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Conserved domains on  [gi|74216145|dbj|BAE23734|]
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unnamed protein product [Mus musculus]

Protein Classification

dual specificity protein phosphatase family protein; phosphatase PAP2/dual specificity phosphatase family protein( domain architecture ID 13134036)

dual specificity protein phosphatase family protein such as dual specificity phosphatases, which dephosphorylate phosphotyrosine, phosphoserine, and phosphothreonine residues, as well as tyrosine-specific protein phosphatases| bifunctional phosphatase PAP2/dual specificity phosphatase (DSP) family protein containing a C-terminal DSP domain that may dephosphorylate phosphotyrosine, phosphoserine, and phosphothreonine residues in target proteins, and an N-terminal phosphatase PAP2 domain that may be a histidine phosphatase that catalyzes the dephosphorylation of phospholipids

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTP_DSP_cys super family cl28904
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 713-932 4.30e-173

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


The actual alignment was detected with superfamily member cd14610:

Pssm-ID: 475123 [Multi-domain]  Cd Length: 283  Bit Score: 503.82  E-value: 4.30e-173
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 713 TGHMILAYMEDHLKNKNRLEKEWEALCAYQAEPNSSLVAQREENAPKNRSLAVLTYDHSRILLKSQNSHGSSDYINASPI 792
Cdd:cd14610   1 TGHMILSYMEDHLKNKNRLEKEWEALCAYQAEPNATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 793 MDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNLYHVYEVNLVSEHIWCQDFL 872
Cdd:cd14610  81 MDHDPRNPAYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSNLYHIYEVNLVSEHIWCEDFL 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 873 VRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCS 932
Cdd:cd14610 161 VRSFYLKNLQTNETRTVTQFHFLSWNDQGVPASTRSLLDFRRKVNKCYRGRSCPIIVHCS 220
Receptor_IA-2 pfam11548
Protein-tyrosine phosphatase receptor IA-2; IA-2 is a protein-tyrosine phosphatase receptor ...
 495-583 1.71e-43

Protein-tyrosine phosphatase receptor IA-2; IA-2 is a protein-tyrosine phosphatase receptor that upon exocytosis, the cytoplasmic domain is cleaved and moves to the nucleus where it enhances transcription of the insulin gene. The mature exodomain of IA-2 participates in adhesion to the extracellular matrix and is self-proteolyzed in vitro by reactive oxygen species which may be a new shedding mechanism.


:

Pssm-ID: 463293  Cd Length: 89  Bit Score: 152.39  E-value: 1.71e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145   495 EQQGYILTGNNPLSPEKGKQLMDQVAHILRVPSSFFADIKVLGPAVTFKVSANIQNMTTADVIKAAADNKDQLEKATGLT 574
Cdd:pfam11548   1 EEYGYIVTDNDPLSWEEGLRLMEKVAELLHLPMSSFADIRVLGPAVTFKVRANNKNLTAADVAKAAVDIKDKLEKETGLK 80


                  ....*....
gi 74216145   575 ILQSGIRPK 583
Cdd:pfam11548  81 ILQAGVGDK 89
RESP18 super family cl20829
RESP18 domain; This domain is found in the glucocorticoid-responsive protein regulated ...
 80-126 2.24e-03

RESP18 domain; This domain is found in the glucocorticoid-responsive protein regulated endocrine-specific protein 18 (RESP18) and in the N-terminal extracellular region of receptor-type tyrosine-protein phosphatases containing the protein-tyrosine phosphatase receptor IA-2 domain (pfam11548).


The actual alignment was detected with superfamily member pfam14948:

Pssm-ID: 464394  Cd Length: 103  Bit Score: 38.66  E-value: 2.24e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 74216145    80 HLKVTLQKLSRTGFTWQDDYTQRVIAQELANLPK-----AYLWHGEASGPAR 126
Cdd:pfam14948  23 HLQVVLHQIVPQGLFWKDDLTQDVMTQKMEHISRlhpqdPCLKDGKAVFPTR 74
 
Name Accession Description Interval E-value
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 713-932 4.30e-173

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: 503.82  E-value: 4.30e-173
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 713 TGHMILAYMEDHLKNKNRLEKEWEALCAYQAEPNSSLVAQREENAPKNRSLAVLTYDHSRILLKSQNSHGSSDYINASPI 792
Cdd:cd14610   1 TGHMILSYMEDHLKNKNRLEKEWEALCAYQAEPNATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 793 MDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNLYHVYEVNLVSEHIWCQDFL 872
Cdd:cd14610  81 MDHDPRNPAYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSNLYHIYEVNLVSEHIWCEDFL 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 873 VRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCS 932
Cdd:cd14610 161 VRSFYLKNLQTNETRTVTQFHFLSWNDQGVPASTRSLLDFRRKVNKCYRGRSCPIIVHCS 220
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
731-932 8.81e-80

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 259.51  E-value: 8.81e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145    731 LEKEWEALCAYQAEPNSSLVAQREENAPKNRSLAVLTYDHSRILLKSQNsHGSSDYINASPIMDHDPRNpAYIATQGPLP 810
Cdd:smart00194   2 LEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPP-GEGSDYINASYIDGPNGPK-AYIATQGPLP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145    811 ATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEG--SNLYHVYEVNLVSEHIwCQDFLVRSFYLKNLQTNETRT 888
Cdd:smart00194  80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEgePLTYGDITVTLKSVEK-VDDYTIRTLEVTNTGCSETRT 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 74216145    889 VTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCS 932
Cdd:smart00194 159 VTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCS 202
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
756-932 1.47e-75

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 247.16  E-value: 1.47e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145   756 NAPKNRSLAVLTYDHSRILLKSQNshGSSDYINASPIMDHdPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLS 835
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTGDP--GPSDYINASYIDGY-KKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145   836 ENGVRQCHHYWPD--EGSNLYHVYEVNLVSEHIWCQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFR 913
Cdd:pfam00102  78 EKGREKCAQYWPEeeGESLEYGDFTVTLKKEKEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLL 157

                         170       180
                  ....*....|....*....|
gi 74216145   914 RKVNKCY-RGRSCPIIVHCS 932
Cdd:pfam00102 158 RKVRKSSlDGRSGPIVVHCS 177
Receptor_IA-2 pfam11548
Protein-tyrosine phosphatase receptor IA-2; IA-2 is a protein-tyrosine phosphatase receptor ...
 495-583 1.71e-43

Protein-tyrosine phosphatase receptor IA-2; IA-2 is a protein-tyrosine phosphatase receptor that upon exocytosis, the cytoplasmic domain is cleaved and moves to the nucleus where it enhances transcription of the insulin gene. The mature exodomain of IA-2 participates in adhesion to the extracellular matrix and is self-proteolyzed in vitro by reactive oxygen species which may be a new shedding mechanism.


Pssm-ID: 463293  Cd Length: 89  Bit Score: 152.39  E-value: 1.71e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145   495 EQQGYILTGNNPLSPEKGKQLMDQVAHILRVPSSFFADIKVLGPAVTFKVSANIQNMTTADVIKAAADNKDQLEKATGLT 574
Cdd:pfam11548   1 EEYGYIVTDNDPLSWEEGLRLMEKVAELLHLPMSSFADIRVLGPAVTFKVRANNKNLTAADVAKAAVDIKDKLEKETGLK 80


                  ....*....
gi 74216145   575 ILQSGIRPK 583
Cdd:pfam11548  81 ILQAGVGDK 89
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 752-932 5.68e-29

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 118.18  E-value: 5.68e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145  752 QREENAPKNRSLAVLTYDHSRILLKSQnSHGSSDYINASPImDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVML 831
Cdd:PHA02747  47 EKPENQPKNRYWDIPCWDHNRVILDSG-GGSTSDYIHANWI-DGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVML 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145  832 TPLSE-NGVRQCHHYW-PDEGSNL----YHVYEVNLVsehiwcqdflVRSFYLKNL------QTNETRTVTQFHFLSWYD 899
Cdd:PHA02747 125 TPTKGtNGEEKCYQYWcLNEDGNIdmedFRIETLKTS----------VRAKYILTLieitdkILKDSRKISHFQCSEWFE 194

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 74216145  900 QGVPSSTRSLLDF-------RRKVNKCYRGRS---CPIIVHCS 932
Cdd:PHA02747 195 DETPSDHPDFIKFikiidinRKKSGKLFNPKDallCPIVVHCS 237
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
729-932 2.00e-22

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 98.24  E-value: 2.00e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 729 NRLEKEWEALcAYQAEPNSSLvaQREENAPKNRSLAVLTYDHSRIllksqnshGSSD-YINASPIMDHDPRNpaYIATQG 807
Cdd:COG5599  18 SRLSTLTNEL-APSHNDPQYL--QNINGSPLNRFRDIQPYKETAL--------RANLgYLNANYIQVIGNHR--YIATQY 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 808 PLPATVADFWQMVWESGCAVIVMLTPLSENGVRQ--CHHYWPDEGSNLYHVYEVNLVSEHIWCQDFLVRSFYLKNLQTN- 884
Cdd:COG5599  85 PLEEQLEDFFQMLFDNNTPVLVVLASDDEISKPKvkMPVYFRQDGEYGKYEVSSELTESIQLRDGIEARTYVLTIKGTGq 164

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 74216145 885 ETRTVTQFHFLSWYDQGVPSST--RSLLDFRRKVNKCYRGRSCPIIVHCS 932
Cdd:COG5599 165 KKIEIPVLHVKNWPDHGAISAEalKNLADLIDKKEKIKDPDKLLPVVHCR 214
RESP18 pfam14948
RESP18 domain; This domain is found in the glucocorticoid-responsive protein regulated ...
 80-126 2.24e-03

RESP18 domain; This domain is found in the glucocorticoid-responsive protein regulated endocrine-specific protein 18 (RESP18) and in the N-terminal extracellular region of receptor-type tyrosine-protein phosphatases containing the protein-tyrosine phosphatase receptor IA-2 domain (pfam11548).


