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Conserved domains on  [gi|1907178461|ref|XP_036008691|]
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tyrosine-protein phosphatase non-receptor type 5 isoform X1 [Mus musculus]

Protein Classification

tyrosine-protein phosphatase non-receptor type 5( domain architecture ID 12998696)

tyrosine-protein phosphatase non-receptor type 5 (PTPN5/STEP) is a tyrosine-specific protein-tyrosine phosphatase (PTP) that may regulate the activity of several effector molecules involved in synaptic plasticity and neuronal cell survival, including MAPKs, Src family kinases and NMDA receptors

EC:  3.1.3.48
Gene Symbol:  PTPN5
Gene Ontology:  GO:0004725|GO:0016791
PubMed:  27514797

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 274-531 0e+00

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: 558.32  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 274 FLLQAEFFEIPMNFVDPKEYDIPGLVRKNRYKTILPNPHSRVRLTSPDPEDPLSSYINANYIRGYSGEEKVYIATQGPIV 353
Cdd:cd14613     1 FLLQAEFFEIPMNFVDPKEYDIPGLVRKNRYKTILPNPHSRVCLTSPDQDDPLSSYINANYIRGYGGEEKVYIATQGPTV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 354 STVADFWRMVWQERTPIIVMITNIEEMNEKCTEYWPEEQVVHDGVEITVQKVIHTEDYRLRLISLRRGTEERSLKHYWFT 433
Cdd:cd14613    81 NTVGDFWRMVWQERSPIIVMITNIEEMNEKCTEYWPEEQVTYEGIEITVKQVIHADDYRLRLITLKSGGEERGLKHYWYT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 434 SWPDQKTPDRAPPLLHLVREVEEAAQQEGPHCSPIIVHCSAGIGRTGCFIATSICCQQLRREGVVDILKTTCQLRQDRGG 513
Cdd:cd14613   161 SWPDQKTPDNAPPLLQLVQEVEEARQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGG 240

                         250
                  ....*....|....*...
gi 1907178461 514 MIQTCEQYQFVHHAMSLY 531
Cdd:cd14613   241 MIQTCEQYQFVHHVLSLY 258
 
Name Accession Description Interval E-value
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 274-531 0e+00

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: 558.32  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 274 FLLQAEFFEIPMNFVDPKEYDIPGLVRKNRYKTILPNPHSRVRLTSPDPEDPLSSYINANYIRGYSGEEKVYIATQGPIV 353
Cdd:cd14613     1 FLLQAEFFEIPMNFVDPKEYDIPGLVRKNRYKTILPNPHSRVCLTSPDQDDPLSSYINANYIRGYGGEEKVYIATQGPTV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 354 STVADFWRMVWQERTPIIVMITNIEEMNEKCTEYWPEEQVVHDGVEITVQKVIHTEDYRLRLISLRRGTEERSLKHYWFT 433
Cdd:cd14613    81 NTVGDFWRMVWQERSPIIVMITNIEEMNEKCTEYWPEEQVTYEGIEITVKQVIHADDYRLRLITLKSGGEERGLKHYWYT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 434 SWPDQKTPDRAPPLLHLVREVEEAAQQEGPHCSPIIVHCSAGIGRTGCFIATSICCQQLRREGVVDILKTTCQLRQDRGG 513
Cdd:cd14613   161 SWPDQKTPDNAPPLLQLVQEVEEARQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGG 240

                         250
                  ....*....|....*...
gi 1907178461 514 MIQTCEQYQFVHHAMSLY 531
Cdd:cd14613   241 MIQTCEQYQFVHHVLSLY 258
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
275-528 3.20e-108

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 323.84  E-value: 3.20e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461  275 LLQAEFFEIPMNFVDPKEYDI---PGLVRKNRYKTILPNPHSRVRLTSPDPEDplSSYINANYIRGYSgEEKVYIATQGP 351
Cdd:smart00194   1 GLEEEFEKLDRLKPDDESCTVaafPENRDKNRYKDVLPYDHTRVKLKPPPGEG--SDYINASYIDGPN-GPKAYIATQGP 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461  352 IVSTVADFWRMVWQERTPIIVMITNIEEMN-EKCTEYWPEEQ---VVHDGVEITVQKVIHTEDYRLRLISLRRGT--EER 425
Cdd:smart00194  78 LPSTVEDFWRMVWEQKVTVIVMLTELVEKGrEKCAQYWPDEEgepLTYGDITVTLKSVEKVDDYTIRTLEVTNTGcsETR 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461  426 SLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQEGPhcsPIIVHCSAGIGRTGCFIATSICCQQLRREGVVDILKTTC 505
Cdd:smart00194 158 TVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTG---PIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVK 234

                          250       260
                   ....*....|....*....|...
gi 1907178461  506 QLRQDRGGMIQTCEQYQFVHHAM 528
Cdd:smart00194 235 ELRSQRPGMVQTEEQYIFLYRAI 257
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
300-528 1.28e-99

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 300.70  E-value: 1.28e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 300 RKNRYKTILPNPHSRVRLTspdPEDPLSSYINANYIRGYSGEeKVYIATQGPIVSTVADFWRMVWQERTPIIVMITNIEE 379
Cdd:pfam00102   3 EKNRYKDVLPYDHTRVKLT---GDPGPSDYINASYIDGYKKP-KKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 380 MN-EKCTEYWP---EEQVVHDGVEITVQK-VIHTEDYRLRLISLRRGT--EERSLKHYWFTSWPDQKTPDRAPPLLHLVR 452
Cdd:pfam00102  79 KGrEKCAQYWPeeeGESLEYGDFTVTLKKeKEDEKDYTVRTLEVSNGGseETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907178461 453 EVEEaaQQEGPHCSPIIVHCSAGIGRTGCFIATSICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHAM 528
Cdd:pfam00102 159 KVRK--SSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAI 232
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 265-525 5.18e-44

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 158.24  E-value: 5.18e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 265 ELHEKALDPFLLQAEFFEIPMNfvdpkeydipglVRKNRYKTILPNPHSRVRLTSPDpeDPLSSYINANYIRGYSgEEKV 344
Cdd:PHA02747   30 EHHQIILKPFDGLIANFEKPEN------------QPKNRYWDIPCWDHNRVILDSGG--GSTSDYIHANWIDGFE-DDKK 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 345 YIATQGPIVSTVADFWRMVWQERTPIIVMITNIEEMN--EKCTEYW-PEE--QVVHDGVEITVQKVIHTEDYRLRLISL- 418
Cdd:PHA02747   95 FIATQGPFAETCADFWKAVWQEHCSIIVMLTPTKGTNgeEKCYQYWcLNEdgNIDMEDFRIETLKTSVRAKYILTLIEIt 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 419 -RRGTEERSLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQEGPH-------CSPIIVHCSAGIGRTGCFIATSICCQ 490
Cdd:PHA02747  175 dKILKDSRKISHFQCSEWFEDETPSDHPDFIKFIKIIDINRKKSGKLfnpkdalLCPIVVHCSDGVGKTGIFCAVDICLN 254

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1907178461 491 QLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVH 525
Cdd:PHA02747  255 QLVKRKAICLAKTAEKIREQRHAGIMNFDDYLFIQ 289
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
286-523 3.24e-40

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 147.16  E-value: 3.24e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 286 NFVDPKEYDIPGLVRKNRYKTILPNPHSRVRltSPDPedplssYINANYIRGysGEEKVYIATQGPIVSTVADFWRMVWQ 365
Cdd:COG5599    30 SHNDPQYLQNINGSPLNRFRDIQPYKETALR--ANLG------YLNANYIQV--IGNHRYIATQYPLEEQLEDFFQMLFD 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 366 ERTPIIVMITNIEEM---NEKCTEYWPE-EQVVHDGVEITVQKVIHTED-YRLRLISLRR---GTEERSLKHYWFTSWPD 437
Cdd:COG5599   100 NNTPVLVVLASDDEIskpKVKMPVYFRQdGEYGKYEVSSELTESIQLRDgIEARTYVLTIkgtGQKKIEIPVLHVKNWPD 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 438 QKTPDrAPPLLHLVREVEEAAQQEGPHCSPIIVHCSAGIGRTGCFIATsICCQQLRREGV---VDILKTTCQLRQDRG-G 513
Cdd:COG5599   180 HGAIS-AEALKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIAC-LALSKSINALVqitLSVEEIVIDMRTSRNgG 257

                         250
                  ....*....|
gi 1907178461 514 MIQTCEQYQF 523
Cdd:COG5599   258 MVQTSEQLDV 267
 
Name Accession Description Interval E-value
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 274-531 0e+00

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: 558.32  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 274 FLLQAEFFEIPMNFVDPKEYDIPGLVRKNRYKTILPNPHSRVRLTSPDPEDPLSSYINANYIRGYSGEEKVYIATQGPIV 353
Cdd:cd14613     1 FLLQAEFFEIPMNFVDPKEYDIPGLVRKNRYKTILPNPHSRVCLTSPDQDDPLSSYINANYIRGYGGEEKVYIATQGPTV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 354 STVADFWRMVWQERTPIIVMITNIEEMNEKCTEYWPEEQVVHDGVEITVQKVIHTEDYRLRLISLRRGTEERSLKHYWFT 433
Cdd:cd14613    81 NTVGDFWRMVWQERSPIIVMITNIEEMNEKCTEYWPEEQVTYEGIEITVKQVIHADDYRLRLITLKSGGEERGLKHYWYT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 434 SWPDQKTPDRAPPLLHLVREVEEAAQQEGPHCSPIIVHCSAGIGRTGCFIATSICCQQLRREGVVDILKTTCQLRQDRGG 513
Cdd:cd14613   161 SWPDQKTPDNAPPLLQLVQEVEEARQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGG 240

                         250
                  ....*....|....*...
gi 1907178461 514 MIQTCEQYQFVHHAMSLY 531
Cdd:cd14613   241 MIQTCEQYQFVHHVLSLY 258
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 302-526 4.72e-155

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: 441.84  E-value: 4.72e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 302 NRYKTILPNPHSRVRLTSpDPEDPLSSYINANYIRGYSGEEKVYIATQGPIVSTVADFWRMVWQERTPIIVMITNIEEMN 381
Cdd:cd14547     1 NRYKTILPNEHSRVCLPS-VDDDPLSSYINANYIRGYDGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 382 EKCTEYWPEEQVV-HDGVEITVQKVIHTEDYRLRLISLRRGTEERSLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQ 460
Cdd:cd14547    80 EKCAQYWPEEENEtYGDFEVTVQSVKETDGYTVRKLTLKYGGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEEARQT 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907178461 461 EgPHCSPIIVHCSAGIGRTGCFIATSICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVHH 526
Cdd:cd14547   160 E-PHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVHR 224
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 284-531 1.56e-128

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: 375.33  E-value: 1.56e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 284 PMNFVDPKEYDIPGLVRKNRYKTILPNPHSRVRLTSPDPEDPLSSYINANYIRGYSGEEKVYIATQGPIVSTVADFWRMV 363
Cdd:cd14612     1 PPNFVSPEELDIPGHASKDRYKTILPNPQSRVCLRRAGSQEEEGSYINANYIRGYDGKEKAYIATQGPMLNTVSDFWEMV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 364 WQERTPIIVMITNIEEMNEKCTEYWPEEQVVHDGVEITVQKVIHTEDYRLRLISLRRGTEERSLKHYWFTSWPDQKTPDR 443
Cdd:cd14612    81 WQEECPIIVMITKLKEKKEKCVHYWPEKEGTYGRFEIRVQDMKECDGYTIRDLTIQLEEESRSVKHYWFSSWPDHQTPES 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 444 APPLLHLVREVEEaAQQEGPHCSPIIVHCSAGIGRTGCFIATSICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQF 523
Cdd:cd14612   161 AGPLLRLVAEVEE-SRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQF 239


