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Conserved domains on  [gi|568915937|ref|XP_006499055|]
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receptor-type tyrosine-protein phosphatase eta isoform X2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 990-1218 5.04e-171

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: 505.51  E-value: 5.04e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  990 NRYNNVLPYDISRVKLSVQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTK 1069
Cdd:cd14615     1 NRYNNVLPYDISRVKLSVQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRTK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1070 CEEYWPSKQAQDYGDITVAMTSEVVLPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQ 1149
Cdd:cd14615    81 CEEYWPSKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVREYMKQ 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568915937 1150 IPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 1218
Cdd:cd14615   161 NPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCALD 229
PTP_tm pfam18861
TM proximal of protein tyrosine phosphatase, receptor type J; Protein tyrosine phosphatases ...
 756-886 2.06e-38

TM proximal of protein tyrosine phosphatase, receptor type J; Protein tyrosine phosphatases (PTPs) are known to be signaling molecules that regulate a variety of cellular processes, including cell growth, differentiation, mitotic cycle, and oncogenic transformation. PTP receptor type J possesses an extracellular region containing five fibronectin type III repeats, the transmembrane region included in this Pfam entry, and a intracytoplasmic catalytic domain. This entry probably contains part of a Fn3 domain at the N-terminus.


:

Pssm-ID: 465889  Cd Length: 126  Bit Score: 139.66  E-value: 2.06e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937   756 VKFSGFEASHGPIKAYAVILTTGE-AAQPSADVLKYTYEDFKRGASDTYVTYLIriEEKGQSQGlSEVLNYEIDVGNQST 834
Cdd:pfam18861    1 IQFSLFNSSNGPIKAYGVIVTTNDsLNRPLKEYLNKTYYDWKYKKTDSYLATVT--PNPFTSPR-SSSRSLTVPVGTGSK 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568915937   835 TLGYYNGRLEPLGSYRACVAGFTNITYnlqNDGLINGDESYVSFSPYSEAVF 886
Cdd:pfam18861   78 WQGYCNGPLKPLGSYRFSVAAFTRLEF---DDGLIDGEESYVSFTPFSEPIA 126
FN3 super family cl27307
Fibronectin type 3 domain [General function prediction only];
106-606 3.30e-10

Fibronectin type 3 domain [General function prediction only];


The actual alignment was detected with superfamily member COG3401:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 64.25  E-value: 3.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  106 TSCNITGLSPGTSYTFSIISVTTNETLNKTITTEPWPVSDLHVTSVGVTQARLTWSNANGTASYRMLIEELTTHSSVNIS 185
Cdd:COG3401    48 TKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATT 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  186 GLKPGTNNSFAFPESNETQADFAVAEEVPADANGTKRIPVTNLSQLHKNSLVSVDPPSGQDPSLTEILLTDLKPDTQYNA 265
Cdd:COG3401   128 ATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYY 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  266 TIYSQAANGtEGQPRNKVFKTNSTQV----SDVRAMNISASSMTLTWKSNYDGSRTS-IVYKIHVAGGTHSVNQTVNKTE 340
Cdd:COG3401   208 RVAATDTGG-ESAPSNEVSVTTPTTPpsapTGLTATADTPGSVTLSWDPVTESDATGyRVYRSNSGDGPFTKVATVTTTS 286

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  341 AIILGLSSSTLYN--ITVHPFLGQTEGTPGFLQVYTS---PDQVSDFRVTNVSTRAIGLAWRSNDS---KSFEIFIKQDG 412
Cdd:COG3401   287 YTDTGLTNGTTYYyrVTAVDAAGNESAPSNVVSVTTDltpPAAPSGLTATAVGSSSITLSWTASSDadvTGYNVYRSTSG 366

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  413 GEKHR--NASTGNQSYMVEDLKPGTSYHFEIIPRGPDGTEGLSS----------TVNGSTDPSAVTDIRVVNISTTEMQL 480
Cdd:COG3401   367 GGTYTkiAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSeevsattasaASGESLTASVDAVPLTDVAGATAAAS 446

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  481 EWQNTDDASGYTYHLVLESKSGSIirTNSSQKWITVGSLTPGTLYNVTIFPEVDQIQGISNSITQYTrPSSVSHIEVNTT 560
Cdd:COG3401   447 AASNPGVSAAVLADGGDTGNAVPF--TTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSV-IGASAAAAVGGA 523

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 568915937  561 TTTAAIRWKNEDAASASYAYSVLILKTGDGSNVTSNFTKDPSILIP 606
Cdd:COG3401   524 PDGTPNVTGASPVTVGASTGDVLITDLVSLTTSASSSVSGAGLGSG 569
fn3 pfam00041
Fibronectin type III domain;
69-129 7.42e-08

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 50.88  E-value: 7.42e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568915937    69 VSPTSVLLTWKHNDSGAS-------ECRIENKMESNLTFPV-KNQTSCNITGLSPGTSYTFSIISVTTN 129
Cdd:pfam00041   11 VTSTSLTVSWTPPPDGNGpitgyevEYRPKNSGEPWNEITVpGTTTSVTLTGLKPGTEYEVRVQAVNGG 79
 
Name Accession Description Interval E-value
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 990-1218 5.04e-171

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: 505.51  E-value: 5.04e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  990 NRYNNVLPYDISRVKLSVQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTK 1069
Cdd:cd14615     1 NRYNNVLPYDISRVKLSVQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRTK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1070 CEEYWPSKQAQDYGDITVAMTSEVVLPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQ 1149
Cdd:cd14615    81 CEEYWPSKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVREYMKQ 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568915937 1150 IPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 1218
Cdd:cd14615   161 NPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCALD 229
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
961-1218 2.56e-120

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 373.15  E-value: 2.56e-120
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937    961 GFAEEYEDLKLIGISLPKYT-AEIAENRGKNRYNNVLPYDISRVKLSVQTHSTDDYINANYMPGYHSKKDFIATQGPLPN 1039
Cdd:smart00194    1 GLEEEFEKLDRLKPDDESCTvAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPLPS 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937   1040 TLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSK--QAQDYGDITVAMTSEVVLPEWTIRDFVVKNMQNSESHPLR 1117
Cdd:smart00194   81 TVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEegEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTVT 160

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937   1118 QFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQipPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRM 1197
Cdd:smart00194  161 HYHYTNWPDHGVPESPESILDLIRAVRKSQST--STGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRS 238

                           250       260
                    ....*....|....*....|.
gi 568915937   1198 HRPLMVQTEDQYVFLNQCVLD 1218
Cdd:smart00194  239 QRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
986-1218 1.71e-110

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 346.15  E-value: 1.71e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937   986 NRGKNRYNNVLPYDISRVKLSVQTHSTDdYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQ 1065
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGPSD-YINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  1066 GRTKCEEYWPSK--QAQDYGDITVAMTSEV-VLPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFRYL 1142
Cdd:pfam00102   80 GREKCAQYWPEEegESLEYGDFTVTLKKEKeDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLRK 159

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568915937  1143 VRDYmKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 1218
Cdd:pfam00102  160 VRKS-SLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PHA02738 PHA02738
hypothetical protein; Provisional
 979-1211 4.78e-46

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 168.56  E-value: 4.78e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  979 YTAEIAeNRGKNRYNNVLPYDISRVKLSVQtHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVM 1058
Cdd:PHA02738   43 FNAEKK-NRKLNRYLDAVCFDHSRVILPAE-RNRGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVM 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1059 LTKCVEQGRTKCEEYWPSKQAQD--YGDITVAMTSEVVLPEWTIRDFVVKNmQNSESHPLRQFHFTSWPDHGVPDTTDLL 1136
Cdd:PHA02738  121 LCKKKENGREKCFPYWSDVEQGSirFGKFKITTTQVETHPHYVKSTLLLTD-GTSATQTVTHFNFTAWPDHDVPKNTSEF 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1137 INFRYLVRDYMKQIPPES-----------PILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQT 1205
Cdd:PHA02738  200 LNFVLEVRQCQKELAQESlqighnrlqppPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFI 279


                  ....*.
gi 568915937 1206 EDQYVF 1211
Cdd:PHA02738  280 PFQYFF 285
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
976-1212 1.21e-44

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 163.34  E-value: 1.21e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  976 LPKYTAEIaENRGKNRYNNVLPYDISRVKlsvqthSTDDYINANYMPGyHSKKDFIATQGPLPNTLKDFWRMVWEKNVYA 1055
Cdd:COG5599    33 DPQYLQNI-NGSPLNRFRDIQPYKETALR------ANLGYLNANYIQV-IGNHRYIATQYPLEEQLEDFFQMLFDNNTPV 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1056 IVMLTKCVE--QGRTKCEEYWPskQAQDYG--DITVAMTSEVVL-PEWTIRDFVVKNMQNS-ESHPLRQFHFTSWPDHGV 1129
Cdd:COG5599   105 LVVLASDDEisKPKVKMPVYFR--QDGEYGkyEVSSELTESIQLrDGIEARTYVLTIKGTGqKKIEIPVLHVKNWPDHGA 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1130 PDTTdLLINFRYLVRDYMK-QIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENEN--TVDVYGIVYDLRMHR-PLMVQT 1205
Cdd:COG5599   183 ISAE-ALKNLADLIDKKEKiKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVqiTLSVEEIVIDMRTSRnGGMVQT 261


                  ....*..
gi 568915937 1206 EDQYVFL 1212
Cdd:COG5599   262 SEQLDVL 268
PTP_tm pfam18861
TM proximal of protein tyrosine phosphatase, receptor type J; Protein tyrosine phosphatases ...
 756-886 2.06e-38

TM proximal of protein tyrosine phosphatase, receptor type J; Protein tyrosine phosphatases (PTPs) are known to be signaling molecules that regulate a variety of cellular processes, including cell growth, differentiation, mitotic cycle, and oncogenic transformation. PTP receptor type J possesses an extracellular region containing five fibronectin type III repeats, the transmembrane region included in this Pfam entry, and a intracytoplasmic catalytic domain. This entry probably contains part of a Fn3 domain at the N-terminus.


Pssm-ID: 465889  Cd Length: 126  Bit Score: 139.66  E-value: 2.06e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937   756 VKFSGFEASHGPIKAYAVILTTGE-AAQPSADVLKYTYEDFKRGASDTYVTYLIriEEKGQSQGlSEVLNYEIDVGNQST 834
Cdd:pfam18861    1 IQFSLFNSSNGPIKAYGVIVTTNDsLNRPLKEYLNKTYYDWKYKKTDSYLATVT--PNPFTSPR-SSSRSLTVPVGTGSK 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568915937   835 TLGYYNGRLEPLGSYRACVAGFTNITYnlqNDGLINGDESYVSFSPYSEAVF 886
Cdd:pfam18861   78 WQGYCNGPLKPLGSYRFSVAAFTRLEF---DDGLIDGEESYVSFTPFSEPIA 126
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
106-606 3.30e-10

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 64.25  E-value: 3.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  106 TSCNITGLSPGTSYTFSIISVTTNETLNKTITTEPWPVSDLHVTSVGVTQARLTWSNANGTASYRMLIEELTTHSSVNIS 185
Cdd:COG3401    48 TKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATT 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  186 GLKPGTNNSFAFPESNETQADFAVAEEVPADANGTKRIPVTNLSQLHKNSLVSVDPPSGQDPSLTEILLTDLKPDTQYNA 265
Cdd:COG3401   128 ATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYY 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  266 TIYSQAANGtEGQPRNKVFKTNSTQV----SDVRAMNISASSMTLTWKSNYDGSRTS-IVYKIHVAGGTHSVNQTVNKTE 340
Cdd:COG3401   208 RVAATDTGG-ESAPSNEVSVTTPTTPpsapTGLTATADTPGSVTLSWDPVTESDATGyRVYRSNSGDGPFTKVATVTTTS 286

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  341 AIILGLSSSTLYN--ITVHPFLGQTEGTPGFLQVYTS---PDQVSDFRVTNVSTRAIGLAWRSNDS---KSFEIFIKQDG 412
Cdd:COG3401   287 YTDTGLTNGTTYYyrVTAVDAAGNESAPSNVVSVTTDltpPAAPSGLTATAVGSSSITLSWTASSDadvTGYNVYRSTSG 366

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  413 GEKHR--NASTGNQSYMVEDLKPGTSYHFEIIPRGPDGTEGLSS----------TVNGSTDPSAVTDIRVVNISTTEMQL 480
Cdd:COG3401   367 GGTYTkiAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSeevsattasaASGESLTASVDAVPLTDVAGATAAAS 446

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  481 EWQNTDDASGYTYHLVLESKSGSIirTNSSQKWITVGSLTPGTLYNVTIFPEVDQIQGISNSITQYTrPSSVSHIEVNTT 560
Cdd:COG3401   447 AASNPGVSAAVLADGGDTGNAVPF--TTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSV-IGASAAAAVGGA 523

