NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|109157329]
View 

Chain A, HUMAN PROTEIN TYROSINE PHOSPHATASE PTPN5

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 40-297 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: 562.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  40 FLLQAEFFEIPMNFVDPKEYDIPGLVRKNRYKTILPNPHSRVCLTSPDPDDPLSSYINANYIRGYGGEEKVYIATQGPIV 119
Cdd:cd14613    1 FLLQAEFFEIPMNFVDPKEYDIPGLVRKNRYKTILPNPHSRVCLTSPDQDDPLSSYINANYIRGYGGEEKVYIATQGPTV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 120 STVADFWRMVWQEHTPIIVMITNIEEMNEKCTEYWPEEQVAYDGVEITVQKVIHTEDYRLRLISLKSGTEERGLKHYWFT 199
Cdd:cd14613   81 NTVGDFWRMVWQERSPIIVMITNIEEMNEKCTEYWPEEQVTYEGIEITVKQVIHADDYRLRLITLKSGGEERGLKHYWYT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 200 SWPDQKTPDRAPPLLHLVREVEEAAQQEGPHCAPIIVHSSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGG 279
Cdd:cd14613  161 SWPDQKTPDNAPPLLQLVQEVEEARQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGG 240

                        250
                 ....*....|....*...
gi 109157329 280 MIQTCEQYQFVHHVMSLY 297
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 ...
 40-297 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: 562.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  40 FLLQAEFFEIPMNFVDPKEYDIPGLVRKNRYKTILPNPHSRVCLTSPDPDDPLSSYINANYIRGYGGEEKVYIATQGPIV 119
Cdd:cd14613    1 FLLQAEFFEIPMNFVDPKEYDIPGLVRKNRYKTILPNPHSRVCLTSPDQDDPLSSYINANYIRGYGGEEKVYIATQGPTV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 120 STVADFWRMVWQEHTPIIVMITNIEEMNEKCTEYWPEEQVAYDGVEITVQKVIHTEDYRLRLISLKSGTEERGLKHYWFT 199
Cdd:cd14613   81 NTVGDFWRMVWQERSPIIVMITNIEEMNEKCTEYWPEEQVTYEGIEITVKQVIHADDYRLRLITLKSGGEERGLKHYWYT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 200 SWPDQKTPDRAPPLLHLVREVEEAAQQEGPHCAPIIVHSSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGG 279
Cdd:cd14613  161 SWPDQKTPDNAPPLLQLVQEVEEARQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGG 240

                        250
                 ....*....|....*...
gi 109157329 280 MIQTCEQYQFVHHVMSLY 297
Cdd:cd14613  241 MIQTCEQYQFVHHVLSLY 258
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
41-294 1.64e-103

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 303.04  E-value: 1.64e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329    41 LLQAEFFEIPMNFVDPKEYDI---PGLVRKNRYKTILPNPHSRVCLTspDPDDPLSSYINANYIRGYGgEEKVYIATQGP 117
Cdd:smart00194   1 GLEEEFEKLDRLKPDDESCTVaafPENRDKNRYKDVLPYDHTRVKLK--PPPGEGSDYINASYIDGPN-GPKAYIATQGP 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329   118 IVSTVADFWRMVWQEHTPIIVMITNIEEMN-EKCTEYWPEEQ---VAYDGVEITVQKVIHTEDYRLRLISLKSGT--EER 191
Cdd:smart00194  78 LPSTVEDFWRMVWEQKVTVIVMLTELVEKGrEKCAQYWPDEEgepLTYGDITVTLKSVEKVDDYTIRTLEVTNTGcsETR 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329   192 GLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQEGPhcaPIIVHSSAGIGRTGCFIATSICCQQLRQEGVVDILKTTC 271
Cdd:smart00194 158 TVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTG---PIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVK 234

                          250       260
                   ....*....|....*....|...
gi 109157329   272 QLRQDRGGMIQTCEQYQFVHHVM 294
Cdd:smart00194 235 ELRSQRPGMVQTEEQYIFLYRAI 257
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
66-294 3.91e-99

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 291.07  E-value: 3.91e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329   66 RKNRYKTILPNPHSRVCLTSPDPDdplSSYINANYIRGYGGEeKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEE 145
Cdd:pfam00102   3 EKNRYKDVLPYDHTRVKLTGDPGP---SDYINASYIDGYKKP-KKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  146 MN-EKCTEYWP---EEQVAYDGVEITVQK-VIHTEDYRLRLISLKSGT--EERGLKHYWFTSWPDQKTPDRAPPLLHLVR 218
Cdd:pfam00102  79 KGrEKCAQYWPeeeGESLEYGDFTVTLKKeKEDEKDYTVRTLEVSNGGseETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109157329  219 EVEEaaQQEGPHCAPIIVHSSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHVM 294
Cdd:pfam00102 159 KVRK--SSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAI 232
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 31-291 4.56e-45

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 155.16  E-value: 4.56e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  31 ELHEKALDPFLLQAEFFEIPMNfvdpkeydipglVRKNRYKTILPNPHSRVCLTSPDpdDPLSSYINANYIRGYGgEEKV 110
Cdd:PHA02747  30 EHHQIILKPFDGLIANFEKPEN------------QPKNRYWDIPCWDHNRVILDSGG--GSTSDYIHANWIDGFE-DDKK 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 111 YIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMN--EKCTEYW-PEEQVAYD--GVEITVQKVIHTEDYRLRLISL- 184
Cdd:PHA02747  95 FIATQGPFAETCADFWKAVWQEHCSIIVMLTPTKGTNgeEKCYQYWcLNEDGNIDmeDFRIETLKTSVRAKYILTLIEIt 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 185 -KSGTEERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQEGPH-------CAPIIVHSSAGIGRTGCFIATSICCQ 256
Cdd:PHA02747 175 dKILKDSRKISHFQCSEWFEDETPSDHPDFIKFIKIIDINRKKSGKLfnpkdalLCPIVVHCSDGVGKTGIFCAVDICLN 254

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 109157329 257 QLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVH 291
Cdd:PHA02747 255 QLVKRKAICLAKTAEKIREQRHAGIMNFDDYLFIQ 289
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
52-289 3.84e-39

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 138.69  E-value: 3.84e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  52 NFVDPKEYDIPGLVRKNRYKTILPNPHSRVclTSPDPddplssYINANYIRGygGEEKVYIATQGPIVSTVADFWRMVWQ 131
Cdd:COG5599   30 SHNDPQYLQNINGSPLNRFRDIQPYKETAL--RANLG------YLNANYIQV--IGNHRYIATQYPLEEQLEDFFQMLFD 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 132 EHTPIIVMITNIEEM---NEKCTEYWPE-EQVAYDGVEITVQKVIHTED---YRLRLISLK-SGTEERGLKHYWFTSWPD 203
Cdd:COG5599  100 NNTPVLVVLASDDEIskpKVKMPVYFRQdGEYGKYEVSSELTESIQLRDgieARTYVLTIKgTGQKKIEIPVLHVKNWPD 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 204 QKTPDrAPPLLHLVREVEEAAQQEGPHCAPIIVHSSAGIGRTGCFIATsICCQQLRQEGV---VDILKTTCQLRQDRG-G 279
Cdd:COG5599  180 HGAIS-AEALKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIAC-LALSKSINALVqitLSVEEIVIDMRTSRNgG 257

                        250
                 ....*....|
gi 109157329 280 MIQTCEQYQF 289
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 ...
 40-297 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: 562.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  40 FLLQAEFFEIPMNFVDPKEYDIPGLVRKNRYKTILPNPHSRVCLTSPDPDDPLSSYINANYIRGYGGEEKVYIATQGPIV 119
Cdd:cd14613    1 FLLQAEFFEIPMNFVDPKEYDIPGLVRKNRYKTILPNPHSRVCLTSPDQDDPLSSYINANYIRGYGGEEKVYIATQGPTV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 120 STVADFWRMVWQEHTPIIVMITNIEEMNEKCTEYWPEEQVAYDGVEITVQKVIHTEDYRLRLISLKSGTEERGLKHYWFT 199
Cdd:cd14613   81 NTVGDFWRMVWQERSPIIVMITNIEEMNEKCTEYWPEEQVTYEGIEITVKQVIHADDYRLRLITLKSGGEERGLKHYWYT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 200 SWPDQKTPDRAPPLLHLVREVEEAAQQEGPHCAPIIVHSSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGG 279
Cdd:cd14613  161 SWPDQKTPDNAPPLLQLVQEVEEARQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGG 240

                        250
                 ....*....|....*...
gi 109157329 280 MIQTCEQYQFVHHVMSLY 297
Cdd:cd14613  241 MIQTCEQYQFVHHVLSLY 258
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 68-292 3.12e-158

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: 440.29  E-value: 3.12e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  68 NRYKTILPNPHSRVCLTSpDPDDPLSSYINANYIRGYGGEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMN 147
Cdd:cd14547    1 NRYKTILPNEHSRVCLPS-VDDDPLSSYINANYIRGYDGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 148 EKCTEYWPEEQV-AYDGVEITVQKVIHTEDYRLRLISLKSGTEERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQ 226
Cdd:cd14547   80 EKCAQYWPEEENeTYGDFEVTVQSVKETDGYTVRKLTLKYGGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEEARQT 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109157329 227 EgPHCAPIIVHSSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHH 292
Cdd:cd14547  160 E-PHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVHR 224
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 50-297 3.34e-132

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: 3.34e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  50 PMNFVDPKEYDIPGLVRKNRYKTILPNPHSRVCLTSPDPDDPLSSYINANYIRGYGGEEKVYIATQGPIVSTVADFWRMV 129
Cdd:cd14612    1 PPNFVSPEELDIPGHASKDRYKTILPNPQSRVCLRRAGSQEEEGSYINANYIRGYDGKEKAYIATQGPMLNTVSDFWEMV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 130 WQEHTPIIVMITNIEEMNEKCTEYWPEEQVAYDGVEITVQKVIHTEDYRLRLISLKSGTEERGLKHYWFTSWPDQKTPDR 209
Cdd:cd14612   81 WQEECPIIVMITKLKEKKEKCVHYWPEKEGTYGRFEIRVQDMKECDGYTIRDLTIQLEEESRSVKHYWFSSWPDHQTPES 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 210 APPLLHLVREVEEaAQQEGPHCAPIIVHSSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQF 289
Cdd:cd14612  161 AGPLLRLVAEVEE-SRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQF 239


                 ....*...
gi 109157329 290 VHHVMSLY 297
Cdd:cd14612  240 LHHTLALY 247
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 67-292 7.79e-123