                  ....*...
gi 1907178461 524 VHHAMSLY 531
Cdd:cd14612   240 LHHTLALY 247
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 301-526 3.28e-119

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: 350.76  E-value: 3.28e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 301 KNRYKTILPNPHSRVRLTSPDPEDPLSSYINANYIRGYSGEEKVYIATQGPIVSTVADFWRMVWQERTPIIVMITNIEEM 380
Cdd:cd14611     2 KNRYKTILPNPHSRVCLKPKNSNDSLSTYINANYIRGYGGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 381 NEKCTEYWPEEQVVHDGVEITVQKVIHTEDYRLRLISLRRGTEERSLKHYWFTSWPDQKTPDRAPPLLHLVREVEEaAQQ 460
Cdd:cd14611    82 NEKCVLYWPEKRGIYGKVEVLVNSVKECDNYTIRNLTLKQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLDVEE-DRL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907178461 461 EGPHCSPIIVHCSAGIGRTGCFIATSICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVHH 526
Cdd:cd14611   161 ASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVHH 226
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
275-528 3.20e-108

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 323.84  E-value: 3.20e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461  275 LLQAEFFEIPMNFVDPKEYDI---PGLVRKNRYKTILPNPHSRVRLTSPDPEDplSSYINANYIRGYSgEEKVYIATQGP 351
Cdd:smart00194   1 GLEEEFEKLDRLKPDDESCTVaafPENRDKNRYKDVLPYDHTRVKLKPPPGEG--SDYINASYIDGPN-GPKAYIATQGP 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461  352 IVSTVADFWRMVWQERTPIIVMITNIEEMN-EKCTEYWPEEQ---VVHDGVEITVQKVIHTEDYRLRLISLRRGT--EER 425
Cdd:smart00194  78 LPSTVEDFWRMVWEQKVTVIVMLTELVEKGrEKCAQYWPDEEgepLTYGDITVTLKSVEKVDDYTIRTLEVTNTGcsETR 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461  426 SLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQEGPhcsPIIVHCSAGIGRTGCFIATSICCQQLRREGVVDILKTTC 505
Cdd:smart00194 158 TVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTG---PIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVK 234

                          250       260
                   ....*....|....*....|...
gi 1907178461  506 QLRQDRGGMIQTCEQYQFVHHAM 528
Cdd:smart00194 235 ELRSQRPGMVQTEEQYIFLYRAI 257
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
300-528 1.28e-99

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 300.70  E-value: 1.28e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 300 RKNRYKTILPNPHSRVRLTspdPEDPLSSYINANYIRGYSGEeKVYIATQGPIVSTVADFWRMVWQERTPIIVMITNIEE 379
Cdd:pfam00102   3 EKNRYKDVLPYDHTRVKLT---GDPGPSDYINASYIDGYKKP-KKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 380 MN-EKCTEYWP---EEQVVHDGVEITVQK-VIHTEDYRLRLISLRRGT--EERSLKHYWFTSWPDQKTPDRAPPLLHLVR 452
Cdd:pfam00102  79 KGrEKCAQYWPeeeGESLEYGDFTVTLKKeKEDEKDYTVRTLEVSNGGseETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907178461 453 EVEEaaQQEGPHCSPIIVHCSAGIGRTGCFIATSICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHAM 528
Cdd:pfam00102 159 KVRK--SSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAI 232
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 329-526 1.15e-82

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: 255.67  E-value: 1.15e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 329 YINANYIRGYSGEEKvYIATQGPIVSTVADFWRMVWQERTPIIVMITNIEEMN-EKCTEYWPEEQ---VVHDGVEITVQK 404
Cdd:cd00047     1 YINASYIDGYRGPKE-YIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGrEKCERYWPEEGgkpLEYGDITVTLVS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 405 VIHTEDYRLRLISLRRGT--EERSLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQEGphcSPIIVHCSAGIGRTGCF 482
Cdd:cd00047    80 EEELSDYTIRTLELSPKGcsESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPN---GPIVVHCSAGVGRTGTF 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1907178461 483 IATSICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVHH 526
Cdd:cd00047   157 IAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 301-531 8.96e-74

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: 234.66  E-value: 8.96e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 301 KNRYKTILPNPHSRVRLTSPDPEDPLSSYINANYIR------GYSGEEKVYIATQGPIVSTVADFWRMVWQERTPIIVMI 374
Cdd:cd14544     4 KNRYKNILPFDHTRVILKDRDPNVPGSDYINANYIRnenegpTTDENAKTYIATQGCLENTVSDFWSMVWQENSRVIVMT 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 375 TN-IEEMNEKCTEYWPEEQVV--HDGVEITVQKVIHTEDYRLRLISLRR---GTEERSLKHYWFTSWPDQKTPDRAPPLL 448
Cdd:cd14544    84 TKeVERGKNKCVRYWPDEGMQkqYGPYRVQNVSEHDTTDYTLRELQVSKldqGDPIREIWHYQYLSWPDHGVPSDPGGVL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 449 HLVREVEEaAQQEGPHCSPIIVHCSAGIGRTGCFIATSICCQQLRREGV---VDILKTTCQLRQDRGGMIQTCEQYQFVH 525
Cdd:cd14544   164 NFLEDVNQ-RQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLdcdIDIQKTIQMVRSQRSGMVQTEAQYKFIY 242


                  ....*.
gi 1907178461 526 HAMSLY 531
Cdd:cd14544   243 VAVAQY 248
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 303-525 9.77e-74

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: 233.40  E-value: 9.77e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 303 RYKTILPNPHSRVRLtSPDPEDPLSSYINANYIRGYSGEEKvYIATQGPIVSTVADFWRMVWQERTPIIVMITN-IEEMN 381
Cdd:cd14548     1 RYTNILPYDHSRVKL-IPINEEEGSDYINANYIPGYNSPRE-FIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQcMEKGR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 382 EKCTEYWPEEQVVHDGVEITVQKV--IHTEDYRLRLISLRRGTEERSLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQ 459
Cdd:cd14548    79 VKCDHYWPFDQDPVYYGDITVTMLseSVLPDWTIREFKLERGDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDYIK 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907178461 460 QEGphcSPIIVHCSAGIGRTGCFIATSICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVH 525
Cdd:cd14548   159 QEK---GPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLH 221
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 296-525 1.55e-72

catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein phosphatase non-receptor type 9 (PTPN9), also called protein-tyrosine phosphatase MEG2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN9 plays an important role in promoting intracellular secretary vesicle fusion in hematopoietic cells and promotes the dephosphorylation of ErbB2 and EGFR in breast cancer cells, leading to impaired activation of STAT5 and STAT3. It also directly dephosphorylates STAT3 at the Tyr705 residue, resulting in its inactivation. PTPN9 has been found to be dysregulated in various human cancers, including breast, colorectal, and gastric cancer.


Pssm-ID: 350391 [Multi-domain]  Cd Length: 271  Bit Score: 232.25  E-value: 1.55e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 296 PGLVRKNRYKTILPNPHSRVRLTSPDpEDPLSSYINANYIRGYSgEEKVYIATQGPIVSTVADFWRMVWQERTPIIVMIT 375
Cdd:cd14543    27 PANQEKNRYGDVLCLDQSRVKLPKRN-GDERTDYINANFMDGYK-QKNAYIATQGPLPKTYSDFWRMVWEQKVLVIVMTT 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 376 NIEEMNE-KCTEYWPEE---QVVHDGVEITVQKVIHTEDYRLRLISLRRGT--EERSLKHYWFTSWPDQKTPDRAPPLLH 449
Cdd:cd14543   105 RVVERGRvKCGQYWPLEegsSLRYGDLTVTNLSVENKEHYKKTTLEIHNTEtdESRQVTHFQFTSWPDFGVPSSAAALLD 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 450 LVREVEE----AAQQEGP----HCS--PIIVHCSAGIGRTGCFIATSICCQQLRREGVVDILKTTCQLRQDRGGMIQTCE 519
Cdd:cd14543   185 FLGEVRQqqalAVKAMGDrwkgHPPgpPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTVRRMRTQRAFSIQTPD 264


                  ....*.
gi 1907178461 520 QYQFVH 525
Cdd:cd14543   265 QYYFCY 270
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 301-528 2.03e-72

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: 230.75  E-value: 2.03e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 301 KNRYKTILPNPHSRVRLtSPDPEDPLSSYINANYIRGYSgEEKVYIATQGPIVSTVADFWRMVWQERTPIIVMITNIEEM 380
Cdd:cd14553     6 KNRYANVIAYDHSRVIL-QPIEGVPGSDYINANYCDGYR-KQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEER 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 381 NE-KCTEYWPEE-QVVHDGVEITVQKVIHTEDYRLRLISLRRG--TEERSLKHYWFTSWPDQKTPDRAPPLLHLVREVEE 456
Cdd:cd14553    84 SRvKCDQYWPTRgTETYGLIQVTLLDTVELATYTVRTFALHKNgsSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKA 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907178461 457 AAQqegPHCSPIIVHCSAGIGRTGCFIATSICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHAM 528
Cdd:cd14553   164 CNP---PDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDAL 232
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 329-525 5.67e-64

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: 207.59  E-value: 5.67e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 329 YINANYIRGYSgEEKVYIATQGPIVSTVADFWRMVWQERTPIIVMITNIEEM-NEKCTEYWPEEQV-VHDGVEITVQKVI 406
Cdd:cd14549     1 YINANYVDGYN-KARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERgRRKCDQYWPKEGTeTYGNIQVTLLSTE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 407 HTEDYRLRLISLRR--------GTEERSLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAaqqEGPHCSPIIVHCSAGIGR 478
Cdd:cd14549    80 VLATYTVRTFSLKNlklkkvkgRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAA---NPPGAGPIVVHCSAGVGR 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1907178461 479 TGCFIATSICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVH 525
Cdd:cd14549   157 TGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 301-528 1.35e-62

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: 205.26  E-value: 1.35e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 301 KNRYKTILPNPHSRVRLTSPDpEDPLSSYINANYIRGYSgEEKVYIATQGPIVSTVADFWRMVWQERTPIIVMITNIEEM 380
Cdd:cd14630     6 KNRYGNIISYDHSRVRLQLLD-GDPHSDYINANYIDGYH-RPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVEV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 381 NE-KCTEYWPEEQVVHDGVEITVQKVIHTEDYRLRLISL-RRGTEE-RSLKHYWFTSWPDQKTPDRAPPLLHLVREVEEA 457
Cdd:cd14630    84 GRvKCVRYWPDDTEVYGDIKVTLIETEPLAEYVIRTFTVqKKGYHEiREIRQFHFTSWPDHGVPCYATGLLGFVRQVKFL 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907178461 458 aqqEGPHCSPIIVHCSAGIGRTGCFIATSICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHAM 528
Cdd:cd14630   164 ---NPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAI 231
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 302-524 4.37e-62

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: 203.51  E-value: 4.37e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 302 NRYKTILPNPHSRVRLTSPDpeDPLSSYINANYIRGYSgEEKVYIATQGPIVSTVADFWRMVWQERTPIIVMITN-IEEM 380
Cdd:cd14615     1 NRYNNVLPYDISRVKLSVQS--HSTDDYINANYMPGYN-SKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKcVEQG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 381 NEKCTEYWPEEQVV-HDGVEITVQKVIHTEDYRLRLISLRRGT--EERSLKHYWFTSWPDQKTPDRAPPLL---HLVREV 454
Cdd:cd14615    78 RTKCEEYWPSKQKKdYGDITVTMTSEIVLPEWTIRDFTVKNAQtnESRTVRHFHFTSWPDHGVPETTDLLInfrHLVREY 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 455 eeaaQQEGPHCSPIIVHCSAGIGRTGCFIATSICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFV 524
Cdd:cd14615   158 ----MKQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFL 223
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 301-531 5.31e-62