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 568915937  561 TTTAAIRWKNEDAASASYAYSVLILKTGDGSNVTSNFTKDPSILIP 606
Cdd:COG3401   524 PDGTPNVTGASPVTVGASTGDVLITDLVSLTTSASSSVSGAGLGSG 569
fn3 pfam00041
Fibronectin type III domain;
69-129 7.42e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 50.88  E-value: 7.42e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568915937    69 VSPTSVLLTWKHNDSGAS-------ECRIENKMESNLTFPV-KNQTSCNITGLSPGTSYTFSIISVTTN 129
Cdd:pfam00041   11 VTSTSLTVSWTPPPDGNGpitgyevEYRPKNSGEPWNEITVpGTTTSVTLTGLKPGTEYEVRVQAVNGG 79
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 462-529 1.00e-06

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 47.61  E-value: 1.00e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568915937    462 PSAVTDIRVVNISTTEMQLEWQ--NTDDASGYTYHLVLESKSGS----IIRTNSSQKWITVGSLTPGTLYNVTI 529
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEppPDDGITGYIVGYRVEYREEGsewkEVNVTPSSTSYTLTGLKPGTEYEFRV 74
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 59-127 1.42e-06

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 47.49  E-value: 1.42e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568915937   59 PNPIFDIEA-VVSPTSVLLTWKHNDSGAS-------ECRIENKME-SNLTFPVKNQTSCNITGLSPGTSYTFSIISVT 127
Cdd:cd00063     1 PSPPTNLRVtDVTSTSVTLSWTPPEDDGGpitgyvvEYREKGSGDwKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 462-547 1.98e-06

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 47.11  E-value: 1.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  462 PSAVTDIRVVNISTTEMQLEWQNTDDA----SGYT--YHLVLESKSGSIIRTNSSQKWITVGSLTPGTLYNVTIFPEVDQ 535
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDggpiTGYVveYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                          90
                  ....*....|...
gi 568915937  536 IQG-ISNSITQYT 547
Cdd:cd00063    81 GESpPSESVTVTT 93
fn3 pfam00041
Fibronectin type III domain;
290-367 2.25e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 47.02  E-value: 2.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937   290 QVSDVRAMNISASSMTLTWKSNYDGSRTSIVYKIHVA---GGTHSVNQTV--NKTEAIILGLSSSTLYNITVHPFLGQTE 364
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRpknSGEPWNEITVpgTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81


                   ...
gi 568915937   365 GTP 367
Cdd:pfam00041   82 GPP 84
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 59-127 4.53e-06

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 46.07  E-value: 4.53e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568915937     59 PNPIFDIEAV-VSPTSVLLTWKHNDSGAS-----ECRIENKMESNLTFPVK---NQTSCNITGLSPGTSYTFSIISVT 127
Cdd:smart00060    1 PSPPSNLRVTdVTSTSVTLSWEPPPDDGItgyivGYRVEYREEGSEWKEVNvtpSSTSYTLTGLKPGTEYEFRVRAVN 78
 
Name Accession Description Interval E-value
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 990-1218 5.04e-171

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: 505.51  E-value: 5.04e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  990 NRYNNVLPYDISRVKLSVQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTK 1069
Cdd:cd14615     1 NRYNNVLPYDISRVKLSVQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRTK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1070 CEEYWPSKQAQDYGDITVAMTSEVVLPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQ 1149
Cdd:cd14615    81 CEEYWPSKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVREYMKQ 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568915937 1150 IPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 1218
Cdd:cd14615   161 NPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCALD 229
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 991-1214 2.30e-136

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: 414.44  E-value: 2.30e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  991 RYNNVLPYDISRVKLSVQT-HSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTK 1069
Cdd:cd14548     1 RYTNILPYDHSRVKLIPINeEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1070 CEEYWPSKQAQ-DYGDITVAMTSEVVLPEWTIRDFVVKNMQnsESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMK 1148
Cdd:cd14548    81 CDHYWPFDQDPvYYGDITVTMLSESVLPDWTIREFKLERGD--EVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDYIK 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568915937 1149 QipPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQ 1214
Cdd:cd14548   159 Q--EKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
961-1218 2.56e-120

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 373.15  E-value: 2.56e-120
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937    961 GFAEEYEDLKLIGISLPKYT-AEIAENRGKNRYNNVLPYDISRVKLSVQTHSTDDYINANYMPGYHSKKDFIATQGPLPN 1039
Cdd:smart00194    1 GLEEEFEKLDRLKPDDESCTvAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPLPS 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937   1040 TLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSK--QAQDYGDITVAMTSEVVLPEWTIRDFVVKNMQNSESHPLR 1117
Cdd:smart00194   81 TVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEegEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTVT 160

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937   1118 QFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQipPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRM 1197
Cdd:smart00194  161 HYHYTNWPDHGVPESPESILDLIRAVRKSQST--STGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRS 238

                           250       260
                    ....*....|....*....|.
gi 568915937   1198 HRPLMVQTEDQYVFLNQCVLD 1218
Cdd:smart00194  239 QRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
986-1218 1.71e-110

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 346.15  E-value: 1.71e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937   986 NRGKNRYNNVLPYDISRVKLSVQTHSTDdYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQ 1065
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGPSD-YINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  1066 GRTKCEEYWPSK--QAQDYGDITVAMTSEV-VLPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFRYL 1142
Cdd:pfam00102   80 GREKCAQYWPEEegESLEYGDFTVTLKKEKeDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLRK 159

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568915937  1143 VRDYmKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 1218
Cdd:pfam00102  160 VRKS-SLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 990-1220 1.92e-104

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: 329.54  E-value: 1.92e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  990 NRYNNVLPYDISRVKLS-VQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRT 1068
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKpIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1069 KCEEYWP-SKQAQDYGDITVAMTSEVVLPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYM 1147
Cdd:cd14619    81 KCEHYWPlDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRQWL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568915937 1148 KQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLDII 1220
Cdd:cd14619   161 DQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDFL 233
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 990-1214 4.68e-104

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: 328.42  E-value: 4.68e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  990 NRYNNVLPYDISRVKLS-VQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRT 1068
Cdd:cd14617     1 NRYNNILPYDSTRVKLSnVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1069 KCEEYWPSKQ-AQDYGDITVAMTSEVVLPEWTIRDFVVKNMQNSESHPL-RQFHFTSWPDHGVPDTTDLLINFRYLVRDY 1146
Cdd:cd14617    81 KCDHYWPADQdSLYYGDLIVQMLSESVLPEWTIREFKICSEEQLDAPRLvRHFHYTVWPDHGVPETTQSLIQFVRTVRDY 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568915937 1147 MKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQ 1214
Cdd:cd14617   161 INRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 1015-1214 9.54e-98

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: 309.99  E-value: 9.54e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1015 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQD--YGDITVAMTSE 1092
Cdd:cd00047     1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPleYGDITVTLVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1093 VVLPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQipPESPILVHCSAGVGRTGTFIA 1172
Cdd:cd00047    81 EELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARK--PNGPIVVHCSAGVGRTGTFIA 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 568915937 1173 IDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQ 1214
Cdd:cd00047   159 IDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 986-1220 2.29e-94

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: 302.39  E-value: 2.29e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  986 NRGKNRYNNVLPYDISRVKLS-VQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVE 1064
Cdd:cd14553     3 NKPKNRYANVIAYDHSRVILQpIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1065 QGRTKCEEYWPSKQAQDYGDITVAMTSEVVLPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVR 1144
Cdd:cd14553    83 RSRVKCDQYWPTRGTETYGLIQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVK 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568915937 1145 DYMkqiPPES-PILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLDII 1220
Cdd:cd14553   163 ACN---PPDAgPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLEAV 236
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 990-1217 7.67e-94

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: 300.71  E-value: 7.67e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  990 NRYNNVLPYDISRVKLSV---QTHStdDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQG 1066
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQlggEPHS--DYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1067 RTKCEEYWPSKQAQ-DYGDITVAMTSEVVLPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRD 1145
Cdd:cd14618    79 RVLCDHYWPSESTPvSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELVRE 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568915937 1146 YMKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVL 1217
Cdd:cd14618   159 HVQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 976-1217 1.11e-91

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: 295.26  E-value: 1.11e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  976 LPKYTAEIAENRGKNRYNNVLPYDISRVKL-SVQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVY 1054
Cdd:cd14614     2 IPHFAADLPVNRCKNRYTNILPYDFSRVKLvSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1055 AIVMLTKCVEQGRTKCEEYWP-SKQAQDYGDITVAMTSEVVLPEWTIRDFVVKnmQNSESHPLRQFHFTSWPDHGVP--D 1131
Cdd:cd14614    82 IIVMLTQCNEKRRVKCDHYWPfTEEPVAYGDITVEMLSEEEQPDWAIREFRVS--YADEVQDVMHFNYTAWPDHGVPtaN 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1132 TTDLLINFRYLVRDymKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVF 1211
Cdd:cd14614   160 AAESILQFVQMVRQ--QAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIF 237


                  ....*.
gi 568915937 1212 LNQCVL 1217
Cdd:cd14614   238 IHQCVQ 243
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 1015-1212 7.09e-89

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: 285.78  E-value: 7.09e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1015 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEVV 1094
Cdd:cd14549     1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTETYGNIQVTLLSTEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1095 LPEWTIRDFVVKNMQNSESHP------LRQFHFTSWPDHGVPDTTDLLINFrylVRDYMKQIPPES-PILVHCSAGVGRT 1167
Cdd:cd14549    81 LATYTVRTFSLKNLKLKKVKGrsservVYQYHYTQWPDHGVPDYTLPVLSF---VRKSSAANPPGAgPIVVHCSAGVGRT 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 568915937 1168 GTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFL 1212
Cdd:cd14549   158 GTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFI 202
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 961-1211 2.00e-83

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: 273.47  E-value: 2.00e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  961 GFAEEYEDLKLigiSLPKYTAEIAE---NRGKNRYNNVLPYDISRVKLS-VQTHSTDDYINANYMPGYHSKKDFIATQGP 1036
Cdd:cd14543     4 GIYEEYEDIRR---EPPAGTFLCSLapaNQEKNRYGDVLCLDQSRVKLPkRNGDERTDYINANFMDGYKQKNAYIATQGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1037 LPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQ--AQDYGDITVAMTSEVVLPEWTIRDFVVKNMQNSESH 1114
Cdd:cd14543    81 LPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEgsSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDESR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1115 PLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQI-----------PPESPILVHCSAGVGRTGTFIAIDRLIYQIENE 1183
Cdd:cd14543   161 QVTHFQFTSWPDFGVPSSAAALLDFLGEVRQQQALAvkamgdrwkghPPGPPIVVHCSAGIGRTGTFCTLDICLSQLEDV 240

                         250       260
                  ....*....|....*....|....*...
gi 568915937 1184 NTVDVYGIVYDLRMHRPLMVQTEDQYVF 1211
Cdd:cd14543   241 GTLNVMQTVRRMRTQRAFSIQTPDQYYF 268
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 952-1218 3.75e-78

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: 259.20  E-value: 3.75e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  952 KKQQADSNCGFAEEYEDLKlIGISLPKYTAEIAENRGKNRYNNVLPYDISRVKL-SVQTHSTDDYINANYMPGYHSKKDF 1030
Cdd:cd14626     8 ERLKANDGLKFSQEYESID-PGQQFTWENSNLEVNKPKNRYANVIAYDHSRVILtSVDGVPGSDYINANYIDGYRKQNAY 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1031 IATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEVVLPEWTIRDFVVKNMQN 1110
Cdd:cd14626    87 IATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTETYGMIQVTLLDTVELATYSVRTFALYKNGS 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1111 SESHPLRQFHFTSWPDHGVPDTTDLLINFrylVRDYMKQIPPES-PILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVY 1189
Cdd:cd14626   167 SEKREVRQFQFMAWPDHGVPEYPTPILAF---LRRVKACNPPDAgPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIY 243

                         250       260
                  ....*....|....*....|....*....
gi 568915937 1190 GIVYDLRMHRPLMVQTEDQYVFLNQCVLD 1218
Cdd:cd14626   244 GHVTCMRSQRNYMVQTEDQYIFIHEALLE 272
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 990-1214 1.30e-76

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: 252.70  E-value: 1.30e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  990 NRYNNVLPYDISRVKL-SVQTHSTDDYINANYMPGYHSK-KDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEqGR 1067
Cdd:cd14547     1 NRYKTILPNEHSRVCLpSVDDDPLSSYINANYIRGYDGEeKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTE-AK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1068 TKCEEYWPSKQAQDYGDITVAMTSEVVLPEWTIRDFVVKNmqNSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYM 1147
Cdd:cd14547    80 EKCAQYWPEEENETYGDFEVTVQSVKETDGYTVRKLTLKY--GGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEEAR 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568915937 1148 KQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQ 1214
Cdd:cd14547   158 QTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVHR 224
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 981-1217 1.02e-75