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: 7.79e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  67 KNRYKTILPNPHSRVCLTSPDPDDPLSSYINANYIRGYGGEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEM 146
Cdd:cd14611    2 KNRYKTILPNPHSRVCLKPKNSNDSLSTYINANYIRGYGGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 147 NEKCTEYWPEEQVAYDGVEITVQKVIHTEDYRLRLISLKSGTEERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEEaAQQ 226
Cdd:cd14611   82 NEKCVLYWPEKRGIYGKVEVLVNSVKECDNYTIRNLTLKQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLDVEE-DRL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109157329 227 EGPHCAPIIVHSSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHH 292
Cdd:cd14611  161 ASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVHH 226
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
41-294 1.64e-103

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 303.04  E-value: 1.64e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329    41 LLQAEFFEIPMNFVDPKEYDI---PGLVRKNRYKTILPNPHSRVCLTspDPDDPLSSYINANYIRGYGgEEKVYIATQGP 117
Cdd:smart00194   1 GLEEEFEKLDRLKPDDESCTVaafPENRDKNRYKDVLPYDHTRVKLK--PPPGEGSDYINASYIDGPN-GPKAYIATQGP 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329   118 IVSTVADFWRMVWQEHTPIIVMITNIEEMN-EKCTEYWPEEQ---VAYDGVEITVQKVIHTEDYRLRLISLKSGT--EER 191
Cdd:smart00194  78 LPSTVEDFWRMVWEQKVTVIVMLTELVEKGrEKCAQYWPDEEgepLTYGDITVTLKSVEKVDDYTIRTLEVTNTGcsETR 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329   192 GLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQEGPhcaPIIVHSSAGIGRTGCFIATSICCQQLRQEGVVDILKTTC 271
Cdd:smart00194 158 TVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTG---PIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVK 234

                          250       260
                   ....*....|....*....|...
gi 109157329   272 QLRQDRGGMIQTCEQYQFVHHVM 294
Cdd:smart00194 235 ELRSQRPGMVQTEEQYIFLYRAI 257
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
66-294 3.91e-99

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 291.07  E-value: 3.91e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329   66 RKNRYKTILPNPHSRVCLTSPDPDdplSSYINANYIRGYGGEeKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEE 145
Cdd:pfam00102   3 EKNRYKDVLPYDHTRVKLTGDPGP---SDYINASYIDGYKKP-KKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  146 MN-EKCTEYWP---EEQVAYDGVEITVQK-VIHTEDYRLRLISLKSGT--EERGLKHYWFTSWPDQKTPDRAPPLLHLVR 218
Cdd:pfam00102  79 KGrEKCAQYWPeeeGESLEYGDFTVTLKKeKEDEKDYTVRTLEVSNGGseETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109157329  219 EVEEaaQQEGPHCAPIIVHSSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHVM 294
Cdd:pfam00102 159 KVRK--SSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAI 232
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 95-292 2.98e-80

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: 241.81  E-value: 2.98e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  95 YINANYIRGYGGEEKvYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMN-EKCTEYWPEEQ---VAYDGVEITVQK 170
Cdd:cd00047    1 YINASYIDGYRGPKE-YIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGrEKCERYWPEEGgkpLEYGDITVTLVS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 171 VIHTEDYRLRLISLKSGT--EERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQEGPhcaPIIVHSSAGIGRTGCF 248
Cdd:cd00047   80 EEELSDYTIRTLELSPKGcsESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNG---PIVVHCSAGVGRTGTF 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 109157329 249 IATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHH 292
Cdd:cd00047  157 IAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 67-297 2.14e-72

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: 223.49  E-value: 2.14e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  67 KNRYKTILPNPHSRVCLTSPDPDDPLSSYINANYIR------GYGGEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMI 140
Cdd:cd14544    4 KNRYKNILPFDHTRVILKDRDPNVPGSDYINANYIRnenegpTTDENAKTYIATQGCLENTVSDFWSMVWQENSRVIVMT 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 141 TN-IEEMNEKCTEYWPEE--QVAYDGVEITVQKVIHTEDYRLRLISLK---SGTEERGLKHYWFTSWPDQKTPDRAPPLL 214
Cdd:cd14544   84 TKeVERGKNKCVRYWPDEgmQKQYGPYRVQNVSEHDTTDYTLRELQVSkldQGDPIREIWHYQYLSWPDHGVPSDPGGVL 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 215 HLVREVEEaAQQEGPHCAPIIVHSSAGIGRTGCFIATSICCQQLRQEGV---VDILKTTCQLRQDRGGMIQTCEQYQFVH 291
Cdd:cd14544  164 NFLEDVNQ-RQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLdcdIDIQKTIQMVRSQRSGMVQTEAQYKFIY 242


                 ....*.
gi 109157329 292 HVMSLY 297
Cdd:cd14544  243 VAVAQY 248
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 67-291 9.59e-71

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: 218.81  E-value: 9.59e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  67 KNRYKTILPNPHSRVCLtSPDPDDPLSSYINANYIRGYGgEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEM 146
Cdd:cd14553    6 KNRYANVIAYDHSRVIL-QPIEGVPGSDYINANYCDGYR-KQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEER 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 147 NE-KCTEYWPEE-QVAYDGVEITVQKVIHTEDYRLRLISL-KSGT-EERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEE 222
Cdd:cd14553   84 SRvKCDQYWPTRgTETYGLIQVTLLDTVELATYTVRTFALhKNGSsEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKA 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 109157329 223 AAQqegPHCAPIIVHSSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVH 291
Cdd:cd14553  164 CNP---PDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIH 229
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 69-291 3.55e-70

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: 216.84  E-value: 3.55e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  69 RYKTILPNPHSRVCLtSPDPDDPLSSYINANYIRGYGGEEKvYIATQGPIVSTVADFWRMVWQEHTPIIVMITN-IEEMN 147
Cdd:cd14548    1 RYTNILPYDHSRVKL-IPINEEEGSDYINANYIPGYNSPRE-FIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQcMEKGR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 148 EKCTEYWPEEQVAYDGVEITVQKV--IHTEDYRLRLISLKSGTEERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQ 225
Cdd:cd14548   79 VKCDHYWPFDQDPVYYGDITVTMLseSVLPDWTIREFKLERGDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDYIK 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109157329 226 QEGphcAPIIVHSSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVH 291
Cdd:cd14548  159 QEK---GPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLH 221
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 62-291 1.09e-69

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: 217.23  E-value: 1.09e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  62 PGLVRKNRYKTILPNPHSRVCLTSPDPDDPlSSYINANYIRGYGgEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMIT 141
Cdd:cd14543   27 PANQEKNRYGDVLCLDQSRVKLPKRNGDER-TDYINANFMDGYK-QKNAYIATQGPLPKTYSDFWRMVWEQKVLVIVMTT 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 142 NIEEMNE-KCTEYWPEE---QVAYDGVEITVQKVIHTEDYRLRLISLKSGT--EERGLKHYWFTSWPDQKTPDRAPPLLH 215
Cdd:cd14543  105 RVVERGRvKCGQYWPLEegsSLRYGDLTVTNLSVENKEHYKKTTLEIHNTEtdESRQVTHFQFTSWPDFGVPSSAAALLD 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 216 LVREVEE----AAQQEGP----HCA--PIIVHSSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCE 285
Cdd:cd14543  185 FLGEVRQqqalAVKAMGDrwkgHPPgpPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTVRRMRTQRAFSIQTPD 264


                 ....*.
gi 109157329 286 QYQFVH 291
Cdd:cd14543  265 QYYFCY 270
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 95-291 4.56e-63

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: 197.96  E-value: 4.56e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  95 YINANYIRGYGgEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEM-NEKCTEYWPEEQV-AYDGVEITVQKVI 172
Cdd:cd14549    1 YINANYVDGYN-KARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERgRRKCDQYWPKEGTeTYGNIQVTLLSTE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 173 HTEDYRLRLISLK--------SGTEERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAaqqEGPHCAPIIVHSSAGIGR 244
Cdd:cd14549   80 VLATYTVRTFSLKnlklkkvkGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAA---NPPGAGPIVVHCSAGVGR 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 109157329 245 TGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVH 291
Cdd:cd14549  157 TGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 67-297 1.55e-61

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: 196.01  E-value: 1.55e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  67 KNRYKTILPNPHSRVCLTSPDPDDPLSSYINANYI-------RGYGGEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVM 139
Cdd:cd14605    5 KNRYKNILPFDHTRVVLHDGDPNEPVSDYINANIImpefetkCNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSRVIVM 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 140 ITN-IEEMNEKCTEYWPEEQV--AYDGVEITVQKVIHTEDYRLRLISLK---SGTEERGLKHYWFTSWPDQKTPDRAPPL 213
Cdd:cd14605   85 TTKeVERGKSKCVKYWPDEYAlkEYGVMRVRNVKESAAHDYILRELKLSkvgQGNTERTVWQYHFRTWPDHGVPSDPGGV 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 214 LHLVREVEEaaQQEG-PHCAPIIVHSSAGIGRTGCFIATSICCQQLRQEGV---VDILKTTCQLRQDRGGMIQTCEQYQF 289
Cdd:cd14605  165 LDFLEEVHH--KQESiMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMVQTEAQYRF 242


                 ....*...
gi 109157329 290 VHHVMSLY 297
Cdd:cd14605  243 IYMAVQHY 250
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 68-290 3.30e-61

catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type tyrosine-protein phosphatase J (PTPRJ or R-PTP-J), also known as receptor-type tyrosine-protein phosphatase eta (R-PTP-eta) or density-enhanced phosphatase 1 (DEP-1) OR CD148, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRJ is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats (eight in PTPRJ) and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed in various cell types including epithelial, hematopoietic, and endothelial cells. It plays a role in cell adhesion, migration, proliferation and differentiation. It dephosphorylates or contributes to the dephosphorylation of various substrates including protein kinases such as FLT3, PDGFRB, MET, RET (variant MEN2A), VEGFR-2, LYN, SRC, MAPK1, MAPK3, and EGFR, as well as PIK3R1 and PIK3R2.