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: 204.10  E-value: 5.31e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 301 KNRYKTILPNPHSRVRLTSPDPEDPLSSYINANYI-------RGYSGEEKVYIATQGPIVSTVADFWRMVWQERTPIIVM 373
Cdd:cd14605     5 KNRYKNILPFDHTRVVLHDGDPNEPVSDYINANIImpefetkCNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSRVIVM 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 374 ITN-IEEMNEKCTEYWPEEQVVHDGVEITVQKVIHT--EDYRLRLISLRR---GTEERSLKHYWFTSWPDQKTPDRAPPL 447
Cdd:cd14605    85 TTKeVERGKSKCVKYWPDEYALKEYGVMRVRNVKESaaHDYILRELKLSKvgqGNTERTVWQYHFRTWPDHGVPSDPGGV 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 448 LHLVREVEEaaQQEG-PHCSPIIVHCSAGIGRTGCFIATSICCQQLRREGV---VDILKTTCQLRQDRGGMIQTCEQYQF 523
Cdd:cd14605   165 LDFLEEVHH--KQESiMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMVQTEAQYRF 242


                  ....*...
gi 1907178461 524 VHHAMSLY 531
Cdd:cd14605   243 IYMAVQHY 250
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 329-526 7.12e-61

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: 199.78  E-value: 7.12e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 329 YINANYIRGYSGEEKVYIATQGPIVSTVADFWRMVWQERTPIIVMITN-IEEMNEKCTEYWPEEQVVHDGVEITVqKVIH 407
Cdd:cd18533     1 YINASYITLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPlVENGREKCDQYWPSGEYEGEYGDLTV-ELVS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 408 TE-----DYRLRLISLRRGT-EERSLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQEgPHCSPIIVHCSAGIGRTGC 481
Cdd:cd18533    80 EEenddgGFIVREFELSKEDgKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNDSA-SLDPPIIVHCSAGVGRTGT 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907178461 482 FIATSICCQQLRR--------EGVVD-ILKTTCQLRQDRGGMIQTCEQYQFVHH 526
Cdd:cd18533   159 FIALDSLLDELKRglsdsqdlEDSEDpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 301-528 3.47e-60

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: 200.26  E-value: 3.47e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 301 KNRYKTILPNPHSRVRLTSPDPEdPLSSYINANYIRGYSgEEKVYIATQGPIVSTVADFWRMVWQERTPIIVMITNIEEM 380
Cdd:cd14626    44 KNRYANVIAYDHSRVILTSVDGV-PGSDYINANYIDGYR-KQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEK 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 381 NE-KCTEYWPEEQVVHDG-VEITVQKVIHTEDYRLRLISLRR--GTEERSLKHYWFTSWPDQKTPDRAPPLLHLVREVEE 456
Cdd:cd14626   122 SRvKCDQYWPIRGTETYGmIQVTLLDTVELATYSVRTFALYKngSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKA 201

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907178461 457 AaqqEGPHCSPIIVHCSAGIGRTGCFIATSICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHAM 528
Cdd:cd14626   202 C---NPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEAL 270
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 301-527 7.52e-60

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: 198.13  E-value: 7.52e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 301 KNRYKTILPNPHSRVRLtSPDPEDPLSSYINANYIRGYSgEEKVYIATQGPIVSTVADFWRMVWQERTPIIVMITNIEEM 380
Cdd:cd14554     9 KNRLVNILPYESTRVCL-QPIRGVEGSDYINASFIDGYR-QRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKLREM 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 381 N-EKCTEYWPEEQVVHDGVEITVQKVIHT-EDYRLR--LISLRRGTEERSLKHYWFTSWPDQKTPDRAPPLLHLVREVEE 456
Cdd:cd14554    87 GrEKCHQYWPAERSARYQYFVVDPMAEYNmPQYILRefKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHK 166

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907178461 457 AAQQEGPHcSPIIVHCSAGIGRTGCFIATSICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHA 527
Cdd:cd14554   167 TKEQFGQE-GPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRA 236
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 301-528 2.07e-59

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: 197.95  E-value: 2.07e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 301 KNRYKTILPNPHSRVRLTS-PDPEDPLSSYINANYIRGYSgEEKVYIATQGPIVSTVADFWRMVWQERTPIIVMITN-IE 378
Cdd:cd17667    30 KNRYINILAYDHSRVKLRPlPGKDSKHSDYINANYVDGYN-KAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNlVE 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 379 EMNEKCTEYWPEEQVVHDG-VEITVQKVIHTEDYRLRLISLR-----RGTE--------ERSLKHYWFTSWPDQKTPDRA 444
Cdd:cd17667   109 KGRRKCDQYWPTENSEEYGnIIVTLKSTKIHACYTVRRFSIRntkvkKGQKgnpkgrqnERTVIQYHYTQWPDMGVPEYA 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 445 PPLLHLVREvEEAAQQegPHCSPIIVHCSAGIGRTGCFIATSICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFV 524
Cdd:cd17667   189 LPVLTFVRR-SSAART--PEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFI 265


                  ....
gi 1907178461 525 HHAM 528
Cdd:cd17667   266 HDAL 269
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 320-528 2.18e-58

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: 193.31  E-value: 2.18e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 320 PDPEDPLSSYINANYIRGYSGEEKvYIATQGPIVSTVADFWRMVWQERTPIIVMITNIEEMNE-KCTEYWPEEQVVHDGV 398
Cdd:cd14631     6 PVEDDPSSDYINANYIDGYQRPSH-YIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRvKCYKYWPDDTEVYGDF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 399 EITVQKVIHTEDYRLRLISL-RRGTEE-RSLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAaqqEGPHCSPIIVHCSAGI 476
Cdd:cd14631    85 KVTCVEMEPLAEYVVRTFTLeRRGYNEiREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLS---NPPSAGPIVVHCSAGA 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907178461 477 GRTGCFIATSICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHAM 528
Cdd:cd14631   162 GRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAI 213
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 329-528 6.55e-58

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: 191.67  E-value: 6.55e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 329 YINANYIRGYSgEEKVYIATQGPIVSTVADFWRMVWQERTPIIVMITNIEEMNE-KCTEYWPEEQVVHDGVEITVQKVIH 407
Cdd:cd14555     1 YINANYIDGYH-RPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRvKCSRYWPDDTEVYGDIKVTLVETEP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 408 TEDYRLRLISL-RRGTEE-RSLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQqegPHCSPIIVHCSAGIGRTGCFIAT 485
Cdd:cd14555    80 LAEYVVRTFALeRRGYHEiREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNP---PSAGPIVVHCSAGAGRTGCYIVI 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1907178461 486 SICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHAM 528
Cdd:cd14555   157 DIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAI 199
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 294-530 1.81e-57

catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type tyrosine-protein phosphatase O (PTPRO or R-PTP-O), also known as glomerular epithelial protein 1 or protein tyrosine phosphatase U2 (PTP-U2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRO is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is essential for sustaining the structure and function of foot processes by regulating tyrosine phosphorylation of podocyte proteins. It has been identified as a synaptic cell adhesion molecule (CAM) that serves as a potent initiator of synapse formation. It is also a tumor suppressor in several types of cancer, such as hepatocellular carcinoma, lung cancer, and breast cancer.


Pssm-ID: 350462 [Multi-domain]  Cd Length: 245  Bit Score: 192.03  E-value: 1.81e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 294 DIPGLVRKNRYKTILPNPHSRVRLTSPDpEDPLSSYINANYIRGYSGEEKvYIATQGPIVSTVADFWRMVWQERTPIIVM 373
Cdd:cd14614     8 DLPVNRCKNRYTNILPYDFSRVKLVSMH-EEEGSDYINANYIPGYNSPQE-YIATQGPLPETRNDFWKMVLQQKSQIIVM 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 374 ITNIEEMNE-KCTEYWP--EEQVVHDgvEITVQKVIHTE--DYRLRLISLRRGTEERSLKHYWFTSWPDQKTP--DRAPP 446
Cdd:cd14614    86 LTQCNEKRRvKCDHYWPftEEPVAYG--DITVEMLSEEEqpDWAIREFRVSYADEVQDVMHFNYTAWPDHGVPtaNAAES 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 447 LLHLVREVEeaaQQEGPHCSPIIVHCSAGIGRTGCFIATSICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVHH 526
Cdd:cd14614   164 ILQFVQMVR---QQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 240


                  ....
gi 1907178461 527 AMSL 530
Cdd:cd14614   241 CVQL 244
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 301-528 2.00e-57

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: 192.95  E-value: 2.00e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 301 KNRYKTILPNPHSRVRLtSPDPEDPLSSYINANYIRGYSGEEKvYIATQGPIVSTVADFWRMVWQERTPIIVMITNIEEM 380
Cdd:cd14633    43 KNRYGNIIAYDHSRVRL-QPIEGETSSDYINGNYIDGYHRPNH-YIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEV 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 381 NE-KCTEYWPEEQVVHDGVEITVQKVIHTEDYRLRLISL-RRGTEE-RSLKHYWFTSWPDQKTPDRAPPLLHLVREVEea 457
Cdd:cd14633   121 GRvKCCKYWPDDTEIYKDIKVTLIETELLAEYVIRTFAVeKRGVHEiREIRQFHFTGWPDHGVPYHATGLLGFVRQVK-- 198

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907178461 458 aQQEGPHCSPIIVHCSAGIGRTGCFIATSICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHAM 528
Cdd:cd14633   199 -SKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAI 268
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 329-528 1.12e-56

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: 188.25  E-value: 1.12e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 329 YINANYIRGYSgEEKVYIATQGPIVSTVADFWRMVWQERTPIIVMITNIEEMN-EKCTEYWPEEQVVHDGvEITV--QKV 405
Cdd:cd14552     1 YINASFIDGYR-QKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSqNKCAQYWPEDGSVSSG-DITVelKDQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 406 IHTEDYRLR--LISLRRGTEERSLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQEGPHcsPIIVHCSAGIGRTGCFI 483
Cdd:cd14552    79 TDYEDYTLRdfLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSGNH--PITVHCSAGAGRTGTFC 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1907178461 484 ATSICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHAM 528
Cdd:cd14552   157 ALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 302-525 1.13e-56

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: 189.38  E-value: 1.13e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 302 NRYKTILPNPHSRVRLTSPdPEDPLSSYINANYIRGYSGEEKvYIATQGPIVSTVADFWRMVWQERTPIIVMIT-NIEEM 380
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQL-GGEPHSDYINANFIPGYTSPQE-FIATQGPLKKTIEDFWRLVWEQQVCNIIMLTvGMENG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 381 NEKCTEYWPEEQ--VVHDGVEITVQKVIHTEDYRLRLISLRRGTE--ERSLKHYWFTSWPDQKTPDRAPPLL---HLVRE 453
Cdd:cd14618    79 RVLCDHYWPSEStpVSYGHITVHLLAQSSEDEWTRREFKLWHEDLrkERRVKHLHYTAWPDHGIPESTSSLMafrELVRE 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907178461 454 VEEAAQQEGPhcspIIVHCSAGIGRTGCFIATSICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVH 525
Cdd:cd14618   159 HVQATKGKGP----TLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLH 226
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 284-531 2.34e-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: 189.71  E-value: 2.34e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 284 PMNFVDPKEYDIPGLVRKNRYKTILPNPHSRVRLTSPDPEDPLSSYINANYIR----GYSGEEKVYIATQGPIVSTVADF 359
Cdd:cd14606     4 VKNLHQRLEGQRPENKSKNRYKNILPFDHSRVILQGRDSNIPGSDYINANYVKnqllGPDENAKTYIASQGCLEATVNDF 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 360 WRMVWQERTPIIVMIT-NIEEMNEKCTEYWPEEQVVHDGVEITVQKV--IHTEDYRLRLISL---RRGTEERSLKHYWFT 433
Cdd:cd14606    84 WQMAWQENSRVIVMTTrEVEKGRNKCVPYWPEVGMQRAYGPYSVTNCgeHDTTEYKLRTLQVsplDNGELIREIWHYQYL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 434 SWPDQKTPDRAPPLLHLVREVEEaAQQEGPHCSPIIVHCSAGIGRTGCFIATSICCQQLRREGV---VDILKTTCQLRQD 510
Cdd:cd14606   164 SWPDHGVPSEPGGVLSFLDQINQ-RQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRAQ 242