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: 250.52  E-value: 1.02e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  981 AEIAENRGKNRYNNVLPYDISRVKLS-VQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVML 1059
Cdd:cd14554     1 ANLPCNKFKNRLVNILPYESTRVCLQpIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1060 TKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEVVLPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINF 1139
Cdd:cd14554    81 TKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDF 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568915937 1140 RYLVRDYMKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVL 1217
Cdd:cd14554   161 IGQVHKTKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRAAL 238
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 962-1220 1.06e-75

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: 251.88  E-value: 1.06e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  962 FAEEYEDLKLIGISLpKYTAEIA---ENRGKNRYNNVLPYDISRVKLSV-----QTHStdDYINANYMPGYHSKKDFIAT 1033
Cdd:cd17667     1 FSEDFEEVQRCTADM-NITAEHSnhpDNKHKNRYINILAYDHSRVKLRPlpgkdSKHS--DYINANYVDGYNKAKAYIAT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1034 QGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEVVLPEWTIRDFVVKNMQ---N 1110
Cdd:cd17667    78 QGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTKvkkG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1111 SESHP--------LRQFHFTSWPDHGVPDTTDLLINFryLVRDYMKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIEN 1182
Cdd:cd17667   158 QKGNPkgrqnertVIQYHYTQWPDMGVPEYALPVLTF--VRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKD 235

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 568915937 1183 ENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLDII 1220
Cdd:cd17667   236 KSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAI 273
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 985-1218 4.17e-75

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: 248.79  E-value: 4.17e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  985 ENRGKNRYNNVLPYDISRVKLSV---QTHStdDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTK 1061
Cdd:cd14630     2 ENRNKNRYGNIISYDHSRVRLQLldgDPHS--DYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1062 CVEQGRTKCEEYWPSkQAQDYGDITVAMTSEVVLPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFry 1141
Cdd:cd14630    80 LVEVGRVKCVRYWPD-DTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGF-- 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568915937 1142 lVRDYMKQIPPES-PILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 1218
Cdd:cd14630   157 -VRQVKFLNPPDAgPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILE 233
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 961-1218 1.83e-72

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: 243.03  E-value: 1.83e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  961 GFAEEYEDLkLIGISLPKYTAEIAENRGKNRYNNVLPYDISRVKL-SVQTHSTDDYINANYMPGYHSKKDFIATQGPLPN 1039
Cdd:cd14633    16 GFKEEYESF-FEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLqPIEGETSSDYINGNYIDGYHRPNHYIATQGPMQE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1040 TLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSkQAQDYGDITVAMTSEVVLPEWTIRDFVVKNMQNSESHPLRQF 1119
Cdd:cd14633    95 TIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPD-DTEIYKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQF 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1120 HFTSWPDHGVPDTTDLLINFrylVRDYMKQIPPES-PILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMH 1198
Cdd:cd14633   174 HFTGWPDHGVPYHATGLLGF---VRQVKSKSPPNAgPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSR 250

                         250       260
                  ....*....|....*....|
gi 568915937 1199 RPLMVQTEDQYVFLNQCVLD 1218
Cdd:cd14633   251 RVNMVQTEEQYVFIHDAILE 270
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 990-1214 1.88e-72

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: 240.96  E-value: 1.88e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  990 NRYNNVLPYDISRVKLSVQTHST-DDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRT 1068
Cdd:cd14616     1 NRFPNIKPYNNNRVKLIADAGVPgSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1069 KCEEYWP--SKQAQDYGDITVAMTSEVVLPEWTIRDFVVKnmQNSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRdy 1146
Cdd:cd14616    81 RCHQYWPedNKPVTVFGDIVITKLMEDVQIDWTIRDLKIE--RHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVR-- 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568915937 1147 MKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQ 1214
Cdd:cd14616   157 ASRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 950-1220 3.98e-72

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: 242.33  E-value: 3.98e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  950 YFKKQQADSNCGFAEEYEDLKlIGISLPKYTAEIAENRGKNRYNNVLPYDISRVKLS-VQTHSTDDYINANYMPGYHSKK 1028
Cdd:cd14624    12 HIERLKANDNLKFSQEYESID-PGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSaIEGIPGSDYINANYIDGYRKQN 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1029 DFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEVVLPEWTIRDFVVKNM 1108
Cdd:cd14624    91 AYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRGTETYGLIQVTLLDTVELATYCVRTFALYKN 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1109 QNSESHPLRQFHFTSWPDHGVPDTTDLLINFrylVRDYMKQIPPES-PILVHCSAGVGRTGTFIAIDRLIYQIENENTVD 1187
Cdd:cd14624   171 GSSEKREVRQFQFTAWPDHGVPEHPTPFLAF---LRRVKTCNPPDAgPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVD 247

                         250       260       270
                  ....*....|....*....|....*....|...
gi 568915937 1188 VYGIVYDLRMHRPLMVQTEDQYVFLNQCVLDII 1220
Cdd:cd14624   248 IYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAV 280
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 942-1220 1.60e-71

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: 240.38  E-value: 1.60e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  942 IRVENFEAYFKKQQADSNCGFAEEYEDLKlIGISLPKYTAEIAENRGKNRYNNVLPYDISRVKL-SVQTHSTDDYINANY 1020
Cdd:cd14625     4 IPISELAEHTERLKANDNLKLSQEYESID-PGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILqPIEGIMGSDYINANY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1021 MPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEVVLPEWTI 1100
Cdd:cd14625    83 IDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRGTETYGMIQVTLLDTIELATFCV 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1101 RDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFrylVRDYMKQIPPES-PILVHCSAGVGRTGTFIAIDRLIYQ 1179
Cdd:cd14625   163 RTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAF---LRRVKTCNPPDAgPIVVHCSAGVGRTGCFIVIDAMLER 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 568915937 1180 IENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLDII 1220
Cdd:cd14625   240 IKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAV 280
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 937-1218 8.90e-70

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: 236.07  E-value: 8.90e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  937 KKSKLIRVENFEAYFKKQQADSNCGFAEEYEDLKLIGISLPKYTAEIAENRGKNRYNNVLPYDISRVKL-SVQTHSTDDY 1015
Cdd:cd14621     3 RKYPPLPVDKLEEEINRRMADDNKLFREEFNALPACPIQATCEAASKEENKEKNRYVNILPYDHSRVHLtPVEGVPDSDY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1016 INANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEVVL 1095
Cdd:cd14621    83 INASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGCWTYGNIRVSVEDVTVL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1096 PEWTIRDFVVKNMQN-SESHPLR---QFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQIPpeSPILVHCSAGVGRTGTFI 1171
Cdd:cd14621   163 VDYTVRKFCIQQVGDvTNKKPQRlitQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYA--GAIVVHCSAGVGRTGTFI 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 568915937 1172 AIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 1218
Cdd:cd14621   241 VIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLE 287
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 1015-1218 1.28e-69

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: 232.11  E-value: 1.28e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1015 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPsKQAQDYGDITVAMTSEVV 1094
Cdd:cd14555     1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWP-DDTEVYGDIKVTLVETEP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1095 LPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFrylVRDYMKQIPPES-PILVHCSAGVGRTGTFIAI 1173
Cdd:cd14555    80 LAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGF---IRRVKASNPPSAgPIVVHCSAGAGRTGCYIVI 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 568915937 1174 DRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 1218
Cdd:cd14555   157 DIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 1015-1214 8.16e-69

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: 229.71  E-value: 8.16e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1015 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPS--KQAQDYGDITVAMTSE 1092
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSmeEGSRAFGDVVVKINEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1093 VVLPEWTIRDFVVKNMQNSES-HPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQIppESPILVHCSAGVGRTGTFI 1171
Cdd:cd14557    81 KICPDYIIRKLNINNKKEKGSgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFF--SGPIVVHCSAGVGRTGTYI 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 568915937 1172 AIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQ 1214
Cdd:cd14557   159 GIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 992-1218 1.09e-66

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: 224.82  E-value: 1.09e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  992 YNNVLPYDISRVKLS-VQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKC 1070
Cdd:cd14620     1 YPNILPYDHSRVILSqLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1071 EEYWPSKQAQDYGDITVAMTSEVVLPEWTIRDFVVKNMQNSESHPLR---QFHFTSWPDHGVPDTTDLLINFRYLVrdym 1147
Cdd:cd14620    81 YQYWPDQGCWTYGNIRVAVEDCVVLVDYTIRKFCIQPQLPDGCKAPRlvtQLHFTSWPDFGVPFTPIGMLKFLKKV---- 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568915937 1148 KQIPP--ESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 1218
Cdd:cd14620   157 KSVNPvhAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 1015-1212 1.50e-66

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: 223.66  E-value: 1.50e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1015 YINANYM-PGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQD-YGDITVAM--T 1090
Cdd:cd18533     1 YINASYItLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGeYGDLTVELvsE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1091 SEVVLPEWTIRDFVVKnMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQIPPESPILVHCSAGVGRTGTF 1170
Cdd:cd18533    81 EENDDGGFIVREFELS-KEDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNDSASLDPPIIVHCSAGVGRTGTF 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568915937 1171 IAIDRLIYQIEN--------ENTVD-VYGIVYDLRMHRPLMVQTEDQYVFL 1212
Cdd:cd18533   160 IALDSLLDELKRglsdsqdlEDSEDpVYEIVNQLRKQRMSMVQTLRQYIFL 210
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 980-1220 2.02e-66

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: 226.53  E-value: 2.02e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  980 TAEIAENRGKNRYNNVLPYDISRVKLS-VQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVM 1058
Cdd:cd14629    47 SANLPCNKFKNRLVNIMPYELTRVCLQpIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVM 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1059 LTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEVVLPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLIN 1138
Cdd:cd14629   127 LTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGEGFID 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1139 FRYLVRDYMKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 1218
Cdd:cd14629   207 FIGQVHKTKEQFGQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALE 286


                  ..
gi 568915937 1219 II 1220
Cdd:cd14629   287 YL 288
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 1015-1218 2.27e-66

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: 223.00  E-value: 2.27e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1015 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPsKQAQDYGDITVAMTSEVV 1094
Cdd:cd14632     1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWP-DDSDTYGDIKITLLKTET 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1095 LPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFrylVRDYMKQIPPES-PILVHCSAGVGRTGTFIAI 1173
Cdd:cd14632    80 LAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAF---IRRVKASTPPDAgPVVVHCSAGAGRTGCYIVL 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 568915937 1174 DRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 1218
Cdd:cd14632   157 DVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 980-1220 2.30e-66

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: 226.15  E-value: 2.30e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  980 TAEIAENRGKNRYNNVLPYDISRVKLS-VQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVM 1058
Cdd:cd14627    47 SANLPCNKFKNRLVNIMPYETTRVCLQpIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVM 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1059 LTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEVVLPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLIN 1138
Cdd:cd14627   127 LTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFID 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1139 FRYLVRDYMKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 1218
Cdd:cd14627   207 FIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALE 286


                  ..
gi 568915937 1219 II 1220
Cdd:cd14627   287 YL 288
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 986-1212 3.42e-66

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


Pssm-ID: 350392 [Multi-domain]  Cd Length: 251  Bit Score: 224.26  E-value: 3.42e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  986 NRGKNRYNNVLPYDISRVKLSVQTHST--DDYINANYM-----PGYHSK--KDFIATQGPLPNTLKDFWRMVWEKNVYAI 1056
Cdd:cd14544     1 NKGKNRYKNILPFDHTRVILKDRDPNVpgSDYINANYIrneneGPTTDEnaKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1057 VMLTKCVEQGRTKCEEYWPSK-QAQDYGDITVAMTSEVVLPEWTIRDFVVKNM-QNSESHPLRQFHFTSWPDHGVPDTTD 1134
Cdd:cd14544    81 VMTTKEVERGKNKCVRYWPDEgMQKQYGPYRVQNVSEHDTTDYTLRELQVSKLdQGDPIREIWHYQYLSWPDHGVPSDPG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1135 LLINFRYLVRDYMKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENEN---TVDVYGIVYDLRMHRPLMVQTEDQYVF 1211
Cdd:cd14544   161 GVLNFLEDVNQRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDIDIQKTIQMVRSQRSGMVQTEAQYKF 240


                  .
gi 568915937 1212 L 1212
Cdd:cd14544   241 I 241
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 942-1220 4.02e-66