Pssm-ID: 464394  Cd Length: 103  Bit Score: 38.66  E-value: 2.24e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 74216145    80 HLKVTLQKLSRTGFTWQDDYTQRVIAQELANLPK-----AYLWHGEASGPAR 126
Cdd:pfam14948  23 HLQVVLHQIVPQGLFWKDDLTQDVMTQKMEHISRlhpqdPCLKDGKAVFPTR 74
 
Name Accession Description Interval E-value
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 713-932 4.30e-173

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: 503.82  E-value: 4.30e-173
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 713 TGHMILAYMEDHLKNKNRLEKEWEALCAYQAEPNSSLVAQREENAPKNRSLAVLTYDHSRILLKSQNSHGSSDYINASPI 792
Cdd:cd14610   1 TGHMILSYMEDHLKNKNRLEKEWEALCAYQAEPNATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 793 MDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNLYHVYEVNLVSEHIWCQDFL 872
Cdd:cd14610  81 MDHDPRNPAYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSNLYHIYEVNLVSEHIWCEDFL 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 873 VRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCS 932
Cdd:cd14610 161 VRSFYLKNLQTNETRTVTQFHFLSWNDQGVPASTRSLLDFRRKVNKCYRGRSCPIIVHCS 220
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 715-932 5.56e-143

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: 425.99  E-value: 5.56e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 715 HMILAYMEDHLKNKNRLEKEWEALCAYQAEPNSSLVAQREENAPKNRSLAVLTYDHSRILLKSQNSHGSSDYINASPIMD 794
Cdd:cd14609   1 HMILAYMEDHLRNRDRLAKEWQALCAYQAEPNTCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPIIE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 795 HDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNLYHVYEVNLVSEHIWCQDFLVR 874
Cdd:cd14609  81 HDPRMPAYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHIYEVNLVSEHIWCEDFLVR 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 74216145 875 SFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCS 932
Cdd:cd14609 161 SFYLKNVQTQETRTLTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCYRGRSCPIIVHCS 218
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 786-932 6.38e-108

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: 332.10  E-value: 6.38e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 786 YINASPIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNLYHVYEVNLVSEH 865
Cdd:cd14546   1 YINASTIYDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEVYHIYEVHLVSEH 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74216145 866 IWCQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCS 932
Cdd:cd14546  81 IWCDDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSCPIVVHCS 147
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
731-932 8.81e-80

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 259.51  E-value: 8.81e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145    731 LEKEWEALCAYQAEPNSSLVAQREENAPKNRSLAVLTYDHSRILLKSQNsHGSSDYINASPIMDHDPRNpAYIATQGPLP 810
Cdd:smart00194   2 LEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPP-GEGSDYINASYIDGPNGPK-AYIATQGPLP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145    811 ATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEG--SNLYHVYEVNLVSEHIwCQDFLVRSFYLKNLQTNETRT 888
Cdd:smart00194  80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEgePLTYGDITVTLKSVEK-VDDYTIRTLEVTNTGCSETRT 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 74216145    889 VTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCS 932
Cdd:smart00194 159 VTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCS 202
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
756-932 1.47e-75

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 247.16  E-value: 1.47e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145   756 NAPKNRSLAVLTYDHSRILLKSQNshGSSDYINASPIMDHdPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLS 835
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTGDP--GPSDYINASYIDGY-KKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145   836 ENGVRQCHHYWPD--EGSNLYHVYEVNLVSEHIWCQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFR 913
Cdd:pfam00102  78 EKGREKCAQYWPEeeGESLEYGDFTVTLKKEKEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLL 157

                         170       180
                  ....*....|....*....|
gi 74216145   914 RKVNKCY-RGRSCPIIVHCS 932
Cdd:pfam00102 158 RKVRKSSlDGRSGPIVVHCS 177
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 786-932 3.51e-60

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: 203.67  E-value: 3.51e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 786 YINASPIMDHDPRNpAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSN--LYHVYEVNLVS 863
Cdd:cd00047   1 YINASYIDGYRGPK-EYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKplEYGDITVTLVS 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74216145 864 EHIwCQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCS 932
Cdd:cd00047  80 EEE-LSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCS 147
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 756-932 2.56e-55

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: 192.58  E-value: 2.56e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 756 NAPKNRSLAVLTYDHSRILLKSQNSHGSSDYINASpIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLS 835
Cdd:cd14543  29 NQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINAN-FMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLVIVMTTRVV 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 836 ENGVRQCHHYWPDEGSNLYHVYEVNLVSEHIWC-QDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRR 914
Cdd:cd14543 108 ERGRVKCGQYWPLEEGSSLRYGDLTVTNLSVENkEHYKKTTLEIHNTETDESRQVTHFQFTSWPDFGVPSSAAALLDFLG 187

                       170       180       190
                ....*....|....*....|....*....|..
gi 74216145 915 KVnKCYRGRSC--------------PIIVHCS 932
Cdd:cd14543 188 EV-RQQQALAVkamgdrwkghppgpPIVVHCS 218
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 754-932 1.45e-54

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: 189.53  E-value: 1.45e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 754 EENAPKNRSLAVLTYDHSRILLKSQNSHGSSDYINASpIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTP 833
Cdd:cd14553   1 EVNKPKNRYANVIAYDHSRVILQPIEGVPGSDYINAN-YCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 834 LSENGVRQCHHYWPDEGSNLYHVYEVNLVsEHIWCQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFR 913
Cdd:cd14553  80 LEERSRVKCDQYWPTRGTETYGLIQVTLL-DTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFL 158

                       170
                ....*....|....*....
gi 74216145 914 RKVNKCYRGRSCPIIVHCS 932
Cdd:cd14553 159 RRVKACNPPDAGPIVVHCS 177
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 756-932 7.96e-52

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: 181.57  E-value: 7.96e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 756 NAPKNRSLAVLTYDHSRILLKSQNSHGSSDYINASPIMDHDPRNpAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLS 835
Cdd:cd14554   6 NKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRG-AYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKLR 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 836 ENGVRQCHHYWPDEGSNLYHVYEVNLVSEHIWCQdFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRK 915
Cdd:cd14554  85 EMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQ-YILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQ 163

                       170
                ....*....|....*....
gi 74216145 916 VNKCYR--GRSCPIIVHCS 932
Cdd:cd14554 164 VHKTKEqfGQEGPITVHCS 182
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 765-932 4.58e-50

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: 176.01  E-value: 4.58e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 765 VLTYDHSRILLKSQNSHGSSDYINASPIMD-HDPRNpaYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCH 843
Cdd:cd14548   5 ILPYDHSRVKLIPINEEEGSDYINANYIPGyNSPRE--FIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVKCD 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 844 HYWP-DEGSNLYHVYEVNLVSEHIwCQDFLVRSFYLKNLQtnETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVnKCYRG 922
Cdd:cd14548  83 HYWPfDQDPVYYGDITVTMLSESV-LPDWTIREFKLERGD--EVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLV-RDYIK 158

                       170
                ....*....|.
gi 74216145 923 RSC-PIIVHCS 932
Cdd:cd14548 159 QEKgPTIVHCS 169
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 760-932 9.34e-48

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: 170.00  E-value: 9.34e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 760 NRSLAVLTYDHSRILLKSQNsHGSSDYINASpIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGV 839
Cdd:cd14615   1 NRYNNVLPYDISRVKLSVQS-HSTDDYINAN-YMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 840 RQCHHYWPDEGSNLYHVYEVNLVSEhIWCQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKC 919
Cdd:cd14615  79 TKCEEYWPSKQKKDYGDITVTMTSE-IVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVREY 157

