    81 VIVMTTKEVERGKSKCVKYWPDEYALKEYGVMRVRNVKESA-AHDYILRELKLS--KVGQGNTE-RTVWQYHFRTWPDHG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 206 VPSSSDHILTMVEEARCLQG--LGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPNFSLFEVVLEMRKQRPAAVQT 283
Cdd:cd14605   157 VPSDPGGVLDFLEEVHHKQEsiMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVDCDIDVPKTIQMVRSQRSGMVQT 236

                         250
                  ....*....|.
gi 1958801479 284 EEQYRFLYHTV 294
Cdd:cd14605   237 EAQYRFIYMAV 247
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 56-296 1.33e-57

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: 187.17  E-value: 1.33e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  56 NSKKNRYKDVVPYDETRVILSLLQEEGHGDYINANFIRGTDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETE 135
Cdd:cd14626    41 NKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEE 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 136 NGRRKCERYWAQeREPLQAGPFCITLTKETALtADITLRtlqvTFQKVPKGQKESRPVHQLQYMSWPDHGVPSSSDHILT 215
Cdd:cd14626   121 KSRVKCDQYWPI-RGTETYGMIQVTLLDTVEL-ATYSVR----TFALYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILA 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 216 MVEEARCLQGLGPGPLCVHCSAGCGRTGVLCAVD-YVRQLLLTQTIppnfSLFEVVLEMRKQRPAAVQTEEQYRFLYHTV 294
Cdd:cd14626   195 FLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDaMLERMKHEKTV----DIYGHVTCMRSQRNYMVQTEDQYIFIHEAL 270


                  ..
gi 1958801479 295 AQ 296
Cdd:cd14626   271 LE 272
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 59-291 4.33e-57

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: 184.52  E-value: 4.33e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  59 KNRYKDVVPYDETRVILSLLQEEGhgDYINANFIRGTDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGR 138
Cdd:cd14545     1 LNRYRDRDPYDHDRSRVKLKQGDN--DYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 139 RKCERYWAQerEPLQAGPFCITLTKETALTADI----TLRTLQVTFQKVPkgqkESRPVHQLQYMSWPDHGVPSSSD--- 211
Cdd:cd14545    79 IKCAQYWPQ--GEGNAMIFEDTGLKVTLLSEEDksyyTVRTLELENLKTQ----ETREVLHFHYTTWPDFGVPESPAafl 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 212 HILTMVEEARCLQGlGPGPLCVHCSAGCGRTGVLCAVDYVrQLLLTQTIPPNFSLFEVVLEMRKQRPAAVQTEEQYRFLY 291
Cdd:cd14545   153 NFLQKVRESGSLSS-DVGPPVVHCSAGIGRSGTFCLVDTC-LVLIEKGNPSSVDVKKVLLEMRKYRMGLIQTPDQLRFSY 230
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 85-289 1.32e-56

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: 182.53  E-value: 1.32e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  85 DYINANF----IRGTDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWAQEREPLQAGPFCIT 160
Cdd:cd14541     1 DYINANYvnmeIPGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGETMQFGNLQIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 161 LTKETAlTADITLRTLQVTFQKvpkgQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEEAR-CLQGLGPgPLCVHCSAGC 239
Cdd:cd14541    81 CVSEEV-TPSFAFREFILTNTN----TGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRqNRVGMVE-PTVVHCSAGI 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958801479 240 GRTGVLCAVDYVrqLLLTQTIPPNFSLfEVVLEMRKQRPAAVQTEEQYRF 289
Cdd:cd14541   155 GRTGVLITMETA--MCLIEANEPVYPL-DIVRTMRDQRAMLIQTPSQYRF 201
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 55-296 1.60e-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: 178.11  E-value: 1.60e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  55 GNSKKNRYKDVVPYDETRVILSLLQ-EEGHGDYINANFIRGTDGS-QAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQ 132
Cdd:cd14612    14 GHASKDRYKTILPNPQSRVCLRRAGsQEEEGSYINANYIRGYDGKeKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITK 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 133 ETEnGRRKCERYWAQEREPLqaGPFCITLtKETALTADITLRTLQVtfqkvpKGQKESRPVHQLQYMSWPDHGVPSSSD- 211
Cdd:cd14612    94 LKE-KKEKCVHYWPEKEGTY--GRFEIRV-QDMKECDGYTIRDLTI------QLEEESRSVKHYWFSSWPDHQTPESAGp 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 212 --HILTMVEEARCLQGlGPGPLCVHCSAGCGRTGVLCAVDY-VRQLLLTQTIppnfSLFEVVLEMRKQRPAAVQTEEQYR 288
Cdd:cd14612   164 llRLVAEVEESRQTAA-SPGPIVVHCSAGIGRTGCFIATSIgCQQLKDTGKV----DILGIVCQLRLDRGGMIQTSEQYQ 238


                  ....*...
gi 1958801479 289 FLYHTVAQ 296
Cdd:cd14612   239 FLHHTLAL 246
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 49-296 1.32e-52

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: 174.44  E-value: 1.32e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  49 KAGSQQGNSKKNRYKDVVPYDETRVILsllqEEGHGDYINANFIRGTDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVIL 128
Cdd:cd14608    18 RVAKLPKNKNRNRYRDVSPFDHSRIKL----HQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVV 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 129 MACQETENGRRKCERYWAQEREplQAGPFCITLTKETALTADI----TLRTLQVTFQKVpkgqKESRPVHQLQYMSWPDH 204
Cdd:cd14608    94 MLNRVMEKGSLKCAQYWPQKEE--KEMIFEDTNLKLTLISEDIksyyTVRQLELENLTT----QETREILHFHYTTWPDF 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 205 GVPSSSDHILTMVEEARCLQGLGP--GPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPNFSLFEVVLEMRKQRPAAVQ 282
Cdd:cd14608   168 GVPESPASFLNFLFKVRESGSLSPehGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQ 247

                         250
                  ....*....|....
gi 1958801479 283 TEEQYRFLYHTVAQ 296
Cdd:cd14608   248 TADQLRFSYLAVIE 261
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 86-296 4.00e-52

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: 171.10  E-value: 4.00e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  86 YINANFIRGTDGSQA--YIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWAQ---EREPLQAGPFCIT 160
Cdd:cd14540     1 YINASHITATVGGKQrfYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTlggEHDALTFGEYKVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 161 LTKETAlTADITLRTLQVtfQKVPKGQkeSRPVHQLQYMSWPDHGVPSSSDHILTMVEEA-----RCLQGLG----PGPL 231
Cdd:cd14540    81 TKFSVS-SGCYTTTGLRV--KHTLSGQ--SRTVWHLQYTDWPDHGCPEDVSGFLDFLEEInsvrrHTNQDVAghnrNPPT 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958801479 232 CVHCSAGCGRTGVLCAVDYVrQLLLTQTIPPNfsLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 296
Cdd:cd14540   156 LVHCSAGVGRTGVVILADLM-LYCLDHNEELD--IPRVLALLRHQRMLLVQTLAQYKFVYNVLIQ 217
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 86-294 1.17e-51