Pssm-ID: 350463 [Multi-domain]  Cd Length: 229  Bit Score: 194.26  E-value: 3.30e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  68 NRYKTILPNPHSRVCLTSPDpdDPLSSYINANYIRGYGgEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITN-IEEM 146
Cdd:cd14615    1 NRYNNVLPYDISRVKLSVQS--HSTDDYINANYMPGYN-SKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKcVEQG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 147 NEKCTEYWPEEQ-VAYDGVEITVQKVIHTEDYRLRLISLKSGT--EERGLKHYWFTSWPDQKTPDRAPPLL---HLVREV 220
Cdd:cd14615   78 RTKCEEYWPSKQkKDYGDITVTMTSEIVLPEWTIRDFTVKNAQtnESRTVRHFHFTSWPDHGVPETTDLLInfrHLVREY 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 221 eeaaQQEGPHCAPIIVHSSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFV 290
Cdd:cd14615  158 ----MKQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFL 223
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 67-291 5.46e-60

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: 191.39  E-value: 5.46e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  67 KNRYKTILPNPHSRVCLTSPDpDDPLSSYINANYIRGYGgEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEM 146
Cdd:cd14630    6 KNRYGNIISYDHSRVRLQLLD-GDPHSDYINANYIDGYH-RPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVEV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 147 NE-KCTEYWPEEQVAYDGVEITVQKVIHTEDYRLRLISL-KSGTEE-RGLKHYWFTSWPDQKTPDRAPPLLHLVREVEEA 223
Cdd:cd14630   84 GRvKCVRYWPDDTEVYGDIKVTLIETEPLAEYVIRTFTVqKKGYHEiREIRQFHFTSWPDHGVPCYATGLLGFVRQVKFL 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 109157329 224 aqqEGPHCAPIIVHSSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVH 291
Cdd:cd14630  164 ---NPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVH 228
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 67-294 6.78e-60

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


Pssm-ID: 350505 [Multi-domain]  Cd Length: 274  Bit Score: 192.56  E-value: 6.78e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  67 KNRYKTILPNPHSRVCLTS-PDPDDPLSSYINANYIRGYGgEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITN-IE 144
Cdd:cd17667   30 KNRYINILAYDHSRVKLRPlPGKDSKHSDYINANYVDGYN-KAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNlVE 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 145 EMNEKCTEYWPEEQV-AYDGVEITVQKVIHTEDYRLRLISLKSGTEERGLK-------------HYWFTSWPDQKTPDRA 210
Cdd:cd17667  109 KGRRKCDQYWPTENSeEYGNIIVTLKSTKIHACYTVRRFSIRNTKVKKGQKgnpkgrqnertviQYHYTQWPDMGVPEYA 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 211 PPLLHLVREvEEAAQQegPHCAPIIVHSSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFV 290
Cdd:cd17667  189 LPVLTFVRR-SSAART--PEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFI 265


                 ....
gi 109157329 291 HHVM 294
Cdd:cd17667  266 HDAL 269
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 67-291 9.71e-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: 190.81  E-value: 9.71e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  67 KNRYKTILPNPHSRVCLtSPDPDDPLSSYINANYIRGYGgEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEM 146
Cdd:cd14554    9 KNRLVNILPYESTRVCL-QPIRGVEGSDYINASFIDGYR-QRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKLREM 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 147 N-EKCTEYWPEE---QVAYDGVEITVQKviHTEDYRLRLISLKSGT--EERGLKHYWFTSWPDQKTPDRAPPLLHLVREV 220
Cdd:cd14554   87 GrEKCHQYWPAErsaRYQYFVVDPMAEY--NMPQYILREFKVTDARdgQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQV 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109157329 221 EEAAQQEGPHcAPIIVHSSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVH 291
Cdd:cd14554  165 HKTKEQFGQE-GPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCY 234
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 67-294 9.94e-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: 192.17  E-value: 9.94e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  67 KNRYKTILPNPHSRVCLTSPDpDDPLSSYINANYIRGYGgEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEM 146
Cdd:cd14626   44 KNRYANVIAYDHSRVILTSVD-GVPGSDYINANYIDGYR-KQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEK 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 147 NE-KCTEYWPEEQV-AYDGVEITVQKVIHTEDYRLRLISL-KSGT-EERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEE 222
Cdd:cd14626  122 SRvKCDQYWPIRGTeTYGMIQVTLLDTVELATYSVRTFALyKNGSsEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKA 201

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109157329 223 AaqqEGPHCAPIIVHSSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHVM 294
Cdd:cd14626  202 C---NPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEAL 270
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 95-292 2.06e-58

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: 186.30  E-value: 2.06e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  95 YINANYIRGYGGEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITN-IEEMNEKCTEYWPEE--QVAYDGVEITVQKV 171
Cdd:cd18533    1 YINASYITLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPlVENGREKCDQYWPSGeyEGEYGDLTVELVSE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 172 IHTEDYRL--RLISLKSGT-EERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQEgPHCAPIIVHSSAGIGRTGCF 248
Cdd:cd18533   81 EENDDGGFivREFELSKEDgKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNDSA-SLDPPIIVHCSAGVGRTGTF 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 109157329 249 IATSICCQQLRQ--------EGVVD-ILKTTCQLRQDRGGMIQTCEQYQFVHH 292
Cdd:cd18533  160 IALDSLLDELKRglsdsqdlEDSEDpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 50-291 3.99e-57

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: 185.08  E-value: 3.99e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  50 PMNFVDPKEYDIPGLVRKNRYKTILPNPHSRVCLTSPDPDDPLSSYINANYIR----GYGGEEKVYIATQGPIVSTVADF 125
Cdd:cd14606    4 VKNLHQRLEGQRPENKSKNRYKNILPFDHSRVILQGRDSNIPGSDYINANYVKnqllGPDENAKTYIASQGCLEATVNDF 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 126 WRMVWQEHTPIIVMIT-NIEEMNEKCTEYWPE--EQVAYDGVEITVQKVIHTEDYRLRLISL---KSGTEERGLKHYWFT 199
Cdd:cd14606   84 WQMAWQENSRVIVMTTrEVEKGRNKCVPYWPEvgMQRAYGPYSVTNCGEHDTTEYKLRTLQVsplDNGELIREIWHYQYL 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 200 SWPDQKTPDRAPPLLHLVREVEEaAQQEGPHCAPIIVHSSAGIGRTGCFIATSICCQQLRQEGV---VDILKTTCQLRQD 276
Cdd:cd14606  164 SWPDHGVPSEPGGVLSFLDQINQ-RQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRAQ 242

                        250
                 ....*....|....*
gi 109157329 277 RGGMIQTCEQYQFVH 291
Cdd:cd14606  243 RSGMVQTEAQYKFIY 257
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 60-296 5.62e-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: 183.94  E-value: 5.62e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  60 DIPGLVRKNRYKTILPNPHSRVCLTSPDpDDPLSSYINANYIRGYGGEEKvYIATQGPIVSTVADFWRMVWQEHTPIIVM 139
Cdd:cd14614    8 DLPVNRCKNRYTNILPYDFSRVKLVSMH-EEEGSDYINANYIPGYNSPQE-YIATQGPLPETRNDFWKMVLQQKSQIIVM 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 140 ITNIEEMNE-KCTEYWP--EEQVAYDgvEITVQKVIHTE--DYRLRLISLKSGTEERGLKHYWFTSWPDQKTP--DRAPP 212
Cdd:cd14614   86 LTQCNEKRRvKCDHYWPftEEPVAYG--DITVEMLSEEEqpDWAIREFRVSYADEVQDVMHFNYTAWPDHGVPtaNAAES 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 213 LLHLVREVEeaaQQEGPHCAPIIVHSSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHH 292
Cdd:cd14614  164 ILQFVQMVR---QQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQ 240


                 ....
gi 109157329 293 VMSL 296
Cdd:cd14614  241 CVQL 244
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 95-291 6.58e-56

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: 179.73  E-value: 6.58e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  95 YINANYIRGYGgEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMNE-KCTEYWPEEQVAYDGVEITVQKVIH 173
Cdd:cd14555    1 YINANYIDGYH-RPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRvKCSRYWPDDTEVYGDIKVTLVETEP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 174 TEDYRLRLISL-KSGTEE-RGLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQqegPHCAPIIVHSSAGIGRTGCFIAT 251
Cdd:cd14555   80 LAEYVVRTFALeRRGYHEiREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNP---PSAGPIVVHCSAGAGRTGCYIVI 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 109157329 252 SICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVH 291
Cdd:cd14555  157 DIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIH 196
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 80-291 7.26e-56

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: 180.22  E-value: 7.26e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  80 RVCLtSPDPDDPLSSYINANYIRGYGGEEKvYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMNE-KCTEYWPEEQ 158
Cdd:cd14631    1 RVIL-QPVEDDPSSDYINANYIDGYQRPSH-YIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRvKCYKYWPDDT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 159 VAYDGVEITVQKVIHTEDYRLRLISL-KSGTEE-RGLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAaqqEGPHCAPIIV 236
Cdd:cd14631   79 EVYGDFKVTCVEMEPLAEYVVRTFTLeRRGYNEiREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLS---NPPSAGPIVV 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 109157329 237 HSSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVH 291
Cdd:cd14631  156 HCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIH 210
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 95-294 2.78e-55

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: 178.23  E-value: 2.78e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  95 YINANYIRGYGgEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMN-EKCTEYWPEE-QVAYDGVEITVQKVI 172
Cdd:cd14552    1 YINASFIDGYR-QKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSqNKCAQYWPEDgSVSSGDITVELKDQT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 173 HTEDYRLR--LISLKSGTEERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQEGPHcaPIIVHSSAGIGRTGCFIA 250
Cdd:cd14552   80 DYEDYTLRdfLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSGNH--PITVHCSAGAGRTGTFCA 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 109157329 251 TSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHVM 294
Cdd:cd14552  158 LSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 68-291 5.45e-55

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: 178.21  E-value: 5.45e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  68 NRYKTILPNPHSRVCLTSPdPDDPLSSYINANYIRGYGGEEKvYIATQGPIVSTVADFWRMVWQEHTPIIVMIT-NIEEM 146
Cdd:cd14618    1 NRYPHVLPYDHSRVRLSQL-GGEPHSDYINANFIPGYTSPQE-FIATQGPLKKTIEDFWRLVWEQQVCNIIMLTvGMENG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 147 NEKCTEYWPEEQ--VAYDGVEITVQKVIHTEDYRLRLISLKSGTE--ERGLKHYWFTSWPDQKTPDRAPPLL---HLVRE 219
Cdd:cd14618   79 RVLCDHYWPSEStpVSYGHITVHLLAQSSEDEWTRREFKLWHEDLrkERRVKHLHYTAWPDHGIPESTSSLMafrELVRE 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109157329 220 VEEAAQQEGPhcapIIVHSSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVH 291
Cdd:cd14618  159 HVQATKGKGP----TLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLH 226
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 67-291 5.98e-54