                         250       260
                  ....*....|....*....|.
gi 1907178461 511 RGGMIQTCEQYQFVHHAMSLY 531
Cdd:cd14606   243 RSGMVQTEAQYKFIYVAIAQF 263
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 302-528 3.68e-55

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: 185.48  E-value: 3.68e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 302 NRYKTILPNPHSRVRLTsPDPEDPLSSYINANYIRGYsGEEKVYIATQGPIVSTVADFWRMVWQERTPIIVMITNIEEMN 381
Cdd:cd14619     1 NRFRNVLPYDWSRVPLK-PIHEEPGSDYINANYMPGY-WSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 382 E-KCTEYWPEEQV--VHDGVEITVQKVIHTEDYRLRLISLRRGTEE--RSLKHYWFTSWPDQKTPDRAPPLL---HLVRE 453
Cdd:cd14619    79 RvKCEHYWPLDYTpcTYGHLRVTVVSEEVMENWTVREFLLKQVEEQktLSVRHFHFTAWPDHGVPSSTDTLLafrRLLRQ 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907178461 454 VEEAAQQEGPhcspIIVHCSAGIGRTGCFIATSICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHAM 528
Cdd:cd14619   159 WLDQTMSGGP----TVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCI 229
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 329-528 1.25e-54

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: 183.26  E-value: 1.25e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 329 YINANYIRGYSgEEKVYIATQGPIVSTVADFWRMVWQERTPIIVMITN-IEEMNEKCTEYWPEEQVVHDGVEITVQKVIH 407
Cdd:cd17668     1 YINANYVDGYN-KPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNlVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 408 T------EDYRLRLISLRRGTE-----ERSLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQEgphCSPIIVHCSAGI 476
Cdd:cd17668    80 VlayytvRNFTLRNTKIKKGSQkgrpsGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHA---VGPVVVHCSAGV 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907178461 477 GRTGCFIATSICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHAM 528
Cdd:cd17668   157 GRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDAL 208
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 301-528 4.21e-54

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: 184.55  E-value: 4.21e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 301 KNRYKTILPNPHSRVRLTSPDpEDPLSSYINANYIRGYSgEEKVYIATQGPIVSTVADFWRMVWQERTPIIVMITNIEEM 380
Cdd:cd14624    50 KNRYANVIAYDHSRVLLSAIE-GIPGSDYINANYIDGYR-KQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEER 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 381 NE-KCTEYWPEEQV-VHDGVEITVQKVIHTEDYRLRLISLRR--GTEERSLKHYWFTSWPDQKTPDRAPPLLHLVREVEE 456
Cdd:cd14624   128 SRvKCDQYWPSRGTeTYGLIQVTLLDTVELATYCVRTFALYKngSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKT 207

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907178461 457 AaqqEGPHCSPIIVHCSAGIGRTGCFIATSICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHAM 528
Cdd:cd14624   208 C---NPPDAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDAL 276
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 301-528 5.96e-54

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: 184.14  E-value: 5.96e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 301 KNRYKTILPNPHSRVRLTsPDPEDPLSSYINANYIRGYSgEEKVYIATQGPIVSTVADFWRMVWQERTPIIVMITNIEEM 380
Cdd:cd14625    50 KNRYANVIAYDHSRVILQ-PIEGIMGSDYINANYIDGYR-KQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEK 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 381 NE-KCTEYWPEEQVVHDG-VEITVQKVIHTEDYRLRLISLRR--GTEERSLKHYWFTSWPDQKTPDRAPPLLHLVREVEE 456
Cdd:cd14625   128 SRiKCDQYWPSRGTETYGmIQVTLLDTIELATFCVRTFSLHKngSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKT 207

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907178461 457 AaqqEGPHCSPIIVHCSAGIGRTGCFIATSICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHAM 528
Cdd:cd14625   208 C---NPPDAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDAL 276
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 299-529 6.19e-53

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: 180.79  E-value: 6.19e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 299 VRKNRYKTILPNPHSRVRLtSPDPEDPLSSYINANYIRGYSGEeKVYIATQGPIVSTVADFWRMVWQERTPIIVM-ITNI 377
Cdd:cd14603    31 VKKNRYKDILPYDQTRVIL-SLLQEEGHSDYINANFIKGVDGS-RAYIATQGPLSHTVLDFWRMIWQYGVKVILMaCREI 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 378 EEMNEKCTEYWPEEQVVHDGVEITVQKVIH---TEDYRLRLISLRRGTEERSLKHYWFTSWPDQKTPDRAPPLLHLVREV 454
Cdd:cd14603   109 EMGKKKCERYWAQEQEPLQTGPFTITLVKEkrlNEEVILRTLKVTFQKESRSVSHFQYMAWPDHGIPDSPDCMLAMIELA 188

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907178461 455 EEaAQQEGPhcSPIIVHCSAGIGRTGCFIATSICCQQLRREGVVD---ILKTTCQLRQDRGGMIQTCEQYQFVHHAMS 529
Cdd:cd14603   189 RR-LQGSGP--EPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPdfsIFDVVLEMRKQRPAAVQTEEQYEFLYHTVA 263
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 329-528 7.45e-53

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: 178.32  E-value: 7.45e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 329 YINANYIRGYSGEEKvYIATQGPIVSTVADFWRMVWQERTPIIVMITNIEEMNE-KCTEYWPEEQVVHDGVEITVQKVIH 407
Cdd:cd14632     1 YINANYIDGYHRSNH-FIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRvKCSKYWPDDSDTYGDIKITLLKTET 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 408 TEDYRLRLISL-RRGTEER-SLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQqegPHCSPIIVHCSAGIGRTGCFIAT 485
Cdd:cd14632    80 LAEYSVRTFALeRRGYSARhEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTP---PDAGPVVVHCSAGAGRTGCYIVL 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1907178461 486 SICCQQLRREGVVDI---LKTTCQLRQDrggMIQTCEQYQFVHHAM 528
Cdd:cd14632   157 DVMLDMAECEGVVDIyncVKTLCSRRIN---MIQTEEQYIFIHDAI 199
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 301-531 1.44e-52

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: 180.70  E-value: 1.44e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 301 KNRYKTILPNPHSRVRLtSPDPEDPLSSYINANYIRGYSgEEKVYIATQGPIVSTVADFWRMVWQERTPIIVMITNIEEM 380
Cdd:cd14628    55 KNRLVNIMPYESTRVCL-QPIRGVEGSDYINASFIDGYR-QQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREM 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 381 N-EKCTEYWPEEQ-------VVHDGVEITVQKVIHTEdyrLRLISLRRGtEERSLKHYWFTSWPDQKTPDRAPPLLHLVR 452
Cdd:cd14628   133 GrEKCHQYWPAERsaryqyfVVDPMAEYNMPQYILRE---FKVTDARDG-QSRTVRQFQFTDWPEQGVPKSGEGFIDFIG 208

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907178461 453 EVEEAAQQEGPHcSPIIVHCSAGIGRTGCFIATSICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHAMSLY 531
Cdd:cd14628   209 QVHKTKEQFGQD-GPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEY 286
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 329-525 3.95e-52

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: 176.17  E-value: 3.95e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 329 YINANYIRGYSgEEKVYIATQGPIVSTVADFWRMVWQERTPIIVMITNIEEMNE-KCTEYWP---EEQVVHDGVEITVQK 404
Cdd:cd14557     1 YINASYIDGFK-EPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRnKCAQYWPsmeEGSRAFGDVVVKINE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 405 VIHTEDYRLRLISL---RRGTEERSLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAaqqEGPHCSPIIVHCSAGIGRTGC 481
Cdd:cd14557    80 EKICPDYIIRKLNInnkKEKGSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAF---NNFFSGPIVVHCSAGVGRTGT 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1907178461 482 FIATSICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVH 525
Cdd:cd14557   157 YIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 301-531 5.38e-52

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: 179.16  E-value: 5.38e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 301 KNRYKTILPNPHSRVRLtSPDPEDPLSSYINANYIRGYSgEEKVYIATQGPIVSTVADFWRMVWQERTPIIVMITNIEEM 380
Cdd:cd14627    56 KNRLVNIMPYETTRVCL-QPIRGVEGSDYINASFIDGYR-QQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREM 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 381 N-EKCTEYWPEEQ-------VVHDGVEITVQKVIHTEdyrLRLISLRRGtEERSLKHYWFTSWPDQKTPDRAPPLLHLVR 452
Cdd:cd14627   134 GrEKCHQYWPAERsaryqyfVVDPMAEYNMPQYILRE---FKVTDARDG-QSRTVRQFQFTDWPEQGVPKSGEGFIDFIG 209

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907178461 453 EVEEAAQQEGPHcSPIIVHCSAGIGRTGCFIATSICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHAMSLY 531
Cdd:cd14627   210 QVHKTKEQFGQD-GPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEY 287
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 329-527 1.59e-51

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: 174.87  E-value: 1.59e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 329 YINANYIRGYSGEEK-VYIATQGPIVSTVADFWRMVWQERTPIIVMIT-NIEEMNEKCTEYWPEE----QVVHDGVEITV 402
Cdd:cd14538     1 YINASHIRIPVGGDTyHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTqDVEGGKVKCHRYWPDSlnkpLICGGRLEVSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 403 QKVIHTEDYRLRLISLR--RGTEERSLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQegphcSPIIVHCSAGIGRTG 480
Cdd:cd14538    81 EKYQSLQDFVIRRISLRdkETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIHNS-----GPIVVHCSAGIGRTG 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1907178461 481 CFIATSICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHA 527
Cdd:cd14538   156 VLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKA 202
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 304-528 5.07e-51

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: 174.36  E-value: 5.07e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 304 YKTILPNPHSRVRLTSPDpEDPLSSYINANYIRGYSGEEKvYIATQGPIVSTVADFWRMVWQERTPIIVMITNIEEMNE- 382
Cdd:cd14620     1 YPNILPYDHSRVILSQLD-GIPCSDYINASYIDGYKEKNK-FIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEe 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 383 KCTEYWPEEQV-VHDGVEITVQKVIHTEDYRLRLISLRRGTEE-----RSLKHYWFTSWPDQKTPDRAPPLLHLVREVEE 456
Cdd:cd14620    79 KCYQYWPDQGCwTYGNIRVAVEDCVVLVDYTIRKFCIQPQLPDgckapRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVKS 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907178461 457 AaqqEGPHCSPIIVHCSAGIGRTGCFIATSICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHAM 528
Cdd:cd14620   159 V---NPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQAL 227
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 302-525 6.71e-51

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: 173.94  E-value: 6.71e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 302 NRYKTILPNPHSRVRLTsPDPEDPLSSYINANYIRGYSGEEKvYIATQGPIVSTVADFWRMVWQERTPIIVMITNIEEMN 381
Cdd:cd14616     1 NRFPNIKPYNNNRVKLI-ADAGVPGSDYINASYISGYLCPNE-FIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 382 E-KCTEYWPEE-QVVHDGVEITVQKVIH--TEDYRLRLISLRRGTEERSLKHYWFTSWPDQKTPDRAPPLLHLVREVEEA 457
Cdd:cd14616    79 RiRCHQYWPEDnKPVTVFGDIVITKLMEdvQIDWTIRDLKIERHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVRAS 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907178461 458 AQQEGphcSPIIVHCSAGIGRTGCFIATSICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVH 525
Cdd:cd14616   159 RAHDN---TPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLH 223
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 329-526 1.95e-50