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: 169.77  E-value: 1.17e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  86 YINANFIRGTDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWAQEREPlQAGPFCITLtKET 165
Cdd:cd17668     1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSE-EYGNFLVTQ-KSV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 166 ALTADITLRTLQVTFQKVPKGQKESRP----VHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGPGPLCVHCSAGCGR 241
Cdd:cd17668    79 QVLAYYTVRNFTLRNTKIKKGSQKGRPsgrvVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSAGVGR 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958801479 242 TGVLCAVD-YVRQLLLTQTIppnfSLFEVVLEMRKQRPAAVQTEEQYRFLYHTV 294
Cdd:cd17668   159 TGTYIVLDsMLQQIQHEGTV----NIFGFLKHIRSQRNYLVQTEEQYVFIHDAL 208
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 86-294 9.02e-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: 167.06  E-value: 9.02e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  86 YINANFIRGTDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWAQEREpLQAGPFCITLTKET 165
Cdd:cd14552     1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGS-VSSGDITVELKDQT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 166 aLTADITLRTLQVTFQKvpkgQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEEA-RCLQGLGPGPLCVHCSAGCGRTGV 244
Cdd:cd14552    80 -DYEDYTLRDFLVTKGK----GGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVqKQQQQSGNHPITVHCSAGAGRTGT 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958801479 245 LCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTV 294
Cdd:cd14552   155 FCALSTVLERVKAEGV---LDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 86-294 2.25e-50

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: 166.08  E-value: 2.25e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  86 YINANFIRGTDGSQA--YIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWA-QEREPLQAGPFCITLT 162
Cdd:cd14596     1 YINASYITMPVGEEElfYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPeTLQEPMELENYQLRLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 163 KETALtADITLRTLQVtfqkVPKGQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLgpGPLCVHCSAGCGRT 242
Cdd:cd14596    81 NYQAL-QYFIIRIIKL----VEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNT--GPIVVHCSAGIGRA 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958801479 243 GVLCAVDYVRQLLLTQTippNFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTV 294
Cdd:cd14596   154 GVLICVDVLLSLIEKDL---SFNIKDIVREMRQQRYGMIQTKDQYLFCYKVV 202
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 43-296 3.24e-50

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: 168.29  E-value: 3.24e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  43 EGVCSTKA-------GSQQGNSKKNRYKDVVPYDETRVILSLLQEEGHGDYINANFIRGTDGSQ-AYIATQGPLPHTLLD 114
Cdd:cd14609    22 QALCAYQAepntcstAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPIIEHDPRMpAYIATQGPLSHTIAD 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 115 FWRLVWEFGVKVILMACQETENGRRKCERYWAQEREPLQaGPFCITLTKETALTADITLRTLqvtFQKVPKGQkESRPVH 194
Cdd:cd14609   102 FWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLY-HIYEVNLVSEHIWCEDFLVRSF---YLKNVQTQ-ETRTLT 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 195 QLQYMSWPDHGVPSSSDHILTMVEEA-RCLQGLGpGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTipPNFSLFEVVLEM 273
Cdd:cd14609   177 QFHFLSWPAEGIPSSTRPLLDFRRKVnKCYRGRS-CPIIVHCSDGAGRTGTYILIDMVLNRMAKGV--KEIDIAATLEHV 253

                         250       260
                  ....*....|....*....|...
gi 1958801479 274 RKQRPAAVQTEEQYRFLYHTVAQ 296
Cdd:cd14609   254 RDQRPGMVRTKDQFEFALTAVAE 276
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 85-298 3.90e-50

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: 165.89  E-value: 3.90e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  85 DYINANFIRGTDGSQA----YIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWAQEREPLQAGPFCIT 160
Cdd:cd14601     1 DYINANYINMEIPSSSiinrYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSSSYGGFQVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 161 LTKETALTADItLRTLQVTFQKvpkgQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGPGPLCVHCSAGCG 240
Cdd:cd14601    81 CHSEEGNPAYV-FREMTLTNLE----KNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVHCSAGIG 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958801479 241 RTGVLCAVDYVrqLLLTQTIPPNFSLfEVVLEMRKQRPAAVQTEEQYRFLYHTVAQLF 298
Cdd:cd14601   156 RTGVLITMETA--MCLIECNQPVYPL-DIVRTMRDQRAMMIQTPSQYRFVCEAILKVY 210
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 43-296 4.55e-50

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: 167.93  E-value: 4.55e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  43 EGVCSTKA-------GSQQGNSKKNRYKDVVPYDETRVILSLLQEEGHGDYINANFIRGTDG-SQAYIATQGPLPHTLLD 114
Cdd:cd14610    24 EALCAYQAepnatnvAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPIMDHDPrNPAYIATQGPLPATVAD 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 115 FWRLVWEFGVKVILMACQETENGRRKCERYWAQEREPLQAgPFCITLTKETALTADITLRTLQVTFQKVpkgqKESRPVH 194
Cdd:cd14610   104 FWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSNLYH-IYEVNLVSEHIWCEDFLVRSFYLKNLQT----NETRTVT 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 195 QLQYMSWPDHGVPSSSDHILTMVEEA-RCLQGLGpGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTipPNFSLFEVVLEM 273
Cdd:cd14610   179 QFHFLSWNDQGVPASTRSLLDFRRKVnKCYRGRS-CPIIVHCSDGAGRSGTYILIDMVLNKMAKGA--KEIDIAATLEHL 255

                         250       260
                  ....*....|....*....|...
gi 1958801479 274 RKQRPAAVQTEEQYRFLYHTVAQ 296
Cdd:cd14610   256 RDQRPGMVQTKEQFEFALTAVAE 278
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 56-296 5.13e-50

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: 167.53  E-value: 5.13e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  56 NSKKNRYKDVVPYDETRVILSLLQEEGHGDYINANFIRGTDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETE 135
Cdd:cd14633    40 NRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVE 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 136 NGRRKCERYWAQEREPLQagPFCITLTkETALTADITLRTLQVTfqkvPKGQKESRPVHQLQYMSWPDHGVPSSSDHILT 215
Cdd:cd14633   120 VGRVKCCKYWPDDTEIYK--DIKVTLI-ETELLAEYVIRTFAVE----KRGVHEIREIRQFHFTGWPDHGVPYHATGLLG 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 216 MVEEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVA 295
Cdd:cd14633   193 FVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGV---VDIYNCVRELRSRRVNMVQTEEQYVFIHDAIL 269


                  .
gi 1958801479 296 Q 296
Cdd:cd14633   270 E 270
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 56-296 5.89e-50

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: 167.58  E-value: 5.89e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  56 NSKKNRYKDVVPYDETRVILSLLQEEGHGDYINANFIRGTDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETE 135
Cdd:cd14625    47 NKPKNRYANVIAYDHSRVILQPIEGIMGSDYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEE 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 136 NGRRKCERYWAQeREPLQAGPFCITLTkETALTADITLRtlqvTFQKVPKGQKESRPVHQLQYMSWPDHGVPSSSDHILT 215
Cdd:cd14625   127 KSRIKCDQYWPS-RGTETYGMIQVTLL-DTIELATFCVR----TFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLA 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 216 MVEEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTippNFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVA 295
Cdd:cd14625   201 FLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEK---TVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALL 277