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: 177.16  E-value: 5.98e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  67 KNRYKTILPNPHSRVCLtSPDPDDPLSSYINANYIRGYGGEEKvYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEM 146
Cdd:cd14633   43 KNRYGNIIAYDHSRVRL-QPIEGETSSDYINGNYIDGYHRPNH-YIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEV 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 147 NE-KCTEYWPEEQVAYDGVEITVQKVIHTEDYRLRLISL-KSGTEE-RGLKHYWFTSWPDQKTPDRAPPLLHLVREVEea 223
Cdd:cd14633  121 GRvKCCKYWPDDTEIYKDIKVTLIETELLAEYVIRTFAVeKRGVHEiREIRQFHFTGWPDHGVPYHATGLLGFVRQVK-- 198

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 109157329 224 aQQEGPHCAPIIVHSSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVH 291
Cdd:cd14633  199 -SKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIH 265
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 67-303 6.50e-54

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: 177.62  E-value: 6.50e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  67 KNRYKTILPNPHSRVCLtSPDPDDPLSSYINANYIRGYGgEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEM 146
Cdd:cd14628   55 KNRLVNIMPYESTRVCL-QPIRGVEGSDYINASFIDGYR-QQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREM 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 147 N-EKCTEYWPEEQVA-YDGVEITVQKVIHTEDYRLRLISLKSGT--EERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEE 222
Cdd:cd14628  133 GrEKCHQYWPAERSArYQYFVVDPMAEYNMPQYILREFKVTDARdgQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHK 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 223 AAQQEGPHcAPIIVHSSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHVMSLYEKQLS 302
Cdd:cd14628  213 TKEQFGQD-GPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYLGSFD 291


                 .
gi 109157329 303 H 303
Cdd:cd14628  292 H 292
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 68-294 1.10e-53

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: 175.08  E-value: 1.10e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  68 NRYKTILPNPHSRVCLTsPDPDDPLSSYINANYIRGYGGEEKvYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMN 147
Cdd:cd14619    1 NRFRNVLPYDWSRVPLK-PIHEEPGSDYINANYMPGYWSSQE-FIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 148 E-KCTEYWPEEQV--AYDGVEITVQKVIHTEDYRLRLISLKSGTEE--RGLKHYWFTSWPDQKTPDRAPPLL---HLVRE 219
Cdd:cd14619   79 RvKCEHYWPLDYTpcTYGHLRVTVVSEEVMENWTVREFLLKQVEEQktLSVRHFHFTAWPDHGVPSSTDTLLafrRLLRQ 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 109157329 220 VEEAAQQEGPhcapIIVHSSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHVM 294
Cdd:cd14619  159 WLDQTMSGGP----TVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCI 229
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 95-291 1.46e-53

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: 174.01  E-value: 1.46e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  95 YINANYIRGYGgEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITN-IEEMNEKCTEYWPEEQVAYDGVEITVQKVIH 173
Cdd:cd17668    1 YINANYVDGYN-KPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNlVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 174 T------EDYRLRLISLKSGTE-----ERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQEgphCAPIIVHSSAGI 242
Cdd:cd17668   80 VlayytvRNFTLRNTKIKKGSQkgrpsGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHA---VGPVVVHCSAGV 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 109157329 243 GRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVH 291
Cdd:cd17668  157 GRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIH 205
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 95-291 1.61e-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: 173.70  E-value: 1.61e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  95 YINANYIRGYGGEEKvYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMNE-KCTEYWPEEQVAYDGVEITVQKVIH 173
Cdd:cd14632    1 YINANYIDGYHRSNH-FIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRvKCSKYWPDDSDTYGDIKITLLKTET 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 174 TEDYRLRLISLksgtEERG------LKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQqegPHCAPIIVHSSAGIGRTGC 247
Cdd:cd14632   80 LAEYSVRTFAL----ERRGysarheVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTP---PDAGPVVVHCSAGAGRTGC 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 109157329 248 FIATSICCQQLRQEGVVDI---LKTTCQLRQDrggMIQTCEQYQFVH 291
Cdd:cd14632  153 YIVLDVMLDMAECEGVVDIyncVKTLCSRRIN---MIQTEEQYIFIH 196
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 67-294 3.53e-53

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: 175.28  E-value: 3.53e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  67 KNRYKTILPNPHSRVCLTsPDPDDPLSSYINANYIRGYGgEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEM 146
Cdd:cd14625   50 KNRYANVIAYDHSRVILQ-PIEGIMGSDYINANYIDGYR-KQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEK 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 147 NE-KCTEYWPEEQV-AYDGVEITVQKVIHTEDYRLRLISL-KSGT-EERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEE 222
Cdd:cd14625  128 SRiKCDQYWPSRGTeTYGMIQVTLLDTIELATFCVRTFSLhKNGSsEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKT 207

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109157329 223 AaqqEGPHCAPIIVHSSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHVM 294
Cdd:cd14625  208 C---NPPDAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDAL 276
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 67-297 4.78e-53

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: 175.31  E-value: 4.78e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  67 KNRYKTILPNPHSRVCLtSPDPDDPLSSYINANYIRGYGgEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEM 146
Cdd:cd14627   56 KNRLVNIMPYETTRVCL-QPIRGVEGSDYINASFIDGYR-QQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREM 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 147 N-EKCTEYWPEEQVA-YDGVEITVQKVIHTEDYRLRLISLKSGT--EERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEE 222
Cdd:cd14627  134 GrEKCHQYWPAERSArYQYFVVDPMAEYNMPQYILREFKVTDARdgQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHK 213

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 109157329 223 AAQQEGPHcAPIIVHSSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHVMSLY 297
Cdd:cd14627  214 TKEQFGQD-GPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEY 287
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 67-294 8.50e-53

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: 174.53  E-value: 8.50e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  67 KNRYKTILPNPHSRVCLTSPDpDDPLSSYINANYIRGYGgEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEM 146
Cdd:cd14624   50 KNRYANVIAYDHSRVLLSAIE-GIPGSDYINANYIDGYR-KQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEER 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 147 NE-KCTEYWPEEQVAYDG-VEITVQKVIHTEDYRLRLISL-KSGT-EERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEE 222
Cdd:cd14624  128 SRvKCDQYWPSRGTETYGlIQVTLLDTVELATYCVRTFALyKNGSsEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKT 207

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109157329 223 AaqqEGPHCAPIIVHSSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHVM 294
Cdd:cd14624  208 C---NPPDAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDAL 276
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 95-291 1.23e-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: 171.16  E-value: 1.23e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  95 YINANYIRGYGgEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMNE-KCTEYWP---EEQVAYDGVEITVQK 170
Cdd:cd14557    1 YINASYIDGFK-EPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRnKCAQYWPsmeEGSRAFGDVVVKINE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 171 VIHTEDYRLRLISL---KSGTEERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAaqqEGPHCAPIIVHSSAGIGRTGC 247
Cdd:cd14557   80 EKICPDYIIRKLNInnkKEKGSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAF---NNFFSGPIVVHCSAGVGRTGT 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 109157329 248 FIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVH 291
Cdd:cd14557  157 YIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 65-292 4.34e-52

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: 171.93  E-value: 4.34e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  65 VRKNRYKTILPNPHSRVCLtSPDPDDPLSSYINANYIRGYGGEeKVYIATQGPIVSTVADFWRMVWQEHTPIIVM-ITNI 143
Cdd:cd14603   31 VKKNRYKDILPYDQTRVIL-SLLQEEGHSDYINANFIKGVDGS-RAYIATQGPLSHTVLDFWRMIWQYGVKVILMaCREI 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 144 EEMNEKCTEYWPEEQVAYDGVEITVQKVIH---TEDYRLRLISLKSGTEERGLKHYWFTSWPDQKTPDRAPPLLHLVREV 220
Cdd:cd14603  109 EMGKKKCERYWAQEQEPLQTGPFTITLVKEkrlNEEVILRTLKVTFQKESRSVSHFQYMAWPDHGIPDSPDCMLAMIELA 188

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 109157329 221 EEaAQQEGPhcAPIIVHSSAGIGRTGCFIATSICCQQLRQEGVVD---ILKTTCQLRQDRGGMIQTCEQYQFVHH 292
Cdd:cd14603  189 RR-LQGSGP--EPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPdfsIFDVVLEMRKQRPAAVQTEEQYEFLYH 260
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 70-294 3.69e-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: 168.58  E-value: 3.69e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  70 YKTILPNPHSRVCLTSPDpDDPLSSYINANYIRGYGGEEKvYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMNE- 148
Cdd:cd14620    1 YPNILPYDHSRVILSQLD-GIPCSDYINASYIDGYKEKNK-FIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEe 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 149 KCTEYWPEEQV-AYDGVEITVQKVIHTEDYRLRLISLKSGTEE-----RGLKHYWFTSWPDQKTPDRAPPLLHLVREVEE 222
Cdd:cd14620   79 KCYQYWPDQGCwTYGNIRVAVEDCVVLVDYTIRKFCIQPQLPDgckapRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVKS 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109157329 223 AaqqEGPHCAPIIVHSSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHVM 294
Cdd:cd14620  159 V---NPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQAL 227
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 67-291 4.37e-51

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: 170.29  E-value: 4.37e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  67 KNRYKTILPNPHSRVCLtSPDPDDPLSSYINANYIRGYGgEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEM 146
Cdd:cd14629   56 KNRLVNIMPYELTRVCL-QPIRGVEGSDYINASFIDGYR-QQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREM 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 147 N-EKCTEYWPEEQVA-YDGVEITVQKVIHTEDYRLRLISLKSGT--EERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEE 222
Cdd:cd14629  134 GrEKCHQYWPAERSArYQYFVVDPMAEYNMPQYILREFKVTDARdgQSRTIRQFQFTDWPEQGVPKTGEGFIDFIGQVHK 213

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 109157329 223 AAQQEGPHcAPIIVHSSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVH 291
Cdd:cd14629  214 TKEQFGQD-GPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCY 281
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 95-289 4.67e-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: 167.55  E-value: 4.67e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  95 YINANYIR-GYGGEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMIT-NIEEMNEKCTEYWPEE----QVAYDGVEITV 168
Cdd:cd14538    1 YINASHIRiPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTqDVEGGKVKCHRYWPDSlnkpLICGGRLEVSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 169 QKVIHTEDYRLRLISL--KSGTEERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQegphcAPIIVHSSAGIGRTG 246
Cdd:cd14538   81 EKYQSLQDFVIRRISLrdKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIHNS-----GPIVVHCSAGIGRTG 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 109157329 247 CFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQF 289
Cdd:cd14538  156 VLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIF 198
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 68-291 8.52e-50