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: 171.84  E-value: 1.95e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 329 YINANYIRGYSGEeKVYIATQGPIVSTVADFWRMVWQERTPIIVMITNIEEMNE-KCTEYWP---EEQVVHDGVEITVQK 404
Cdd:cd14542     1 YINANFIKGVSGS-KAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKkKCERYWPeegEEQLQFGPFKISLEK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 405 V-IHTEDYRLRLISLRRGTEERSLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQEGPhcsPIIVHCSAGIGRTGCFI 483
Cdd:cd14542    80 EkRVGPDFLIRTLKVTFQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDV---PICVHCSAGCGRTGTIC 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1907178461 484 ATSICCQQLRREG------VVDILKttcQLRQDRGGMIQTCEQYQFVHH 526
Cdd:cd14542   157 AIDYVWNLLKTGKipeefsLFDLVR---EMRKQRPAMVQTKEQYELVYR 202
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 299-535 2.17e-50

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: 175.12  E-value: 2.17e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 299 VRKNRYKTILPNPHSRVRLTSPDPEDPlSSYINANYIRGYSGEeKVYIATQGPIVSTVADFWRMVWQERTPIIVMITNIE 378
Cdd:cd14604    58 VKKNRYKDILPFDHSRVKLTLKTSSQD-SDYINANFIKGVYGP-KAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREF 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 379 EMN-EKCTEYWP---EEQVVHDGVEITVQKVIHTEDYRLRLISLRRGTEERSLKHYWFTSWPDQKTPDRAPPLLHLVREV 454
Cdd:cd14604   136 EMGrKKCERYWPlygEEPMTFGPFRISCEAEQARTDYFIRTLLLEFQNETRRLYQFHYVNWPDHDVPSSFDSILDMISLM 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 455 EEAAQQEGphcSPIIVHCSAGIGRTGCFIATSICCQQLRREGV---VDILKTTCQLRQDRGGMIQTCEQYQFVHHAMS-L 530
Cdd:cd14604   216 RKYQEHED---VPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAqL 292


                  ....*
gi 1907178461 531 YEKQL 535
Cdd:cd14604   293 FEKQL 297
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 301-531 6.02e-50

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: 173.76  E-value: 6.02e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 301 KNRYKTILPNPHSRVRLtSPDPEDPLSSYINANYIRGYSgEEKVYIATQGPIVSTVADFWRMVWQERTPIIVMITNIEEM 380
Cdd:cd14629    56 KNRLVNIMPYELTRVCL-QPIRGVEGSDYINASFIDGYR-QQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREM 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 381 N-EKCTEYWPEEQ-------VVHDGVEITVQKVIHTEdyrLRLISLRRGtEERSLKHYWFTSWPDQKTPDRAPPLLHLVR 452
Cdd:cd14629   134 GrEKCHQYWPAERsaryqyfVVDPMAEYNMPQYILRE---FKVTDARDG-QSRTIRQFQFTDWPEQGVPKTGEGFIDFIG 209

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907178461 453 EVEEAAQQEGPHcSPIIVHCSAGIGRTGCFIATSICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHAMSLY 531
Cdd:cd14629   210 QVHKTKEQFGQD-GPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALEY 287
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 300-531 6.65e-50

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: 171.55  E-value: 6.65e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 300 RKNRYKTILPNPHSRVRLTSPdpedplSSYINANYIR-GYSGEEKVYIATQGPIVSTVADFWRMVWQERTPIIVMITN-I 377
Cdd:cd14597     5 KKNRYKNILPYDTTRVPLGDE------GGYINASFIKmPVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQeV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 378 EEMNEKCTEYWPEE----QVVHDGVEITVQKVIHTEDYRLRLISLR--RGTEERSLKHYWFTSWPDQKTPDRAPPLLHLV 451
Cdd:cd14597    79 EGGKIKCQRYWPEIlgktTMVDNRLQLTLVRMQQLKNFVIRVLELEdiQTREVRHITHLNFTAWPDHDTPSQPEQLLTFI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 452 ---REVEEAAqqegphcsPIIVHCSAGIGRTGCFIATSICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHAM 528
Cdd:cd14597   159 symRHIHKSG--------PIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVI 230


                  ...
gi 1907178461 529 sLY 531
Cdd:cd14597   231 -LY 232
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 329-525 9.79e-50

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: 170.19  E-value: 9.79e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 329 YINANYIRGYSgEEKVYIATQGPIVSTVADFWRMVWQERTPIIVMITNIEEM-NEKCTEYWPEEQVVHDG---VEITVQK 404
Cdd:cd14622     2 YINASFIDGYR-QKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEReQEKCVQYWPSEGSVTHGeitIEIKNDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 405 VIHTEDYRLRLISLRRGTEERSLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQEGPHcsPIIVHCSAGIGRTGCFIA 484
Cdd:cd14622    81 LLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQTGNH--PIVVHCSAGAGRTGTFIA 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1907178461 485 TSICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVH 525
Cdd:cd14622   159 LSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCY 199
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 302-525 1.16e-49

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: 170.87  E-value: 1.16e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 302 NRYKTILPNPHSRVRLTSPDpEDPLSSYINANYIRGYSGEEKvYIATQGPIVSTVADFWRMVWQERTPIIVMITN-IEEM 380
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNVD-DDPCSDYINASYIPGNNFRRE-YIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQcVEKG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 381 NEKCTEYWPEEQ-VVHDG---VEITVQKVIHTEDYR-LRLISLRRGTEERSLKHYWFTSWPDQKTPDRAPPLLHLVREVE 455
Cdd:cd14617    79 RVKCDHYWPADQdSLYYGdliVQMLSESVLPEWTIReFKICSEEQLDAPRLVRHFHYTVWPDHGVPETTQSLIQFVRTVR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 456 EAAQQEgPHCSPIIVHCSAGIGRTGCFIATSICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVH 525
Cdd:cd14617   159 DYINRT-PGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 301-523 7.88e-49

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: 168.72  E-value: 7.88e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 301 KNRYKTILPNPHSRVRLTSPDPEdplSSYINANYIRGYSGEEKvYIATQGPIVSTVADFWRMVWQERTPIIVMITNIEEM 380
Cdd:cd14545     1 LNRYRDRDPYDHDRSRVKLKQGD---NDYINASLVEVEEAKRS-YILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 381 NE-KCTEYWPEEQV-----VHDGVEITVQKVIHTEDYRLRLISLRR--GTEERSLKHYWFTSWPDQKTPDRAPPLLHLVR 452
Cdd:cd14545    77 GQiKCAQYWPQGEGnamifEDTGLKVTLLSEEDKSYYTVRTLELENlkTQETREVLHFHYTTWPDFGVPESPAAFLNFLQ 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907178461 453 EVEEAAQQEGPHcSPIIVHCSAGIGRTGCFIATSICCQQLRREGV--VDILKTTCQLRQDRGGMIQTCEQYQF 523
Cdd:cd14545   157 KVRESGSLSSDV-GPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQLRF 228
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 303-525 1.36e-48

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type tyrosine-protein phosphatase A (PTPRA), also known as receptor-type tyrosine-protein phosphatase alpha (R-PTP-alpha), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA is a positive regulator of Src and Src family kinases via dephosphorylation of the Src-inhibitory tyrosine 527. Thus, it affects transformation and tumorigenesis, inhibition of proliferation, cell cycle arrest, integrin signaling, neuronal differentiation and outgrowth, and ion channel activity. It is also involved in interleukin-1 signaling in fibroblasts through its interaction with the focal adhesion targeting domain of focal adhesion kinase. PTPRA comprises a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350471 [Multi-domain]  Cd Length: 228  Bit Score: 167.91  E-value: 1.36e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 303 RYKTILPNPHSRVRLTSPDPEDPlSSYINANYIRGYSgEEKVYIATQGPIVSTVADFWRMVWQERTPIIVMITNIEEM-N 381
Cdd:cd14623     1 RVLQIIPYEFNRVIIPVKRGEEN-TDYVNASFIDGYR-QKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERgQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 382 EKCTEYWPEEQVVHDG-VEITVQKVIHTEDYRLR--LISLRRGTEERSLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAA 458
Cdd:cd14623    79 EKCAQYWPSDGSVSYGdITIELKKEEECESYTVRdlLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQ 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907178461 459 QQEGPHcsPIIVHCSAGIGRTGCFIATSICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVH 525
Cdd:cd14623   159 QQSGNH--PITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCY 223
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 329-532 1.88e-48

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: 166.80  E-value: 1.88e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 329 YINANYIRGYSGEeKVYIATQGPIVSTVADFWRMVWQERTPIIVMITN-IEEMNEKCTEYWPEEQVVHDGVEITVQKVIH 407
Cdd:cd14558     1 YINASFIDGYWGP-KSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTElKEGDQEQCAQYWGDEKKTYGDIEVELKDTEK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 408 TEDYRLRLISLR--RGTEERSLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQEGPHCS---PIIVHCSAGIGRTGCF 482
Cdd:cd14558    80 SPTYTVRVFEIThlKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKNSKHGrsvPIVVHCSDGSSRTGIF 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907178461 483 IATSICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFvhhamsLYE 532
Cdd:cd14558   160 CALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQF------LYD 203
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 301-528 9.21e-48

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: 167.89  E-value: 9.21e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 301 KNRYKTILPNPHSRVRLTsPDPEDPLSSYINANYIRGYSGEEKvYIATQGPIVSTVADFWRMVWQERTPIIVMITNIEEM 380
Cdd:cd14621    55 KNRYVNILPYDHSRVHLT-PVEGVPDSDYINASFINGYQEKNK-FIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKER 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 381 NE-KCTEYWPEEQV-VHDGVEITVQKVIHTEDYRLRLISLRRGTE------ERSLKHYWFTSWPDQKTPDRAPPLLHLVR 452
Cdd:cd14621   133 KEcKCAQYWPDQGCwTYGNIRVSVEDVTVLVDYTVRKFCIQQVGDvtnkkpQRLITQFHFTSWPDFGVPFTPIGMLKFLK 212

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907178461 453 EVEEAAQQegpHCSPIIVHCSAGIGRTGCFIATSICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHAM 528
Cdd:cd14621   213 KVKNCNPQ---YAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQAL 285
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 329-525 5.41e-47

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: 162.94  E-value: 5.41e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 329 YINANYIRGYSGEEKVYIATQGPIVSTVADFWRMVWQERTPIIVMITNIEEMNE-KCTEYWPEE---QVVHDGVEITVQK 404
Cdd:cd14539     1 YINASLIEDLTPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKqKVHRYWPTErgqALVYGAITVSLQS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 405 VIHTEDYRLRLISL--RRGTEERSLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQEGPHCSPIIVHCSAGIGRTGCF 482
Cdd:cd14539    81 VRTTPTHVERIISIqhKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYLQQRSLQTPIVVHCSSGVGRTGAF 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1907178461 483 IATSICCQQLRRE-GVVDILKTTCQLRQDRGGMIQTCEQYQFVH 525
Cdd:cd14539   161 CLLYAAVQEIEAGnGIPDLPQLVRKMRQQRKYMLQEKEHLKFCY 204
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 329-525 2.10e-46

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: 161.23  E-value: 2.10e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 329 YINANYIRGYSgEEKVYIATQGPIVSTVADFWRMVWQERTPIIVMITNIEEMNE-KCTEYWPEEQVVHDG-VEITVQKVI 406
Cdd:cd14551     1 YINASYIDGYQ-EKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEkKCSQYWPDQGCWTYGnLRVRVEDTV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 407 HTEDYRLRLISLR---RGTEERSLK---HYWFTSWPDQKTPDRAPPLLHLVREVEEAAQqegPHCSPIIVHCSAGIGRTG 480
Cdd:cd14551    80 VLVDYTTRKFCIQkvnRGIGEKRVRlvtQFHFTSWPDFGVPFTPIGMLKFLKKVKSANP---PRAGPIVVHCSAGVGRTG 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1907178461 481 CFIATSICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVH 525
Cdd:cd14551   157 TFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 301-528 9.03e-46

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: 160.78  E-value: 9.03e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 301 KNRYKTILPNPHSRVRLtSPDPEDPLSSYINANYIRGYSGEeKVYIATQGPIVSTVADFWRMVWQERTPIIVMITNIEEM 380
Cdd:cd14602     1 KNRYKDILPYDHSRVEL-SLITSDEDSDYINANFIKGVYGP-RAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 381 -NEKCTEYWPE--EQVVHDG-VEITVQKVIHTEDYRLRLISLRRGTEERSLKHYWFTSWPDQKTPDRAPPLLHLVREVEE 456
Cdd:cd14602    79 gKKKCERYWAEpgEMQLEFGpFSVTCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRC 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907178461 457 AAQQEGPhcsPIIVHCSAGIGRTGCFIATSIcCQQLRREGVV----DILKTTCQLRQDRGGMIQTCEQYQFVHHAM 528
Cdd:cd14602   159 YQEDDSV---PICIHCSAGCGRTGVICAIDY-TWMLLKDGIIpenfSVFSLIQEMRTQRPSLVQTKEQYELVYNAV 230
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 329-524 1.17e-45

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: 159.42  E-value: 1.17e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 329 YINANY----IRGySGEEKVYIATQGPIVSTVADFWRMVWQERTPIIVMIT-NIEEMNEKCTEYWPE--EQVVHDGVEIT 401
Cdd:cd14541     2 YINANYvnmeIPG-SGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTtLVERGRVKCHQYWPDlgETMQFGNLQIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 402 VQKVIHTEDYRLRLISLR--RGTEERSLKHYWFTSWPDQKTPDRAPPLLHLVREVEeaAQQEGPhCSPIIVHCSAGIGRT 479
Cdd:cd14541    81 CVSEEVTPSFAFREFILTntNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVR--QNRVGM-VEPTVVHCSAGIGRT 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1907178461 480 GCFIA--TSICcqQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFV 524
Cdd:cd14541   158 GVLITmeTAMC--LIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFV 202
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 299-529 6.30e-45

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: 159.84  E-value: 6.30e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 299 VRKNRYKTILPNPHSRVRLTSPDPEDPlSSYINANYIRGYSGEEKVYIATQGPIVSTVADFWRMVWQERTPIIVMITNIE 378
Cdd:cd14610    45 VQKNRSLAVLPYDHSRIILKAENSHSH-SDYINASPIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCVVIVMLTPLA 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 379 EMN-EKCTEYWPEE--QVVHDGVEITVQKVIHTEDYRLRLISLR--RGTEERSLKHYWFTSWPDQKTPDRAPPLLHLVRE 453
Cdd:cd14610   124 ENGvKQCYHYWPDEgsNLYHIYEVNLVSEHIWCEDFLVRSFYLKnlQTNETRTVTQFHFLSWNDQGVPASTRSLLDFRRK 203

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907178461 454 VEEAAQqeGPHCsPIIVHCSAGIGRTGCFIATSICCQQLRREGV-VDILKTTCQLRQDRGGMIQTCEQYQFVHHAMS 529
Cdd:cd14610   204 VNKCYR--GRSC-PIIVHCSDGAGRSGTYILIDMVLNKMAKGAKeIDIAATLEHLRDQRPGMVQTKEQFEFALTAVA 277
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 329-524 9.44e-45

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: 156.84  E-value: 9.44e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 329 YINANYIRGYSGEEKVYIATQGPIVSTVADFWRMVWQERTPIIVMITNIEEM-NEKCTEYWPEE--QVVHDgVEIT-VQK 404
Cdd:cd14546     1 YINASTIYDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENgVKQCARYWPEEgsEVYHI-YEVHlVSE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 405 VIHTEDYRLRLISLR--RGTEERSLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAaqQEGPHCsPIIVHCSAGIGRTGCF 482
Cdd:cd14546    80 HIWCDDYLVRSFYLKnlQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKS--YRGRSC-PIVVHCSDGAGRTGTY 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1907178461 483 IATSICCQQLRReGV--VDILKTTCQLRQDRGGMIQTCEQYQFV 524
Cdd:cd14546   157 ILIDMVLNRMAK-GAkeIDIAATLEHLRDQRPGMVKTKDQFEFV 199
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 299-529 1.18e-44

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: 159.05  E-value: 1.18e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 299 VRKNRYKTILPNPHSRVRLTSpDPEDPLSSYINANYIRGYSGEEKVYIATQGPIVSTVADFWRMVWQERTPIIVMITNIE 378
Cdd:cd14609    43 VKKNRNPDFVPYDHARIKLKA-ESNPSRSDYINASPIIEHDPRMPAYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLV 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 379 EMNEK-CTEYWPEE-QVVHDGVEIT-VQKVIHTEDYRLRLISLR--RGTEERSLKHYWFTSWPDQKTPDRAPPLLHLVRE 453
Cdd:cd14609   122 EDGVKqCDRYWPDEgSSLYHIYEVNlVSEHIWCEDFLVRSFYLKnvQTQETRTLTQFHFLSWPAEGIPSSTRPLLDFRRK 201

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907178461 454 VEEAAQqeGPHCsPIIVHCSAGIGRTGCFIATSICCQQLRReGV--VDILKTTCQLRQDRGGMIQTCEQYQFVHHAMS 529
Cdd:cd14609   202 VNKCYR--GRSC-PIIVHCSDGAGRTGTYILIDMVLNRMAK-GVkeIDIAATLEHVRDQRPGMVRTKDQFEFALTAVA 275
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 329-528 4.12e-44

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: 155.29  E-value: 4.12e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 329 YINANYIRGYSGEEK-VYIATQGPIVSTVADFWRMVWQERTPIIVMIT-NIEEMNEKCTEYWPEeqvvhdgveiTVQKVI 406
Cdd:cd14596     1 YINASYITMPVGEEElFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTrEVERGKVKCHRYWPE----------TLQEPM 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 407 HTEDYRLRLIS--------------LRRGTEE-RSLKHYWFTSWPDQKTPDRAPPLLHLVREVEeAAQQEGPhcspIIVH 471
Cdd:cd14596    71 ELENYQLRLENyqalqyfiiriiklVEKETGEnRLIKHLQFTTWPDHGTPQSSDQLVKFICYMR-KVHNTGP----IVVH 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907178461 472 CSAGIGRTGCFIATSICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHAM 528
Cdd:cd14596   146 CSAGIGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVV 202
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 265-525 5.18e-44

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 158.24  E-value: 5.18e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 265 ELHEKALDPFLLQAEFFEIPMNfvdpkeydipglVRKNRYKTILPNPHSRVRLTSPDpeDPLSSYINANYIRGYSgEEKV 344
Cdd:PHA02747   30 EHHQIILKPFDGLIANFEKPEN------------QPKNRYWDIPCWDHNRVILDSGG--GSTSDYIHANWIDGFE-DDKK 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 345 YIATQGPIVSTVADFWRMVWQERTPIIVMITNIEEMN--EKCTEYW-PEE--QVVHDGVEITVQKVIHTEDYRLRLISL- 418
Cdd:PHA02747   95 FIATQGPFAETCADFWKAVWQEHCSIIVMLTPTKGTNgeEKCYQYWcLNEdgNIDMEDFRIETLKTSVRAKYILTLIEIt 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 419 -RRGTEERSLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQEGPH-------CSPIIVHCSAGIGRTGCFIATSICCQ 490
Cdd:PHA02747  175 dKILKDSRKISHFQCSEWFEDETPSDHPDFIKFIKIIDINRKKSGKLfnpkdalLCPIVVHCSDGVGKTGIFCAVDICLN 254

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1907178461 491 QLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVH 525
Cdd:PHA02747  255 QLVKRKAICLAKTAEKIREQRHAGIMNFDDYLFIQ 289
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 329-525 9.73e-44

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: 154.10  E-value: 9.73e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 329 YINANYIRGYSgEEKVYIATQGPIVSTVADFWRMVWQERTPIIVMITNIEEMNEKCTEYWPEEQVVHDGVeITVQKVIHT 408
Cdd:cd14556     1 YINAALLDSYK-QPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQSCPQYWPDEGSGTYGP-IQVEFVSTT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 409 EDYRL-----RLISLRRGTEE-RSLKHYWFTSWP-DQKTPDRAPPLLHLVREVEEAAQQEGPhcSPIIVHCSAGIGRTGC 481
Cdd:cd14556    79 IDEDVisrifRLQNTTRPQEGyRMVQQFQFLGWPrDRDTPPSKRALLKLLSEVEKWQEQSGE--GPIVVHCLNGVGRSGV 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1907178461 482 FIATSICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVH 525
Cdd:cd14556   157 FCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 301-528 5.30e-41

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: 149.02  E-value: 5.30e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 301 KNRYKTILPNPHSRVRLTSPDpedplSSYINANYIRGYSGEEKvYIATQGPIVSTVADFWRMVWQERTPIIVMITN-IEE 379
Cdd:cd14608    28 RNRYRDVSPFDHSRIKLHQED-----NDYINASLIKMEEAQRS-YILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRvMEK 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 380 MNEKCTEYWP---EEQVVHDGVEITVQKVihTED----YRLRLISLRRGT--EERSLKHYWFTSWPDQKTPDRAPPLLHL 450
Cdd:cd14608   102 GSLKCAQYWPqkeEKEMIFEDTNLKLTLI--SEDiksyYTVRQLELENLTtqETREILHFHYTTWPDFGVPESPASFLNF 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 451 VREVEEAAQQEgPHCSPIIVHCSAGIGRTGCFIATSICC---QQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHA 527
Cdd:cd14608   180 LFKVRESGSLS-PEHGPVVVHCSAGIGRSGTFCLADTCLllmDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLA 258


                  .
gi 1907178461 528 M 528
Cdd:cd14608   259 V 259
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 259-528 7.04e-41

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 150.18  E-value: 7.04e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 259 RVLRAEELHEKALDP----FLLQ--AEFFEIPM-----NFVDPKEydipglVRKNRYKTILPNPHSRVRLTS-------- 319
Cdd:PHA02746    7 EIFNAFDFFDKTNHAkfceFVLLehAEVMDIPIrgttnHFLKKEN------LKKNRFHDIPCWDHSRVVINAheslkmfd 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 320 ---PDP-------EDPLSSYINANYIRGYSgEEKVYIATQGPIVSTVADFWRMVWQERTPIIVMITNIEEMNEKCTEYWP 389
Cdd:PHA02746   81 vgdSDGkkievtsEDNAENYIHANFVDGFK-EANKFICAQGPKEDTSEDFFKLISEHESQVIVSLTDIDDDDEKCFELWT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 390 EEQvvhdGVEIT----VQKVIHTED------YRLRLISLRRGTEeRSLKHYWFTSWPDQKTPDRAPPLLHLVREVEE--- 456
Cdd:PHA02746  160 KEE----DSELAfgrfVAKILDIIEelsftkTRLMITDKISDTS-REIHHFWFPDWPDNGIPTGMAEFLELINKVNEeqa 234

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907178461 457 ----AAQQEGPHCSPIIVHCSAGIGRTGCFIATSICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHAM 528
Cdd:PHA02746  235 elikQADNDPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 301-528 7.45e-41

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: 148.46  E-value: 7.45e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 301 KNRYKTILPNPHSRVRLTSPDpedplsSYINANYIR-GYSGEEKV--YIATQGPIVSTVADFWRMVWQERTPIIVMITNI 377
Cdd:cd14600    43 KNRYKDVLPYDATRVVLQGNE------DYINASYVNmEIPSANIVnkYIATQGPLPHTCAQFWQVVWEQKLSLIVMLTTL 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 378 EEMNE-KCTEYWPEEQVVHDGVEITVQkvIHTEDY------RLRLISLRRGTEERSLKHYWFTSWPDQKTPDRAPPLLHL 450
Cdd:cd14600   117 TERGRtKCHQYWPDPPDVMEYGGFRVQ--CHSEDCtiayvfREMLLTNTQTGEERTVTHLQYVAWPDHGVPDDSSDFLEF 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 451 VREVEEAAQQEgphcSPIIVHCSAGIGRTGCFIA--TSICCqqLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHAM 528
Cdd:cd14600   195 VNYVRSKRVEN----EPVLVHCSAGIGRTGVLVTmeTAMCL--TERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAI 268
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 268-528 1.63e-40

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: 148.22  E-value: 1.63e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 268 EKALDPFLLQAEFFEIPMNFVDP--KEYDIPGLVRKNRYKTILPNPHSRVRLTsPDPEDPlSSYINANYIR-GYSGEEKV 344
Cdd:cd14599     6 ERKLEEGMVFTEYEQIPKKKADGvfTTATLPENAERNRIREVVPYEENRVELV-PTKENN-TGYINASHIKvTVGGEEWH 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 345 YIATQGPIVSTVADFWRMVWQERTPIIVMITNIEEMNE-KCTEYWPEEQVVHDGVeiTVQKVIHTEDYR----------L 413
Cdd:cd14599    84 YIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRsKSHRYWPKLGSKHSSA--TYGKFKVTTKFRtdsgcyattgL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 414 RLISLRRGtEERSLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQEGP------HCSP-IIVHCSAGIGRTGCFIATS 486
Cdd:cd14599   162 KVKHLLSG-QERTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVRRHTNSmldstkNCNPpIVVHCSAGVGRTGVVILTE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1907178461 487 ICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHAM 528
Cdd:cd14599   241 LMIGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVL 282
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
286-523 3.24e-40

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 147.16  E-value: 3.24e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 286 NFVDPKEYDIPGLVRKNRYKTILPNPHSRVRltSPDPedplssYINANYIRGysGEEKVYIATQGPIVSTVADFWRMVWQ 365
Cdd:COG5599    30 SHNDPQYLQNINGSPLNRFRDIQPYKETALR--ANLG------YLNANYIQV--IGNHRYIATQYPLEEQLEDFFQMLFD 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 366 ERTPIIVMITNIEEM---NEKCTEYWPE-EQVVHDGVEITVQKVIHTED-YRLRLISLRR---GTEERSLKHYWFTSWPD 437
Cdd:COG5599   100 NNTPVLVVLASDDEIskpKVKMPVYFRQdGEYGKYEVSSELTESIQLRDgIEARTYVLTIkgtGQKKIEIPVLHVKNWPD 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 438 QKTPDrAPPLLHLVREVEEAAQQEGPHCSPIIVHCSAGIGRTGCFIATsICCQQLRREGV---VDILKTTCQLRQDRG-G 513
Cdd:COG5599   180 HGAIS-AEALKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIAC-LALSKSINALVqitLSVEEIVIDMRTSRNgG 257

                         250
                  ....*....|
gi 1907178461 514 MIQTCEQYQF 523
Cdd:COG5599   258 MVQTSEQLDV 267
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 329-525 5.10e-40

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: 144.52  E-value: 5.10e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 329 YINANYIR-GYSGEEKVYIATQGPIVSTVADFWRMVWQERTPIIVMITNIEE-MNEKCTEYWPEEQVVHDGV-----EIT 401
Cdd:cd14540     1 YINASHITaTVGGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEgGREKCFRYWPTLGGEHDALtfgeyKVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 402 VQKVIHTEDYRLRLISLRRGTE--ERSLKHYWFTSWPDQKTPDRAPPLLHLVREVEE----AAQQEGPHCS--PIIVHCS 473
Cdd:cd14540    81 TKFSVSSGCYTTTGLRVKHTLSgqSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSvrrhTNQDVAGHNRnpPTLVHCS 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907178461 474 AGIGRTGCFIATSICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVH 525
Cdd:cd14540   161 AGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVY 212
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 301-528 1.07e-39

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: 145.11  E-value: 1.07e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 301 KNRYKTILPNPHSRVRLTSPDpedplSSYINANYIRgYSGEEKVYIATQGPIVSTVADFWRMVWQERTPIIVMITNI-EE 379
Cdd:cd14607    27 RNRYRDVSPYDHSRVKLQNTE-----NDYINASLVV-IEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIvEK 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 380 MNEKCTEYWP---EEQVVHDGVEITVQKVihTED----YRLRLISLR--RGTEERSLKHYWFTSWPDQKTPDRAPPLLHL 450
Cdd:cd14607   101 DSVKCAQYWPtdeEEVLSFKETGFSVKLL--SEDvksyYTVHLLQLEniNSGETRTISHFHYTTWPDFGVPESPASFLNF 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 451 VREVEEAAQQeGPHCSPIIVHCSAGIGRTGCF--IATSICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHAM 528
Cdd:cd14607   179 LFKVRESGSL-SPEHGPAVVHCSAGIGRSGTFslVDTCLVLMEKKDPDSVDIKQVLLDMRKYRMGLIQTPDQLRFSYMAV 257
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 329-523 3.01e-39

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: 142.22  E-value: 3.01e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 329 YINANYIRGYSGEE-KVYIATQGPIVSTVADFWRMVWQERTPIIVMITNIEEMNE--KCTEYWP---EEQVVHDGVEITV 402
Cdd:cd17658     1 YINASLVETPASESlPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYStaKCADYFPaeeNESREFGRISVTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 403 QKVIHTED-YRLRLISLR-RGTEE--RSLKHYWFTSWPDQKTPDRAPPllhlVREVEEAAQQEGPHCSPIIVHCSAGIGR 478
Cdd:cd17658    81 KKLKHSQHsITLRVLEVQyIESEEppLSVLHIQYPEWPDHGVPKDTRS----VRELLKRLYGIPPSAGPIVVHCSAGIGR 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907178461 479 TGCFIATSiccQQLRR--EG---VVDILKTTCQLRQDRGGMIQTCEQYQF 523
Cdd:cd17658   157 TGAYCTIH---NTIRRilEGdmsAVDLSKTVRKFRSQRIGMVQTQDQYIF 203
PHA02738 PHA02738
hypothetical protein; Provisional
 302-531 1.89e-37

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 140.83  E-value: 1.89e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 302 NRYKTILPNPHSRVRLTSpdpEDPLSSYINANYIRGYSGEEKvYIATQGPIVSTVADFWRMVWQERTPIIVMITNIEE-M 380
Cdd:PHA02738   53 NRYLDAVCFDHSRVILPA---ERNRGDYINANYVDGFEYKKK-FICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKEnG 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 381 NEKCTEYWPE-EQ--VVHDGVEITVQKVIHTEDYRLRLISLRRGTEE-RSLKHYWFTSWPDQKTPDRAPPLLHLVREVEE 456
Cdd:PHA02738  129 REKCFPYWSDvEQgsIRFGKFKITTTQVETHPHYVKSTLLLTDGTSAtQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRQ 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 457 AAQ-------QEGPHCS---PIIVHCSAGIGRTGCFIATSICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVHH 526
Cdd:PHA02738  209 CQKelaqeslQIGHNRLqppPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYR 288


                  ....*
gi 1907178461 527 AMSLY 531
Cdd:PHA02738  289 AVKRY 293
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 329-528 2.31e-37

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: 137.41  E-value: 2.31e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 329 YINANYIR-GYSGEEKVYIATQGPIVSTVADFWRMVWQERTPIIVMITNIEEM-NEKCTEYWPEEQVVHDGVEITVQKVi 406
Cdd:cd14598     1 YINASHIKvTVGGKEWDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGgREKSFRYWPRLGSRHNTVTYGRFKI- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 407 hTEDYR----------LRLISLRRGtEERSLKHYWFTSWPDQKTPDRAPPLLHLVREVEE-------AAQQEGPHcSPII 469
Cdd:cd14598    80 -TTRFRtdsgcyattgLKIKHLLTG-QERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSvrrhtnsTIDPKSPN-PPVL 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907178461 470 VHCSAGIGRTGCFIATSICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHAM 528
Cdd:cd14598   157 VHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVL 215
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
426-528 4.87e-37

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 132.48  E-value: 4.87e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461  426 SLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQEGPHcSPIIVHCSAGIGRTGCFIATSICCQQLRRE-GVVDILKTT 504
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESS-GPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTV 79

                           90       100
                   ....*....|....*....|....
gi 1907178461  505 CQLRQDRGGMIQTCEQYQFVHHAM 528
Cdd:smart00404  80 KELRSQRPGMVQTEEQYLFLYRAL 103
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 426-528 4.87e-37

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: 132.48  E-value: 4.87e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461  426 SLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQEGPHcSPIIVHCSAGIGRTGCFIATSICCQQLRRE-GVVDILKTT 504
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESS-GPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTV 79

                           90       100
                   ....*....|....*....|....
gi 1907178461  505 CQLRQDRGGMIQTCEQYQFVHHAM 528
Cdd:smart00012  80 KELRSQRPGMVQTEEQYLFLYRAL 103
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 329-533 3.22e-36

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: 133.92  E-value: 3.22e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 329 YINANYIR---GYSGEEKVYIATQGPIVSTVADFWRMVWQERTPIIVMI-TNIEEMNEKCTEYWPE--EQVVHDGVEITV 402
Cdd:cd14601     2 YINANYINmeiPSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLtTQVERGRVKCHQYWPEpsGSSSYGGFQVTC 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 403 QKVIHTEDYRLRLISLR--RGTEERSLKHYWFTSWPDQKTPDRAPPLLHLVREVEeaaQQEGPHCSPIIVHCSAGIGRTG 480
Cdd:cd14601    82 HSEEGNPAYVFREMTLTnlEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVR---NKRAGKDEPVVVHCSAGIGRTG 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907178461 481 CFIA--TSIC---CQQLRREgvVDILKTtcqLRQDRGGMIQTCEQYQFVHHA-MSLYEK 533
Cdd:cd14601   159 VLITmeTAMClieCNQPVYP--LDIVRT---MRDQRAMMIQTPSQYRFVCEAiLKVYEE 212
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 300-536 1.36e-34

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 132.43  E-value: 1.36e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 300 RKNRYKTILPNPHSRVRLTSpdpEDPLSSYINANYIRGYSGEEKvYIATQGPIVSTVADFWRMVWQERTPIIVMITNIEE 379
Cdd:PHA02742   54 KKCRYPDAPCFDRNRVILKI---EDGGDDFINASYVDGHNAKGR-FICTQAPLEETALDFWQAIFQDQVRVIVMITKIME 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 380 MN-EKCTEYW-PEEQ--VVHDGVEITVQKVIHTEDYRLRLISLRRGTEERSL--KHYWFTSWPDQKTPDRAPPLLHLVRE 453
Cdd:PHA02742  130 DGkEACYPYWmPHERgkATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLdiKHFAYEDWPHGGLPRDPNKFLDFVLA 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 454 VEEA--------AQQEGPHCSPIIVHCSAGIGRTGCFIATSICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVH 525
Cdd:PHA02742  210 VREAdlkadvdiKGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIFCY 289