                  .
gi 1958801479 296 Q 296
Cdd:cd14625   278 E 278
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 56-291 2.03e-49

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: 166.45  E-value: 2.03e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  56 NSKKNRYKDVVPYDETRVILSLLQEEGHGDYINANFIRGTDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETE 135
Cdd:cd14628    52 NKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLRE 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 136 NGRRKCERYWAQEREPlQAGPFCITLTKETALTADItLRTLQVTFQKvpkgQKESRPVHQLQYMSWPDHGVPSSSDHILT 215
Cdd:cd14628   132 MGREKCHQYWPAERSA-RYQYFVVDPMAEYNMPQYI-LREFKVTDAR----DGQSRTVRQFQFTDWPEQGVPKSGEGFID 205

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958801479 216 MVEEA-RCLQGLGP-GPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLY 291
Cdd:cd14628   206 FIGQVhKTKEQFGQdGPISVHCSAGVGRTGVFITLSIVLERMRYEGV---VDIFQTVKMLRTQRPAMVQTEDQYQFCY 280
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 56-291 5.08e-49

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: 165.29  E-value: 5.08e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  56 NSKKNRYKDVVPYDETRVILSLLQEEGHGDYINANFIRGTDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETE 135
Cdd:cd14624    47 NKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEE 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 136 NGRRKCERYWAQeREPLQAGPFCITLTkETALTADITLRtlqvTFQKVPKGQKESRPVHQLQYMSWPDHGVPSSSDHILT 215
Cdd:cd14624   127 RSRVKCDQYWPS-RGTETYGLIQVTLL-DTVELATYCVR----TFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLA 200

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958801479 216 MVEEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTippNFSLFEVVLEMRKQRPAAVQTEEQYRFLY 291
Cdd:cd14624   201 FLRRVKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEK---TVDIYGHVTLMRAQRNYMVQTEDQYIFIH 273
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 60-291 6.26e-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: 163.15  E-value: 6.26e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  60 NRYKDVVPYDETRVilSLLQEEG--HGDYINANFIRGTDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENG 137
Cdd:cd14616     1 NRFPNIKPYNNNRV--KLIADAGvpGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 138 RRKCERYWAQEREPLQA-GPFCIT-LTKETALtaDITLRTLQVtfqkvpKGQKESRPVHQLQYMSWPDHGVPSSSDHILT 215
Cdd:cd14616    79 RIRCHQYWPEDNKPVTVfGDIVITkLMEDVQI--DWTIRDLKI------ERHGDYMMVRQCNFTSWPEHGVPESSAPLIH 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958801479 216 MVEEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYvrqllLTQTIPPN--FSLFEVVLEMRKQRPAAVQTEEQYRFLY 291
Cdd:cd14616   151 FVKLVRASRAHDNTPMIVHCSAGVGRTGVFIALDH-----LTQHINDHdfVDIYGLVAELRSERMCMVQNLAQYIFLH 223
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 46-294 6.72e-49

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: 163.98  E-value: 6.72e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  46 CSTKAGSQQGNSKKNRYKDVVPYDETRVILsllqEEGHGDYINANFIRGTDGSQAYIATQGPLPHTLLDFWRLVWEFGVK 125
Cdd:cd14607    14 YPHRVAKYPENRNRNRYRDVSPYDHSRVKL----QNTENDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTK 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 126 VILMACQETENGRRKCERYW-AQEREPL--QAGPFCITLTKETaLTADITLRTLQVtfQKVPKGqkESRPVHQLQYMSWP 202
Cdd:cd14607    90 AVVMLNRIVEKDSVKCAQYWpTDEEEVLsfKETGFSVKLLSED-VKSYYTVHLLQL--ENINSG--ETRTISHFHYTTWP 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 203 DHGVPSSSDHILTM---VEEARCLqGLGPGPLCVHCSAGCGRTGVLCAVDYVrQLLLTQTIPPNFSLFEVVLEMRKQRPA 279
Cdd:cd14607   165 DFGVPESPASFLNFlfkVRESGSL-SPEHGPAVVHCSAGIGRSGTFSLVDTC-LVLMEKKDPDSVDIKQVLLDMRKYRMG 242

                         250
                  ....*....|....*
gi 1958801479 280 AVQTEEQYRFLYHTV 294
Cdd:cd14607   243 LIQTPDQLRFSYMAV 257
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 56-296 1.05e-48

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: 164.52  E-value: 1.05e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  56 NSKKNRYKDVVPYDETRVILSLLQEEGHGDYINANFIRGTDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETE 135
Cdd:cd14627    53 NKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLRE 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 136 NGRRKCERYWAQEREPlQAGPFCITLTKETALTADItLRTLQVTFQKvpkgQKESRPVHQLQYMSWPDHGVPSSSDHILT 215
Cdd:cd14627   133 MGREKCHQYWPAERSA-RYQYFVVDPMAEYNMPQYI-LREFKVTDAR----DGQSRTVRQFQFTDWPEQGVPKSGEGFID 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 216 MVEEA-RCLQGLGP-GPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLYHT 293
Cdd:cd14627   207 FIGQVhKTKEQFGQdGPISVHCSAGVGRTGVFITLSIVLERMRYEGV---VDIFQTVKMLRTQRPAMVQTEDEYQFCYQA 283


                  ...
gi 1958801479 294 VAQ 296
Cdd:cd14627   284 ALE 286
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 62-294 2.16e-48

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: 162.03  E-value: 2.16e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  62 YKDVVPYDETRVILSLLQEEGHGDYINANFIRGTDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKC 141
Cdd:cd14620     1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 142 ERYWaqerePLQA----GPFCITLTKETALTaDITLRTLQVTFQkVPKGQKESRPVHQLQYMSWPDHGVPSSSDHILTMV 217
Cdd:cd14620    81 YQYW-----PDQGcwtyGNIRVAVEDCVVLV-DYTIRKFCIQPQ-LPDGCKAPRLVTQLHFTSWPDFGVPFTPIGMLKFL 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958801479 218 EEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTippNFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTV 294
Cdd:cd14620   154 KKVKSVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQ---KVDVFEFVSRIRNQRPQMVQTDMQYSFIYQAL 227
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 41-298 6.89e-48

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: 162.47  E-value: 6.89e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  41 KTEGVCSTKAGSQqgNSKKNRYKDVVPYDETRVILSLLQEEGHGdYINANFIRGTDGSQA--YIATQGPLPHTLLDFWRL 118
Cdd:cd14599    25 KADGVFTTATLPE--NAERNRIREVVPYEENRVELVPTKENNTG-YINASHIKVTVGGEEwhYIATQGPLPHTCHDFWQM 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 119 VWEFGVKVILMACQETENGRRKCERYWAQ---EREPLQAGPFCITlTKETalTADITLRTLQVTFQKVPKGQKesRPVHQ 195
Cdd:cd14599   102 VWEQGVNVIAMVTAEEEGGRSKSHRYWPKlgsKHSSATYGKFKVT-TKFR--TDSGCYATTGLKVKHLLSGQE--RTVWH 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 196 LQYMSWPDHGVPSSSDHILTMVEEARCLQ-----------GLGPgPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTippNF 264
Cdd:cd14599   177 LQYTDWPDHGCPEEVQGFLSYLEEIQSVRrhtnsmldstkNCNP-PIVVHCSAGVGRTGVVILTELMIGCLEHNE---KV 252

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1958801479 265 SLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQLF 298
Cdd:cd14599   253 EVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQFL 286
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 61-296 8.95e-48

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: 160.21  E-value: 8.95e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  61 RYKDVVPYDETRVILSLLQEEGHGDYINANFIRGTDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRK 140
Cdd:cd14623     1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 141 CERYWAQEREpLQAGPFCITLTKETAlTADITLRTLQVTFQKvpkgQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEEA 220
Cdd:cd14623    81 CAQYWPSDGS-VSYGDITIELKKEEE-CESYTVRDLLVTNTR----ENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAV 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958801479 221 -RCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 296
Cdd:cd14623   155 qKQQQQSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGI---LDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
PHA02738 PHA02738
hypothetical protein; Provisional
 11-323 3.47e-47

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 161.63  E-value: 3.47e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  11 FLEQQEARDHREgaILAREFSDIkarsVAWKTEGVCStkagSQQGNSKKNRYKDVVPYDETRVILSllQEEGHGDYINAN 90
Cdd:PHA02738   14 FLALMEKSDCEE--VITREHQKV----ISEKVDGTFN----AEKKNRKLNRYLDAVCFDHSRVILP--AERNRGDYINAN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  91 FIRGTDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWAQ-EREPLQAGPFCITLTKETALTA 169
Cdd:PHA02738   82 YVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDvEQGSIRFGKFKITTTQVETHPH 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 170 DITlRTLQVTfqkvpKGQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQ-------------GLGPGPLCVHCS 236
Cdd:PHA02738  162 YVK-STLLLT-----DGTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRQCQkelaqeslqighnRLQPPPIVVHCN 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 237 AGCGRTGVLCAVDY-VRQLLLTQTIppnfSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAqlfsrtlqnnspLYQNLKEN 315
Cdd:PHA02738  236 AGLGRTPCYCVVDIsISRFDACATV----SIPSIVSSIRNQRYYSLFIPFQYFFCYRAVK------------RYVNLTVN 299


                  ....*...
gi 1958801479 316 SLLPQAVP 323
Cdd:PHA02738  300 KVSKKLIP 307
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 56-291 6.72e-47

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: 159.89  E-value: 6.72e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  56 NSKKNRYKDVVPYDETRVILSLLQEEGHGDYINANFIRGTDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETE 135
Cdd:cd14629    53 NKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLRE 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 136 NGRRKCERYWAQEREPlQAGPFCITLTKETALTADItLRTLQVTFQKvpkgQKESRPVHQLQYMSWPDHGVPSSSDHILT 215
Cdd:cd14629   133 MGREKCHQYWPAERSA-RYQYFVVDPMAEYNMPQYI-LREFKVTDAR----DGQSRTIRQFQFTDWPEQGVPKTGEGFID 206

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958801479 216 MVEEA-RCLQGLGP-GPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLY 291
Cdd:cd14629   207 FIGQVhKTKEQFGQdGPITVHCSAGVGRTGVFITLSIVLERMRYEGV---VDMFQTVKTLRTQRPAMVQTEDQYQLCY 281
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 86-294 7.07e-47

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: 157.00  E-value: 7.07e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  86 YINANFIRGTDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWAQEREPLqaGPFCITLTkET 165
Cdd:cd14555     1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTEVY--GDIKVTLV-ET 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 166 ALTADITLRTLqvTFQKvpKGQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGPGPLCVHCSAGCGRTGVL 245
Cdd:cd14555    78 EPLAEYVVRTF--ALER--RGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTGCY 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1958801479 246 CAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTV 294
Cdd:cd14555   154 IVIDIMLDMAEREGV---VDIYNCVKELRSRRVNMVQTEEQYIFIHDAI 199
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 86-296 3.92e-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: 155.29  E-value: 3.92e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  86 YINANFIRGTDGSQ-AYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWAQEREPLQaGPFCITLTKE 164
Cdd:cd14546     1 YINASTIYDHDPRNpAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEVY-HIYEVHLVSE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 165 TALTADITLRTLqvtFQKVPKGQkESRPVHQLQYMSWPDHGVPSSSDHILTMVEEA-RCLQGLGpGPLCVHCSAGCGRTG 243
Cdd:cd14546    80 HIWCDDYLVRSF---YLKNLQTS-ETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVnKSYRGRS-CPIVVHCSDGAGRTG 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958801479 244 VLCAVDYVRQLLLTQTipPNFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 296
Cdd:cd14546   155 TYILIDMVLNRMAKGA--KEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAE 205
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
55-290 1.08e-45

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 156.40  E-value: 1.08e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  55 GNSKKNRYKDVVPYDETRVilsllQEEGhgDYINANFIRGTDGSQaYIATQGPLPHTLLDFWRLVWEFGVKVI--LMACQ 132
Cdd:COG5599    41 NGSPLNRFRDIQPYKETAL-----RANL--GYLNANYIQVIGNHR-YIATQYPLEEQLEDFFQMLFDNNTPVLvvLASDD 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 133 ETENGRRKCERYWAQEReplQAGPFCI--TLTKETALTADITLRTLQVTFQKvpKGQKeSRPVHQLQYMSWPDHGVPSSS 210
Cdd:COG5599   113 EISKPKVKMPVYFRQDG---EYGKYEVssELTESIQLRDGIEARTYVLTIKG--TGQK-KIEIPVLHVKNWPDHGAISAE 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 211 ---DHILTMVEEARCLQGLGpGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIpPNFSLFEVVLEMRKQR-PAAVQTEEQ 286
Cdd:COG5599   187 alkNLADLIDKKEKIKDPDK-LLPVVHCRAGVGRTGTLIACLALSKSINALVQ-ITLSVEEIVIDMRTSRnGGMVQTSEQ 264


                  ....
gi 1958801479 287 YRFL 290
Cdd:COG5599   265 LDVL 268
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 72-296 1.73e-44

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: 151.33  E-value: 1.73e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  72 RVILSLLQEEGHGDYINANFIRGTDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWAQEREP 151
Cdd:cd14631     1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 152 LqaGPFCITLTkETALTADITLRTLqvTFQKvpKGQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGPGPL 231
Cdd:cd14631    81 Y--GDFKVTCV-EMEPLAEYVVRTF--TLER--RGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPI 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958801479 232 CVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 296
Cdd:cd14631   154 VVHCSAGAGRTGCYIVIDIMLDMAEREGV---VDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 86-291 4.05e-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: 149.98  E-value: 4.05e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  86 YINANFIRGTDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYW-AQEREPLQAGPFCITLTKE 164
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWpSMEEGSRAFGDVVVKINEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 165 TaLTADITLRTLQVTFQKVPKGQKEsrpVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGPGPLCVHCSAGCGRTGV 244
Cdd:cd14557    81 K-ICPDYIIRKLNINNKKEKGSGRE---VTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGT 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1958801479 245 LCAVDYVRQLLLTQTippNFSLFEVVLEMRKQRPAAVQTEEQYRFLY 291
Cdd:cd14557   157 YIGIDAMLEGLEAEG---RVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 86-291 4.92e-44

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: 149.92  E-value: 4.92e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  86 YINANFIRGT---DGSQaYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRR-KCERYW-AQEREPLQAGPFCIT 160
Cdd:cd17658     1 YINASLVETPaseSLPK-FIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTaKCADYFpAEENESREFGRISVT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 161 LTKETALTADITLRTLQVTFQKVPkgqKESRPVHQLQYMSWPDHGVPSSSDHILTMVeeaRCLQGLGP--GPLCVHCSAG 238
Cdd:cd17658    80 NKKLKHSQHSITLRVLEVQYIESE---EPPLSVLHIQYPEWPDHGVPKDTRSVRELL---KRLYGIPPsaGPIVVHCSAG 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958801479 239 CGRTGVLCAVDYVRQLLLTQTIPPnFSLFEVVLEMRKQRPAAVQTEEQYRFLY 291
Cdd:cd17658   154 IGRTGAYCTIHNTIRRILEGDMSA-VDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 86-291 5.22e-44

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: 149.85  E-value: 5.22e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  86 YINANFIRGTDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWAQEREPLqaGPFCITLtKET 165
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKTY--GDIEVEL-KDT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 166 ALTADITLRTLQVTFQKvpkgQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGPG------PLCVHCSAGC 239
Cdd:cd14558    78 EKSPTYTVRVFEITHLK----RKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKNSkhgrsvPIVVHCSDGS 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958801479 240 GRTGVLCAvdyVRQLLLTQTIPPNFSLFEVVLEMRKQRPAAVQTEEQYRFLY 291
Cdd:cd14558   154 SRTGIFCA---LWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 86-291 5.22e-44

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: 149.84  E-value: 5.22e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  86 YINANFIRG-TDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWAQER-EPLQAGPFCITLTK 163
Cdd:cd14539     1 YINASLIEDlTPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERgQALVYGAITVSLQS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 164 ETALTADITlRTLQVTFqkvpKGQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEEA-------RCLQglgpGPLCVHCS 236
Cdd:cd14539    81 VRTTPTHVE-RIISIQH----KDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVhshylqqRSLQ----TPIVVHCS 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958801479 237 AGCGRTGVLCAV-DYVRQLLLTQTIPpnfSLFEVVLEMRKQRPAAVQTEEQYRFLY 291
Cdd:cd14539   152 SGVGRTGAFCLLyAAVQEIEAGNGIP---DLPQLVRKMRQQRKYMLQEKEHLKFCY 204
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 85-294 8.15e-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: 149.39  E-value: 8.15e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  85 DYINANFIRGTDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWAQEREpLQAGPFCITLTKE 164
Cdd:cd14622     1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGS-VTHGEITIEIKND 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 165 TALTAdITLRTLQVTFQKvpkgQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEEA-RCLQGLGPGPLCVHCSAGCGRTG 243
Cdd:cd14622    80 TLLET-ISIRDFLVTYNQ----EKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVqKQQQQTGNHPIVVHCSAGAGRTG 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958801479 244 VLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTV 294
Cdd:cd14622   155 TFIALSNILERVKAEGL---LDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 47-296 8.40e-43

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: 149.40  E-value: 8.40e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  47 STKAGSQQGNSKKNRYKDVVPYDETRVILSLLQEEGHGDYINANFIRGTDGSQAYIATQGPLPHTLLDFWRLVWEFGVKV 126
Cdd:cd14621    43 TCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTAT 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 127 ILMACQETENGRRKCERYWaqerePLQAgpfCITL------TKETALTADITLRTLQVTFQKVPKGQKESRPVHQLQYMS 200
Cdd:cd14621   123 IVMVTNLKERKECKCAQYW-----PDQG---CWTYgnirvsVEDVTVLVDYTVRKFCIQQVGDVTNKKPQRLITQFHFTS 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 201 WPDHGVPSSSDHILTMVEEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTippNFSLFEVVLEMRKQRPAA 280
Cdd:cd14621   195 WPDFGVPFTPIGMLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAER---KVDVYGFVSRIRAQRCQM 271

                         250
                  ....*....|....*.
gi 1958801479 281 VQTEEQYRFLYHTVAQ 296
Cdd:cd14621   272 VQTDMQYVFIYQALLE 287
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 86-296 3.33e-42

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: 3.33e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  86 YINANFIRGTDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWAQEREplQAGPFCITLTKET 165
Cdd:cd14632     1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSD--TYGDIKITLLKTE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 166 ALtADITLRTLqvTFQKvpKGQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGPGPLCVHCSAGCGRTGVL 245
Cdd:cd14632    79 TL-AEYSVRTF--ALER--RGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCY 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958801479 246 CAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 296
Cdd:cd14632   154 IVLDVMLDMAECEGV---VDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 86-291 9.27e-42

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: 143.90  E-value: 9.27e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  86 YINANFIRGTDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYWAQEREpLQAGPFCITLtKET 165
Cdd:cd14551     1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGC-WTYGNLRVRV-EDT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 166 ALTADITLRTLQVTFQKVPKGQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGPGPLCVHCSAGCGRTGVL 245
Cdd:cd14551    79 VVLVDYTTRKFCIQKVNRGIGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGRTGTF 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1958801479 246 CAVDYVRQLLLTQTippNFSLFEVVLEMRKQRPAAVQTEEQYRFLY 291
Cdd:cd14551   159 IVIDAMLDMMHAEG---KVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 86-291 9.29e-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: 143.70  E-value: 9.29e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  86 YINANFIRGTDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGrRKCERYWAQErEPLQAGPFCITLTKET 165
Cdd:cd14556     1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKD-QSCPQYWPDE-GSGTYGPIQVEFVSTT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 166 aLTADITLRTLQVtfQKVPKGQKESRPVHQLQYMSWPDHG-VPSSSDHILTMVEEA-RCLQGLGPGPLCVHCSAGCGRTG 243
Cdd:cd14556    79 -IDEDVISRIFRL--QNTTRPQEGYRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVeKWQEQSGEGPIVVHCLNGVGRSG 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1958801479 244 VLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLY 291
Cdd:cd14556   156 VFCAISSVCERIKVENV---VDVFQAVKTLRNHRPNMVETEEQYKFCY 200
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 55-295 9.72e-42

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: 145.39  E-value: 9.72e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  55 GNSKKNRYKDVVPYDETRVIL-SLLQEEGHGDYINANFIRGTDGSQ-AYIATQGPLPHTLLDFWRLVWEFGVKVILMACQ 132
Cdd:cd14613    24 GLVRKNRYKTILPNPHSRVCLtSPDQDDPLSSYINANYIRGYGGEEkVYIATQGPTVNTVGDFWRMVWQERSPIIVMITN 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 133 eTENGRRKCERYWAQERepLQAGPFCITLTKETAlTADITLRTLQVtfqkvpKGQKESRPVHQLQYMSWPDHGVPSSSDH 212
Cdd:cd14613   104 -IEEMNEKCTEYWPEEQ--VTYEGIEITVKQVIH-ADDYRLRLITL------KSGGEERGLKHYWYTSWPDQKTPDNAPP 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 213 ILTM---VEEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRF 289
Cdd:cd14613   174 LLQLvqeVEEARQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGV---VDILRTTCQLRLDRGGMIQTCEQYQF 250


                  ....*.
gi 1958801479 290 LYHTVA 295
Cdd:cd14613   251 VHHVLS 256
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 59-292 3.10e-41

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: 143.13  E-value: 3.10e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  59 KNRYKDVVPYDETRVILSLLQ-EEGHGDYINANFIRGTDGSQ-AYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETEN 136
Cdd:cd14611     2 KNRYKTILPNPHSRVCLKPKNsNDSLSTYINANYIRGYGGKEkAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 137 GrRKCERYWAQEREPLQAGPFCITLTKEtalTADITLRTLQVtfqkvpKGQKESRPVHQLQYMSWPDHGVPSSSDHILTM 216
Cdd:cd14611    82 N-EKCVLYWPEKRGIYGKVEVLVNSVKE---CDNYTIRNLTL------KQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 217 ---VEEARcLQGLGPGPLCVHCSAGCGRTGVLCAVDY-VRQLLLTQTIppnfSLFEVVLEMRKQRPAAVQTEEQYRFLYH 292
Cdd:cd14611   152 mldVEEDR-LASPGRGPVVVHCSAGIGRTGCFIATTIgCQQLKEEGVV----DVLSIVCQLRVDRGGMVQTSEQYEFVHH 226
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 1-296 2.07e-40

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 143.22  E-value: 2.07e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479   1 MSRQSDLVRSFLEQQEARDHREgaILAREFSDIKARSVAWKTEGVCSTKagsqqgNSKKNRYKDVVPYDETRVILSLlqE 80
Cdd:PHA02742    5 CSKKNSFAKNCEQLIEESNLAE--ILKEEHEHIMQEIVAFSCNESLELK------NMKKCRYPDAPCFDRNRVILKI--E 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  81 EGHGDYINANFIRGTDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYW-AQEREPLQAGPFCI 159
Cdd:PHA02742   75 DGGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIMEDGKEACYPYWmPHERGKATHGEFKI 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 160 TlTKETALTADITLRTLQVTfqkvPKGQKESRPVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQG-----------LGP 228
Cdd:PHA02742  155 K-TKKIKSFRNYAVTNLCLT----DTNTGASLDIKHFAYEDWPHGGLPRDPNKFLDFVLAVREADLkadvdikgeniVKE 229

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958801479 229 GPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPnfsLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 296
Cdd:PHA02742  230 PPILVHCSAGLDRAGAFCAIDICISKYNERAIIP---LLSIVRDLRKQRHNCLSLPQQYIFCYFIVLI 294
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 56-307 4.11e-40

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 142.83  E-value: 4.11e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  56 NSKKNRYKDVVPYDETRVILsllqEEGHG---DYINANFIRGTDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMAC- 131
Cdd:PHA02747   51 NQPKNRYWDIPCWDHNRVIL----DSGGGstsDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTp 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 132 QETENGRRKCERYWA-QEREPLQAGPFCITlTKETALTADITLRTLQVTfqkvPKGQKESRPVHQLQYMSWPDHGVPssS 210
Cdd:PHA02747  127 TKGTNGEEKCYQYWClNEDGNIDMEDFRIE-TLKTSVRAKYILTLIEIT----DKILKDSRKISHFQCSEWFEDETP--S 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 211 DHI-----LTMVEEARCLQG--LGP-----GPLCVHCSAGCGRTGVLCAVDY-VRQLLLTQTIppnfSLFEVVLEMRKQR 277
Cdd:PHA02747  200 DHPdfikfIKIIDINRKKSGklFNPkdallCPIVVHCSDGVGKTGIFCAVDIcLNQLVKRKAI----CLAKTAEKIREQR 275

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1958801479 278 PAAVQTEEQYRFL---YHTVAQLFSRTLQNNSP 307
Cdd:PHA02747  276 HAGIMNFDDYLFIqpgYEVLHYFLSKIKAIDKI 308
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 192-296 4.94e-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: 135.95  E-value: 4.94e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  192 PVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGP--GPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPNFslFEV 269
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSEssGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGEVDI--FDT 78

                           90       100
                   ....*....|....*....|....*..
gi 1958801479  270 VLEMRKQRPAAVQTEEQYRFLYHTVAQ 296
Cdd:smart00012  79 VKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
192-296 4.94e-40

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 135.95  E-value: 4.94e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  192 PVHQLQYMSWPDHGVPSSSDHILTMVEEARCLQGLGP--GPLCVHCSAGCGRTGVLCAVDYVRQLLLTQTIPPNFslFEV 269
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSEssGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGEVDI--FDT 78

                           90       100
                   ....*....|....*....|....*..
gi 1958801479  270 VLEMRKQRPAAVQTEEQYRFLYHTVAQ 296
Cdd:smart00404  79 VKELRSQRPGMVQTEEQYLFLYRALLE 105
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 56-306 1.34e-39

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 141.70  E-value: 1.34e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  56 NSKKNRYKDVVPYDETRVILS-------------------LLQEEGHGDYINANFIRGTDGSQAYIATQGPLPHTLLDFW 116
Cdd:PHA02746   51 NLKKNRFHDIPCWDHSRVVINaheslkmfdvgdsdgkkieVTSEDNAENYIHANFVDGFKEANKFICAQGPKEDTSEDFF 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 117 RLVWEFGVKVILmACQETENGRRKCERYWAQERE-PLQAGPFcITLTKETALTADITLRTLQVTfqkvPKGQKESRPVHQ 195
Cdd:PHA02746  131 KLISEHESQVIV-SLTDIDDDDEKCFELWTKEEDsELAFGRF-VAKILDIIEELSFTKTRLMIT----DKISDTSREIHH 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 196 LQYMSWPDHGVPSSSDHILTMV-----EEARCL-----QGLGPGPLCVHCSAGCGRTGVLCAVD-YVRQLLLTQTIppnf 264
Cdd:PHA02746  205 FWFPDWPDNGIPTGMAEFLELInkvneEQAELIkqadnDPQTLGPIVVHCSAGIGRAGTFCAIDnALEQLEKEKEV---- 280

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1958801479 265 SLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQLFSRTLQNNS 306
Cdd:PHA02746  281 CLGEIVLKIRKQRHSSVFLPEQYAFCYKALKYAIIEEAKKKF 322
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 86-298 2.70e-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: 130.10  E-value: 2.70e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  86 YINANFIRGTDGSQA--YIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCERYW---AQEREPLQAGPFCIT 160
Cdd:cd14598     1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWprlGSRHNTVTYGRFKIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 161 LTKEtalTADITLRTLQVTFQKVPKGQKesRPVHQLQYMSWPDHGVPSSSDHILTMVEEARCL----------QGLGPgP 230
Cdd:cd14598    81 TRFR---TDSGCYATTGLKIKHLLTGQE--RTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVrrhtnstidpKSPNP-P 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 231 LCVHCSAGCGRTGVLcavdyVRQLLLTQTIPPNFSL-FEVVLEM-RKQRPAAVQTEEQYRFLYHTVAQLF 298
Cdd:cd14598   155 VLVHCSAGVGRTGVV-----ILSEIMIACLEHNEMLdIPRVLDMlRQQRMMMVQTLSQYTFVYKVLIQFL 219
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 86-291 1.33e-27

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: 107.03  E-value: 1.33e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  86 YINANFIRGTDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQ-ETENGrrkCERYWAQEREpLQAGPF---CITl 161
Cdd:cd14636     1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEvDLAQG---CPQYWPEEGM-LRYGPIqveCMS- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 162 tkeTALTADITLRTLQVTfqKVPKGQKESRPVHQLQYMSWPDH-GVPSSSDHILTMVEEARCLQ---GLGPGPLCVHCSA 237
Cdd:cd14636    76 ---CSMDCDVISRIFRIC--NLTRPQEGYLMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQeecDEGEGRTIIHCLN 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958801479 238 GCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLY 291
Cdd:cd14636   151 GGGRSGMFCAISIVCEMIKRQNV---VDVFHAVKTLRNSKPNMVETPEQYRFCY 201
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 86-291 6.37e-27

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: 6.37e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  86 YINANFIRGTDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQetENGRRKCERYWAqEREPLQAGPFCITLtket 165
Cdd:cd14634     1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNE--MDAAQLCMQYWP-EKTSCCYGPIQVEF---- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 166 aLTADITLRTLQVTFQ--KVPKGQKESRPVHQLQYMSWPDH-GVPSSSDHILTMVEEARCLQGL---GPGPLCVHCSAGC 239
Cdd:cd14634    74 -VSADIDEDIISRIFRicNMARPQDGYRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEQydgREGRTVVHCLNGG 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958801479 240 GRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLY 291
Cdd:cd14634   153 GRSGTFCAICSVCEMIQQQNI---IDVFHTVKTLRNNKSNMVETLEQYKFVY 201
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 86-291 3.06e-24

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: 98.06  E-value: 3.06e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  86 YINANFIRGTDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETE-NGRRKCERYWAqerEP--LQAGPFCITLT 162
Cdd:cd14637     1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQsNSAWPCLQYWP---EPglQQYGPMEVEFV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 163 KETAlTADITLRTLQVtfQKVPKGQKESRPVHQLQYMSW-PDHGVPSSSD---HILTMVE--EARClqglGPGPLCVHCS 236
Cdd:cd14637    78 SGSA-DEDIVTRLFRV--QNITRLQEGHLMVRHFQFLRWsAYRDTPDSKKaflHLLASVEkwQRES----GEGRTVVHCL 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958801479 237 AGCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLY 291
Cdd:cd14637   151 NGGGRSGTYCASAMILEMIRCHNI---VDVFYAVKTLRNYKPNMVETLEQYRFCY 202
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 86-291 1.57e-22

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: 93.20  E-value: 1.57e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  86 YINANFIRGTDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMAcqETENGRRKCER-YWAQEREPLQAGPFCITL--- 161
Cdd:cd17670     1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVML--PDNQGLAEDEFvYWPSREESMNCEAFTVTLisk 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 162 ------TKETALTADITLRTLQVTFqkvpkgqkeSRPVHQLQYMSWPDHGVPSSSDHILTMV--EEARCLQglgpGPLCV 233
Cdd:cd17670    79 drlclsNEEQIIIHDFILEATQDDY---------VLEVRHFQCPKWPNPDAPISSTFELINVikEEALTRD----GPTIV 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958801479 234 HCSAGCGRTGVLCAVDYVRQLLLTQTIppnFSLFEVVLEMRKQRPAAVQTEEQYRFLY 291
Cdd:cd17670   146 HDEFGAVSAGTLCALTTLSQQLENENA---VDVYQVAKMINLMRPGVFTDIEQYQFLY 200
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 86-296 7.13e-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: 91.67  E-value: 7.13e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  86 YINANFIRGTDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMAcqETENGRRKCERYWAqEREPLQAGPFCITLTkET 165
Cdd:cd14635     1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVML--NDVDPAQLCPQYWP-ENGVHRHGPIQVEFV-SA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 166 ALTADITLRTLQVTFQKVPkgQKESRPVHQLQYMSWPDH-GVPSSSDHILTMVEEARCLQ---GLGPGPLCVHCSAGCGR 241
Cdd:cd14635    77 DLEEDIISRIFRIYNAARP--QDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQeeyNGGEGRTVVHCLNGGGR 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958801479 242 TGVLCAVDYVRQLLLTQTippNFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTVAQ 296
Cdd:cd14635   155 SGTFCAISIVCEMLRHQR---AVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 86-294 7.66e-20

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: 85.82  E-value: 7.66e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  86 YINANFIRGTDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGRRKCErYWAQEREPLQAGPFCITL---- 161
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWPNKDEPINCETFKVTLiaee 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 162 -----TKETALTADITLRTLQVTFqkvpkgqkeSRPVHQLQYMSWPDHGVP-SSSDHILTMVEEARCLQGlgpGPLCVHC 235
Cdd:cd17669    80 hkclsNEEKLIIQDFILEATQDDY---------VLEVRHFQCPKWPNPDSPiSKTFELISIIKEEAANRD---GPMIVHD 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958801479 236 SAGCGRTGVLCAVDYVRQLLLTQTippNFSLFEVVLEMRKQRPAAVQTEEQYRFLYHTV 294
Cdd:cd17669   148 EHGGVTAGTFCALTTLMHQLEKEN---SVDVYQVAKMINLMRPGVFTDIEQYQFLYKAI 203
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 86-291 1.23e-19