                       170
                ....*....|....*
gi 74216145 920 YRG--RSCPIIVHCS 932
Cdd:cd14615 158 MKQnpPNSPILVHCS 172
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 785-932 1.05e-47

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: 169.05  E-value: 1.05e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 785 DYINASPIMDHDPRNPA---YIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEG-SNLYHVYEVN 860
Cdd:cd14541   1 DYINANYVNMEIPGSGIvnrYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGeTMQFGNLQIT 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74216145 861 LVSEHIwCQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCS 932
Cdd:cd14541  81 CVSEEV-TPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCS 151
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 786-932 3.09e-47

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: 167.53  E-value: 3.09e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 786 YINASPImDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNLYHVYEVNLVSEH 865
Cdd:cd14549   1 YINANYV-DGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTETYGNIQVTLLSTE 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74216145 866 IWCQdFLVRSFYLKNLQ------TNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCS 932
Cdd:cd14549  80 VLAT-YTVRTFSLKNLKlkkvkgRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCS 151
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 786-932 3.45e-47

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: 167.43  E-value: 3.45e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 786 YINASPI-MDHDPRNpAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNLYH-VYEVNLVS 863
Cdd:cd18533   1 YINASYItLPGTSSK-RYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGEYgDLTVELVS 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74216145 864 EH-IWCQDFLVRSFYLKNlQTNETRTVTQFHFLSWYDQGVPSSTRSLL---DFRRKVNKCYRGRScPIIVHCS 932
Cdd:cd18533  80 EEeNDDGGFIVREFELSK-EDGKVKKVYHIQYKSWPDFGVPDSPEDLLtliKLKRELNDSASLDP-PIIVHCS 150
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 730-932 6.23e-47

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: 169.06  E-value: 6.23e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 730 RLEKEWEALCAYQ--AEPNSSLvaqrEENAPKNRSLAVLTYDHSRILLKSQNSHGSSDYINASPIMDHDPRNpAYIATQG 807
Cdd:cd14626  17 KFSQEYESIDPGQqfTWENSNL----EVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGYRKQN-AYIATQG 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 808 PLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNLYHVYEVNLVsEHIWCQDFLVRSFYLKNLQTNETR 887
Cdd:cd14626  92 PLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTETYGMIQVTLL-DTVELATYSVRTFALYKNGSSEKR 170

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 74216145 888 TVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCS 932
Cdd:cd14626 171 EVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCS 215
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 759-932 8.65e-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: 164.10  E-value: 8.65e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 759 KNRSLAVLTYDHSRILLKSQNshGSSDYINASPI-MDHDPRNpaYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSEN 837
Cdd:cd14545   1 LNRYRDRDPYDHDRSRVKLKQ--GDNDYINASLVeVEEAKRS--YILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEK 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 838 GVRQCHHYWP---DEGSNLYHV-YEVNLVSEHIWcQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFR 913
Cdd:cd14545  77 GQIKCAQYWPqgeGNAMIFEDTgLKVTLLSEEDK-SYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFL 155

                       170       180
                ....*....|....*....|.
gi 74216145 914 RKVNK--CYRGRSCPIIVHCS 932
Cdd:cd14545 156 QKVREsgSLSSDVGPPVVHCS 176
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 760-932 9.67e-46

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: 164.29  E-value: 9.67e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 760 NRSLAVLTYDHSRILLKSQNSHGSSDYINASpIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGV 839
Cdd:cd14619   1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINAN-YMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 840 RQCHHYWP-DEGSNLYHVYEVNLVSEHIwCQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNK 918
Cdd:cd14619  80 VKCEHYWPlDYTPCTYGHLRVTVVSEEV-MENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRQ 158

                       170
                ....*....|....*.
gi 74216145 919 CYRGR--SCPIIVHCS 932
Cdd:cd14619 159 WLDQTmsGGPTVVHCS 174
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 756-932 4.12e-44

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: 160.32  E-value: 4.12e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 756 NAPKNRSLAVLTYDHSRILLKS-QNSHGSSDYINASPIM------DHDPRNPAYIATQGPLPATVADFWQMVWESGCAVI 828
Cdd:cd14544   1 NKGKNRYKNILPFDHTRVILKDrDPNVPGSDYINANYIRnenegpTTDENAKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 829 VMLTPLSENGVRQCHHYWPDEG-SNLYHVYEVNLVSEHIwCQDFLVRSFYLKNL-QTNETRTVTQFHFLSWYDQGVPSST 906
Cdd:cd14544  81 VMTTKEVERGKNKCVRYWPDEGmQKQYGPYRVQNVSEHD-TTDYTLRELQVSKLdQGDPIREIWHYQYLSWPDHGVPSDP 159

                       170       180
                ....*....|....*....|....*...
gi 74216145 907 RSLLDFRRKVNKCYRGR--SCPIIVHCS 932
Cdd:cd14544 160 GGVLNFLEDVNQRQESLphAGPIVVHCS 187
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 718-932 5.19e-44

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: 161.03  E-value: 5.19e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 718 LAYMEDHLKNKN--RLEKEWEALcayqaEPNSSLVAQR---EENAPKNRSLAVLTYDHSRILLKSQNSHGSSDYINASPI 792
Cdd:cd14625   9 LAEHTERLKANDnlKLSQEYESI-----DPGQQFTWEHsnlEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINANYI 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 793 mDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNLYHVYEVNLVsEHIWCQDFL 872
Cdd:cd14625  84 -DGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRGTETYGMIQVTLL-DTIELATFC 161

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 873 VRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCS 932
Cdd:cd14625 162 VRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCS 221
Receptor_IA-2 pfam11548
Protein-tyrosine phosphatase receptor IA-2; IA-2 is a protein-tyrosine phosphatase receptor ...
 495-583 1.71e-43

Protein-tyrosine phosphatase receptor IA-2; IA-2 is a protein-tyrosine phosphatase receptor that upon exocytosis, the cytoplasmic domain is cleaved and moves to the nucleus where it enhances transcription of the insulin gene. The mature exodomain of IA-2 participates in adhesion to the extracellular matrix and is self-proteolyzed in vitro by reactive oxygen species which may be a new shedding mechanism.


Pssm-ID: 463293  Cd Length: 89  Bit Score: 152.39  E-value: 1.71e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145   495 EQQGYILTGNNPLSPEKGKQLMDQVAHILRVPSSFFADIKVLGPAVTFKVSANIQNMTTADVIKAAADNKDQLEKATGLT 574
Cdd:pfam11548   1 EEYGYIVTDNDPLSWEEGLRLMEKVAELLHLPMSSFADIRVLGPAVTFKVRANNKNLTAADVAKAAVDIKDKLEKETGLK 80


                  ....*....
gi 74216145   575 ILQSGIRPK 583
Cdd:pfam11548  81 ILQAGVGDK 89
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 750-932 8.55e-42

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: 155.09  E-value: 8.55e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 750 VAQREENAPKNRSLAVLTYDHSRILLKSQNSHGSSDYINASPIMD-HDPRnpAYIATQGPLPATVADFWQMVWESGCAVI 828
Cdd:cd14604  51 TGEKEENVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGvYGPK--AYIATQGPLANTVIDFWRMIWEYNVAII 128

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 829 VMLTPLSENGVRQCHHYWPdegsnLYHVYEVNLVSEHIWCQ------DFLVRSFYLKnLQtNETRTVTQFHFLSWYDQGV 902
Cdd:cd14604 129 VMACREFEMGRKKCERYWP-----LYGEEPMTFGPFRISCEaeqartDYFIRTLLLE-FQ-NETRRLYQFHYVNWPDHDV 201

                       170       180       190
                ....*....|....*....|....*....|
gi 74216145 903 PSSTRSLLDFRRKVNKCYRGRSCPIIVHCS 932
Cdd:cd14604 202 PSSFDSILDMISLMRKYQEHEDVPICIHCS 231
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 760-932 1.14e-41

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: 152.17  E-value: 1.14e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 760 NRSLAVLTYDHSRILLKSQNSHGSSDYINASPIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGV 839
Cdd:cd14547   1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYDGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAKE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 840 RqCHHYWPDEGSNLYHVYEVnLVSEHIWCQDFLVRSFYLKNlqTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKC 919
Cdd:cd14547  81 K-CAQYWPEEENETYGDFEV-TVQSVKETDGYTVRKLTLKY--GGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEEA 156

                       170
                ....*....|....*
gi 74216145 920 -YRGRSC-PIIVHCS 932
Cdd:cd14547 157 rQTEPHRgPIVVHCS 171
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 786-932 1.38e-41

PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type tyrosine-protein phosphatase C (PTPRC), also known as CD45, leukocyte common antigen (LCA) or GP180, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRC/CD45 is found in all nucleated hematopoietic cells and is an essential regulator of T- and B-cell antigen receptor signaling. It controls immune response, both positively and negatively, by dephosphorylating a number of signaling molecules such as the Src family kinases, the CD3zeta chain of TCY, and ZAP-70 kinase. Mutations in the human PTPRC/CD45 gene are associated with severe combined immunodeficiency (SCID) and multiple sclerosis. PTPRC/CD45 contains an extracellular receptor-like region with fibronectin type III (FN3) repeats, a short transmembrane segment, and a cytoplasmic region comprising of a membrane proximal catalytically active PTP domain (repeat 1 or D1) and a membrane distal catalytically impaired PTP-like domain (repeat 2, or D2). This model represents repeat 2.


Pssm-ID: 350406 [Multi-domain]  Cd Length: 203  Bit Score: 151.39  E-value: 1.38e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 786 YINASPIMD-HDPRnpAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNlYHVYEVNLVSE 864
Cdd:cd14558   1 YINASFIDGyWGPK--SLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKT-YGDIEVELKDT 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74216145 865 HIwCQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKV------NKCYRGRSCPIIVHCS 932
Cdd:cd14558  78 EK-SPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIkqklpyKNSKHGRSVPIVVHCS 150
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 786-932 5.61e-41

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: 149.83  E-value: 5.61e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 786 YINASPI-MDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPD---EGSNLYHVYEVNL 861
Cdd:cd14538   1 YINASHIrIPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDslnKPLICGGRLEVSL 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74216145 862 VSEHIWcQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYrgRSCPIIVHCS 932
Cdd:cd14538  81 EKYQSL-QDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIH--NSGPIVVHCS 148
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 786-932 5.68e-41

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: 149.50  E-value: 5.68e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 786 YINASPIMDHDpRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNL--YHVYEVNLVS 863
Cdd:cd14542   1 YINANFIKGVS-GSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQlqFGPFKISLEK 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74216145 864 EHIWCQDFLVRSfyLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCS 932
Cdd:cd14542  80 EKRVGPDFLIRT--LKVTFQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCS 146
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 726-932 1.12e-40

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: 151.81  E-value: 1.12e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 726 KNKNRLEKEWEALCAYQAEPNSSLVAQREENAPKNRSLAVLTYDHSRILLKSQNSHGSSDYINASpIMDHDPRNPAYIAT 805
Cdd:cd14628  22 ENVTGMELEFKRLASSKAHTSRFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINAS-FIDGYRQQKAYIAT 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 806 QGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNLYHVYEVNLVSEHIWCQdFLVRSFYLKNLQTNE 885
Cdd:cd14628 101 QGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQ-YILREFKVTDARDGQ 179

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 74216145 886 TRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYR--GRSCPIIVHCS 932
Cdd:cd14628 180 SRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEqfGQDGPISVHCS 228
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 765-932 2.04e-40

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: 148.94  E-value: 2.04e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 765 VLTYDHSRILLKSQNSHGSSDYINASPIMDHDPRNpAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHH 844
Cdd:cd14620   4 ILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKN-KFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKCYQ 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 845 YWPDEGSNLYHVYEVNlVSEHIWCQDFLVRSFYLKNLQTNET---RTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYR 921
Cdd:cd14620  83 YWPDQGCWTYGNIRVA-VEDCVVLVDYTIRKFCIQPQLPDGCkapRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVKSVNP 161

                       170
                ....*....|.
gi 74216145 922 GRSCPIIVHCS 932
Cdd:cd14620 162 VHAGPIVVHCS 172
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 721-932 2.05e-40

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: 150.65  E-value: 2.05e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 721 MEDHLK----NKN-RLEKEWEALcayqaEPNSSLVAQR---EENAPKNRSLAVLTYDHSRILLKSQNSHGSSDYINASPI 792
Cdd:cd14624   9 LADHIErlkaNDNlKFSQEYESI-----DPGQQFTWEHsnlEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINANYI 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 793 MDHDPRNpAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNLYHVYEVNLVsEHIWCQDFL 872
Cdd:cd14624  84 DGYRKQN-AYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRGTETYGLIQVTLL-DTVELATYC 161

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 873 VRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCS 932
Cdd:cd14624 162 VRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPPDAGPMVVHCS 221
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 731-932 2.87e-40

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: 150.65  E-value: 2.87e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 731 LEKEWEALCAYQAEPNSSLVAQREENAPKNRSLAVLTYDHSRILLKSQNSHGSSDYINASpIMDHDPRNPAYIATQGPLP 810
Cdd:cd14627  28 MELEFKRLANSKAHTSRFISANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINAS-FIDGYRQQKAYIATQGPLA 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 811 ATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNLYHVYEVNLVSEHIWCQdFLVRSFYLKNLQTNETRTVT 890
Cdd:cd14627 107 ETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQ-YILREFKVTDARDGQSRTVR 185

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 74216145 891 QFHFLSWYDQGVPSSTRSLLDFRRKVNKCYR--GRSCPIIVHCS 932
Cdd:cd14627 186 QFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEqfGQDGPISVHCS 229
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 747-932 6.32e-40

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: 148.82  E-value: 6.32e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 747 SSLVAQREENAPKNRSLAVLTYDHSRILLKSQNSHGSSDYINASPIMDHDpRNPAYIATQGPLPATVADFWQMVWESGCA 826
Cdd:cd14603  21 STVAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVD-GSRAYIATQGPLSHTVLDFWRMIWQYGVK 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 827 VIVMLTPLSENGVRQCHHYWPDEGSNL-YHVYEVNLVSEHIWCQDFLVRSFYLKNLQtnETRTVTQFHFLSWYDQGVPSS 905
Cdd:cd14603 100 VILMACREIEMGKKKCERYWAQEQEPLqTGPFTITLVKEKRLNEEVILRTLKVTFQK--ESRSVSHFQYMAWPDHGIPDS 177

                       170       180
                ....*....|....*....|....*...
gi 74216145 906 TRSLLDFRRKVNKcYRGRS-CPIIVHCS 932
Cdd:cd14603 178 PDCMLAMIELARR-LQGSGpEPLCVHCS 204
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 721-932 9.59e-40

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


Pssm-ID: 350469 [Multi-domain]  Cd Length: 296  Bit Score: 149.02  E-value: 9.59e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 721 MEDHLKNKNRL-EKEWEAL--CAYQAepnSSLVAQREENAPKNRSLAVLTYDHSRILLKSQNSHGSSDYINASPIMDHDP 797
Cdd:cd14621  17 INRRMADDNKLfREEFNALpaCPIQA---TCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINASFINGYQE 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 798 RNpAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNLYHVYEVNlVSEHIWCQDFLVRSFY 877
Cdd:cd14621  94 KN-KFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGCWTYGNIRVS-VEDVTVLVDYTVRKFC 171

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 74216145 878 LKNL----QTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCS 932
Cdd:cd14621 172 IQQVgdvtNKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYAGAIVVHCS 230
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 741-932 1.97e-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: 147.69  E-value: 1.97e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 741 YQAEPNSSLV-AQREENAPKNRSLAVLTYDHSRILLKsqnshGSSDYINASPIMDHDPRNP---AYIATQGPLPATVADF 816
Cdd:cd14600  24 YRKKPGLAITcAKLPQNMDKNRYKDVLPYDATRVVLQ-----GNEDYINASYVNMEIPSANivnKYIATQGPLPHTCAQF 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 817 WQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNL-YHVYEVNLVSEHiwCQ-DFLVRSFYLKNLQTNETRTVTQFHF 894
Cdd:cd14600  99 WQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDPPDVMeYGGFRVQCHSED--CTiAYVFREMLLTNTQTGEERTVTHLQY 176

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 74216145 895 LSWYDQGVPSSTRSLLDFRRKVnKCYRGRSCPIIVHCS 932
Cdd:cd14600 177 VAWPDHGVPDDSSDFLEFVNYV-RSKRVENEPVLVHCS 213
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 731-932 2.22e-39

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: 147.95  E-value: 2.22e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 731 LEKEWEALCAYQAEPNSSLVAQREENAPKNRSLAVLTYDHSRILLKSQNSHGSSDYINASpIMDHDPRNPAYIATQGPLP 810
Cdd:cd14629  28 MELEFKLLANSKAHTSRFISANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINAS-FIDGYRQQKAYIATQGPLA 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 811 ATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNLYHVYEVNLVSEHIWCQdFLVRSFYLKNLQTNETRTVT 890
Cdd:cd14629 107 ETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQ-YILREFKVTDARDGQSRTIR 185

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 74216145 891 QFHFLSWYDQGVPSSTRSLLDFRRKVNKCYR--GRSCPIIVHCS 932
Cdd:cd14629 186 QFQFTDWPEQGVPKTGEGFIDFIGQVHKTKEqfGQDGPITVHCS 229
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 731-932 4.88e-39

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: 146.34  E-value: 4.88e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 731 LEKEWEALCAYQAEPNSSlvAQREENAPKNRSLAVLTYDHSRILLKSQNSHGSSDYINASPImDHDPRNPAYIATQGPLP 810
Cdd:cd14633  17 FKEEYESFFEGQSAPWDS--AKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYI-DGYHRPNHYIATQGPMQ 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 811 ATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEgSNLYHVYEVNLVSEHIwCQDFLVRSFYLKNLQTNETRTVT 890
Cdd:cd14633  94 ETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDD-TEIYKDIKVTLIETEL-LAEYVIRTFAVEKRGVHEIREIR 171

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 74216145 891 QFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCS 932
Cdd:cd14633 172 QFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCS 213
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 755-932 6.72e-39

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: 145.95  E-value: 6.72e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 755 ENAPKNRSLAVLTYDHSRILLKSQNSHGS--SDYINASPIMDHDpRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLT 832
Cdd:cd17667  26 DNKHKNRYINILAYDHSRVKLRPLPGKDSkhSDYINANYVDGYN-KAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMIT 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 833 PLSENGVRQCHHYWPDEGSNLYHVYEVNLVSEHIW-CqdFLVRSFYLKNLQT------------NEtRTVTQFHFLSWYD 899
Cdd:cd17667 105 NLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHaC--YTVRRFSIRNTKVkkgqkgnpkgrqNE-RTVIQYHYTQWPD 181

                       170       180       190
                ....*....|....*....|....*....|...
gi 74216145 900 QGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCS 932
Cdd:cd17667 182 MGVPEYALPVLTFVRRSSAARTPEMGPVLVHCS 214
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 754-932 3.28e-38

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: 142.86  E-value: 3.28e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 754 EENAPKNRSLAVLTYDHSRILLKSQNSHGSSDYINASPIMD-HDPRNpaYIATQGPLPATVADFWQMVWESGCAVIVMLT 832
Cdd:cd14630   1 DENRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGyHRPRH--YIATQGPMQETVKDFWRMIWQENSASVVMVT 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 833 PLSENGVRQCHHYWPDEgSNLYHVYEVNLVsEHIWCQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDF 912
Cdd:cd14630  79 NLVEVGRVKCVRYWPDD-TEVYGDIKVTLI-ETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGF 156

                       170       180
                ....*....|....*....|
gi 74216145 913 RRKVNKCYRGRSCPIIVHCS 932
Cdd:cd14630 157 VRQVKFLNPPDAGPIVVHCS 176
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 754-932 3.53e-38

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: 142.66  E-value: 3.53e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 754 EENAPKNRSLAVLTYDHSRILLKSQNshgssDYINASPI-MDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLT 832
Cdd:cd14597   1 KENRKKNRYKNILPYDTTRVPLGDEG-----GYINASFIkMPVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMT 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 833 PLSENGVRQCHHYWPDE-GSNLYHVYEVNLVSEHIWCQD-FLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLL 910
Cdd:cd14597  76 QEVEGGKIKCQRYWPEIlGKTTMVDNRLQLTLVRMQQLKnFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPEQLL 155

                       170       180
                ....*....|....*....|..
gi 74216145 911 DFRRKVNKCYrgRSCPIIVHCS 932
Cdd:cd14597 156 TFISYMRHIH--KSGPIITHCS 175
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 750-932 4.66e-38

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: 143.63  E-value: 4.66e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 750 VAQREENAPKNRSLAVLTYDHSRILLKsqnsHGSSDYINASPI-MDHDPRnpAYIATQGPLPATVADFWQMVWESGCAVI 828
Cdd:cd14608  19 VAKLPKNKNRNRYRDVSPFDHSRIKLH----QEDNDYINASLIkMEEAQR--SYILTQGPLPNTCGHFWEMVWEQKSRGV 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 829 VMLTPLSENGVRQCHHYWPD--------EGSNLyhvyEVNLVSEHIWCQdFLVRSFYLKNLQTNETRTVTQFHFLSWYDQ 900
Cdd:cd14608  93 VMLNRVMEKGSLKCAQYWPQkeekemifEDTNL----KLTLISEDIKSY-YTVRQLELENLTTQETREILHFHYTTWPDF 167

                       170       180       190
                ....*....|....*....|....*....|....
gi 74216145 901 GVPSSTRSLLDFRRKVNK--CYRGRSCPIIVHCS 932
Cdd:cd14608 168 GVPESPASFLNFLFKVREsgSLSPEHGPVVVHCS 201
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 746-932 6.50e-38

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: 143.10  E-value: 6.50e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 746 NSSLVAQREENAPKNRSLAVLTYDHSRILLKSQNSH-GSSDYINASPIMDH--DPRNPA--YIATQGPLPATVADFWQMV 820
Cdd:cd14606   8 HQRLEGQRPENKSKNRYKNILPFDHSRVILQGRDSNiPGSDYINANYVKNQllGPDENAktYIASQGCLEATVNDFWQMA 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 821 WESGCAVIVMLTPLSENGVRQCHHYWPDEGSN-LYHVYEVNLVSEHIwCQDFLVRSFYLKNLQTNET-RTVTQFHFLSWY 898
Cdd:cd14606  88 WQENSRVIVMTTREVEKGRNKCVPYWPEVGMQrAYGPYSVTNCGEHD-TTEYKLRTLQVSPLDNGELiREIWHYQYLSWP 166

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 74216145 899 DQGVPSSTRSLLDFRRKVNKCYRG--RSCPIIVHCS 932
Cdd:cd14606 167 DHGVPSEPGGVLSFLDQINQRQESlpHAGPIIVHCS 202
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 760-932 9.27e-38

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: 141.21  E-value: 9.27e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 760 NRSLAVLTYDHSRILLKSQNSHGSSDYINASPIMDHDPRNpAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGV 839
Cdd:cd14617   1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRR-EYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 840 RQCHHYWP-DEGSNLYHVYEVNLVSEHIWcQDFLVRSFYLKNL-QTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVN 917
Cdd:cd14617  80 VKCDHYWPaDQDSLYYGDLIVQMLSESVL-PEWTIREFKICSEeQLDAPRLVRHFHYTVWPDHGVPETTQSLIQFVRTVR 158

                       170
                ....*....|....*...
gi 74216145 918 KcYRGRS---CPIIVHCS 932
Cdd:cd14617 159 D-YINRTpgsGPTVVHCS 175
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 785-932 1.79e-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: 139.69  E-value: 1.79e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 785 DYINASPIMDHDPRNP---AYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPD-EGSNLYHVYEVN 860
Cdd:cd14601   1 DYINANYINMEIPSSSiinRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEpSGSSSYGGFQVT 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74216145 861 LVSEHiWCQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCS 932
Cdd:cd14601  81 CHSEE-GNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVHCS 151
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 786-932 2.31e-37

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: 139.11  E-value: 2.31e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 786 YINASPI-MDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNLYHV--YEVNLV 862
Cdd:cd14596   1 YINASYItMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELenYQLRLE 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 863 SEHIwCQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYrgRSCPIIVHCS 932
Cdd:cd14596  81 NYQA-LQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVH--NTGPIVVHCS 147
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 755-932 1.18e-36

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: 139.00  E-value: 1.18e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 755 ENAPKNRSLAVLTYDHSRILLKSQN-SHGSSDYINASPIM-DHD-PRNPA-----YIATQGPLPATVADFWQMVWESGCA 826
Cdd:cd14605   1 ENKNKNRYKNILPFDHTRVVLHDGDpNEPVSDYINANIIMpEFEtKCNNSkpkksYIATQGCLQNTVNDFWRMVFQENSR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 827 VIVMLTPLSENGVRQCHHYWPDEGS-NLYHVYEVNLVSEHIwCQDFLVRSFYLKNL-QTNETRTVTQFHFLSWYDQGVPS 904
Cdd:cd14605  81 VIVMTTKEVERGKSKCVKYWPDEYAlKEYGVMRVRNVKESA-AHDYILRELKLSKVgQGNTERTVWQYHFRTWPDHGVPS 159

                       170       180       190
                ....*....|....*....|....*....|
gi 74216145 905 STRSLLDFRRKVNKCYRG--RSCPIIVHCS 932
Cdd:cd14605 160 DPGGVLDFLEEVHHKQESimDAGPVVVHCS 189
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 786-932 3.73e-36

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: 135.88  E-value: 3.73e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 786 YINASpIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNLYHVYEVNLVSEH 865
Cdd:cd17668   1 YINAN-YVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQ 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74216145 866 IWCQdFLVRSFYLKNLQTNE--------TRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCS 932
Cdd:cd17668  80 VLAY-YTVRNFTLRNTKIKKgsqkgrpsGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCS 153
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 786-932 6.59e-36