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: 225.38  E-value: 4.02e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  942 IRVENFEAYFKK----QQADSNCGFAEEYEDLKLIGISLPKY-TAEIAENRGKNRYNNVLPYDISRVKLS-VQTHSTDDY 1015
Cdd:cd14628     3 VPARNLYAYIQKltqiETGENVTGMELEFKRLASSKAHTSRFiSANLPCNKFKNRLVNIMPYESTRVCLQpIRGVEGSDY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1016 INANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEVVL 1095
Cdd:cd14628    83 INASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNM 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1096 PEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQIPPESPILVHCSAGVGRTGTFIAIDR 1175
Cdd:cd14628   163 PQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITLSI 242

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 568915937 1176 LIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLDII 1220
Cdd:cd14628   243 VLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYL 287
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 1015-1213 9.62e-66

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: 221.01  E-value: 9.62e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1015 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEVV 1094
Cdd:cd17668     1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1095 LPEWTIRDFVVKNMQ--------NSESHPLRQFHFTSWPDHGVPDTTDLLINFryLVRDYMKQIPPESPILVHCSAGVGR 1166
Cdd:cd17668    81 LAYYTVRNFTLRNTKikkgsqkgRPSGRVVTQYHYTQWPDMGVPEYTLPVLTF--VRKASYAKRHAVGPVVVHCSAGVGR 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 568915937 1167 TGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLN 1213
Cdd:cd17668   159 TGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIH 205
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 1015-1220 3.04e-65

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: 219.55  E-value: 3.04e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1015 YINANYM--PGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPS---KQAQDYGDITVAM 1089
Cdd:cd14538     1 YINASHIriPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDslnKPLICGGRLEVSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1090 TSEVVLPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFrylVRdYMKQIPPESPILVHCSAGVGRTGT 1169
Cdd:cd14538    81 EKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRF---IR-YMRRIHNSGPIVVHCSAGIGRTGV 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568915937 1170 FIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLDII 1220
Cdd:cd14538   157 LITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 977-1223 7.88e-65

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: 222.12  E-value: 7.88e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  977 PKYTAEIAENRGKNRYNNVLPYDISRVKLSVQTHSTD-DYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYA 1055
Cdd:cd14604    48 PTATGEKEENVKKNRYKDILPFDHSRVKLTLKTSSQDsDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAI 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1056 IVMLTKCVEQGRTKCEEYWP--SKQAQDYGDITVAMTSEVVLPEWTIRDFVVKnMQNsESHPLRQFHFTSWPDHGVPDTT 1133
Cdd:cd14604   128 IVMACREFEMGRKKCERYWPlyGEEPMTFGPFRISCEAEQARTDYFIRTLLLE-FQN-ETRRLYQFHYVNWPDHDVPSSF 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1134 DLLINFRYLVRDYmkQIPPESPILVHCSAGVGRTGTFIAID---RLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYV 1210
Cdd:cd14604   206 DSILDMISLMRKY--QEHEDVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYE 283

                         250
                  ....*....|...
gi 568915937 1211 FLNQCVLDIIRAQ 1223
Cdd:cd14604   284 LVHRAIAQLFEKQ 296
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 1015-1214 2.81e-64

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: 216.52  E-value: 2.81e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1015 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQD--YGDITVAMTSE 1092
Cdd:cd14542     1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQlqFGPFKISLEKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1093 vvlpEWTIRDFVVKNMQ---NSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYmkQIPPESPILVHCSAGVGRTGT 1169
Cdd:cd14542    81 ----KRVGPDFLIRTLKvtfQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDY--QGSEDVPICVHCSAGCGRTGT 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 568915937 1170 FIAIDR----LIYQIENENtVDVYGIVYDLRMHRPLMVQTEDQYVFLNQ 1214
Cdd:cd14542   155 ICAIDYvwnlLKTGKIPEE-FSLFDLVREMRKQRPAMVQTKEQYELVYR 202
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 1015-1216 3.67e-64

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: 216.37  E-value: 3.67e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1015 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEVV 1094
Cdd:cd14552     1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGSVSSGDITVELKDQTD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1095 LPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQiPPESPILVHCSAGVGRTGTFIAID 1174
Cdd:cd14552    81 YEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQ-SGNHPITVHCSAGAGRTGTFCALS 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 568915937 1175 RLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCV 1216
Cdd:cd14552   160 TVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 981-1221 4.33e-63

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: 216.25  E-value: 4.33e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  981 AEIAENRGKNRYNNVLPYDISRVKLsvqtHSTDDYINANYM----PGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAI 1056
Cdd:cd14600    35 AKLPQNMDKNRYKDVLPYDATRVVL----QGNEDYINASYVnmeiPSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSLI 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1057 VMLTKCVEQGRTKCEEYWPSKQ-AQDYGDITVAMTSEVVLPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDL 1135
Cdd:cd14600   111 VMLTTLTERGRTKCHQYWPDPPdVMEYGGFRVQCHSEDCTIAYVFREMLLTNTQTGEERTVTHLQYVAWPDHGVPDDSSD 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1136 LINFRYLVRDymKQIPPEsPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQC 1215
Cdd:cd14600   191 FLEFVNYVRS--KRVENE-PVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEA 267


                  ....*.
gi 568915937 1216 VLDIIR 1221
Cdd:cd14600   268 ILRVYE 273
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1014-1217 1.12e-62

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: 212.57  E-value: 1.12e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1014 DYINANY----MPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPS-KQAQDYGDITVA 1088
Cdd:cd14541     1 DYINANYvnmeIPGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDlGETMQFGNLQIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1089 MTSEVVLPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRdyMKQIPPESPILVHCSAGVGRTG 1168
Cdd:cd14541    81 CVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVR--QNRVGMVEPTVVHCSAGIGRTG 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 568915937 1169 TFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVL 1217
Cdd:cd14541   159 VLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAIL 207
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 989-1211 1.13e-62

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: 213.41  E-value: 1.13e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  989 KNRYNNVLPYDISRVKLSVQTHSTDdYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRT 1068
Cdd:cd14545     1 LNRYRDRDPYDHDRSRVKLKQGDND-YINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1069 KCEEYWPSKQAQDYG----DITVAMTSEVVLPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVR 1144
Cdd:cd14545    80 KCAQYWPQGEGNAMIfedtGLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQKVR 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568915937 1145 DYMKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENT--VDVYGIVYDLRMHRPLMVQTEDQYVF 1211
Cdd:cd14545   160 ESGSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQLRF 228
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 985-1216 1.44e-62

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: 214.30  E-value: 1.44e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  985 ENRGKNRYNNVLPYDISRVKLS-VQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCV 1063
Cdd:cd14603    29 ENVKKNRYKDILPYDQTRVILSlLQEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVILMACREI 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1064 EQGRTKCEEYWPSKQAQ-DYGDITVAMTSEVVL-PEWTIRDFVVKNMQnsESHPLRQFHFTSWPDHGVPDTTDLLINFRY 1141
Cdd:cd14603   109 EMGKKKCERYWAQEQEPlQTGPFTITLVKEKRLnEEVILRTLKVTFQK--ESRSVSHFQYMAWPDHGIPDSPDCMLAMIE 186

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568915937 1142 LVRDYMKQIPpeSPILVHCSAGVGRTGTFIAID---RLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCV 1216
Cdd:cd14603   187 LARRLQGSGP--EPLCVHCSAGCGRTGVICTVDyvrQLLLTQRIPPDFSIFDVVLEMRKQRPAAVQTEEQYEFLYHTV 262
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 1015-1214 2.13e-62

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: 211.31  E-value: 2.13e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1015 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEVV 1094
Cdd:cd14551     1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCWTYGNLRVRVEDTVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1095 LPEWTIRDFVV-KNMQNSESHPLR---QFHFTSWPDHGVPDTTDLLINFRYLVrdyMKQIPPES-PILVHCSAGVGRTGT 1169
Cdd:cd14551    81 LVDYTTRKFCIqKVNRGIGEKRVRlvtQFHFTSWPDFGVPFTPIGMLKFLKKV---KSANPPRAgPIVVHCSAGVGRTGT 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 568915937 1170 FIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQ 1214
Cdd:cd14551   158 FIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 985-1220 3.40e-62

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: 212.00  E-value: 3.40e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  985 ENRGKNRYNNVLPYDISRVKLSVQthstDDYINANY--MPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKC 1062
Cdd:cd14597     2 ENRKKNRYKNILPYDTTRVPLGDE----GGYINASFikMPVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1063 VEQGRTKCEEYWP-----SKQAQDYGDITVAMTSEvvLPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLI 1137
Cdd:cd14597    78 VEGGKIKCQRYWPeilgkTTMVDNRLQLTLVRMQQ--LKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPEQLL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1138 NFRylvrDYMKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVL 1217
Cdd:cd14597   156 TFI----SYMRHIHKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVIL 231


                  ...
gi 568915937 1218 DII 1220
Cdd:cd14597   232 YVL 234
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 982-1212 4.29e-62

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: 212.39  E-value: 4.29e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  982 EIAENRGKNRYNNVLPYDISRVKLSVQTHS--TDDYINANYMPGYHSK-KDFIATQGPLPNTLKDFWRMVWEKNVYAIVM 1058
Cdd:cd14612    11 DIPGHASKDRYKTILPNPQSRVCLRRAGSQeeEGSYINANYIRGYDGKeKAYIATQGPMLNTVSDFWEMVWQEECPIIVM 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1059 LTKcVEQGRTKCEEYWPSKQAQdYGDITVAMTSEVVLPEWTIRDFVVKnmQNSESHPLRQFHFTSWPDHGVPDTTDLLIN 1138
Cdd:cd14612    91 ITK-LKEKKEKCVHYWPEKEGT-YGRFEIRVQDMKECDGYTIRDLTIQ--LEEESRSVKHYWFSSWPDHQTPESAGPLLR 166

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568915937 1139 FRYLVRDYMKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFL 1212
Cdd:cd14612   167 LVAEVEESRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFL 240
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 989-1219 7.62e-62

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: 210.85  E-value: 7.62e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  989 KNRYNNVLPYDISRVKLSVQTHSTD-DYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGR 1067
Cdd:cd14602     1 KNRYKDILPYDHSRVELSLITSDEDsDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1068 TKCEEYW--PSKQAQDYGDITVAMTSEVVLPEWTIRdfVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRD 1145
Cdd:cd14602    81 KKCERYWaePGEMQLEFGPFSVTCEAEKRKSDYIIR--TLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRC 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568915937 1146 YmkQIPPESPILVHCSAGVGRTGTFIAID---RLIYQ-IENENtVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLDI 1219
Cdd:cd14602   159 Y--QEDDSVPICIHCSAGCGRTGVICAIDytwMLLKDgIIPEN-FSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIEL 233
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 1014-1218 1.46e-61

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: 209.09  E-value: 1.46e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1014 DYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEV 1093
Cdd:cd14622     1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGSVTHGEITIEIKNDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1094 VLPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQiPPESPILVHCSAGVGRTGTFIAI 1173
Cdd:cd14622    81 LLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQ-TGNHPIVVHCSAGAGRTGTFIAL 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 568915937 1174 DRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 1218
Cdd:cd14622   160 SNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQD 204
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 962-1211 1.61e-61

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: 211.81  E-value: 1.61e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  962 FAEEYEDLKLIGISLPKYTAEIAENRGKNRYNNVLPYDISRVKLSVQThstDDYINANYMPGYHSKKDFIATQGPLPNTL 1041
Cdd:cd14608     1 WAAIYQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQED---NDYINASLIKMEEAQRSYILTQGPLPNTC 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1042 KDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQ----DYGDITVAMTSEVVLPEWTIRDFVVKNMQNSESHPLR 1117
Cdd:cd14608    78 GHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKemifEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREIL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1118 QFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQIPPESPILVHCSAGVGRTGTFIAIDR---LIYQIENENTVDVYGIVYD 1194
Cdd:cd14608   158 HFHYTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTcllLMDKRKDPSSVDIKKVLLE 237

                         250
                  ....*....|....*..
gi 568915937 1195 LRMHRPLMVQTEDQYVF 1211
Cdd:cd14608   238 MRKFRMGLIQTADQLRF 254
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 991-1216 2.36e-61

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: 209.52  E-value: 2.36e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  991 RYNNVLPYDISRVKLSVQT-HSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTK 1069
Cdd:cd14623     1 RVLQIIPYEFNRVIIPVKRgEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1070 CEEYWPSKQAQDYGDITVAMTSEVVLPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQ 1149
Cdd:cd14623    81 CAQYWPSDGSVSYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQQQ 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568915937 1150 iPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCV 1216
Cdd:cd14623   161 -SGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVV 226
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 1007-1218 1.20e-59

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: 204.10  E-value: 1.20e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1007 VQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPsKQAQDYGDIT 1086
Cdd:cd14631     7 VEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWP-DDTEVYGDFK 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1087 VAMTSEVVLPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFryLVRDYMKQIPPESPILVHCSAGVGR 1166
Cdd:cd14631    86 VTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSF--IRRVKLSNPPSAGPIVVHCSAGAGR 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568915937 1167 TGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 1218
Cdd:cd14631   164 TGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 985-1216 5.64e-59