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: 164.71  E-value: 8.52e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  68 NRYKTILPNPHSRVCLTSPDpDDPLSSYINANYIRGYGGEEKvYIATQGPIVSTVADFWRMVWQEHTPIIVMITN-IEEM 146
Cdd:cd14617    1 NRYNNILPYDSTRVKLSNVD-DDPCSDYINASYIPGNNFRRE-YIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQcVEKG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 147 NEKCTEYWPEEQVAYDGVEITVQKVIHTEDYRLRLISLKSGTEE-----RGLKHYWFTSWPDQKTPDRAPPLLHLVREVE 221
Cdd:cd14617   79 RVKCDHYWPADQDSLYYGDLIVQMLSESVLPEWTIREFKICSEEqldapRLVRHFHYTVWPDHGVPETTQSLIQFVRTVR 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 222 EAAQQEgPHCAPIIVHSSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVH 291
Cdd:cd14617  159 DYINRT-PGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 66-297 1.35e-49

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: 164.62  E-value: 1.35e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  66 RKNRYKTILPNPHSRVCLTSPdpddplSSYINANYIR-GYGGEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITN-I 143
Cdd:cd14597    5 KKNRYKNILPYDTTRVPLGDE------GGYINASFIKmPVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQeV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 144 EEMNEKCTEYWPEE----QVAYDGVEITVQKVIHTEDYRLRLISLK--SGTEERGLKHYWFTSWPDQKTPDRAPPLLHLV 217
Cdd:cd14597   79 EGGKIKCQRYWPEIlgktTMVDNRLQLTLVRMQQLKNFVIRVLELEdiQTREVRHITHLNFTAWPDHDTPSQPEQLLTFI 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 218 ---REVEEAaqqegphcAPIIVHSSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHVM 294
Cdd:cd14597  159 symRHIHKS--------GPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVI 230


                 ...
gi 109157329 295 sLY 297
Cdd:cd14597  231 -LY 232
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 95-292 2.05e-49

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: 162.98  E-value: 2.05e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  95 YINANYIRGYGGEeKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMNE-KCTEYWP---EEQVAYDGVEITVQK 170
Cdd:cd14542    1 YINANFIKGVSGS-KAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKkKCERYWPeegEEQLQFGPFKISLEK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 171 V-IHTEDYRLRLISLKSGTEERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQEGPhcaPIIVHSSAGIGRTGCFI 249
Cdd:cd14542   80 EkRVGPDFLIRTLKVTFQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDV---PICVHCSAGCGRTGTIC 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 109157329 250 ATSICCQQLRQEG------VVDILKttcQLRQDRGGMIQTCEQYQFVHH 292
Cdd:cd14542  157 AIDYVWNLLKTGKipeefsLFDLVR---EMRKQRPAMVQTKEQYELVYR 202
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 95-297 9.41e-49

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: 161.33  E-value: 9.41e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  95 YINANYIRGYGgEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEM-NEKCTEYWPEEQVAYDG---VEITVQK 170
Cdd:cd14622    2 YINASFIDGYR-QKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEReQEKCVQYWPSEGSVTHGeitIEIKNDT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 171 VIHTEDYRLRLISLKSGTEERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQEGPHcaPIIVHSSAGIGRTGCFIA 250
Cdd:cd14622   81 LLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQTGNH--PIVVHCSAGAGRTGTFIA 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 109157329 251 TSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHVMSLY 297
Cdd:cd14622  159 LSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQDF 205
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 65-301 1.10e-48

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: 164.34  E-value: 1.10e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  65 VRKNRYKTILPNPHSRVCLTSPDPDDPlSSYINANYIRGYGGEeKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIE 144
Cdd:cd14604   58 VKKNRYKDILPFDHSRVKLTLKTSSQD-SDYINANFIKGVYGP-KAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREF 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 145 EM-NEKCTEYWP---EEQVAYDGVEITVQKVIHTEDYRLRLISLKSGTEERGLKHYWFTSWPDQKTPDRAPPLLHLVREV 220
Cdd:cd14604  136 EMgRKKCERYWPlygEEPMTFGPFRISCEAEQARTDYFIRTLLLEFQNETRRLYQFHYVNWPDHDVPSSFDSILDMISLM 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 221 EEAAQQEGphcAPIIVHSSAGIGRTGCFIATSICCQQLRQEGV---VDILKTTCQLRQDRGGMIQTCEQYQFVHHVMS-L 296
Cdd:cd14604  216 RKYQEHED---VPICIHCSAGCGRTGAICAIDYTWNLLKAGKIpeeFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAqL 292


                 ....*
gi 109157329 297 YEKQL 301
Cdd:cd14604  293 FEKQL 297
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 68-291 1.21e-48

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: 161.61  E-value: 1.21e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  68 NRYKTILPNPHSRVCLTsPDPDDPLSSYINANYIRGYGGEEKvYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMN 147
Cdd:cd14616    1 NRFPNIKPYNNNRVKLI-ADAGVPGSDYINASYISGYLCPNE-FIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 148 E-KCTEYWPEEQ--VAYDGvEITVQKVIH--TEDYRLRLISLKSGTEERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEE 222
Cdd:cd14616   79 RiRCHQYWPEDNkpVTVFG-DIVITKLMEdvQIDWTIRDLKIERHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVRA 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 109157329 223 AAQQEGphcAPIIVHSSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVH 291
Cdd:cd14616  158 SRAHDN---TPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLH 223
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 67-294 3.03e-47

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: 160.57  E-value: 3.03e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  67 KNRYKTILPNPHSRVCLTsPDPDDPLSSYINANYIRGYGGEEKvYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEM 146
Cdd:cd14621   55 KNRYVNILPYDHSRVHLT-PVEGVPDSDYINASFINGYQEKNK-FIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKER 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 147 NE-KCTEYWPEEQV-AYDGVEITVQKVIHTEDYRLRLISLK------SGTEERGLKHYWFTSWPDQKTPDRAPPLLHLVR 218
Cdd:cd14621  133 KEcKCAQYWPDQGCwTYGNIRVSVEDVTVLVDYTVRKFCIQqvgdvtNKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLK 212

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109157329 219 EVEEAAQQegpHCAPIIVHSSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHVM 294
Cdd:cd14621  213 KVKNCNPQ---YAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQAL 285
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 69-294 4.98e-47

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


Pssm-ID: 350471 [Multi-domain]  Cd Length: 228  Bit Score: 157.90  E-value: 4.98e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  69 RYKTILPNPHSRVCLTSPDPDDPlSSYINANYIRGYGgEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEM-N 147
Cdd:cd14623    1 RVLQIIPYEFNRVIIPVKRGEEN-TDYVNASFIDGYR-QKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERgQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 148 EKCTEYWPEE-QVAYDGVEITVQKVIHTEDYRLR--LISLKSGTEERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAA 224
Cdd:cd14623   79 EKCAQYWPSDgSVSYGDITIELKKEEECESYTVRdlLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQ 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 225 QQEGPHcaPIIVHSSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHVM 294
Cdd:cd14623  159 QQSGNH--PITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVV 226
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 95-298 6.40e-47

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: 156.78  E-value: 6.40e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  95 YINANYIRGYGGEeKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITN-IEEMNEKCTEYWPEEQVAYDGVEITVQKVIH 173
Cdd:cd14558    1 YINASFIDGYWGP-KSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTElKEGDQEQCAQYWGDEKKTYGDIEVELKDTEK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 174 TEDYRLRLISLKS--GTEERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEE---AAQQEGPHCAPIIVHSSAGIGRTGCF 248
Cdd:cd14558   80 SPTYTVRVFEITHlkRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQklpYKNSKHGRSVPIVVHCSDGSSRTGIF 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 109157329 249 IATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFvhhvmsLYE 298
Cdd:cd14558  160 CALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQF------LYD 203
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 65-289 1.00e-46

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: 158.68  E-value: 1.00e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  65 VRKNRYKTILPNPHSRVCLTSPDPDDPlSSYINANYIRGYGGEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIE 144
Cdd:cd14610   45 VQKNRSLAVLPYDHSRIILKAENSHSH-SDYINASPIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCVVIVMLTPLA 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 145 EMN-EKCTEYWPEE-QVAYDGVEIT-VQKVIHTEDYRLRLISLKS--GTEERGLKHYWFTSWPDQKTPDRAPPLLHLVRE 219
Cdd:cd14610  124 ENGvKQCYHYWPDEgSNLYHIYEVNlVSEHIWCEDFLVRSFYLKNlqTNETRTVTQFHFLSWNDQGVPASTRSLLDFRRK 203

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109157329 220 VEEAAQqeGPHCaPIIVHSSAGIGRTGCFIATSICCQQLRQEGV-VDILKTTCQLRQDRGGMIQTCEQYQF 289
Cdd:cd14610  204 VNKCYR--GRSC-PIIVHCSDGAGRSGTYILIDMVLNKMAKGAKeIDIAATLEHLRDQRPGMVQTKEQFEF 271
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 67-289 1.66e-46

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: 156.40  E-value: 1.66e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  67 KNRYKTILPNPHSRVCLTSPDPDdplSSYINANYIRGYGGEEKvYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEM 146
Cdd:cd14545    1 LNRYRDRDPYDHDRSRVKLKQGD---NDYINASLVEVEEAKRS-YILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 147 NE-KCTEYWPEEQVA-----YDGVEITVQKVIHTEDYRLRLISL--KSGTEERGLKHYWFTSWPDQKTPDRAPPLLHLVR 218
Cdd:cd14545   77 GQiKCAQYWPQGEGNamifeDTGLKVTLLSEEDKSYYTVRTLELenLKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQ 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 109157329 219 EVEEAAQQEGPHcAPIIVHSSAGIGRTGCFIATSICCQQLRQEGV--VDILKTTCQLRQDRGGMIQTCEQYQF 289
Cdd:cd14545  157 KVRESGSLSSDV-GPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQLRF 228
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 95-291 4.88e-46

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: 154.46  E-value: 4.88e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  95 YINANYIRGYGGEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMNE-KCTEYWPEE---QVAYDGVEITVQK 170
Cdd:cd14539    1 YINASLIEDLTPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKqKVHRYWPTErgqALVYGAITVSLQS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 171 VIHTEDYRLRLISLKSGT--EERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQEGPHCAPIIVHSSAGIGRTGCF 248
Cdd:cd14539   81 VRTTPTHVERIISIQHKDtrLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYLQQRSLQTPIVVHCSSGVGRTGAF 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 109157329 249 IATSICCQQLRQE-GVVDILKTTCQLRQDRGGMIQTCEQYQFVH 291
Cdd:cd14539  161 CLLYAAVQEIEAGnGIPDLPQLVRKMRQQRKYMLQEKEHLKFCY 204
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 95-290 8.87e-46