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: 135.04  E-value: 6.59e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 786 YINASPIMDHDPRNpAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNLYHVYEVNlVSEH 865
Cdd:cd14551   1 YINASYIDGYQEKN-KFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCWTYGNLRVR-VEDT 78

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74216145 866 IWCQDFLVRSFYLK--NLQTNE--TRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCS 932
Cdd:cd14551  79 VVLVDYTTRKFCIQkvNRGIGEkrVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCS 149
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 760-932 7.49e-36

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: 135.84  E-value: 7.49e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 760 NRSLAVLTYDHSRILLKSQNSHGSSDYINASPImdhdprnPAY------IATQGPLPATVADFWQMVWESGCAVIVMLTP 833
Cdd:cd14618   1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFI-------PGYtspqefIATQGPLKKTIEDFWRLVWEQQVCNIIMLTV 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 834 LSENGVRQCHHYWPDEGSNLYHVY-EVNLVSEHIwCQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDF 912
Cdd:cd14618  74 GMENGRVLCDHYWPSESTPVSYGHiTVHLLAQSS-EDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAF 152

                       170       180
                ....*....|....*....|...
gi 74216145 913 RRKVN---KCYRGRScPIIVHCS 932
Cdd:cd14618 153 RELVRehvQATKGKG-PTLVHCS 174
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 750-932 8.79e-36

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: 136.63  E-value: 8.79e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 750 VAQREENAPKNRSLAVLTYDHSRIllKSQNShgSSDYINASpIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIV 829
Cdd:cd14607  18 VAKYPENRNRNRYRDVSPYDHSRV--KLQNT--ENDYINAS-LVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVV 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 830 MLTPLSENGVRQCHHYWPDEGSNLYHVYE----VNLVSEHIWCQdFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSS 905
Cdd:cd14607  93 MLNRIVEKDSVKCAQYWPTDEEEVLSFKEtgfsVKLLSEDVKSY-YTVHLLQLENINSGETRTISHFHYTTWPDFGVPES 171

                       170       180
                ....*....|....*....|....*....
gi 74216145 906 TRSLLDFRRKV--NKCYRGRSCPIIVHCS 932
Cdd:cd14607 172 PASFLNFLFKVreSGSLSPEHGPAVVHCS 200
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 757-932 1.12e-35

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: 135.73  E-value: 1.12e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 757 APKNRSLAVLTYDHSRILLKS-QNSHGSSDYINASPIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLS 835
Cdd:cd14612  16 ASKDRYKTILPNPQSRVCLRRaGSQEEEGSYINANYIRGYDGKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITKLK 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 836 EnGVRQCHHYWPD-EGSNLYHVYEVNLVSEhiwCQDFLVRSFYLKnlQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRR 914
Cdd:cd14612  96 E-KKEKCVHYWPEkEGTYGRFEIRVQDMKE---CDGYTIRDLTIQ--LEEESRSVKHYWFSSWPDHQTPESAGPLLRLVA 169

                       170       180
                ....*....|....*....|
gi 74216145 915 KVNKCYR--GRSCPIIVHCS 932
Cdd:cd14612 170 EVEESRQtaASPGPIVVHCS 189
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 786-932 2.66e-35

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: 133.16  E-value: 2.66e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 786 YINASPIMDHDPRNpAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNLYHVYEVNLVSEH 865
Cdd:cd14552   1 YINASFIDGYRQKD-AYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGSVSSGDITVELKDQT 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74216145 866 IwCQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGR-SCPIIVHCS 932
Cdd:cd14552  80 D-YEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSgNHPITVHCS 146
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 772-932 3.03e-35

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: 133.61  E-value: 3.03e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 772 RILLKSQNSHGSSDYINASPImDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEgS 851
Cdd:cd14631   1 RVILQPVEDDPSSDYINANYI-DGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDD-T 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 852 NLYHVYEVNLVS-EHIwcQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVH 930
Cdd:cd14631  79 EVYGDFKVTCVEmEPL--AEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVH 156


                ..
gi 74216145 931 CS 932
Cdd:cd14631 157 CS 158
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 759-932 3.35e-35

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: 134.20  E-value: 3.35e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 759 KNRSLAVLTYDHSRILLKSQNSHGSSDYINASPIMD-HDPRnpAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSEN 837
Cdd:cd14602   1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGvYGPR--AYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEM 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 838 GVRQCHHYWPDEGSNLYHVYEVNLVSE-HIWCQDFLVRSfyLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKV 916
Cdd:cd14602  79 GKKKCERYWAEPGEMQLEFGPFSVTCEaEKRKSDYIIRT--LKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDV 156

                       170
                ....*....|....*.
gi 74216145 917 NKCYRGRSCPIIVHCS 932
Cdd:cd14602 157 RCYQEDDSVPICIHCS 172
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 786-932 3.05e-34

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: 130.42  E-value: 3.05e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 786 YINASPImDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEgSNLYHVYEVNLVSEH 865
Cdd:cd14555   1 YINANYI-DGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDD-TEVYGDIKVTLVETE 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74216145 866 IWCQdFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCS 932
Cdd:cd14555  79 PLAE-YVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCS 144
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 786-932 6.61e-34

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: 129.43  E-value: 6.61e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 786 YINASPIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDE-GSNL-YHVYEVNLVS 863
Cdd:cd14539   1 YINASLIEDLTPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTErGQALvYGAITVSLQS 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74216145 864 EHIwcQDFLV-RSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCY---RGRSCPIIVHCS 932
Cdd:cd14539  81 VRT--TPTHVeRIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYlqqRSLQTPIVVHCS 151
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 756-932 9.97e-34

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: 130.01  E-value: 9.97e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 756 NAPKNRSLAVLTYDHSRILLKSQNSHGSSDYINASPIMDHD-PRNpaYIATQGPLPATVADFWQMVWESGCAVIVMLTPL 834
Cdd:cd14614  12 NRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNsPQE--YIATQGPLPETRNDFWKMVLQQKSQIIVMLTQC 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 835 SENGVRQCHHYWP-DEGSNLYHVYEVNLVSEHiWCQDFLVRSFYLKnlQTNETRTVTQFHFLSWYDQGVPS--STRSLLD 911
Cdd:cd14614  90 NEKRRVKCDHYWPfTEEPVAYGDITVEMLSEE-EQPDWAIREFRVS--YADEVQDVMHFNYTAWPDHGVPTanAAESILQ 166

                       170       180
                ....*....|....*....|....*
gi 74216145 912 F----RRKVNKcyrgRSCPIIVHCS 932
Cdd:cd14614 167 FvqmvRQQAVK----SKGPMIIHCS 187
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 761-932 1.58e-33

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: 129.01  E-value: 1.58e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 761 RSLAVLTYDHSRILLKSQNSHGSSDYINASpIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVR 840
Cdd:cd14623   1 RVLQIIPYEFNRVIIPVKRGEENTDYVNAS-FIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 841 QCHHYWPDEGSNLYHVYEVNLVSEHiWCQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCY 920
Cdd:cd14623  80 KCAQYWPSDGSVSYGDITIELKKEE-ECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQ 158

                       170
                ....*....|...
gi 74216145 921 RGR-SCPIIVHCS 932
Cdd:cd14623 159 QQSgNHPITVHCS 171
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 786-932 1.77e-33

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: 128.73  E-value: 1.77e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 786 YINASPI-MDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSN----LYHVYEVN 860
Cdd:cd14540   1 YINASHItATVGGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGEhdalTFGEYKVS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 861 LVSEHIwCQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDF-------RRKVNKCYRGRS--CPIIVHC 931
Cdd:cd14540  81 TKFSVS-SGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFleeinsvRRHTNQDVAGHNrnPPTLVHC 159


                .
gi 74216145 932 S 932
Cdd:cd14540 160 S 160
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 785-932 2.66e-33

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: 127.43  E-value: 2.66e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 785 DYINASPImDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNLYHVYEVNLVSE 864
Cdd:cd14622   1 DYINASFI-DGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGSVTHGEITIEIKND 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74216145 865 HIwCQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGR-SCPIIVHCS 932
Cdd:cd14622  80 TL-LETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQTgNHPIVVHCS 147
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 786-932 8.16e-33

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: 126.09  E-value: 8.16e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 786 YINASPIMDH-DPRNpaYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWP--DEGSNLYHVYEVNLV 862
Cdd:cd14557   1 YINASYIDGFkEPRK--YIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPsmEEGSRAFGDVVVKIN 78

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74216145 863 SEHIwCQDFLVRSFYLKNLQTNET-RTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCS 932
Cdd:cd14557  79 EEKI-CPDYIIRKLNINNKKEKGSgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCS 148
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 759-932 1.62e-32