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: 203.71  E-value: 5.64e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  985 ENRGKNRYNNVLPYDISRVKLsvqtHSTD------DYINANY-MPGYHS-------KKDFIATQGPLPNTLKDFWRMVWE 1050
Cdd:cd14605     1 ENKNKNRYKNILPFDHTRVVL----HDGDpnepvsDYINANIiMPEFETkcnnskpKKSYIATQGCLQNTVNDFWRMVFQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1051 KNVYAIVMLTKCVEQGRTKCEEYWPSKQA-QDYGDITVAMTSEVVLPEWTIRDFVVKNM-QNSESHPLRQFHFTSWPDHG 1128
Cdd:cd14605    77 ENSRVIVMTTKEVERGKSKCVKYWPDEYAlKEYGVMRVRNVKESAAHDYILRELKLSKVgQGNTERTVWQYHFRTWPDHG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1129 VPDTTDLLINFRYLVRDYMKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENT---VDVYGIVYDLRMHRPLMVQT 1205
Cdd:cd14605   157 VPSDPGGVLDFLEEVHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMVQT 236

                         250
                  ....*....|.
gi 568915937 1206 EDQYVFLNQCV 1216
Cdd:cd14605   237 EAQYRFIYMAV 247
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 1015-1212 7.86e-58

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: 198.39  E-value: 7.86e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1015 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQaQDYGDITVAMTSEVV 1094
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEK-KTYGDIEVELKDTEK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1095 LPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQIPPES----PILVHCSAGVGRTGTF 1170
Cdd:cd14558    80 SPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKNSKHgrsvPIVVHCSDGSSRTGIF 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 568915937 1171 IAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFL 1212
Cdd:cd14558   160 CALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFL 201
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 989-1214 1.20e-57

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: 198.60  E-value: 1.20e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  989 KNRYNNVLPYDISRVKLSVQ--THSTDDYINANYMPGYHSK-KDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQ 1065
Cdd:cd14611     2 KNRYKTILPNPHSRVCLKPKnsNDSLSTYINANYIRGYGGKeKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1066 GRtKCEEYWPSKQAQdYGDITVAMTSEVVLPEWTIRDFVVKnmQNSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRD 1145
Cdd:cd14611    82 NE-KCVLYWPEKRGI-YGKVEVLVNSVKECDNYTIRNLTLK--QGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLDVEE 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568915937 1146 YMKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQ 1214
Cdd:cd14611   158 DRLASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVHH 226
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 966-1211 1.52e-57

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: 199.42  E-value: 1.52e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  966 YEDLKLIGISLPKYTAEIAENRGKNRYNNVLPYDISRVKLSvqtHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFW 1045
Cdd:cd14607     4 YLEIRNESHDYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQ---NTENDYINASLVVIEEAQRSYILTQGPLPNTCCHFW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1046 RMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQD--YGD--ITVAMTSEVVLPEWTIRDFVVKNMQNSESHPLRQFHF 1121
Cdd:cd14607    81 LMVWQQKTKAVVMLNRIVEKDSVKCAQYWPTDEEEVlsFKEtgFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFHY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1122 TSWPDHGVPDTTDLLINFRYLVRDYMKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENEN--TVDVYGIVYDLRMHR 1199
Cdd:cd14607   161 TTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRKYR 240

                         250
                  ....*....|..
gi 568915937 1200 PLMVQTEDQYVF 1211
Cdd:cd14607   241 MGLIQTPDQLRF 252
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 980-1211 1.70e-57

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: 200.26  E-value: 1.70e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  980 TAEIAENRGKNRYNNVLPYDISRVKLSVQTH-STDDYINAN-------YMPGYhskkdfIATQGPLPNTLKDFWRMVWEK 1051
Cdd:cd14609    36 TAQGEANVKKNRNPDFVPYDHARIKLKAESNpSRSDYINASpiiehdpRMPAY------IATQGPLSHTIADFWQMVWEN 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1052 NVYAIVMLTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEVVLPE-WTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVP 1130
Cdd:cd14609   110 GCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHIYEVNLVSEHIWCEdFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGIP 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1131 DTTDLLINFRYLVRDYMKQipPESPILVHCSAGVGRTGTFIAIDRLIYQI-ENENTVDVYGIVYDLRMHRPLMVQTEDQY 1209
Cdd:cd14609   190 SSTRPLLDFRRKVNKCYRG--RSCPIIVHCSDGAGRTGTYILIDMVLNRMaKGVKEIDIAATLEHVRDQRPGMVRTKDQF 267


                  ..
gi 568915937 1210 VF 1211
Cdd:cd14609   268 EF 269
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 985-1220 4.99e-56

catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein phosphatase non-receptor type 6 (PTPN6), also called SH2 domain-containing protein-tyrosine phosphatase 1 (SHP1 or SHP-1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN6 expression is restricted mainly to hematopoietic and epithelial cells. It is an important regulator of hematopoietic cells, downregulating pathways that promote cell growth, survival, adhesion, and activation. It regulates glucose homeostasis by modulating insulin signalling in the liver and muscle, and it also negatively regulates bone resorption, affecting both the formation and the function of osteoclasts. PTPN6 contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.


Pssm-ID: 350454 [Multi-domain]  Cd Length: 266  Bit Score: 195.48  E-value: 4.99e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  985 ENRGKNRYNNVLPYDISRVKLSVQTHST--DDYINANY-----MPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIV 1057
Cdd:cd14606    17 ENKSKNRYKNILPFDHSRVILQGRDSNIpgSDYINANYvknqlLGPDENAKTYIASQGCLEATVNDFWQMAWQENSRVIV 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1058 MLTKCVEQGRTKCEEYWPSKQAQ-DYGDITVAMTSEVVLPEWTIRDFVVKNMQNSES-HPLRQFHFTSWPDHGVPDTTDL 1135
Cdd:cd14606    97 MTTREVEKGRNKCVPYWPEVGMQrAYGPYSVTNCGEHDTTEYKLRTLQVSPLDNGELiREIWHYQYLSWPDHGVPSEPGG 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1136 LINFRYLVRDYMKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENT---VDVYGIVYDLRMHRPLMVQTEDQYVFL 1212
Cdd:cd14606   177 VLSFLDQINQRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRAQRSGMVQTEAQYKFI 256


                  ....*...
gi 568915937 1213 NQCVLDII 1220
Cdd:cd14606   257 YVAIAQFI 264
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 979-1222 7.86e-56

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: 195.66  E-value: 7.86e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  979 YTAEIAENRGKNRYNNVLPYDISRVKLSVQ-THSTDDYINANYMPGYHSKKD-FIATQGPLPNTLKDFWRMVWEKNVYAI 1056
Cdd:cd14610    37 NVAQREENVQKNRSLAVLPYDHSRIILKAEnSHSHSDYINASPIMDHDPRNPaYIATQGPLPATVADFWQMVWESGCVVI 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1057 VMLTKCVEQGRTKCEEYWPSKQAQDYGDITVAMTSEVVLPE-WTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDL 1135
Cdd:cd14610   117 VMLTPLAENGVKQCYHYWPDEGSNLYHIYEVNLVSEHIWCEdFLVRSFYLKNLQTNETRTVTQFHFLSWNDQGVPASTRS 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1136 LINFRYLVRDYMKQipPESPILVHCSAGVGRTGTFIAIDRLIYQI-ENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQ 1214
Cdd:cd14610   197 LLDFRRKVNKCYRG--RSCPIIVHCSDGAGRSGTYILIDMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALT 274


                  ....*...
gi 568915937 1215 CVLDIIRA 1222
Cdd:cd14610   275 AVAEEVNA 282
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 1014-1221 8.40e-55

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: 190.16  E-value: 8.40e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1014 DYINANYM----PGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQ-DYGDITVA 1088
Cdd:cd14601     1 DYINANYInmeiPSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSsSYGGFQVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1089 MTSEVVLPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDymKQIPPESPILVHCSAGVGRTG 1168
Cdd:cd14601    81 CHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRN--KRAGKDEPVVVHCSAGIGRTG 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568915937 1169 TFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLDIIR 1221
Cdd:cd14601   159 VLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKVYE 211
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 989-1213 2.41e-54

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: 190.46  E-value: 2.41e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  989 KNRYNNVLPYDISRVKLSvqTHSTDD----YINANYMPGYHSK-KDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKcV 1063
Cdd:cd14613    28 KNRYKTILPNPHSRVCLT--SPDQDDplssYINANYIRGYGGEeKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITN-I 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1064 EQGRTKCEEYWPSKQAQdYGDITVAMTSEVVLPEWTIRDFVVKNmqNSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLV 1143
Cdd:cd14613   105 EEMNEKCTEYWPEEQVT-YEGIEITVKQVIHADDYRLRLITLKS--GGEERGLKHYWYTSWPDQKTPDNAPPLLQLVQEV 181

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568915937 1144 RDYMKQIPPE-SPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLN 1213
Cdd:cd14613   182 EEARQQAEPNcGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVH 252
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 1015-1221 1.41e-53

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: 186.11  E-value: 1.41e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1015 YINANY--MPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPS--KQAQDYGDITVAMT 1090
Cdd:cd14596     1 YINASYitMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPEtlQEPMELENYQLRLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1091 SEVVLPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFrylVRdYMKQIPPESPILVHCSAGVGRTGTF 1170
Cdd:cd14596    81 NYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKF---IC-YMRKVHNTGPIVVHCSAGIGRAGVL 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568915937 1171 IAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLDIIR 1221
Cdd:cd14596   157 ICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVLQ 207
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1015-1220 1.20e-51

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: 181.12  E-value: 1.20e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1015 YINANY--MPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPS----KQAQDYGDITVA 1088
Cdd:cd14540     1 YINASHitATVGGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTlggeHDALTFGEYKVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1089 MTSEVVLPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINF----RYLVRDYMKQIP---PESPILVHCS 1161
Cdd:cd14540    81 TKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFleeiNSVRRHTNQDVAghnRNPPTLVHCS 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568915937 1162 AGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLDII 1220
Cdd:cd14540   161 AGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQYL 219
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 1015-1216 2.41e-51

PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type tyrosine-protein phosphatase-like N (PTPRN) and N2 (PTPRN2) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). They consist of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. They are mainly expressed in neuropeptidergic neurons and peptide-secreting endocrine cells, including insulin-producing pancreatic beta-cells, and are involved in involved in the generation, cargo storage, traffic, exocytosis and recycling of insulin secretory granules, as well as in beta-cell proliferation. They also are major autoantigens in type 1 diabetes and are involved in the regulation of insulin secretion.


Pssm-ID: 350394 [Multi-domain]  Cd Length: 208  Bit Score: 179.95  E-value: 2.41e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1015 YINANY-------MPGYhskkdfIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQDYGDITV 1087
Cdd:cd14546     1 YINASTiydhdprNPAY------IATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEVYHIYEV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1088 AMTSEVVLPE-WTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLV-RDYMKQIppeSPILVHCSAGVG 1165
Cdd:cd14546    75 HLVSEHIWCDdYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVnKSYRGRS---CPIVVHCSDGAG 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568915937 1166 RTGTFIAIDRLIYQI-ENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCV 1216
Cdd:cd14546   152 RTGTYILIDMVLNRMaKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAV 203
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 1015-1212 6.21e-51

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: 178.37  E-value: 6.21e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1015 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKcVEQGRTKCEEYWPSKQAQDYGDITVAMTSEVV 1094
Cdd:cd14556     1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQ-LDPKDQSCPQYWPDEGSGTYGPIQVEFVSTTI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1095 LPEWTIRDFVVKNMQN-SESHPL-RQFHFTSWPDHG-VPDTTDLLINFRYLVRDYMKQIPpESPILVHCSAGVGRTGTFI 1171
Cdd:cd14556    80 DEDVISRIFRLQNTTRpQEGYRMvQQFQFLGWPRDRdTPPSKRALLKLLSEVEKWQEQSG-EGPIVVHCLNGVGRSGVFC 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 568915937 1172 AIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFL 1212
Cdd:cd14556   159 AISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFC 199
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 1015-1211 9.53e-50

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: 175.26  E-value: 9.53e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1015 YINANYMPGY-HSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSK--QAQDYGDITVAMTS 1091
Cdd:cd14539     1 YINASLIEDLtPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTErgQALVYGAITVSLQS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1092 EVVLPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQIPPE-SPILVHCSAGVGRTGTF 1170
Cdd:cd14539    81 VRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYLQQRSLqTPIVVHCSSGVGRTGAF 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 568915937 1171 IAIDRLIYQIENEN-TVDVYGIVYDLRMHRPLMVQTEDQYVF 1211
Cdd:cd14539   161 CLLYAAVQEIEAGNgIPDLPQLVRKMRQQRKYMLQEKEHLKF 202
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 980-1221 7.74e-47