                         250
                  ....*....|.
gi 1907178461 526 HAMSLYEKQLS 536
Cdd:PHA02742  290 FIVLIFAKLMA 300
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 329-523 1.67e-30

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: 117.81  E-value: 1.67e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 329 YINANYIRGYSgEEKVYIATQGPIVSTVADFWRMVWQERTPIIVMITNIEEmNEKCTEYWPEEQVVHDGVEITV------ 402
Cdd:cd14550     1 YINASYLQGYR-RSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNEL-NEDEPIYWPTKEKPLECETFKVtlsged 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 403 -QKVIHTEDYRLRLISLRRGTEERSL--KHYWFTSWPDQKTPDRAppLLHLVREV-EEAAQQEGphcsPIIVHCSAGIGR 478
Cdd:cd14550    79 hSCLSNEIRLIVRDFILESTQDDYVLevRQFQCPSWPNPCSPIHT--VFELINTVqEWAQQRDG----PIVVHDRYGGVQ 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1907178461 479 TGCFIATSICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQF 523
Cdd:cd14550   153 AATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQF 197
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 329-528 8.01e-29

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: 113.55  E-value: 8.01e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 329 YINANYIRGYSgEEKVYIATQGPIVSTVADFWRMVWQERTPIIVMITNIEEMNEKCTEYWP--EEQVVHDGVEITV---- 402
Cdd:cd17669     1 YINASYIMGYY-QSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFVYWPnkDEPINCETFKVTLiaee 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 403 QKVIHTEDYRLRLISLRRGTEER---SLKHYWFTSWPDQKTP-DRAPPLLHLVRevEEAAQQEGphcsPIIVHCSAGIGR 478
Cdd:cd17669    80 HKCLSNEEKLIIQDFILEATQDDyvlEVRHFQCPKWPNPDSPiSKTFELISIIK--EEAANRDG----PMIVHDEHGGVT 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907178461 479 TGCFIATSICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHAM 528
Cdd:cd17669   154 AGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAI 203
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 329-525 4.28e-28

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: 111.27  E-value: 4.28e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 329 YINANYIRGYSgEEKVYIATQGPIVSTVADFWRMVWQERTPIIVMITNIEEMnEKCTEYWPEEQVVHDG---VEITVQKV 405
Cdd:cd14634     1 YINAALMDSHK-QPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDAA-QLCMQYWPEKTSCCYGpiqVEFVSADI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 406 IHTEDYRL-RLISLRRGTE-ERSLKHYWFTSWPDQK-TPDRAPPLLHLVREVEEAAQQEGPHCSPIIVHCSAGIGRTGCF 482
Cdd:cd14634    79 DEDIISRIfRICNMARPQDgYRIVQHLQYIGWPAYRdTPPSKRSILKVVRRLEKWQEQYDGREGRTVVHCLNGGGRSGTF 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1907178461 483 IATSICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVH 525
Cdd:cd14634   159 CAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVY 201
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 329-525 1.12e-25

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: 104.61  E-value: 1.12e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 329 YINANYIRGYSgEEKVYIATQGPIVSTVADFWRMVWQERTPIIVMITNIEEMNEK--CTEYWPEEQVVHDG------VEI 400
Cdd:cd14637     1 YINAALTDSYT-RSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwpCLQYWPEPGLQQYGpmevefVSG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 401 TVQKVIHTEDYRLRLISlRRGTEERSLKHYWFTSW-PDQKTPDRAPPLLHLVREVEEAAQQEGPHCSpiIVHCSAGIGRT 479
Cdd:cd14637    80 SADEDIVTRLFRVQNIT-RLQEGHLMVRHFQFLRWsAYRDTPDSKKAFLHLLASVEKWQRESGEGRT--VVHCLNGGGRS 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1907178461 480 GCFIATSICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVH 525
Cdd:cd14637   157 GTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCY 202
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 329-528 2.62e-25

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: 103.60  E-value: 2.62e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 329 YINANYIRGYSGEEKvYIATQGPIVSTVADFWRMVWQERTPIIVMITNIEEMNEKCTEYWPEEQVVHDGVEITV------ 402
Cdd:cd17670     1 YINASYIMGYYRSNE-FIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDEFVYWPSREESMNCEAFTVtliskd 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 403 --------QKVIHteDYRLRLISLRRGTEERslkHYWFTSWPDQKTPDRAP-PLLHLVRevEEAAQQEGphcsPIIVHCS 473
Cdd:cd17670    80 rlclsneeQIIIH--DFILEATQDDYVLEVR---HFQCPKWPNPDAPISSTfELINVIK--EEALTRDG----PTIVHDE 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907178461 474 AGIGRTGCFIATSICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHAM 528
Cdd:cd17670   149 FGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAM 203
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 329-525 1.30e-24

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: 101.64  E-value: 1.30e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 329 YINANYIRGYSgEEKVYIATQGPIVSTVADFWRMVWQERTPIIVMITNIEeMNEKCTEYWPEEQVVHDGvEITVQKVIHT 408
Cdd:cd14636     1 YINAALMDSYR-QPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVD-LAQGCPQYWPEEGMLRYG-PIQVECMSCS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 409 EDYRL-----RLISLRRGTEERSL-KHYWFTSWPDQK-TPDRAPPLLHLVREVEEAAQQEGPHCSPIIVHCSAGIGRTGC 481
Cdd:cd14636    78 MDCDVisrifRICNLTRPQEGYLMvQQFQYLGWASHReVPGSKRSFLKLILQVEKWQEECDEGEGRTIIHCLNGGGRSGM 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1907178461 482 FIATSICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVH 525
Cdd:cd14636   158 FCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCY 201
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 329-525 4.02e-24

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: 100.15  E-value: 4.02e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 329 YINANYIRGYSgEEKVYIATQGPIVSTVADFWRMVWQERTPIIVMITNIEEMnEKCTEYWPEEQV-VHDGVEITVQKVIH 407
Cdd:cd14635     1 YINAALMDSYK-QPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPA-QLCPQYWPENGVhRHGPIQVEFVSADL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 408 TEDYRLRLISLRRGTEE----RSLKHYWFTSWPDQK-TPDRAPPLLHLVREVEEAAQQEGPHCSPIIVHCSAGIGRTGCF 482
Cdd:cd14635    79 EEDIISRIFRIYNAARPqdgyRMVQQFQFLGWPMYRdTPVSKRSFLKLIRQVDKWQEEYNGGEGRTVVHCLNGGGRSGTF 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1907178461 483 IATSICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVH 525
Cdd:cd14635   159 CAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCY 201
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 312-534 1.42e-18

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 86.56  E-value: 1.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 312 HSRVRLTSPDpedplsSYINANYIRGYSGEEKvYIATQGPIVSTVADFWRMVWQERTPIIVMITNIEEmnEKC-TEYWPE 390
Cdd:PHA02740   67 HRRIKLFNDE------KVLDARFVDGYDFEQK-FICIINLCEDACDKFLQALSDNKVQIIVLISRHAD--KKCfNQFWSL 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 391 EQ---VVHDGVEITVQKVIHTEDYRLRLISL--RRGtEERSLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQEGPHC 465
Cdd:PHA02740  138 KEgcvITSDKFQIETLEIIIKPHFNLTLLSLtdKFG-QAQKISHFQYTAWPADGFSHDPDAFIDFFCNIDDLCADLEKHK 216

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907178461 466 S-----PIIVHCSAGIGRTGCFIATSICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHAMSLYEKQ 534
Cdd:PHA02740  217 AdgkiaPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLIAAYLKE 290
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 330-522 7.83e-14

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: 70.89  E-value: 7.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 330 INANYIRgySGEEKVYIATQGPIVSTVADFWRMVWQERTPIIVMITNIEEMNEK-CTEYW-PEEQvvHDGVEITVQKV-- 405
Cdd:cd14559    18 LNANRVQ--IGNKNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKgLPPYFrQSGT--YGSVTVKSKKTgk 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 406 ------IHTEDYRLRLislRRGTEERSLKHYWFTSWPDQKTPDrAPPLLHLVREVEEAAQQ-----EGPHCSPI------ 468
Cdd:cd14559    94 delvdgLKADMYNLKI---TDGNKTITIPVVHVTNWPDHTAIS-SEGLKELADLVNKSAEEkrnfyKSKGSSAIndknkl 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907178461 469 --IVHCSAGIGRTGCFIATSICCQQLRREGVVDILKttcQLRQDRGG-MIQTCEQYQ 522
Cdd:cd14559   170 lpVIHCRAGVGRTGQLAAAMELNKSPNNLSVEDIVS---DMRTSRNGkMVQKDEQLD 223
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 448-526 2.99e-11

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: 60.44  E-value: 2.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 448 LHLVREVEEAAQQEGPHCSPIIVHCSAGIGRTGCFIATSICCQQlrREGVVDILkttCQLRQDRGGMI-QTCEQYQFVHH 526
Cdd:cd14494    39 LAMVDRFLEVLDQAEKPGEPVLVHCKAGVGRTGTLVACYLVLLG--GMSAEEAV---RIVRLIRPGGIpQTIEQLDFLIK 113
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
414-526 9.05e-08

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 51.12  E-value: 9.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 414 RLISLRRGTE-------ERSLKHYWFTsWPDQKTPDRAPpLLHLVREVEEAAQQEGPhcspIIVHCSAGIGRTGCFIAts 486
Cdd:COG2453    28 AVVSLTEEEElllglleEAGLEYLHLP-IPDFGAPDDEQ-LQEAVDFIDEALREGKK----VLVHCRGGIGRTGTVAA-- 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1907178461 487 iccQQLRREGV--VDILKttcQLRQDRGGMIQTCEQYQFVHH 526
Cdd:COG2453   100 ---AYLVLLGLsaEEALA---RVRAARPGAVETPAQRAFLER 135
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 468-525 1.11e-06

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: 48.80  E-value: 1.11e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907178461 468 IIVHCSAGIGRTGCFIAtsicCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVH 525
Cdd:cd14505   109 VLIHCKGGLGRTGLIAA----CLLLELGDTLDPEQAIAAVRALRPGAIQTPKQENFLH 162
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 423-534 4.47e-05

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: 43.42  E-value: 4.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 423 EERSLKHYWFtswpdqKTPDRAPPLLHLVRE----VEEA-AQQEgphcsPIIVHCSAGIGRTGCFIAtsiCcqQLRREGV 497
Cdd:cd14504    46 TCPGLRYHHI------PIEDYTPPTLEQIDEfldiVEEAnAKNE-----AVLVHCLAGKGRTGTMLA---C--YLVKTGK 109

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1907178461 498 VDILKTTCQLRQDRGGMIQTCEQYQFVhhamSLYEKQ 534
Cdd:cd14504   110 ISAVDAINEIRRIRPGSIETSEQEKFV----IQFAKT 142
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 424-525 1.22e-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: 1.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178461 424 ERSLKHYWFtSWPDQKTPDRAPpLLHLVReVEEAAQQEGphcSPIIVHCSAGIGRTGCFIATS-ICCQQLRREGVVDIlk 502
Cdd:cd14506    74 RAGIYFYNF-GWKDYGVPSLTT-ILDIVK-VMAFALQEG---GKVAVHCHAGLGRTGVLIACYlVYALRMSADQAIRL-- 145

                          90       100
                  ....*....|....*....|...
gi 1907178461 503 ttcqLRQDRGGMIQTCEQYQFVH 525
Cdd:cd14506   146 ----VRSKRPNSIQTRGQVLCVR 164
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
450-484 8.14e-03

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 36.88  E-value: 8.14e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1907178461  450 LVREVEEAAQQEGPhcspIIVHCSAGIGRTGCFIA 484
Cdd:smart00195  67 AVEFIEDAESKGGK----VLVHCQAGVSRSATLII 97
 
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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