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: 154.02  E-value: 8.87e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  95 YINANY----IRGYGGEEKvYIATQGPIVSTVADFWRMVWQEHTPIIVMIT-NIEEMNEKCTEYWPE--EQVAYDGVEIT 167
Cdd:cd14541    2 YINANYvnmeIPGSGIVNR-YIAAQGPLPNTCADFWQMVWEQKSTLIVMLTtLVERGRVKCHQYWPDlgETMQFGNLQIT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 168 VQKVIHTEDYRLRLISLK--SGTEERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEeaAQQEGPhCAPIIVHSSAGIGRT 245
Cdd:cd14541   81 CVSEEVTPSFAFREFILTntNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVR--QNRVGM-VEPTVVHCSAGIGRT 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 109157329 246 GCFIA--TSICCQQLRQEgvVDILKTTCQLRQDRGGMIQTCEQYQFV 290
Cdd:cd14541  158 GVLITmeTAMCLIEANEP--VYPLDIVRTMRDQRAMLIQTPSQYRFV 202
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 95-291 2.33e-45

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: 152.76  E-value: 2.33e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  95 YINANYIRGYGgEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMNE-KCTEYWPEEQVAYDG-VEITVQKVI 172
Cdd:cd14551    1 YINASYIDGYQ-EKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEkKCSQYWPDQGCWTYGnLRVRVEDTV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 173 HTEDYRLRLISLKSGTEERGLK------HYWFTSWPDQKTPDRAPPLLHLVREVEEAAQqegPHCAPIIVHSSAGIGRTG 246
Cdd:cd14551   80 VLVDYTTRKFCIQKVNRGIGEKrvrlvtQFHFTSWPDFGVPFTPIGMLKFLKKVKSANP---PRAGPIVVHCSAGVGRTG 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 109157329 247 CFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVH 291
Cdd:cd14551  157 TFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 31-291 4.56e-45

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 155.16  E-value: 4.56e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  31 ELHEKALDPFLLQAEFFEIPMNfvdpkeydipglVRKNRYKTILPNPHSRVCLTSPDpdDPLSSYINANYIRGYGgEEKV 110
Cdd:PHA02747  30 EHHQIILKPFDGLIANFEKPEN------------QPKNRYWDIPCWDHNRVILDSGG--GSTSDYIHANWIDGFE-DDKK 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 111 YIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMN--EKCTEYW-PEEQVAYD--GVEITVQKVIHTEDYRLRLISL- 184
Cdd:PHA02747  95 FIATQGPFAETCADFWKAVWQEHCSIIVMLTPTKGTNgeEKCYQYWcLNEDGNIDmeDFRIETLKTSVRAKYILTLIEIt 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 185 -KSGTEERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQEGPH-------CAPIIVHSSAGIGRTGCFIATSICCQ 256
Cdd:PHA02747 175 dKILKDSRKISHFQCSEWFEDETPSDHPDFIKFIKIIDINRKKSGKLfnpkdalLCPIVVHCSDGVGKTGIFCAVDICLN 254

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 109157329 257 QLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVH 291
Cdd:PHA02747 255 QLVKRKAICLAKTAEKIREQRHAGIMNFDDYLFIQ 289
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 65-289 5.99e-45

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: 154.04  E-value: 5.99e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  65 VRKNRYKTILPNPHSRVCLTSpDPDDPLSSYINANYIRGYGGEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIE 144
Cdd:cd14609   43 VKKNRNPDFVPYDHARIKLKA-ESNPSRSDYINASPIIEHDPRMPAYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLV 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 145 EMNEK-CTEYWPEEQVA-YDGVEIT-VQKVIHTEDYRLRLISLKS--GTEERGLKHYWFTSWPDQKTPDRAPPLLHLVRE 219
Cdd:cd14609  122 EDGVKqCDRYWPDEGSSlYHIYEVNlVSEHIWCEDFLVRSFYLKNvqTQETRTLTQFHFLSWPAEGIPSSTRPLLDFRRK 201

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109157329 220 VEEAAQqeGPHCaPIIVHSSAGIGRTGCFIATSICCQQLrQEGV--VDILKTTCQLRQDRGGMIQTCEQYQF 289
Cdd:cd14609  202 VNKCYR--GRSC-PIIVHCSDGAGRTGTYILIDMVLNRM-AKGVkeIDIAATLEHVRDQRPGMVRTKDQFEF 269
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 67-291 7.07e-45

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: 152.30  E-value: 7.07e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  67 KNRYKTILPNPHSRVCLT--SPDPDdplSSYINANYIRG-YGgeEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNI 143
Cdd:cd14602    1 KNRYKDILPYDHSRVELSliTSDED---SDYINANFIKGvYG--PRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACME 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 144 EEM-NEKCTEYWP---EEQVAYDGVEITVQKVIHTEDYRLRLISLKSGTEERGLKHYWFTSWPDQKTPDRAPPLLHLVRE 219
Cdd:cd14602   76 FEMgKKKCERYWAepgEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWD 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109157329 220 VEEAAQQEGPhcaPIIVHSSAGIGRTGCFIATSICCQQLRqEGVV----DILKTTCQLRQDRGGMIQTCEQYQFVH 291
Cdd:cd14602  156 VRCYQEDDSV---PICIHCSAGCGRTGVICAIDYTWMLLK-DGIIpenfSVFSLIQEMRTQRPSLVQTKEQYELVY 227
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 95-294 1.90e-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: 150.28  E-value: 1.90e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  95 YINANYIR-GYGGEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMIT-NIEEMNEKCTEYWPEeqvaydgveiTVQKVI 172
Cdd:cd14596    1 YINASYITmPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTrEVERGKVKCHRYWPE----------TLQEPM 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 173 HTEDYRLRL----------ISL-----KSGTEERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEeAAQQEGPhcapIIVH 237
Cdd:cd14596   71 ELENYQLRLenyqalqyfiIRIiklveKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMR-KVHNTGP----IVVH 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 109157329 238 SSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHVM 294
Cdd:cd14596  146 CSAGIGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVV 202
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 95-290 5.93e-44

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: 149.13  E-value: 5.93e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  95 YINANYIRGYGGEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEM-NEKCTEYWPEE-QVAYDGVEIT-VQKV 171
Cdd:cd14546    1 YINASTIYDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENgVKQCARYWPEEgSEVYHIYEVHlVSEH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 172 IHTEDYRLRLISLKS--GTEERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAaqQEGPHCaPIIVHSSAGIGRTGCFI 249
Cdd:cd14546   81 IWCDDYLVRSFYLKNlqTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKS--YRGRSC-PIVVHCSDGAGRTGTYI 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 109157329 250 ATSICCQQL-RQEGVVDILKTTCQLRQDRGGMIQTCEQYQFV 290
Cdd:cd14546  158 LIDMVLNRMaKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFV 199
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 95-291 5.73e-43

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: 146.40  E-value: 5.73e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  95 YINANYIRGYGgEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMNEKCTEYWPEEQVAYDGVeITVQKVIHT 174
Cdd:cd14556    1 YINAALLDSYK-QPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQSCPQYWPDEGSGTYGP-IQVEFVSTT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 175 EDYRL-----RLISLKSGTEE-RGLKHYWFTSWP-DQKTPDRAPPLLHLVREVEEAAQQEGPhcAPIIVHSSAGIGRTGC 247
Cdd:cd14556   79 IDEDVisrifRLQNTTRPQEGyRMVQQFQFLGWPrDRDTPPSKRALLKLLSEVEKWQEQSGE--GPIVVHCLNGVGRSGV 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 109157329 248 FIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVH 291
Cdd:cd14556  157 FCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 95-297 2.67e-42

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: 145.29  E-value: 2.67e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  95 YINANYIR-GYGGEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEE-MNEKCTEYWPEEQVAYDGV-----EIT 167
Cdd:cd14540    1 YINASHITaTVGGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEgGREKCFRYWPTLGGEHDALtfgeyKVS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 168 VQKVIHTEDY---RLRLISLKSGTeERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEE----AAQQEGPHC--APIIVHS 238
Cdd:cd14540   81 TKFSVSSGCYtttGLRVKHTLSGQ-SRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSvrrhTNQDVAGHNrnPPTLVHC 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 109157329 239 SAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHVMSLY 297
Cdd:cd14540  160 SAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQY 218
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 67-289 7.53e-42

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: 145.94  E-value: 7.53e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  67 KNRYKTILPNPHSRVCLTSPDPDdplssYINANYIRGYGGEEKvYIATQGPIVSTVADFWRMVWQEHTPIIVMITN-IEE 145
Cdd:cd14608   28 RNRYRDVSPFDHSRIKLHQEDND-----YINASLIKMEEAQRS-YILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRvMEK 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 146 MNEKCTEYWP---EEQVAYDGVEITVQKVihTED----YRLRLISLK--SGTEERGLKHYWFTSWPDQKTPDRAPPLLHL 216
Cdd:cd14608  102 GSLKCAQYWPqkeEKEMIFEDTNLKLTLI--SEDiksyYTVRQLELEnlTTQETREILHFHYTTWPDFGVPESPASFLNF 179

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109157329 217 VREVEEAAQQEgPHCAPIIVHSSAGIGRTGCFIATSICC---QQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQF 289
Cdd:cd14608  180 LFKVRESGSLS-PEHGPVVVHCSAGIGRSGTFCLADTCLllmDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRF 254
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 25-294 1.51e-41

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 146.33  E-value: 1.51e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  25 RVLQAEELHEKALDP----FLLQ--AEFFEIPM-----NFVDPKEydipglVRKNRYKTILPNPHSRVCLTS-------- 85
Cdd:PHA02746   7 EIFNAFDFFDKTNHAkfceFVLLehAEVMDIPIrgttnHFLKKEN------LKKNRFHDIPCWDHSRVVINAheslkmfd 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  86 ---PDP-------DDPLSSYINANYIRGYGgEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMNEKCTEYWP 155
Cdd:PHA02746  81 vgdSDGkkievtsEDNAENYIHANFVDGFK-EANKFICAQGPKEDTSEDFFKLISEHESQVIVSLTDIDDDDEKCFELWT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 156 EE---QVAYDGVEITVQKVIHTEDY---RLRLISLKSGTeERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEE------- 222
Cdd:PHA02746 160 KEedsELAFGRFVAKILDIIEELSFtktRLMITDKISDT-SREIHHFWFPDWPDNGIPTGMAEFLELINKVNEeqaelik 238