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: 126.19  E-value: 1.62e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 759 KNRSLAVLTYDHSRILLKSQNSHGS-SDYINASPIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSEN 837
Cdd:cd14611   2 KNRYKTILPNPHSRVCLKPKNSNDSlSTYINANYIRGYGGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 838 GvRQCHHYWPdEGSNLYHVYE--VNLVSEhiwCQDFLVRSFYLKnlQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRK 915
Cdd:cd14611  82 N-EKCVLYWP-EKRGIYGKVEvlVNSVKE---CDNYTIRNLTLK--QGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLD 154

                       170       180
                ....*....|....*....|
gi 74216145 916 VN---KCYRGRScPIIVHCS 932
Cdd:cd14611 155 VEedrLASPGRG-PVVVHCS 173
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 760-932 1.74e-32

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: 125.79  E-value: 1.74e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 760 NRSLAVLTYDHSRILLKSQNSHGSSDYINASPIMDHDPRNpAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGV 839
Cdd:cd14616   1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPN-EFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 840 RQCHHYWPDEGS--NLYHVYEVNLVSEHIWcQDFLVRSfyLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVN 917
Cdd:cd14616  80 IRCHQYWPEDNKpvTVFGDIVITKLMEDVQ-IDWTIRD--LKIERHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVR 156

                       170
                ....*....|....*
gi 74216145 918 KCYRGRSCPIIVHCS 932
Cdd:cd14616 157 ASRAHDNTPMIVHCS 171
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 786-932 7.66e-32

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: 123.24  E-value: 7.66e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 786 YINASPImDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEgSNLYHVYEVNLVSEH 865
Cdd:cd14632   1 YINANYI-DGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDD-SDTYGDIKITLLKTE 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74216145 866 IWCQdFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCS 932
Cdd:cd14632  79 TLAE-YSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCS 144
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 759-932 2.53e-31

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: 123.43  E-value: 2.53e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 759 KNRSLAVLTYDHSRILLKSQNSHGS-SDYINASPIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSEN 837
Cdd:cd14613  28 KNRYKTILPNPHSRVCLTSPDQDDPlSSYINANYIRGYGGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEM 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 838 GvRQCHHYWPDEgSNLYHVYEVNlVSEHIWCQDFLVRSFYLKNlqTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVN 917
Cdd:cd14613 108 N-EKCTEYWPEE-QVTYEGIEIT-VKQVIHADDYRLRLITLKS--GGEERGLKHYWYTSWPDQKTPDNAPPLLQLVQEVE 182

                       170
                ....*....|....*...
gi 74216145 918 ---KCYRGRSCPIIVHCS 932
Cdd:cd14613 183 earQQAEPNCGPVIVHCS 200
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 786-931 1.13e-30

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: 119.82  E-value: 1.13e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 786 YINASpIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGvRQCHHYWPDEGSNLYHVYEVNLVSEH 865
Cdd:cd14556   1 YINAA-LLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKD-QSCPQYWPDEGSGTYGPIQVEFVSTT 78

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74216145 866 IWCqDFLVRSFYLKNLQ--TNETRTVTQFHFLSW-YDQGVPSSTRSLLDFRRKVNK----CYRGrscPIIVHC 931
Cdd:cd14556  79 IDE-DVISRIFRLQNTTrpQEGYRMVQQFQFLGWpRDRDTPPSKRALLKLLSEVEKwqeqSGEG---PIVVHC 147
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 752-932 5.68e-29

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 118.18  E-value: 5.68e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145  752 QREENAPKNRSLAVLTYDHSRILLKSQnSHGSSDYINASPImDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVML 831
Cdd:PHA02747  47 EKPENQPKNRYWDIPCWDHNRVILDSG-GGSTSDYIHANWI-DGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVML 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145  832 TPLSE-NGVRQCHHYW-PDEGSNL----YHVYEVNLVsehiwcqdflVRSFYLKNL------QTNETRTVTQFHFLSWYD 899
Cdd:PHA02747 125 TPTKGtNGEEKCYQYWcLNEDGNIdmedFRIETLKTS----------VRAKYILTLieitdkILKDSRKISHFQCSEWFE 194

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 74216145  900 QGVPSSTRSLLDF-------RRKVNKCYRGRS---CPIIVHCS 932
Cdd:PHA02747 195 DETPSDHPDFIKFikiidinRKKSGKLFNPKDallCPIVVHCS 237
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 755-932 1.15e-27

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: 113.94  E-value: 1.15e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 755 ENAPKNRSLAVLTYDHSRILL--KSQNSHGssdYINASPI-MDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVML 831
Cdd:cd14599  37 ENAERNRIREVVPYEENRVELvpTKENNTG---YINASHIkVTVGGEEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMV 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 832 TPLSENGVRQCHHYWPDEGSN----LYHVYEVNL-VSEHIWCqdFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSST 906
Cdd:cd14599 114 TAEEEGGRSKSHRYWPKLGSKhssaTYGKFKVTTkFRTDSGC--YATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEEV 191

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 74216145 907 RSLLDF-------RRKVNKCYRG-RSC--PIIVHCS 932
Cdd:cd14599 192 QGFLSYleeiqsvRRHTNSMLDStKNCnpPIVVHCS 227
PHA02738 PHA02738
hypothetical protein; Provisional
 756-932 6.96e-27

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 112.33  E-value: 6.96e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145  756 NAPKNRSLAVLTYDHSRILLKSQNSHGssDYINASPImDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLS 835
Cdd:PHA02738  49 NRKLNRYLDAVCFDHSRVILPAERNRG--DYINANYV-DGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKK 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145  836 ENGVRQCHHYWPD-EGSNL----YHVYEVNlVSEHIwcqdFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLL 910
Cdd:PHA02738 126 ENGREKCFPYWSDvEQGSIrfgkFKITTTQ-VETHP----HYVKSTLLLTDGTSATQTVTHFNFTAWPDHDVPKNTSEFL 200

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 74216145  911 DFRRKVNKCY-------------RGRSCPIIVHCS 932
Cdd:PHA02738 201 NFVLEVRQCQkelaqeslqighnRLQPPPIVVHCN 235
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 786-930 5.95e-26

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: 106.25  E-value: 5.95e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 786 YINASPIMDHDpRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGvrQCHHYWPDEGSNLYHV-YEVNLVSE 864
Cdd:cd14550   1 YINASYLQGYR-RSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWPTKEKPLECEtFKVTLSGE 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 865 HIWC----QDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTrsLLDFRRKVNKCYRGRSCPIIVH 930
Cdd:cd14550  78 DHSClsneIRLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPIHT--VFELINTVQEWAQQRDGPIVVH 145
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 786-932 7.82e-25

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: 103.31  E-value: 7.82e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 786 YINASPIMDHDPRN-PAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVR-QCHHYWPDEGSNLYHVYEVNLVS 863
Cdd:cd17658   1 YINASLVETPASESlPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTaKCADYFPAEENESREFGRISVTN 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74216145 864 EHIWCQD--FLVRSFYLKNLQTNET-RTVTQFHFLSWYDQGVPSSTRSLldfrRKVNKCYRG---RSCPIIVHCS 932
Cdd:cd17658  81 KKLKHSQhsITLRVLEVQYIESEEPpLSVLHIQYPEWPDHGVPKDTRSV----RELLKRLYGippSAGPIVVHCS 151
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 745-932 8.91e-24

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 102.77  E-value: 8.91e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145  745 PNSSLVAQREENAPKNRSLAVLTYDHSRILLKSQNshGSSDYINASPIMDHDPRNpAYIATQGPLPATVADFWQMVWESG 824
Cdd:PHA02742  41 AFSCNESLELKNMKKCRYPDAPCFDRNRVILKIED--GGDDFINASYVDGHNAKG-RFICTQAPLEETALDFWQAIFQDQ 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145  825 CAVIVMLTPLSENGVRQCHHYW-PDEGSNLYHvYEVNLVSEHIwcQDFlvRSFYLKNLQTNETRT-----VTQFHFLSWY 898
Cdd:PHA02742 118 VRVIVMITKIMEDGKEACYPYWmPHERGKATH-GEFKIKTKKI--KSF--RNYAVTNLCLTDTNTgasldIKHFAYEDWP 192

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 74216145  899 DQGVPSSTRSLLDFRRKVNKC-----------YRGRSCPIIVHCS 932
Cdd:PHA02742 193 HGGLPRDPNKFLDFVLAVREAdlkadvdikgeNIVKEPPILVHCS 237
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 786-931 1.14e-23

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: 99.71  E-value: 1.14e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 786 YINASpIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLseNGVRQCHHYWPDEGSNLYHVYEVNLVSEH 865
Cdd:cd14634   1 YINAA-LMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEM--DAAQLCMQYWPEKTSCCYGPIQVEFVSAD 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74216145 866 IwCQDFLVRSFYLKNLQTNET--RTVTQFHFLSW--YdQGVPSSTRSLLDFRRKVNKC---YRGRSCPIIVHC 931
Cdd:cd14634  78 I-DEDIISRIFRICNMARPQDgyRIVQHLQYIGWpaY-RDTPPSKRSILKVVRRLEKWqeqYDGREGRTVVHC 148
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
729-932 2.00e-22