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: 169.79  E-value: 7.74e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  980 TAEIAENRGKNRYNNVLPYDISRVKLSVQTHSTDDYINANYMPGYHSKKD--FIATQGPLPNTLKDFWRMVWEKNVYAIV 1057
Cdd:cd14599    32 TATLPENAERNRIREVVPYEENRVELVPTKENNTGYINASHIKVTVGGEEwhYIATQGPLPHTCHDFWQMVWEQGVNVIA 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1058 MLTKCVEQGRTKCEEYWP---SKQ-AQDYGDITVAMTSEVVLPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTT 1133
Cdd:cd14599   112 MVTAEEEGGRSKSHRYWPklgSKHsSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEEV 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1134 DLLINFRYLVRDYMKQIPPES--------PILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQT 1205
Cdd:cd14599   192 QGFLSYLEEIQSVRRHTNSMLdstkncnpPIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVPVMLRHLREQRMFMIQT 271

                         250
                  ....*....|....*.
gi 568915937 1206 EDQYVFLNQCVLDIIR 1221
Cdd:cd14599   272 IAQYKFVYQVLIQFLK 287
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 1015-1211 2.11e-46

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: 165.72  E-value: 2.11e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1015 YINANYM--PGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRT-KCEEYWPSK--QAQDYGDITVAM 1089
Cdd:cd17658     1 YINASLVetPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTaKCADYFPAEenESREFGRISVTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1090 ----TSEVVLpewTIRDFVVKNMQnSESHPLRQFH--FTSWPDHGVPDTTdllinfrYLVRDYMK---QIPP-ESPILVH 1159
Cdd:cd17658    81 kklkHSQHSI---TLRVLEVQYIE-SEEPPLSVLHiqYPEWPDHGVPKDT-------RSVRELLKrlyGIPPsAGPIVVH 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568915937 1160 CSAGVGRTGTFIAIDRLIYQI--ENENTVDVYGIVYDLRMHRPLMVQTEDQYVF 1211
Cdd:cd17658   150 CSAGIGRTGAYCTIHNTIRRIleGDMSAVDLSKTVRKFRSQRIGMVQTQDQYIF 203
PHA02738 PHA02738
hypothetical protein; Provisional
 979-1211 4.78e-46

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 168.56  E-value: 4.78e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  979 YTAEIAeNRGKNRYNNVLPYDISRVKLSVQtHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVM 1058
Cdd:PHA02738   43 FNAEKK-NRKLNRYLDAVCFDHSRVILPAE-RNRGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVM 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1059 LTKCVEQGRTKCEEYWPSKQAQD--YGDITVAMTSEVVLPEWTIRDFVVKNmQNSESHPLRQFHFTSWPDHGVPDTTDLL 1136
Cdd:PHA02738  121 LCKKKENGREKCFPYWSDVEQGSirFGKFKITTTQVETHPHYVKSTLLLTD-GTSATQTVTHFNFTAWPDHDVPKNTSEF 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1137 INFRYLVRDYMKQIPPES-----------PILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQT 1205
Cdd:PHA02738  200 LNFVLEVRQCQKELAQESlqighnrlqppPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFI 279


                  ....*.
gi 568915937 1206 EDQYVF 1211
Cdd:PHA02738  280 PFQYFF 285
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
976-1212 1.21e-44

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 163.34  E-value: 1.21e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  976 LPKYTAEIaENRGKNRYNNVLPYDISRVKlsvqthSTDDYINANYMPGyHSKKDFIATQGPLPNTLKDFWRMVWEKNVYA 1055
Cdd:COG5599    33 DPQYLQNI-NGSPLNRFRDIQPYKETALR------ANLGYLNANYIQV-IGNHRYIATQYPLEEQLEDFFQMLFDNNTPV 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1056 IVMLTKCVE--QGRTKCEEYWPskQAQDYG--DITVAMTSEVVL-PEWTIRDFVVKNMQNS-ESHPLRQFHFTSWPDHGV 1129
Cdd:COG5599   105 LVVLASDDEisKPKVKMPVYFR--QDGEYGkyEVSSELTESIQLrDGIEARTYVLTIKGTGqKKIEIPVLHVKNWPDHGA 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1130 PDTTdLLINFRYLVRDYMK-QIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENEN--TVDVYGIVYDLRMHR-PLMVQT 1205
Cdd:COG5599   183 ISAE-ALKNLADLIDKKEKiKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVqiTLSVEEIVIDMRTSRnGGMVQT 261


                  ....*..
gi 568915937 1206 EDQYVFL 1212
Cdd:COG5599   262 SEQLDVL 268
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 985-1212 2.97e-44

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 163.25  E-value: 2.97e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  985 ENRGKNRYNNVLPYDISRVKLSVQTHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVML--TKC 1062
Cdd:PHA02747   50 ENQPKNRYWDIPCWDHNRVILDSGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLtpTKG 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1063 VeQGRTKCEEYW-PSKQAQ-DYGDITVAMTSEVVLPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFR 1140
Cdd:PHA02747  130 T-NGEEKCYQYWcLNEDGNiDMEDFRIETLKTSVRAKYILTLIEITDKILKDSRKISHFQCSEWFEDETPSDHPDFIKFI 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1141 YLV----RDYMKQIPPE----SPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFL 1212
Cdd:PHA02747  209 KIIdinrKKSGKLFNPKdallCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDYLFI 288
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 1015-1212 1.23e-42

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: 154.40  E-value: 1.23e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1015 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCveQGRTKCEEYWPSK-QAQDYGDITVAMTSEV 1093
Cdd:cd14550     1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDN--ELNEDEPIYWPTKeKPLECETFKVTLSGED 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1094 VLPEW-----TIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLliNFRYLVRDYMKQipPESPILVHCSAGVGRTG 1168
Cdd:cd14550    79 HSCLSneirlIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPIHTVF--ELINTVQEWAQQ--RDGPIVVHDRYGGVQAA 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 568915937 1169 TFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFL 1212
Cdd:cd14550   155 TFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFL 198
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 985-1217 3.46e-42

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 157.09  E-value: 3.46e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  985 ENRGKNRYNNVLPYDISRVKLSVQThSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVE 1064
Cdd:PHA02742   51 KNMKKCRYPDAPCFDRNRVILKIED-GGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIME 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1065 QGRTKCEEYWPSKQAQD--YGDITVAMTSEVVLPEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDTTDLLINFRYL 1142
Cdd:PHA02742  130 DGKEACYPYWMPHERGKatHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLDIKHFAYEDWPHGGLPRDPNKFLDFVLA 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1143 VRDYM---------KQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLN 1213
Cdd:PHA02742  210 VREADlkadvdikgENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIFCY 289


                  ....
gi 568915937 1214 QCVL 1217
Cdd:PHA02742  290 FIVL 293
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1115-1218 2.09e-41

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 147.51  E-value: 2.09e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937   1115 PLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENE-NTVDVYGIVY 1193
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 568915937   1194 DLRMHRPLMVQTEDQYVFLNQCVLD 1218
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1115-1218 2.09e-41

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: 147.51  E-value: 2.09e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937   1115 PLRQFHFTSWPDHGVPDTTDLLINFRYLVRDYMKQIPPESPILVHCSAGVGRTGTFIAIDRLIYQIENE-NTVDVYGIVY 1193
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 568915937   1194 DLRMHRPLMVQTEDQYVFLNQCVLD 1218
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTP_tm pfam18861
TM proximal of protein tyrosine phosphatase, receptor type J; Protein tyrosine phosphatases ...
 756-886 2.06e-38

TM proximal of protein tyrosine phosphatase, receptor type J; Protein tyrosine phosphatases (PTPs) are known to be signaling molecules that regulate a variety of cellular processes, including cell growth, differentiation, mitotic cycle, and oncogenic transformation. PTP receptor type J possesses an extracellular region containing five fibronectin type III repeats, the transmembrane region included in this Pfam entry, and a intracytoplasmic catalytic domain. This entry probably contains part of a Fn3 domain at the N-terminus.


Pssm-ID: 465889  Cd Length: 126  Bit Score: 139.66  E-value: 2.06e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937   756 VKFSGFEASHGPIKAYAVILTTGE-AAQPSADVLKYTYEDFKRGASDTYVTYLIriEEKGQSQGlSEVLNYEIDVGNQST 834
Cdd:pfam18861    1 IQFSLFNSSNGPIKAYGVIVTTNDsLNRPLKEYLNKTYYDWKYKKTDSYLATVT--PNPFTSPR-SSSRSLTVPVGTGSK 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568915937   835 TLGYYNGRLEPLGSYRACVAGFTNITYnlqNDGLINGDESYVSFSPYSEAVF 886
Cdd:pfam18861   78 WQGYCNGPLKPLGSYRFSVAAFTRLEF---DDGLIDGEESYVSFTPFSEPIA 126
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 1015-1221 1.55e-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: 137.80  E-value: 1.55e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1015 YINANYMPGYHSKK--DFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCEEYWPSKQAQD----YG--DIT 1086
Cdd:cd14598     1 YINASHIKVTVGGKewDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLGSRHntvtYGrfKIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1087 VAMTSEVVLpeWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVPDttDLLINFRYL-----VRDYMKQI----PPESPIL 1157
Cdd:cd14598    81 TRFRTDSGC--YATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPE--DLKGFLSYLeeiqsVRRHTNSTidpkSPNPPVL 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568915937 1158 VHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLDIIR 1221
Cdd:cd14598   157 VHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFLK 220
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 985-1211 5.41e-36

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 139.78  E-value: 5.41e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  985 ENRGKNRYNNVLPYDISRVKLSVQTHST--------------------DDYINANYMPGYHSKKDFIATQGPLPNTLKDF 1044
Cdd:PHA02746   50 ENLKKNRFHDIPCWDHSRVVINAHESLKmfdvgdsdgkkievtsednaENYIHANFVDGFKEANKFICAQGPKEDTSEDF 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1045 WRMVWEKNVYAIVMLTKcVEQGRTKCEEYWPSKQAQD--YGDITVAMTSEVVLPEWTIRDFVVKNMQNSESHPLRQFHFT 1122
Cdd:PHA02746  130 FKLISEHESQVIVSLTD-IDDDDEKCFELWTKEEDSElaFGRFVAKILDIIEELSFTKTRLMITDKISDTSREIHHFWFP 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1123 SWPDHGVPDTTDLLINFRYLVRDYMKQIPPES--------PILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYD 1194
Cdd:PHA02746  209 DWPDNGIPTGMAEFLELINKVNEEQAELIKQAdndpqtlgPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIVLK 288

                         250
                  ....*....|....*..
gi 568915937 1195 LRMHRPLMVQTEDQYVF 1211
Cdd:PHA02746  289 IRKQRHSSVFLPEQYAF 305
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 1015-1217 1.80e-34

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: 131.27  E-value: 1.80e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1015 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTKCeEYWPSK-QAQDYGDITVAMTSE- 1092
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEF-VYWPNKdEPINCETFKVTLIAEe 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1093 -VVLP---EWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVP-DTTDLLINfryLVRDymKQIPPESPILVHCSAGVGRT 1167
Cdd:cd17669    80 hKCLSneeKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPiSKTFELIS---IIKE--EAANRDGPMIVHDEHGGVTA 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 568915937 1168 GTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVL 1217
Cdd:cd17669   155 GTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 1015-1217 2.24e-33

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: 128.26  E-value: 2.24e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1015 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKcvEQGRTKCEE-YWPSK-QAQDYGDITVAMTSE 1092
Cdd:cd17670     1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPD--NQGLAEDEFvYWPSReESMNCEAFTVTLISK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1093 VVL-----PEWTIRDFVVKNMQNSESHPLRQFHFTSWPDHGVP-DTTDLLINF---RYLVRDymkqippeSPILVHCSAG 1163
Cdd:cd17670    79 DRLclsneEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPiSSTFELINVikeEALTRD--------GPTIVHDEFG 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568915937 1164 VGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVL 1217
Cdd:cd17670   151 AVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 1015-1218 1.03e-32

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: 126.29  E-value: 1.03e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1015 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTkcvEQGRTK-CEEYWPSKQAQDYGDITVAMTSEV 1093
Cdd:cd14634     1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLN---EMDAAQlCMQYWPEKTSCCYGPIQVEFVSAD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1094 VLPEWTIRDFVVKNMQNSES--HPLRQFHFTSWPDH--GVPDTTDLLINFRYLVRDYMKQIPPESPILVHCSAGVGRTGT 1169
Cdd:cd14634    78 IDEDIISRIFRICNMARPQDgyRIVQHLQYIGWPAYrdTPPSKRSILKVVRRLEKWQEQYDGREGRTVVHCLNGGGRSGT 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 568915937 1170 FIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 1218
Cdd:cd14634   158 FCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 1015-1218 4.08e-32

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: 124.64  E-value: 4.08e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1015 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRT-KCEEYWPSKQAQDYGDITVAMTSEV 1093
Cdd:cd14637     1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEPGLQQYGPMEVEFVSGS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1094 VLPEWTIRDFVVKNM-QNSESHPL-RQFHFTSW-PDHGVPDTTDLLINFRYLVRDYMKQiPPESPILVHCSAGVGRTGTF 1170
Cdd:cd14637    81 ADEDIVTRLFRVQNItRLQEGHLMvRHFQFLRWsAYRDTPDSKKAFLHLLASVEKWQRE-SGEGRTVVHCLNGGGRSGTY 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 568915937 1171 IAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 1218
Cdd:cd14637   160 CASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 1015-1211 3.62e-30

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: 118.97  E-value: 3.62e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1015 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKC-VEQGrtkCEEYWPSKQAQDYGDITVAMTSEV 1093
Cdd:cd14636     1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVdLAQG---CPQYWPEEGMLRYGPIQVECMSCS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1094 VLPEWTIRDFVVKNMQNSESHPL--RQFHFTSWPDH-GVPDTTDLLINFRYLVRDYMKQIPP-ESPILVHCSAGVGRTGT 1169
Cdd:cd14636    78 MDCDVISRIFRICNLTRPQEGYLmvQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQEECDEgEGRTIIHCLNGGGRSGM 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 568915937 1170 FIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVF 1211
Cdd:cd14636   158 FCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRF 199
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 1015-1218 7.20e-29

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: 115.17  E-value: 7.20e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1015 YINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKcVEQGRTkCEEYWPSKQAQDYGDITVAMTSEVV 1094
Cdd:cd14635     1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLND-VDPAQL-CPQYWPENGVHRHGPIQVEFVSADL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1095 LPEWTIRDFVVKNMQNSES--HPLRQFHFTSWPDHgvPDTTDLLINFRYLVRDYMKQIPP----ESPILVHCSAGVGRTG 1168
Cdd:cd14635    79 EEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMY--RDTPVSKRSFLKLIRQVDKWQEEynggEGRTVVHCLNGGGRSG 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 568915937 1169 TFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCVLD 1218
Cdd:cd14635   157 TFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 990-1212 6.31e-18

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: 84.37  E-value: 6.31e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  990 NRYNNVLpydiSRVKLSVQTHstddyINANYMPgYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLTKCVEQGRTK 1069
Cdd:cd14559     1 NRFTNIQ----TRVSTPVGKN-----LNANRVQ-IGNKNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKG 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1070 CEEYWpsKQAQDYGDITVamTSEVVLPEWTIRDFVVK--NMQNSES---HPLRQFHFTSWPDHGVPDTTDLL-------- 1136
Cdd:cd14559    71 LPPYF--RQSGTYGSVTV--KSKKTGKDELVDGLKADmyNLKITDGnktITIPVVHVTNWPDHTAISSEGLKeladlvnk 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1137 -----INFRYL-----VRDYMKQIPpespiLVHCSAGVGRTGTFIAIdrlIYQIENENTVDVYGIVYDLRMHR-PLMVQT 1205
Cdd:cd14559   147 saeekRNFYKSkgssaINDKNKLLP-----VIHCRAGVGRTGQLAAA---MELNKSPNNLSVEDIVSDMRTSRnGKMVQK 218


                  ....*..
gi 568915937 1206 EDQYVFL 1212
Cdd:cd14559   219 DEQLDTL 225
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 984-1214 1.36e-14

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 76.16  E-value: 1.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  984 AENRGKNRyNNVLP---YDISRVKLsvqtHSTDDYINANYMPGYHSKKDFIATQGPLPNTLKDFWRMVWEKNVYAIVMLT 1060
Cdd:PHA02740   49 AENKAKDE-NLALHitrLLHRRIKL----FNDEKVLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLIS 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1061 KCVEQgrtKC-EEYWPSKQ--AQDYGDITVAMTSEVVLPEWTIRDFVVKNmQNSESHPLRQFHFTSWPDHGVPDTTDLLI 1137
Cdd:PHA02740  124 RHADK---KCfNQFWSLKEgcVITSDKFQIETLEIIIKPHFNLTLLSLTD-KFGQAQKISHFQYTAWPADGFSHDPDAFI 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1138 NFRYLVRDYMKQIPPES------PILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYDLRMHRPLMVQTEDQYVF 1211
Cdd:PHA02740  200 DFFCNIDDLCADLEKHKadgkiaPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVF 279


                  ...
gi 568915937 1212 LNQ 1214
Cdd:PHA02740  280 CYH 282
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
106-606 3.30e-10

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 64.25  E-value: 3.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  106 TSCNITGLSPGTSYTFSIISVTTNETLNKTITTEPWPVSDLHVTSVGVTQARLTWSNANGTASYRMLIEELTTHSSVNIS 185
Cdd:COG3401    48 TKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATT 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  186 GLKPGTNNSFAFPESNETQADFAVAEEVPADANGTKRIPVTNLSQLHKNSLVSVDPPSGQDPSLTEILLTDLKPDTQYNA 265
Cdd:COG3401   128 ATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYY 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  266 TIYSQAANGtEGQPRNKVFKTNSTQV----SDVRAMNISASSMTLTWKSNYDGSRTS-IVYKIHVAGGTHSVNQTVNKTE 340
Cdd:COG3401   208 RVAATDTGG-ESAPSNEVSVTTPTTPpsapTGLTATADTPGSVTLSWDPVTESDATGyRVYRSNSGDGPFTKVATVTTTS 286

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  341 AIILGLSSSTLYN--ITVHPFLGQTEGTPGFLQVYTS---PDQVSDFRVTNVSTRAIGLAWRSNDS---KSFEIFIKQDG 412
Cdd:COG3401   287 YTDTGLTNGTTYYyrVTAVDAAGNESAPSNVVSVTTDltpPAAPSGLTATAVGSSSITLSWTASSDadvTGYNVYRSTSG 366

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  413 GEKHR--NASTGNQSYMVEDLKPGTSYHFEIIPRGPDGTEGLSS----------TVNGSTDPSAVTDIRVVNISTTEMQL 480
Cdd:COG3401   367 GGTYTkiAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSeevsattasaASGESLTASVDAVPLTDVAGATAAAS 446

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  481 EWQNTDDASGYTYHLVLESKSGSIirTNSSQKWITVGSLTPGTLYNVTIFPEVDQIQGISNSITQYTrPSSVSHIEVNTT 560
Cdd:COG3401   447 AASNPGVSAAVLADGGDTGNAVPF--TTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSV-IGASAAAAVGGA 523

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 568915937  561 TTTAAIRWKNEDAASASYAYSVLILKTGDGSNVTSNFTKDPSILIP 606
Cdd:COG3401   524 PDGTPNVTGASPVTVGASTGDVLITDLVSLTTSASSSVSGAGLGSG 569
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1112-1214 1.92e-09

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 57.29  E-value: 1.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1112 ESHPLRQFHFTsWPDHGVPDTTDllinFRYLVRDYMKQIPPESPILVHCSAGVGRTGTFIAIDrLIYQ-IENENTVDVyg 1190
Cdd:COG2453    44 EEAGLEYLHLP-IPDFGAPDDEQ----LQEAVDFIDEALREGKKVLVHCRGGIGRTGTVAAAY-LVLLgLSAEEALAR-- 115

                          90       100
                  ....*....|....*....|....
gi 568915937 1191 ivydLRMHRPLMVQTEDQYVFLNQ 1214
Cdd:COG2453   116 ----VRAARPGAVETPAQRAFLER 135
fn3 pfam00041
Fibronectin type III domain;
69-129 7.42e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 50.88  E-value: 7.42e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568915937    69 VSPTSVLLTWKHNDSGAS-------ECRIENKMESNLTFPV-KNQTSCNITGLSPGTSYTFSIISVTTN 129
Cdd:pfam00041   11 VTSTSLTVSWTPPPDGNGpitgyevEYRPKNSGEPWNEITVpGTTTSVTLTGLKPGTEYEVRVQAVNGG 79
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1152-1212 6.53e-07

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: 49.27  E-value: 6.53e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568915937 1152 PESPILVHCSAGVGRTGTFIAIDRLIYQieNENTVDVYGIVYDLRMHRplMVQTEDQYVFL 1212
Cdd:cd14494    55 PGEPVLVHCKAGVGRTGTLVACYLVLLG--GMSAEEAVRIVRLIRPGG--IPQTIEQLDFL 111
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 462-529 1.00e-06

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 47.61  E-value: 1.00e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568915937    462 PSAVTDIRVVNISTTEMQLEWQ--NTDDASGYTYHLVLESKSGS----IIRTNSSQKWITVGSLTPGTLYNVTI 529
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEppPDDGITGYIVGYRVEYREEGsewkEVNVTPSSTSYTLTGLKPGTEYEFRV 74
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 59-127 1.42e-06

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 47.49  E-value: 1.42e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568915937   59 PNPIFDIEA-VVSPTSVLLTWKHNDSGAS-------ECRIENKME-SNLTFPVKNQTSCNITGLSPGTSYTFSIISVT 127
Cdd:cd00063     1 PSPPTNLRVtDVTSTSVTLSWTPPEDDGGpitgyvvEYREKGSGDwKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 462-547 1.98e-06

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 47.11  E-value: 1.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  462 PSAVTDIRVVNISTTEMQLEWQNTDDA----SGYT--YHLVLESKSGSIIRTNSSQKWITVGSLTPGTLYNVTIFPEVDQ 535
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDggpiTGYVveYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                          90
                  ....*....|...
gi 568915937  536 IQG-ISNSITQYT 547
Cdd:cd00063    81 GESpPSESVTVTT 93
fn3 pfam00041
Fibronectin type III domain;
290-367 2.25e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 47.02  E-value: 2.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937   290 QVSDVRAMNISASSMTLTWKSNYDGSRTSIVYKIHVA---GGTHSVNQTV--NKTEAIILGLSSSTLYNITVHPFLGQTE 364
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRpknSGEPWNEITVpgTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81


                   ...
gi 568915937   365 GTP 367
Cdd:pfam00041   82 GPP 84
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 376-460 2.36e-06

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 47.11  E-value: 2.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  376 PDQVSDFRVTNVSTRAIGLAWRSNDS-----KSFEIFIKQDGGEKHRNASTGN---QSYMVEDLKPGTSYHFEIIPRGPD 447
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDdggpiTGYVVEYREKGSGDWKEVEVTPgseTSYTLTGLKPGTEYEFRVRAVNGG 80

                          90
                  ....*....|...
gi 568915937  448 GTEGLSSTVNGST 460
Cdd:cd00063    81 GESPPSESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 59-127 4.53e-06

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 46.07  E-value: 4.53e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568915937     59 PNPIFDIEAV-VSPTSVLLTWKHNDSGAS-----ECRIENKMESNLTFPVK---NQTSCNITGLSPGTSYTFSIISVT 127
Cdd:smart00060    1 PSPPSNLRVTdVTSTSVTLSWEPPPDDGItgyivGYRVEYREEGSEWKEVNvtpSSTSYTLTGLKPGTEYEFRVRAVN 78
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 291-365 8.98e-06

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 44.91  E-value: 8.98e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937    291 VSDVRAMNISASSMTLTWKSNYDGSRTSIVYKIHVAGGT-----HSVNQTVNKTEAIILGLSSSTLYNITVHPFLGQTEG 365
Cdd:smart00060    4 PSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREegsewKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGEG 83
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
 1125-1171 1.02e-05

protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase/transmembrane phosphatase with tensin homology; Voltage-sensitive phosphatase (VSP) proteins comprise a family of phosphoinositide phosphatases with substrates that include phosphatidylinositol-4,5-diphosphate and phosphatidylinositol-3,4,5-trisphosphate. This family is conserved in deuterostomes; VSP was first identified as a sperm flagellar plasma membrane protein in Ciona intestinalis. Gene duplication events in primates resulted in the presence of paralogs, transmembrane phosphatase with tensin homology (TPTE) and TPTE2, that retain protein domain architecture but, in the case of TPTE, have lost catalytic activity. TPTE, also called cancer/testis antigen 44 (CT44), may play a role in the signal transduction pathways of the endocrine or spermatogenic function of the testis. TPTE2, also called TPTE and PTEN homologous inositol lipid phosphatase (TPIP), occurs in several differentially spliced forms; TPIP alpha displays phosphoinositide 3-phosphatase activity and is localized on the endoplasmic reticulum, while TPIP beta is cytosolic and lacks detectable phosphatase activity. VSP/TPTE proteins contain an N-terminal voltage sensor consisting of four transmembrane segments, a protein tyrosine phosphatase (PTP)-like phosphoinositide phosphatase catalytic domain, followed by a regulatory C2 domain.


Pssm-ID: 350360 [Multi-domain]  Cd Length: 177  Bit Score: 47.36  E-value: 1.02e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 568915937 1125 PDHGVPdTTDLLINFRYLVRDYMKQiPPESPILVHCSAGVGRTGTFI 1171
Cdd:cd14510    82 DDHNVP-TLDEMLSFTAEVREWMAA-DPKNVVAIHCKGGKGRTGTMV 126
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 376-448 1.85e-05

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 44.14  E-value: 1.85e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937    376 PDQVSDFRVTNVSTRAIGLAWRSNDSKSFEIFI--------KQDGGEKHRNASTGNQSYMVEDLKPGTSYHFEIIPRGPD 447
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIvgyrveyrEEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80


                    .
gi 568915937    448 G 448
Cdd:smart00060   81 G 81
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 291-367 1.91e-05

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 44.41  E-value: 1.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  291 VSDVRAMNISASSMTLTWKSNYDGSRTSIVYKIHV----AGGTHSVN-QTVNKTEAIILGLSSSTLYNITVHPFLGQTEG 365
Cdd:cd00063     4 PTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYrekgSGDWKEVEvTPGSETSYTLTGLKPGTEYEFRVRAVNGGGES 83


                  ..
gi 568915937  366 TP 367
Cdd:cd00063    84 PP 85
fn3 pfam00041
Fibronectin type III domain;
377-442 2.52e-05

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 43.94  E-value: 2.52e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568915937   377 DQVSDFRVTNVSTRAIGLAWRSNDSKS-----FEIFIKQDGGE---KHRNASTGNQSYMVEDLKPGTSYHFEII 442
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNgpitgYEVEYRPKNSGepwNEITVPGTTTSVTLTGLKPGTEYEVRVQ 74
PTPlike_phytase pfam14566
Inositol hexakisphosphate; Inositol hexakisphosphate, often called phytate, is found in ...
 1125-1177 1.53e-04

Inositol hexakisphosphate; Inositol hexakisphosphate, often called phytate, is found in abundance in seeds and acting as an inorganic phosphate reservoir. Phytases are phosphatases that hydrolyze phytate to less-phosphorylated myo-inositol derivatives and inorganic phosphate. The active-site sequence (HCXXGXGR) of the phytase identified from the gut micro-organizm Selenomonas ruminantium forms a loop (P loop) at the base of a substrate binding pocket that is characteriztic of protein tyrosine phosphatases (PTPs). The depth of this pocket is an important determinant of the substrate specificity of PTPs. In humans this enzyme is thought to aid bone mineralization and salvage the inositol moiety prior to apoptosis.


Pssm-ID: 464208 [Multi-domain]  Cd Length: 157  Bit Score: 43.45  E-value: 1.53e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568915937  1125 PDHGVPDTTDllinFRYLVrDYMKQIPPESPILVHCSAGVGRTGTFIAIDRLI 1177
Cdd:pfam14566  109 TDEKAPLEED----FDALI-SIVKDAPEDTALVFNCQMGRGRTTTAMVIADLV 156
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 1124-1172 1.55e-04

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: 43.34  E-value: 1.55e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 568915937 1124 WPDHGVPdTTDLLINFRYLVRDYMKQiPPESPILVHCSAGVGRTGTFIA 1172
Cdd:cd14497    68 FPDHHPP-PLGLLLEIVDDIDSWLSE-DPNNVAVVHCKAGKGRTGTVIC 114
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 1112-1214 1.82e-04

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: 43.41  E-value: 1.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1112 ESHPLRQFHFtSWPDHGVPDTTDlliNFRYLVRDYMKQIPPESPILVHCSAGVGRTGTFIAidRLIYQIENENTVDVygI 1191
Cdd:cd14505    69 QQAGITWHHL-PIPDGGVPSDIA---QWQELLEELLSALENGKKVLIHCKGGLGRTGLIAA--CLLLELGDTLDPEQ--A 140

                          90       100
                  ....*....|....*....|...
gi 568915937 1192 VYDLRMHRPLMVQTEDQYVFLNQ 1214
Cdd:cd14505   141 IAAVRALRPGAIQTPKQENFLHQ 163
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
51-367 2.10e-04

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 45.38  E-value: 2.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937   51 RVLCAGAAPNPIFDIEAVV-SPTSVLLTW-KHNDSGASECRIENKMESNLTF---PVKNQTSCNITGLSPGTSYTFSIIS 125
Cdd:COG3401   225 SVTTPTTPPSAPTGLTATAdTPGSVTLSWdPVTESDATGYRVYRSNSGDGPFtkvATVTTTSYTDTGLTNGTTYYYRVTA 304

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  126 VTTNETLN--------KTITTEPWPVSDLHVTSVGVTQARLTWSNA--NGTASYRM-----------LIEELTTHSSVNI 184
Cdd:COG3401   305 VDAAGNESapsnvvsvTTDLTPPAAPSGLTATAVGSSSITLSWTASsdADVTGYNVyrstsgggtytKIAETVTTTSYTD 384

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  185 SGLKPGTNNSFAF-------PESNETQADFAVAEEVPADANGTKRIPVTNLSQLHKNSLVSVDPPSGQDPSLTEILLTDL 257
Cdd:COG3401   385 TGLTPGTTYYYKVtavdaagNESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDT 464

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  258 KPDTQYNATIYSQAANGTEGQPRNKVFKTNSTQVSDVRAMNISASSMTLTWKSNYDGSRTSivyKIHVAGGTHSVNQTVN 337
Cdd:COG3401   465 GNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPD---GTPNVTGASPVTVGAS 541

                         330       340       350
                  ....*....|....*....|....*....|
gi 568915937  338 KTEAIILGLSSSTLYNITVHPFLGQTEGTP 367
Cdd:COG3401   542 TGDVLITDLVSLTTSASSSVSGAGLGSGNL 571
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 1119-1212 3.41e-04

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


Pssm-ID: 350356 [Multi-domain]  Cd Length: 206  Bit Score: 43.49  E-value: 3.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1119 FHFTSWPDHGVPDTTDLLINFRylVRDYMKQipPESPILVHCSAGVGRTGTFIAIdRLIYqIENENTVDVYGIVydlRMH 1198
Cdd:cd14506    79 FYNFGWKDYGVPSLTTILDIVK--VMAFALQ--EGGKVAVHCHAGLGRTGVLIAC-YLVY-ALRMSADQAIRLV---RSK 149

                          90
                  ....*....|....
gi 568915937 1199 RPLMVQTEDQYVFL 1212
Cdd:cd14506   150 RPNSIQTRGQVLCV 163
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 1155-1194 8.33e-04

bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa TpbA; This subfamily contains bacterial protein tyrosine phosphatases (PTPs) and dual-specificity phosphatases (DUSPs) related to Pseudomonas aeruginosa TpbA, a DUSP that negatively regulates biofilm formation by converting extracellular quorum sensing signals and to Mycobacterium tuberculosis PtpB, a PTP virulence factor that attenuates host immune defenses by interfering with signal transduction pathways in macrophages. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides, while DUSPs function as protein-serine/threonine phosphatases (EC 3.1.3.16) and PTPs.


Pssm-ID: 350378 [Multi-domain]  Cd Length: 158  Bit Score: 41.21  E-value: 8.33e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 568915937 1155 PILVHCSAGVGRTGTFIAIDRLIYQIENENTVDVYGIVYD 1194
Cdd:cd14529    91 PVLIHCKHGKDRTGLVSALYRIVYGGSKEEANEDYRLSNR 130
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 1155-1214 1.14e-03

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: 40.72  E-value: 1.14e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1155 PILVHCSAGVGRTGTFIAidrlIYQIENENTVDVYGIVyDLRMHRPLMVQTEDQYVFLNQ 1214
Cdd:cd14504    84 AVLVHCLAGKGRTGTMLA----CYLVKTGKISAVDAIN-EIRRIRPGSIETSEQEKFVIQ 138
fn3 pfam00041
Fibronectin type III domain;
463-530 1.40e-03

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 38.94  E-value: 1.40e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568915937   463 SAVTDIRVVNISTTEMQLEWQNTDDASG-YTYHLVLESKSGSI-----IRTNSSQKWITVGSLTPGTLYNVTIF 530
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGpITGYEVEYRPKNSGepwneITVPGTTTSVTLTGLKPGTEYEVRVQ 74
PTPLP-like cd14495
Protein tyrosine phosphatase-like domains of phytases and similar domains; This subfamily ...
 1120-1198 1.91e-03

Protein tyrosine phosphatase-like domains of phytases and similar domains; This subfamily contains the tandem protein tyrosine phosphatase (PTP)-like domains of protein tyrosine phosphatase-like phytases (PTPLPs) and similar domains including the PTP domain of Pseudomonas syringae tyrosine-protein phosphatase hopPtoD2. PTPLPs, also known as cysteine phytases, are one of four known classes of phytases, enzymes that degrade phytate (inositol hexakisphosphate [InsP(6)]) to less-phosphorylated myo-inositol derivatives. Phytate is the most abundant cellular inositol phosphate and plays important roles in a broad scope of cellular processes, including DNA repair, RNA processing and export, development, apoptosis, and pathogenicity. PTPLPs adopt a PTP fold, including the active-site signature sequence (CX5R(S/T)) and utilize a classical PTP reaction mechanism. However, these enzymes display no catalytic activity against classical PTP substrates due to several unique structural features that confer specificity for myo-inositol polyphosphates.


Pssm-ID: 350345  Cd Length: 278  Bit Score: 41.59  E-value: 1.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937 1120 HFtsWPDhgvPDTTDLLINFrylvrdyMKQIPPESPILVHCSAGVGRTGTFIAI-DRLIyqieNENTVDVYGIVYdlRMH 1198
Cdd:cd14495   165 HV--WPD---DEEIDAFVAF-------YRSLPADAWLHFHCRAGKGRTTTFMVMyDMLK----NPKDVSFDDIIA--RQY 226
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 549-628 2.13e-03

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 38.63  E-value: 2.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937  549 PSSVSHIEV-NTTTTTAAIRWK---NEDAASASYAYSVLILKTGDGSNVTSNFTKDPSILIPELIPGVSYTVKI--LTQV 622
Cdd:cd00063     1 PSPPTNLRVtDVTSTSVTLSWTppeDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVraVNGG 80


                  ....*.
gi 568915937  623 GDGTTS 628
Cdd:cd00063    81 GESPPS 86
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 1155-1196 2.27e-03

Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The enzyme's tertiary fold is highly similar to that of tyrosine-specific phosphatases, except for a "recognition" region.


Pssm-ID: 395632 [Multi-domain]  Cd Length: 127  Bit Score: 39.55  E-value: 2.27e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 568915937  1155 PILVHCSAGVGRTGTFIAidRLIYQIENENTVDVYGIVYDLR 1196
Cdd:pfam00782   71 KVLVHCQAGISRSATLII--AYLMKTRNLSLNEAYSFVKERR 110
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
1155-1196 5.73e-03

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 38.42  E-value: 5.73e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 568915937   1155 PILVHCSAGVGRTGTFIAidRLIYQIENENTVDVYGIVYDLR 1196
Cdd:smart00195   80 KVLVHCQAGVSRSATLII--AYLMKTRNMSLNDAYDFVKDRR 119
PTP-IVa cd14500
protein tyrosine phosphatase type IVA family; Protein tyrosine phosphatases type IVA (PTP-IVa), ...
 1120-1173 9.44e-03

protein tyrosine phosphatase type IVA family; Protein tyrosine phosphatases type IVA (PTP-IVa), also known as protein-tyrosine phosphatases of regenerating liver (PRLs) constitute a family of small, prenylated phosphatases that are the most oncogenic of all PTPs. They stimulate progression from G1 into S phase during mitosis and enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. They associate with magnesium transporters of the cyclin M (CNNM) family, which results in increased intracellular magnesium levels that promote oncogenic transformation. Vertebrates contain three members: PRL-1, PRL-2, and PRL-3.


Pssm-ID: 350350 [Multi-domain]  Cd Length: 156  Bit Score: 38.36  E-value: 9.44e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568915937 1120 HFTSWP-DHGVPDTTDLLINFRYLVRDYMKQ-IPPESPILVHCSAGVGRTGTFIAI 1173
Cdd:cd14500    60 KVHDWPfDDGSPPPDDVVDDWLDLLKTRFKEeGKPGACIAVHCVAGLGRAPVLVAI 115
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 549-625 9.96e-03

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 36.44  E-value: 9.96e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915937    549 PSSVSHIEV-NTTTTTAAIRWKN-EDAASASYA--YSVLILKTGDGSNVTSNFTKDPSILIPELIPGVSYTVKILTQVGD 624
Cdd:smart00060    1 PSPPSNLRVtDVTSTSVTLSWEPpPDDGITGYIvgYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80


                    .
gi 568915937    625 G 625
Cdd:smart00060   81 G 81
 
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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