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109157329 223 AAQQEGPHCAPIIVHSSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHVM 294
Cdd:PHA02746 239 QADNDPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 34-294 7.40e-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: 140.90  E-value: 7.40e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  34 EKALDPFLLQAEFFEIPMNFVDP--KEYDIPGLVRKNRYKTILPNPHSRVCLTsPDPDDPlSSYINANYIR-GYGGEEKV 110
Cdd:cd14599    6 ERKLEEGMVFTEYEQIPKKKADGvfTTATLPENAERNRIREVVPYEENRVELV-PTKENN-TGYINASHIKvTVGGEEWH 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 111 YIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMNE-KCTEYWPE-----EQVAYDGVEITVQKVIHTEDYR---LRL 181
Cdd:cd14599   84 YIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRsKSHRYWPKlgskhSSATYGKFKVTTKFRTDSGCYAttgLKV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 182 ISLKSGtEERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQEGPHC-------APIIVHSSAGIGRTGCFIATSIC 254
Cdd:cd14599  164 KHLLSG-QERTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVRRHTNSMLdstkncnPPIVVHCSAGVGRTGVVILTELM 242

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 109157329 255 CQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHVM 294
Cdd:cd14599  243 IGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVL 282
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 67-290 1.91e-39

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: 139.60  E-value: 1.91e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  67 KNRYKTILPNPHSRVCLTSPDpddplsSYINANY----IRGYGGEEKvYIATQGPIVSTVADFWRMVWQEHTPIIVMITN 142
Cdd:cd14600   43 KNRYKDVLPYDATRVVLQGNE------DYINASYvnmeIPSANIVNK-YIATQGPLPHTCAQFWQVVWEQKLSLIVMLTT 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 143 IEEMNE-KCTEYWPE--EQVAYDGVEITVqkviHTEDY-------RLRLISLKSGtEERGLKHYWFTSWPDQKTPDRAPP 212
Cdd:cd14600  116 LTERGRtKCHQYWPDppDVMEYGGFRVQC----HSEDCtiayvfrEMLLTNTQTG-EERTVTHLQYVAWPDHGVPDDSSD 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 213 LLHLVREVEEAAQQEgphcAPIIVHSSAGIGRTGCFIA--TSICCQQLRQEgvVDILKTTCQLRQDRGGMIQTCEQYQFV 290
Cdd:cd14600  191 FLEFVNYVRSKRVEN----EPVLVHCSAGIGRTGVLVTmeTAMCLTERNQP--VYPLDIVRKMRDQRAMMVQTSSQYKFV 264
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 95-294 3.49e-39

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: 137.03  E-value: 3.49e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  95 YINANYIR-GYGGEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEM-NEKCTEYWP-----EEQVAYDGVEIT 167
Cdd:cd14598    1 YINASHIKvTVGGKEWDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGgREKSFRYWPrlgsrHNTVTYGRFKIT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 168 VQKVIHTEDYR---LRLISLKSGtEERGLKHYWFTSWPDQKTPDRAPPLLHLVREVE-------EAAQQEGPHcAPIIVH 237
Cdd:cd14598   81 TRFRTDSGCYAttgLKIKHLLTG-QERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQsvrrhtnSTIDPKSPN-PPVLVH 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 109157329 238 SSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHVM 294
Cdd:cd14598  159 CSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVL 215
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
52-289 3.84e-39

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 138.69  E-value: 3.84e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  52 NFVDPKEYDIPGLVRKNRYKTILPNPHSRVclTSPDPddplssYINANYIRGygGEEKVYIATQGPIVSTVADFWRMVWQ 131
Cdd:COG5599   30 SHNDPQYLQNINGSPLNRFRDIQPYKETAL--RANLG------YLNANYIQV--IGNHRYIATQYPLEEQLEDFFQMLFD 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 132 EHTPIIVMITNIEEM---NEKCTEYWPE-EQVAYDGVEITVQKVIHTED---YRLRLISLK-SGTEERGLKHYWFTSWPD 203
Cdd:COG5599  100 NNTPVLVVLASDDEIskpKVKMPVYFRQdGEYGKYEVSSELTESIQLRDgieARTYVLTIKgTGQKKIEIPVLHVKNWPD 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 204 QKTPDrAPPLLHLVREVEEAAQQEGPHCAPIIVHSSAGIGRTGCFIATsICCQQLRQEGV---VDILKTTCQLRQDRG-G 279
Cdd:COG5599  180 HGAIS-AEALKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIAC-LALSKSINALVqitLSVEEIVIDMRTSRNgG 257

                        250
                 ....*....|
gi 109157329 280 MIQTCEQYQF 289
Cdd:COG5599  258 MVQTSEQLDV 267
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 67-289 4.05e-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: 138.18  E-value: 4.05e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  67 KNRYKTILPNPHSRVCLTSPDPDdplssYINANYIRgYGGEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNI-EE 145
Cdd:cd14607   27 RNRYRDVSPYDHSRVKLQNTEND-----YINASLVV-IEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIvEK 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 146 MNEKCTEYWP---EEQVAYDGVEITVQKVihTED----YRLRLISL---KSGtEERGLKHYWFTSWPDQKTPDRAPPLLH 215
Cdd:cd14607  101 DSVKCAQYWPtdeEEVLSFKETGFSVKLL--SEDvksyYTVHLLQLeniNSG-ETRTISHFHYTTWPDFGVPESPASFLN 177

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109157329 216 LVREVEEAAQQeGPHCAPIIVHSSAGIGRTGCF--IATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQF 289
Cdd:cd14607  178 FLFKVRESGSL-SPEHGPAVVHCSAGIGRSGTFslVDTCLVLMEKKDPDSVDIKQVLLDMRKYRMGLIQTPDQLRF 252
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 95-289 9.29e-37

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: 130.28  E-value: 9.29e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  95 YINANYIRGYGGEE-KVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMNE--KCTEYWP---EEQVAYDGVEITV 168
Cdd:cd17658    1 YINASLVETPASESlPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYStaKCADYFPaeeNESREFGRISVTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 169 QKVIHTED-YRLRLISLKSGTEE---RGLKHYWFTSWPDQKTPDRAPPllhlVREVEEAAQQEGPHCAPIIVHSSAGIGR 244
Cdd:cd17658   81 KKLKHSQHsITLRVLEVQYIESEeppLSVLHIQYPEWPDHGVPKDTRS----VRELLKRLYGIPPSAGPIVVHCSAGIGR 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 109157329 245 TGCFIATSICCQQLRQEGV--VDILKTTCQLRQDRGGMIQTCEQYQF 289
Cdd:cd17658  157 TGAYCTIHNTIRRILEGDMsaVDLSKTVRKFRSQRIGMVQTQDQYIF 203
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 95-299 9.71e-37

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: 130.45  E-value: 9.71e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  95 YINANYIR---GYGGEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMI-TNIEEMNEKCTEYWPE--EQVAYDGVEITV 168
Cdd:cd14601    2 YINANYINmeiPSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLtTQVERGRVKCHQYWPEpsGSSSYGGFQVTC 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 169 QKVIHTEDYRLRLISLKS--GTEERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEeaaQQEGPHCAPIIVHSSAGIGRTG 246
Cdd:cd14601   82 HSEEGNPAYVFREMTLTNleKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVR---NKRAGKDEPVVVHCSAGIGRTG 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 109157329 247 CFIA--TSICCQQLRQEGV-VDILKTtcqLRQDRGGMIQTCEQYQFV-HHVMSLYEK 299
Cdd:cd14601  159 VLITmeTAMCLIECNQPVYpLDIVRT---MRDQRAMMIQTPSQYRFVcEAILKVYEE 212
PHA02738 PHA02738
hypothetical protein; Provisional
 68-297 1.16e-36

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 133.51  E-value: 1.16e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  68 NRYKTILPNPHSRVCLTSpdpDDPLSSYINANYIRGYGGEEKvYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEE-M 146
Cdd:PHA02738  53 NRYLDAVCFDHSRVILPA---ERNRGDYINANYVDGFEYKKK-FICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKEnG 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 147 NEKCTEYWPE-EQ--VAYDGVEITVQKVIHTEDYRLRLISLKSGTEE-RGLKHYWFTSWPDQKTPDRAPPLLHLVREVEE 222
Cdd:PHA02738 129 REKCFPYWSDvEQgsIRFGKFKITTTQVETHPHYVKSTLLLTDGTSAtQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVRQ 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 223 AAQQ----------EGPHCAPIIVHSSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHH 292
Cdd:PHA02738 209 CQKElaqeslqighNRLQPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYR 288


                 ....*
gi 109157329 293 VMSLY 297
Cdd:PHA02738 289 AVKRY 293
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
193-294 4.69e-36

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 125.16  E-value: 4.69e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329   193 LKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQEGPHcAPIIVHSSAGIGRTGCFIATSICCQQLRQE-GVVDILKTTC 271
Cdd:smart00404   2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESS-GPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                           90       100
                   ....*....|....*....|...
gi 109157329   272 QLRQDRGGMIQTCEQYQFVHHVM 294
Cdd:smart00404  81 ELRSQRPGMVQTEEQYLFLYRAL 103
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 193-294 4.69e-36

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: 125.16  E-value: 4.69e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329   193 LKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQEGPHcAPIIVHSSAGIGRTGCFIATSICCQQLRQE-GVVDILKTTC 271
Cdd:smart00012   2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESS-GPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                           90       100
                   ....*....|....*....|...
gi 109157329   272 QLRQDRGGMIQTCEQYQFVHHVM 294
Cdd:smart00012  81 ELRSQRPGMVQTEEQYLFLYRAL 103
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 66-302 8.27e-34

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 125.50  E-value: 8.27e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  66 RKNRYKTILPNPHSRVCLTSpdpDDPLSSYINANYIRGYGGEEKvYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEE 145
Cdd:PHA02742  54 KKCRYPDAPCFDRNRVILKI---EDGGDDFINASYVDGHNAKGR-FICTQAPLEETALDFWQAIFQDQVRVIVMITKIME 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 146 MN-EKCTEYW-PEEQ--VAYDGVEITVQKVIHTEDYR---LRLISLKSGTEeRGLKHYWFTSWPDQKTPDRAPPLLHLVR 218
Cdd:PHA02742 130 DGkEACYPYWmPHERgkATHGEFKIKTKKIKSFRNYAvtnLCLTDTNTGAS-LDIKHFAYEDWPHGGLPRDPNKFLDFVL 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 219 EVEEA--------AQQEGPHCAPIIVHSSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFV 290
Cdd:PHA02742 209 AVREAdlkadvdiKGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIFC 288

                        250
                 ....*....|..
gi 109157329 291 HHVMSLYEKQLS 302
Cdd:PHA02742 289 YFIVLIFAKLMA 300
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 95-289 5.86e-33