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 98.24  E-value: 2.00e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 729 NRLEKEWEALcAYQAEPNSSLvaQREENAPKNRSLAVLTYDHSRIllksqnshGSSD-YINASPIMDHDPRNpaYIATQG 807
Cdd:COG5599  18 SRLSTLTNEL-APSHNDPQYL--QNINGSPLNRFRDIQPYKETAL--------RANLgYLNANYIQVIGNHR--YIATQY 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 808 PLPATVADFWQMVWESGCAVIVMLTPLSENGVRQ--CHHYWPDEGSNLYHVYEVNLVSEHIWCQDFLVRSFYLKNLQTN- 884
Cdd:COG5599  85 PLEEQLEDFFQMLFDNNTPVLVVLASDDEISKPKvkMPVYFRQDGEYGKYEVSSELTESIQLRDGIEARTYVLTIKGTGq 164

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 74216145 885 ETRTVTQFHFLSWYDQGVPSST--RSLLDFRRKVNKCYRGRSCPIIVHCS 932
Cdd:COG5599 165 KKIEIPVLHVKNWPDHGAISAEalKNLADLIDKKEKIKDPDKLLPVVHCR 214
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 786-932 4.69e-22

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: 95.81  E-value: 4.69e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 786 YINASPI------MDHDprnpaYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSN----LYH 855
Cdd:cd14598   1 YINASHIkvtvggKEWD-----YIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLGSRhntvTYG 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 856 VYEVNL-VSEHIWCqdFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDF-------RRKVNKCY--RGRSC 925
Cdd:cd14598  76 RFKITTrFRTDSGC--YATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYleeiqsvRRHTNSTIdpKSPNP 153


                ....*..
gi 74216145 926 PIIVHCS 932
Cdd:cd14598 154 PVLVHCS 160
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 786-931 4.24e-21

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: 92.40  E-value: 4.24e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 786 YINASpIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLseNGVRQCHHYWPDEGSNLYHVYEVNLVSEH 865
Cdd:cd14636   1 YINAA-LMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEV--DLAQGCPQYWPEEGMLRYGPIQVECMSCS 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74216145 866 IWCqDFLVRSFYLKNLQTNET--RTVTQFHFLSWYD-QGVPSSTRSLLDFRRKVNK----CYRGRSCPIIvHC 931
Cdd:cd14636  78 MDC-DVISRIFRICNLTRPQEgyLMVQQFQYLGWAShREVPGSKRSFLKLILQVEKwqeeCDEGEGRTII-HC 148
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 786-931 4.98e-21

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: 92.28  E-value: 4.98e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 786 YINASpIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSE-NGVRQCHHYWPDEGSNLYHVYEVNLVSE 864
Cdd:cd14637   1 YINAA-LTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQsNSAWPCLQYWPEPGLQQYGPMEVEFVSG 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74216145 865 HIwCQDFLVRSFYLKNLQ--TNETRTVTQFHFLSWYD-QGVPSSTRSLLDFRRKVNK----CYRGRScpiIVHC 931
Cdd:cd14637  80 SA-DEDIVTRLFRVQNITrlQEGHLMVRHFQFLRWSAyRDTPDSKKAFLHLLASVEKwqreSGEGRT---VVHC 149
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 745-932 8.87e-21

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 94.33  E-value: 8.87e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145  745 PNSSLVAQ--REENAPKNRSLAVLTYDHSRILLKSQNS-----HGSSD--------------YINASPIMDHDPRNpAYI 803
Cdd:PHA02746  38 PIRGTTNHflKKENLKKNRFHDIPCWDHSRVVINAHESlkmfdVGDSDgkkievtsednaenYIHANFVDGFKEAN-KFI 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145  804 ATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGvRQCHHYW-PDEGSNLYHVYEVNLVSEHIWCQDFLVRSFYLKNLQ 882
Cdd:PHA02746 117 CAQGPKEDTSEDFFKLISEHESQVIVSLTDIDDDD-EKCFELWtKEEDSELAFGRFVAKILDIIEELSFTKTRLMITDKI 195

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74216145  883 TNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKcYRGR-----------SCPIIVHCS 932
Cdd:PHA02746 196 SDTSREIHHFWFPDWPDNGIPTGMAEFLELINKVNE-EQAElikqadndpqtLGPIVVHCS 255
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 786-931 1.68e-18

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: 85.12  E-value: 1.68e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 786 YINASpIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLseNGVRQCHHYWPDEGSNLYHVYEVNLVSEH 865
Cdd:cd14635   1 YINAA-LMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDV--DPAQLCPQYWPENGVHRHGPIQVEFVSAD 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74216145 866 IWcQDFLVRSFYLKNLQTNET--RTVTQFHFLSW-YDQGVPSSTRSLLDFRRKVNKC---YRGRSCPIIVHC 931
Cdd:cd14635  78 LE-EDIISRIFRIYNAARPQDgyRMVQQFQFLGWpMYRDTPVSKRSFLKLIRQVDKWqeeYNGGEGRTVVHC 148
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 786-930 1.16e-14

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: 73.94  E-value: 1.16e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 786 YINASPIMDHdPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLtPLSENGVRQCHHYWP--DEGSNLyHVYEVNLVS 863
Cdd:cd17670   1 YINASYIMGY-YRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVML-PDNQGLAEDEFVYWPsrEESMNC-EAFTVTLIS 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74216145 864 EHIWC----QDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVP-SSTRSLLDFrrkVNKCYRGRSCPIIVH 930
Cdd:cd17670  78 KDRLClsneEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPiSSTFELINV---IKEEALTRDGPTIVH 146
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 786-930 4.53e-14

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: 71.95  E-value: 4.53e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145 786 YINASPIMDHDPRNpAYIATQGPLPATVADFWQMVWESGCAVIVMLtPLSENGVRQCHHYWP--DEGSNLyHVYEVNLVS 863
Cdd:cd17669   1 YINASYIMGYYQSN-EFIITQHPLLHTIKDFWRMIWDHNAQLIVML-PDGQNMAEDEFVYWPnkDEPINC-ETFKVTLIA 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74216145 864 EHIWC----QDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVP-SSTRSLLDFrrkVNKCYRGRSCPIIVH 930
Cdd:cd17669  78 EEHKClsneEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPiSKTFELISI---IKEEAANRDGPMIVH 146
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
888-932 1.26e-11

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 61.99  E-value: 1.26e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 74216145    888 TVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSC--PIIVHCS 932
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESsgPVVVHCS 47
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 888-932 1.26e-11

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: 61.99  E-value: 1.26e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 74216145    888 TVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSC--PIIVHCS 932
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESsgPVVVHCS 47
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 729-931 1.04e-07

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 54.59  E-value: 1.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145  729 NRLEKEWEALCAYQAEPNSSLVAQREENAPK-NRSLAVLTYDHSRILLKSQNSHGSSDYINAspiMDHDPRnpaYIATQG 807
Cdd:PHA02740  25 SCIIKEYRAIVPEHEDEANKACAQAENKAKDeNLALHITRLLHRRIKLFNDEKVLDARFVDG---YDFEQK---FICIIN 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74216145  808 PLPATVADFWQMVWESGCAVIVMLTPLSEngvRQCHH-YWP-DEG----SNLYHVYEVNLVSEhiwcQDFLVRSFYLKNl 881
Cdd:PHA02740  99 LCEDACDKFLQALSDNKVQIIVLISRHAD---KKCFNqFWSlKEGcvitSDKFQIETLEIIIK----PHFNLTLLSLTD- 170

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 74216145  882 QTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYR--------GRSCPIIVHC 931
Cdd:PHA02740 171 KFGQAQKISHFQYTAWPADGFSHDPDAFIDFFCNIDDLCAdlekhkadGKIAPIIIDC 228
RESP18 pfam14948
RESP18 domain; This domain is found in the glucocorticoid-responsive protein regulated ...
 80-126 2.24e-03

RESP18 domain; This domain is found in the glucocorticoid-responsive protein regulated endocrine-specific protein 18 (RESP18) and in the N-terminal extracellular region of receptor-type tyrosine-protein phosphatases containing the protein-tyrosine phosphatase receptor IA-2 domain (pfam11548).


Pssm-ID: 464394  Cd Length: 103  Bit Score: 38.66  E-value: 2.24e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 74216145    80 HLKVTLQKLSRTGFTWQDDYTQRVIAQELANLPK-----AYLWHGEASGPAR 126
Cdd:pfam14948  23 HLQVVLHQIVPQGLFWKDDLTQDVMTQKMEHISRlhpqdPCLKDGKAVFPTR 74
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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