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: 85.07  E-value: 1.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  86 YINANFIRGTDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILMACQETENGrrKCERYWAQEREPLQAGPFCITLTKET 165
Cdd:cd14550     1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWPTKEKPLECETFKVTLSGED 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 166 ---------ALTADITLRTLQVTFQkvpkgqkesRPVHQLQYMSWPDHGVP-SSSDHILTMVEEaRCLQglGPGPLCVHC 235
Cdd:cd14550    79 hsclsneirLIVRDFILESTQDDYV---------LEVRQFQCPSWPNPCSPiHTVFELINTVQE-WAQQ--RDGPIVVHD 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958801479 236 SAGCGRTGVLCAVdyvrQLLLTQTIPPN-FSLFEVVLEMRKQRPAAVQTEEQYRFLY 291
Cdd:cd14550   147 RYGGVQAATFCAL----TTLHQQLEHESsVDVYQVAKLYHLMRPGVFTSKEDYQFLY 199
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 211-292 5.60e-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: 67.37  E-value: 5.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 211 DHILTMVEEARCLQGLGPGPLCVHCSAGCGRTGVLCAVDYVRQLlltqtippNFSLFEVVLEMRKQRPA-AVQTEEQYRF 289
Cdd:cd14494    39 LAMVDRFLEVLDQAEKPGEPVLVHCKAGVGRTGTLVACYLVLLG--------GMSAEEAVRIVRLIRPGgIPQTIEQLDF 110


                  ...
gi 1958801479 290 LYH 292
Cdd:cd14494   111 LIK 113
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 51-302 1.38e-10

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 61.14  E-value: 1.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479  51 GSQQGNSKKNRYKD-VVPYDETRVILSLLQEEGHGDYINANFIRGTDGSQAYIATQGPLPHTLLDFWRLVWEFGVKVILM 129
Cdd:PHA02740   42 ANKACAQAENKAKDeNLALHITRLLHRRIKLFNDEKVLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVL 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 130 ACQETEngrRKC-ERYWA-QEREPLQAGPFCITlTKETALTADITLRTLQVTFQkvpKGQkeSRPVHQLQYMSWPDHGVP 207
Cdd:PHA02740  122 ISRHAD---KKCfNQFWSlKEGCVITSDKFQIE-TLEIIIKPHFNLTLLSLTDK---FGQ--AQKISHFQYTAWPADGFS 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 208 SSSD-------HILTMVEEARCLQGLGP-GPLCVHCSAGCGRTGVLCAVDyvrqLLLTQTIPPN-FSLFEVVLEMRKQRP 278
Cdd:PHA02740  193 HDPDafidffcNIDDLCADLEKHKADGKiAPIIIDCIDGISSSAVFCVFD----ICATEFDKTGmLSIANALKKVRQKKY 268

                         250       260
                  ....*....|....*....|....
gi 1958801479 279 AAVQTEEQYRFLYHTVAQLFSRTL 302
Cdd:PHA02740  269 GCMNCLDDYVFCYHLIAAYLKEKF 292
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 200-290 1.33e-09

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: 56.97  E-value: 1.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 200 SWPDHGVPSSsDHILTMVE-EARCLQGlgPGPLCVHCSAGCGRTGVLCAVdyvrQLLLTQTIPPNfslfEVVLEMRKQRP 278
Cdd:cd14506    83 GWKDYGVPSL-TTILDIVKvMAFALQE--GGKVAVHCHAGLGRTGVLIAC----YLVYALRMSAD----QAIRLVRSKRP 151

                          90
                  ....*....|..
gi 1958801479 279 AAVQTEEQYRFL 290
Cdd:cd14506   152 NSIQTRGQVLCV 163
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
201-292 2.73e-09

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 54.98  E-value: 2.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 201 WPDHGVPSSsDHILTMVEEARCLQGLGpGPLCVHCSAGCGRTGVLCAvdyvrQLLLTQTIPPNfslfEVVLEMRKQRPAA 280
Cdd:COG2453    55 IPDFGAPDD-EQLQEAVDFIDEALREG-KKVLVHCRGGIGRTGTVAA-----AYLVLLGLSAE----EALARVRAARPGA 123

                          90
                  ....*....|..
gi 1958801479 281 VQTEEQYRFLYH 292
Cdd:COG2453   124 VETPAQRAFLER 135
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 201-290 7.55e-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: 52.40  E-value: 7.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 201 WPDHGVPSS------SDHI-------LTMVEEARCLQGLGPGPL--CVHCSAGCGRTGVLCAVDYVRQllltqtiPPN-F 264
Cdd:cd14559   126 WPDHTAISSeglkelADLVnksaeekRNFYKSKGSSAINDKNKLlpVIHCRAGVGRTGQLAAAMELNK-------SPNnL 198

                          90       100
                  ....*....|....*....|....*..
gi 1958801479 265 SLFEVVLEMRKQRPA-AVQTEEQYRFL 290
Cdd:cd14559   199 SVEDIVSDMRTSRNGkMVQKDEQLDTL 225
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 195-291 2.70e-07

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: 49.57  E-value: 2.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 195 QLQYMSW-----PDHGVPSSSDHILTMVEEAR-CLQGlGPGPLcVHCSAGCGRTGVLCAvdyVRQLLLTQTIPPNfslfE 268
Cdd:cd14505    69 QQAGITWhhlpiPDGGVPSDIAQWQELLEELLsALEN-GKKVL-IHCKGGLGRTGLIAA---CLLLELGDTLDPE----Q 139

                          90       100
                  ....*....|....*....|...
gi 1958801479 269 VVLEMRKQRPAAVQTEEQYRFLY 291
Cdd:cd14505   140 AIAAVRALRPGAIQTPKQENFLH 162
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 193-290 5.65e-07

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: 48.04  E-value: 5.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801479 193 VHQLQY--MSWPDHGVPSSS--DHILTMVEEARCLqglgPGPLCVHCSAGCGRTGVLCAVdYvrqLLLTQTIPPNfslfE 268
Cdd:cd14504    47 CPGLRYhhIPIEDYTPPTLEqiDEFLDIVEEANAK----NEAVLVHCLAGKGRTGTMLAC-Y---LVKTGKISAV----D 114

                          90       100
                  ....*....|....*....|..
gi 1958801479 269 VVLEMRKQRPAAVQTEEQYRFL 290
Cdd:cd14504   115 AINEIRRIRPGSIETSEQEKFV 136
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 202-245 1.55e-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: 1.55e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1958801479 202 PDHGVPSssDHI----LTMVEEArclqglgPGPLCVHCSAGCGRTGVL 245
Cdd:cd14499    88 PDGSTPS--DDIvkkfLDICENE-------KGAIAVHCKAGLGRTGTL 126
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 194-247 4.22e-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: 4.22e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958801479 194 HQLQYMSWPDHGVPSSsDHILTMVEEARCLQGLGPGPLCV-HCSAGCGRTGVLCA 247
Cdd:cd14497    61 GRVLHYGFPDHHPPPL-GLLLEIVDDIDSWLSEDPNNVAVvHCKAGKGRTGTVIC 114
Y_phosphatase3 pfam13350
Tyrosine phosphatase family; This family is closely related to the pfam00102 and pfam00782 ...
 227-257 8.04e-03

Tyrosine phosphatase family; This family is closely related to the pfam00102 and pfam00782 families.


Pssm-ID: 463853 [Multi-domain]  Cd Length: 243  Bit Score: 37.22  E-value: 8.04e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1958801479 227 GPGPLCVHCSAGCGRTGVLCAvdyvrqLLLT 257
Cdd:pfam13350 128 NDGPVLFHCTAGKDRTGVAAA------LLLS 152
 
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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