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: 120.12  E-value: 5.86e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  95 YINANYIRGYGgEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEmNEKCTEYWPEEQVAYDGVEITV------ 168
Cdd:cd14550    1 YINASYLQGYR-RSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNEL-NEDEPIYWPTKEKPLECETFKVtlsged 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 169 -QKVIHTEDYRLRLISLKSGTEERGL--KHYWFTSWPDQKTPDRAppLLHLVREV-EEAAQQEGphcaPIIVHSSAGIGR 244
Cdd:cd14550   79 hSCLSNEIRLIVRDFILESTQDDYVLevRQFQCPSWPNPCSPIHT--VFELINTVqEWAQQRDG----PIVVHDRYGGVQ 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 109157329 245 TGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQF 289
Cdd:cd14550  153 AATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQF 197
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 95-294 1.33e-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: 111.62  E-value: 1.33e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  95 YINANYIRGYGgEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMNEKCTEYWP--EEQVAYDGVEITVQKVI 172
Cdd:cd17669    1 YINASYIMGYY-QSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFVYWPnkDEPINCETFKVTLIAEE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 173 HT-----EDYRLRLISLKSGTEERGL--KHYWFTSWPDQKTP-DRAPPLLHLVRevEEAAQQEGphcaPIIVHSSAGIGR 244
Cdd:cd17669   80 HKclsneEKLIIQDFILEATQDDYVLevRHFQCPKWPNPDSPiSKTFELISIIK--EEAANRDG----PMIVHDEHGGVT 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 109157329 245 TGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHVM 294
Cdd:cd17669  154 AGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAI 203
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 95-293 4.25e-29

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: 110.50  E-value: 4.25e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  95 YINANYIRGYGgEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMnEKCTEYWPEE-QVAYDGVEITVQKVIH 173
Cdd:cd14634    1 YINAALMDSHK-QPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDAA-QLCMQYWPEKtSCCYGPIQVEFVSADI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 174 TEDYRLRLISL----KSGTEERGLKHYWFTSWPDQK-TPDRAPPLLHLVREVEEAAQQEGPHCAPIIVHSSAGIGRTGCF 248
Cdd:cd14634   79 DEDIISRIFRIcnmaRPQDGYRIVQHLQYIGWPAYRdTPPSKRSILKVVRRLEKWQEQYDGREGRTVVHCLNGGGRSGTF 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 109157329 249 IATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHV 293
Cdd:cd14634  159 CAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEV 203
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 95-294 4.61e-26

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: 102.45  E-value: 4.61e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  95 YINANYIRGYGGEEKvYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMNEKCTEYWPEEQVAYDGVEITV------ 168
Cdd:cd17670    1 YINASYIMGYYRSNE-FIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDEFVYWPSREESMNCEAFTVtliskd 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 169 --------QKVIHteDYRLRLISLKSGTEERglkHYWFTSWPDQKTPDRAP-PLLHLVRevEEAAQQEGphcaPIIVHSS 239
Cdd:cd17670   80 rlclsneeQIIIH--DFILEATQDDYVLEVR---HFQCPKWPNPDAPISSTfELINVIK--EEALTRDG----PTIVHDE 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 109157329 240 AGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHVM 294
Cdd:cd17670  149 FGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAM 203
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 95-293 6.40e-25

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: 99.38  E-value: 6.40e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  95 YINANYIRGYGgEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMnEKCTEYWPEEQVAYDG-VEITVQKVIH 173
Cdd:cd14635    1 YINAALMDSYK-QPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPA-QLCPQYWPENGVHRHGpIQVEFVSADL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 174 TEDYRLRLISLKSGTEE----RGLKHYWFTSWPDQK-TPDRAPPLLHLVREVEEAAQQEGPHCAPIIVHSSAGIGRTGCF 248
Cdd:cd14635   79 EEDIISRIFRIYNAARPqdgyRMVQQFQFLGWPMYRdTPVSKRSFLKLIRQVDKWQEEYNGGEGRTVVHCLNGGGRSGTF 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 109157329 249 IATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHV 293
Cdd:cd14635  159 CAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEV 203
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 95-293 1.31e-23

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: 95.75  E-value: 1.31e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  95 YINANYIRGYGgEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMNEK--CTEYWPEEQVA-YDGVEITVQKV 171
Cdd:cd14637    1 YINAALTDSYT-RSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwpCLQYWPEPGLQqYGPMEVEFVSG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 172 IHTEDYRLRLISLKSGT----EERGLKHYWFTSW-PDQKTPDRAPPLLHLVREVEEAAQQEGPHcaPIIVHSSAGIGRTG 246
Cdd:cd14637   80 SADEDIVTRLFRVQNITrlqeGHLMVRHFQFLRWsAYRDTPDSKKAFLHLLASVEKWQRESGEG--RTVVHCLNGGGRSG 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 109157329 247 CFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHV 293
Cdd:cd14637  158 TYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEI 204
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 95-295 5.34e-23

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: 94.32  E-value: 5.34e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  95 YINANYIRGYGgEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEeMNEKCTEYWPEE-QVAYDGVEITVQKVIH 173
Cdd:cd14636    1 YINAALMDSYR-QPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVD-LAQGCPQYWPEEgMLRYGPIQVECMSCSM 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 174 TEDYRLRLISLKSGTEERG----LKHYWFTSWPDQK-TPDRAPPLLHLVREVEEAAQQEGPHCAPIIVHSSAGIGRTGCF 248
Cdd:cd14636   79 DCDVISRIFRICNLTRPQEgylmVQQFQYLGWASHReVPGSKRSFLKLILQVEKWQEECDEGEGRTIIHCLNGGGRSGMF 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 109157329 249 IATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHVMS 295
Cdd:cd14636  159 CAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVAL 205
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 78-300 9.96e-18

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 81.55  E-value: 9.96e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  78 HSRVCLTSPDpddplsSYINANYIRGYGGEEKvYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEmnEKC-TEYWPE 156
Cdd:PHA02740  67 HRRIKLFNDE------KVLDARFVDGYDFEQK-FICIINLCEDACDKFLQALSDNKVQIIVLISRHAD--KKCfNQFWSL 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 157 EQ---VAYDGVEITVQKVIHTEDYRLRLISL--KSGtEERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQEGPH- 230
Cdd:PHA02740 138 KEgcvITSDKFQIETLEIIIKPHFNLTLLSLtdKFG-QAQKISHFQYTAWPADGFSHDPDAFIDFFCNIDDLCADLEKHk 216

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109157329 231 ----CAPIIVHSSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHVMSLYEKQ 300
Cdd:PHA02740 217 adgkIAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLIAAYLKE 290
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 76-288 4.66e-12

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: 64.34  E-value: 4.66e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329  76 NPHSRVCLTSPDPDDPLssyINANYIRGygGEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMNEK-CTEYW 154
Cdd:cd14559    1 NRFTNIQTRVSTPVGKN---LNANRVQI--GNKNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKgLPPYF 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 155 -PEEQvaYDGVEITVQKV--------IHTEDYRLRlisLKSGTEERGLKHYWFTSWPDQKTPDrAPPLLHLVREVEEAAQ 225
Cdd:cd14559   76 rQSGT--YGSVTVKSKKTgkdelvdgLKADMYNLK---ITDGNKTITIPVVHVTNWPDHTAIS-SEGLKELADLVNKSAE 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 109157329 226 Q-----EGPHCAPI--------IVHSSAGIGRTGCFIATSICCQQLRQEGVVDILKttcQLRQDRGG-MIQTCEQYQ 288
Cdd:cd14559  150 EkrnfyKSKGSSAIndknkllpVIHCRAGVGRTGQLAAAMELNKSPNNLSVEDIVS---DMRTSRNGkMVQKDEQLD 223
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 214-292 1.27e-10

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: 57.74  E-value: 1.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 214 LHLVREVEEAAQQEGPHCAPIIVHSSAGIGRTGCFIATSICCQQLRqeGVVDILkttCQLRQDRGGMI-QTCEQYQFVHH 292
Cdd:cd14494   39 LAMVDRFLEVLDQAEKPGEPVLVHCKAGVGRTGTLVACYLVLLGGM--SAEEAV---RIVRLIRPGGIpQTIEQLDFLIK 113
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
189-292 1.93e-06

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 46.50  E-value: 1.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 189 EERGLKHYWFTsWPDQKTPDRAPpLLHLVREVEEAAQQEGPhcapIIVHSSAGIGRTGCFIAtsiccQQLRQEGV--VDI 266
Cdd:COG2453   44 EEAGLEYLHLP-IPDFGAPDDEQ-LQEAVDFIDEALREGKK----VLVHCRGGIGRTGTVAA-----AYLVLLGLsaEEA 112

                         90       100
                 ....*....|....*....|....*.
gi 109157329 267 LKttcQLRQDRGGMIQTCEQYQFVHH 292
Cdd:COG2453  113 LA---RVRAARPGAVETPAQRAFLER 135
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 178-291 1.05e-05

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: 44.95  E-value: 1.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 178 RLRLISLKSGTEERGLKHYWFtSWPDQKTPDRAPPLLHLVREVEEAAQQeGPHcapIIVHSSAGIGRTGCFIAtsiCCQQ 257
Cdd:cd14505   58 ELGVPDLLEQYQQAGITWHHL-PIPDGGVPSDIAQWQELLEELLSALEN-GKK---VLIHCKGGLGRTGLIAA---CLLL 129

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 109157329 258 LRQEGVV--DILKttcQLRQDRGGMIQTCEQYQFVH 291
Cdd:cd14505  130 ELGDTLDpeQAIA---AVRALRPGAIQTPKQENFLH 162
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 190-291 4.21e-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: 40.80  E-value: 4.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 190 ERGLKHYWFtSWPDQKTPDRAPpLLHLVReVEEAAQQEGphcAPIIVHSSAGIGRTGCFIATS-ICCQQLRQEGVVDIlk 268
Cdd:cd14506   74 RAGIYFYNF-GWKDYGVPSLTT-ILDIVK-VMAFALQEG---GKVAVHCHAGLGRTGVLIACYlVYALRMSADQAIRL-- 145

                         90       100
                 ....*....|....*....|...
gi 109157329 269 ttcqLRQDRGGMIQTCEQYQFVH 291
Cdd:cd14506  146 ----VRSKRPNSIQTRGQVLCVR 164
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 189-300 1.84e-03

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


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 38.03  E-value: 1.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109157329 189 EERGLKHYWFtswpdqKTPDRAPPLLHLVRE----VEEA-AQQEgphcaPIIVHSSAGIGRTGCFIAtsiCcqQLRQEGV 263
Cdd:cd14504   46 TCPGLRYHHI------PIEDYTPPTLEQIDEfldiVEEAnAKNE-----AVLVHCLAGKGRTGTMLA---C--YLVKTGK 109

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 109157329 264 VDILKTTCQLRQDRGGMIQTCEQYQFVhhvmSLYEKQ 300
Cdd:cd14504  110 ISAVDAINEIRRIRPGSIETSEQEKFV----IQFAKT 142
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH