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Conserved domains on  [gi|226052731|ref|NP_035345|]
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receptor-type tyrosine-protein phosphatase N2 precursor [Mus musculus]

Protein Classification

protein-tyrosine phosphatase family protein; phosphatase PAP2/dual specificity phosphatase family protein( domain architecture ID 13134034)

cys-based protein-tyrosine phosphatase (PTP) family protein may be a PTP or a dual-specificity phosphatase (DUSP or DSP), and may catalyze the dephosphorylation of target phosphoproteins at tyrosine or tyrosine and serine/threonine residues, respectively| 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
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 713-995 0e+00

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: 644.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  713 TGHMILAYMEDHLKNKNRLEKEWEALCAYQAEPNSSLVAQREENAPKNRSLAVLTYDHSRILLKSQNSHGSSDYINASPI 792
Cdd:cd14610     1 TGHMILSYMEDHLKNKNRLEKEWEALCAYQAEPNATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  793 MDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNLYHVYEVNLVSEHIWCQDFL 872
Cdd:cd14610    81 MDHDPRNPAYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSNLYHIYEVNLVSEHIWCEDFL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  873 VRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYVLIDMVLNKMA 952
Cdd:cd14610   161 VRSFYLKNLQTNETRTVTQFHFLSWNDQGVPASTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMA 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 226052731  953 KGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEVNAI 995
Cdd:cd14610   241 KGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEVNAI 283
Receptor_IA-2 pfam11548
Protein-tyrosine phosphatase receptor IA-2; IA-2 is a protein-tyrosine phosphatase receptor ...
 495-583 1.87e-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: 1.87e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731   495 EQQGYILTGNNPLSPEKGKQLMDQVAHILRVPSSFFADIKVLGPAVTFKVSANIQNMTTADVIKAAADNKDQLEKATGLT 574
Cdd:pfam11548    1 EEYGYIVTDNDPLSWEEGLRLMEKVAELLHLPMSSFADIRVLGPAVTFKVRANNKNLTAADVAKAAVDIKDKLEKETGLK 80


                   ....*....
gi 226052731   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 2.17e-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: 2.17e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 226052731    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 ...
 713-995 0e+00

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: 644.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  713 TGHMILAYMEDHLKNKNRLEKEWEALCAYQAEPNSSLVAQREENAPKNRSLAVLTYDHSRILLKSQNSHGSSDYINASPI 792
Cdd:cd14610     1 TGHMILSYMEDHLKNKNRLEKEWEALCAYQAEPNATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  793 MDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNLYHVYEVNLVSEHIWCQDFL 872
Cdd:cd14610    81 MDHDPRNPAYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSNLYHIYEVNLVSEHIWCEDFL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  873 VRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYVLIDMVLNKMA 952
Cdd:cd14610   161 VRSFYLKNLQTNETRTVTQFHFLSWNDQGVPASTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMA 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 226052731  953 KGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEVNAI 995
Cdd:cd14610   241 KGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEVNAI 283
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
731-990 3.25e-107

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 333.47  E-value: 3.25e-107
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731    731 LEKEWEALCAYQAEPNSSLVAQREENAPKNRSLAVLTYDHSRILLKSQNsHGSSDYINASPIMDHDPRNpAYIATQGPLP 810
Cdd:smart00194    2 LEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPP-GEGSDYINASYIDGPNGPK-AYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731    811 ATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEG--SNLYHVYEVNLVSEHIwCQDFLVRSFYLKNLQTNETRT 888
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEgePLTYGDITVTLKSVEK-VDDYTIRTLEVTNTGCSETRT 158

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731    889 VTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYVLIDMVLNKMAKGaKEIDIAATLEHLR 968
Cdd:smart00194  159 VTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAG-KEVDIFEIVKELR 237

                           250       260
                    ....*....|....*....|..
gi 226052731    969 DQRPGMVQTKEQFEFALTAVAE 990
Cdd:smart00194  238 SQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
756-990 3.35e-103

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 321.88  E-value: 3.35e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731   756 NAPKNRSLAVLTYDHSRILLKSQNshGSSDYINASPIMDHdPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLS 835
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDP--GPSDYINASYIDGY-KKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731   836 ENGVRQCHHYWPD--EGSNLYHVYEVNLVSEHIWCQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFR 913
Cdd:pfam00102   78 EKGREKCAQYWPEeeGESLEYGDFTVTLKKEKEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLL 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 226052731   914 RKVNKCY-RGRSCPIIVHCSDGAGRSGTYVLIDMVLNKMAKGaKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAE 990
Cdd:pfam00102  158 RKVRKSSlDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAE-GEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
Receptor_IA-2 pfam11548
Protein-tyrosine phosphatase receptor IA-2; IA-2 is a protein-tyrosine phosphatase receptor ...
 495-583 1.87e-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: 1.87e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731   495 EQQGYILTGNNPLSPEKGKQLMDQVAHILRVPSSFFADIKVLGPAVTFKVSANIQNMTTADVIKAAADNKDQLEKATGLT 574
Cdd:pfam11548    1 EEYGYIVTDNDPLSWEEGLRLMEKVAELLHLPMSSFADIRVLGPAVTFKVRANNKNLTAADVAKAAVDIKDKLEKETGLK 80


                   ....*....
gi 226052731   575 ILQSGIRPK 583
Cdd:pfam11548   81 ILQAGVGDK 89
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 752-983 3.05e-41

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 154.00  E-value: 3.05e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  752 QREENAPKNRSLAVLTYDHSRILLKSQnSHGSSDYINASPImDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVML 831
Cdd:PHA02747   47 EKPENQPKNRYWDIPCWDHNRVILDSG-GGSTSDYIHANWI-DGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVML 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  832 TPLSE-NGVRQCHHYW-PDEGSNL----YHVYEVNLVsehiwcqdflVRSFYLKNL------QTNETRTVTQFHFLSWYD 899
Cdd:PHA02747  125 TPTKGtNGEEKCYQYWcLNEDGNIdmedFRIETLKTS----------VRAKYILTLieitdkILKDSRKISHFQCSEWFE 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  900 QGVPSSTRSLLDF-------RRKVNKCYRGRS---CPIIVHCSDGAGRSGTYVLIDMVLNKMAKgAKEIDIAATLEHLRD 969
Cdd:PHA02747  195 DETPSDHPDFIKFikiidinRKKSGKLFNPKDallCPIVVHCSDGVGKTGIFCAVDICLNQLVK-RKAICLAKTAEKIRE 273

                         250
                  ....*....|....
gi 226052731  970 QRPGMVQTKEQFEF 983
Cdd:PHA02747  274 QRHAGIMNFDDYLF 287
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
729-996 8.60e-37

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 140.23  E-value: 8.60e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  729 NRLEKEWEALcAYQAEPNSSLvaQREENAPKNRSLAVLTYDHSRIllksqnshGSSD-YINASPIMDHDPRNpaYIATQG 807
Cdd:COG5599    18 SRLSTLTNEL-APSHNDPQYL--QNINGSPLNRFRDIQPYKETAL--------RANLgYLNANYIQVIGNHR--YIATQY 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  808 PLPATVADFWQMVWESGCAVIVMLTPLSENGVRQ--CHHYWPDEGSNLYHVYEVNLVSEHIWCQDFLVRSFYLKNLQTN- 884
Cdd:COG5599    85 PLEEQLEDFFQMLFDNNTPVLVVLASDDEISKPKvkMPVYFRQDGEYGKYEVSSELTESIQLRDGIEARTYVLTIKGTGq 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  885 ETRTVTQFHFLSWYDQGVPSST--RSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYVLIdMVLNKMAKGAKEIDIAA 962
Cdd:COG5599   165 KKIEIPVLHVKNWPDHGAISAEalKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIAC-LALSKSINALVQITLSV 243

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 226052731  963 --TLEHLRDQR-PGMVQTKEQFEFaLTAVAEEVNAIL 996
Cdd:COG5599   244 eeIVIDMRTSRnGGMVQTSEQLDV-LVKLAEQQIRPL 279
RESP18 pfam14948
RESP18 domain; This domain is found in the glucocorticoid-responsive protein regulated ...
 80-126 2.17e-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: 2.17e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 226052731    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 ...
 713-995 0e+00

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: 644.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  713 TGHMILAYMEDHLKNKNRLEKEWEALCAYQAEPNSSLVAQREENAPKNRSLAVLTYDHSRILLKSQNSHGSSDYINASPI 792
Cdd:cd14610     1 TGHMILSYMEDHLKNKNRLEKEWEALCAYQAEPNATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  793 MDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNLYHVYEVNLVSEHIWCQDFL 872
Cdd:cd14610    81 MDHDPRNPAYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSNLYHIYEVNLVSEHIWCEDFL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  873 VRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYVLIDMVLNKMA 952
Cdd:cd14610   161 VRSFYLKNLQTNETRTVTQFHFLSWNDQGVPASTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMA 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 226052731  953 KGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEVNAI 995
Cdd:cd14610   241 KGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEVNAI 283
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 715-995 0e+00

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: 557.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  715 HMILAYMEDHLKNKNRLEKEWEALCAYQAEPNSSLVAQREENAPKNRSLAVLTYDHSRILLKSQNSHGSSDYINASPIMD 794
Cdd:cd14609     1 HMILAYMEDHLRNRDRLAKEWQALCAYQAEPNTCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPIIE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  795 HDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNLYHVYEVNLVSEHIWCQDFLVR 874
Cdd:cd14609    81 HDPRMPAYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHIYEVNLVSEHIWCEDFLVR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  875 SFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYVLIDMVLNKMAKG 954
Cdd:cd14609   161 SFYLKNVQTQETRTLTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKG 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 226052731  955 AKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEVNAI 995
Cdd:cd14609   241 VKEIDIAATLEHVRDQRPGMVRTKDQFEFALTAVAEEVNAI 281
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 786-993 1.23e-158

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: 465.38  E-value: 1.23e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  786 YINASPIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNLYHVYEVNLVSEH 865
Cdd:cd14546     1 YINASTIYDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEVYHIYEVHLVSEH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  866 IWCQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYVLID 945
Cdd:cd14546    81 IWCDDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSCPIVVHCSDGAGRTGTYILID 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 226052731  946 MVLNKMAKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEVN 993
Cdd:cd14546   161 MVLNRMAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAEEVN 208
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
731-990 3.25e-107

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 333.47  E-value: 3.25e-107
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731    731 LEKEWEALCAYQAEPNSSLVAQREENAPKNRSLAVLTYDHSRILLKSQNsHGSSDYINASPIMDHDPRNpAYIATQGPLP 810
Cdd:smart00194    2 LEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPP-GEGSDYINASYIDGPNGPK-AYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731    811 ATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEG--SNLYHVYEVNLVSEHIwCQDFLVRSFYLKNLQTNETRT 888
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEgePLTYGDITVTLKSVEK-VDDYTIRTLEVTNTGCSETRT 158

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731    889 VTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYVLIDMVLNKMAKGaKEIDIAATLEHLR 968
Cdd:smart00194  159 VTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAG-KEVDIFEIVKELR 237

                           250       260
                    ....*....|....*....|..
gi 226052731    969 DQRPGMVQTKEQFEFALTAVAE 990
Cdd:smart00194  238 SQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
756-990 3.35e-103

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 321.88  E-value: 3.35e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731   756 NAPKNRSLAVLTYDHSRILLKSQNshGSSDYINASPIMDHdPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLS 835
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDP--GPSDYINASYIDGY-KKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731   836 ENGVRQCHHYWPD--EGSNLYHVYEVNLVSEHIWCQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFR 913
Cdd:pfam00102   78 EKGREKCAQYWPEeeGESLEYGDFTVTLKKEKEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLL 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 226052731   914 RKVNKCY-RGRSCPIIVHCSDGAGRSGTYVLIDMVLNKMAKGaKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAE 990
Cdd:pfam00102  158 RKVRKSSlDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAE-GEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 786-983 3.01e-86

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: 275.32  E-value: 3.01e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  786 YINASPIMDHDPRNpAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSN--LYHVYEVNLVS 863
Cdd:cd00047     1 YINASYIDGYRGPK-EYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKplEYGDITVTLVS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  864 EHIwCQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYVL 943
Cdd:cd00047    80 EEE-LSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTGTFIA 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 226052731  944 IDMVLNKMAKGaKEIDIAATLEHLRDQRPGMVQTKEQFEF 983
Cdd:cd00047   159 IDILLERLEAE-GEVDVFEIVKALRKQRPGMVQTLEQYEF 197
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 754-994 3.68e-72

catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs) include three vertebrate members: LAR (or PTPRF), R-PTP-delta (or PTPRD), and R-PTP-sigma (or PTPRS). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules; they bind to distinct synaptic membrane proteins and are physiologically responsible for mediating presynaptic development by shaping various synaptic adhesion pathways. They play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. LAR-RPTPs contain an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350401 [Multi-domain]  Cd Length: 238  Bit Score: 238.84  E-value: 3.68e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  754 EENAPKNRSLAVLTYDHSRILLKSQNSHGSSDYINASpIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTP 833
Cdd:cd14553     1 EVNKPKNRYANVIAYDHSRVILQPIEGVPGSDYINAN-YCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  834 LSENGVRQCHHYWPDEGSNLYHVYEVNLVsEHIWCQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFR 913
Cdd:cd14553    80 LEERSRVKCDQYWPTRGTETYGLIQVTLL-DTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  914 RKVNKCYRGRSCPIIVHCSDGAGRSGTYVLIDMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEVN 993
Cdd:cd14553   159 RRVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERI-KHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLEAVT 237


                  .
gi 226052731  994 A 994
Cdd:cd14553   238 C 238
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 756-983 3.28e-70

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: 234.57  E-value: 3.28e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  756 NAPKNRSLAVLTYDHSRILLKSQNSHGSSDYINASpIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLS 835
Cdd:cd14543    29 NQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINAN-FMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLVIVMTTRVV 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  836 ENGVRQCHHYWPDEGSNLYHVYEVNLVSEHIWC-QDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRR 914
Cdd:cd14543   108 ERGRVKCGQYWPLEEGSSLRYGDLTVTNLSVENkEHYKKTTLEIHNTETDESRQVTHFQFTSWPDFGVPSSAAALLDFLG 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  915 KVnKCYRGRSC--------------PIIVHCSDGAGRSGTYVLIDMVLNKMAKGAKeIDIAATLEHLRDQRPGMVQTKEQ 980
Cdd:cd14543   188 EV-RQQQALAVkamgdrwkghppgpPIVVHCSAGIGRTGTFCTLDICLSQLEDVGT-LNVMQTVRRMRTQRAFSIQTPDQ 265


                  ...
gi 226052731  981 FEF 983
Cdd:cd14543   266 YYF 268
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 756-987 1.71e-69

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: 231.64  E-value: 1.71e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  756 NAPKNRSLAVLTYDHSRILLKSQNSHGSSDYINASPIMDHDPRNpAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLS 835
Cdd:cd14554     6 NKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRG-AYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKLR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  836 ENGVRQCHHYWPDEGSNLYHVYEVNLVSEHIWCQdFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRK 915
Cdd:cd14554    85 EMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQ-YILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQ 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 226052731  916 VNKCYR--GRSCPIIVHCSDGAGRSGTYVLIDMVLNKM-AKGAkeIDIAATLEHLRDQRPGMVQTKEQFEFALTA 987
Cdd:cd14554   164 VHKTKEqfGQEGPITVHCSAGVGRTGVFITLSIVLERMrYEGV--VDVFQTVKLLRTQRPAMVQTEDQYQFCYRA 236
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 786-983 3.67e-66

fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae protein-tyrosine phosphatases 1 (PTP1) and 2 (PTP2), Schizosaccharomyces pombe PTP1, PTP2, and PTP3, and similar fungal proteins. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. PTP2, together with PTP3, is the major phosphatase that dephosphorylates and inactivates the MAP kinase HOG1 and also modulates its subcellular localization.


Pssm-ID: 350509 [Multi-domain]  Cd Length: 212  Bit Score: 221.35  E-value: 3.67e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  786 YINASPI-MDHDPRNpAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNLYH-VYEVNLVS 863
Cdd:cd18533     1 YINASYItLPGTSSK-RYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGEYgDLTVELVS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  864 EH-IWCQDFLVRSFYLKNlQTNETRTVTQFHFLSWYDQGVPSSTRSLL---DFRRKVNKCYRGRScPIIVHCSDGAGRSG 939
Cdd:cd18533    80 EEeNDDGGFIVREFELSK-EDGKVKKVYHIQYKSWPDFGVPDSPEDLLtliKLKRELNDSASLDP-PIIVHCSAGVGRTG 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 226052731  940 TYVLIDMVLNKMAKGA-------KEID-IAATLEHLRDQRPGMVQTKEQFEF 983
Cdd:cd18533   158 TFIALDSLLDELKRGLsdsqdleDSEDpVYEIVNQLRKQRMSMVQTLRQYIF 209
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 765-983 1.23e-65

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: 220.30  E-value: 1.23e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  765 VLTYDHSRILLKSQNSHGSSDYINASPIMD-HDPRNpaYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCH 843
Cdd:cd14548     5 ILPYDHSRVKLIPINEEEGSDYINANYIPGyNSPRE--FIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVKCD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  844 HYWP-DEGSNLYHVYEVNLVSEHIwCQDFLVRSFYLKNLQtnETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVnKCYRG 922
Cdd:cd14548    83 HYWPfDQDPVYYGDITVTMLSESV-LPDWTIREFKLERGD--EVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLV-RDYIK 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226052731  923 RSC-PIIVHCSDGAGRSGTYVLIDMVLNKMAKgAKEIDIAATLEHLRDQRPGMVQTKEQFEF 983
Cdd:cd14548   159 QEKgPTIVHCSAGVGRTGTFIALDRLLQQIES-EDYVDIFGIVYDLRKHRPLMVQTEAQYIF 219
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 786-983 6.26e-65

catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 subfamily of receptor-type phosphotyrosine phosphatases (RPTP) is composed of receptor-type tyrosine-protein phosphatase Z (PTPRZ) and G (PTPRG). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. They are type 1 integral membrane proteins consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350397 [Multi-domain]  Cd Length: 204  Bit Score: 217.60  E-value: 6.26e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  786 YINASPImDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNLYHVYEVNLVSEH 865
Cdd:cd14549     1 YINANYV-DGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTETYGNIQVTLLSTE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  866 IWCQdFLVRSFYLKNLQ------TNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSG 939
Cdd:cd14549    80 VLAT-YTVRTFSLKNLKlkkvkgRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVGRTG 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 226052731  940 TYVLIDMVLnKMAKGAKEIDIAATLEHLRDQRPGMVQTKEQFEF 983
Cdd:cd14549   159 TYIVIDSML-QQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIF 201
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 756-989 5.75e-64

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: 216.56  E-value: 5.75e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  756 NAPKNRSLAVLTYDHSRILLKS-QNSHGSSDYINASPIM------DHDPRNPAYIATQGPLPATVADFWQMVWESGCAVI 828
Cdd:cd14544     1 NKGKNRYKNILPFDHTRVILKDrDPNVPGSDYINANYIRnenegpTTDENAKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  829 VMLTPLSENGVRQCHHYWPDEG-SNLYHVYEVNLVSEHIwCQDFLVRSFYLKNL-QTNETRTVTQFHFLSWYDQGVPSST 906
Cdd:cd14544    81 VMTTKEVERGKNKCVRYWPDEGmQKQYGPYRVQNVSEHD-TTDYTLRELQVSKLdQGDPIREIWHYQYLSWPDHGVPSDP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  907 RSLLDFRRKVNKCYRGR--SCPIIVHCSDGAGRSGTYVLIDMVLNKMAKG--AKEIDIAATLEHLRDQRPGMVQTKEQFE 982
Cdd:cd14544   160 GGVLNFLEDVNQRQESLphAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKglDCDIDIQKTIQMVRSQRSGMVQTEAQYK 239


                  ....*..
gi 226052731  983 FALTAVA 989
Cdd:cd14544   240 FIYVAVA 246
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 730-992 6.39e-62

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: 211.82  E-value: 6.39e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  730 RLEKEWEALCAYQ--AEPNSSLvaqrEENAPKNRSLAVLTYDHSRILLKSQNSHGSSDYINASPIMDHDPRNpAYIATQG 807
Cdd:cd14626    17 KFSQEYESIDPGQqfTWENSNL----EVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGYRKQN-AYIATQG 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  808 PLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNLYHVYEVNLVsEHIWCQDFLVRSFYLKNLQTNETR 887
Cdd:cd14626    92 PLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTETYGMIQVTLL-DTVELATYSVRTFALYKNGSSEKR 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  888 TVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYVLIDMVLNKMaKGAKEIDIAATLEHL 967
Cdd:cd14626   171 EVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERM-KHEKTVDIYGHVTCM 249

                         250       260
                  ....*....|....*....|....*
gi 226052731  968 RDQRPGMVQTKEQFEFALTAVAEEV 992
Cdd:cd14626   250 RSQRNYMVQTEDQYIFIHEALLEAA 274
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 785-998 2.42e-61

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: 207.95  E-value: 2.42e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  785 DYINASPIMDHDPRNPA---YIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEG-SNLYHVYEVN 860
Cdd:cd14541     1 DYINANYVNMEIPGSGIvnrYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGeTMQFGNLQIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  861 LVSEHIwCQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGT 940
Cdd:cd14541    81 CVSEEV-TPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCSAGIGRTGV 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 226052731  941 YVLIDMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFaltaVAEevnAILKA 998
Cdd:cd14541   160 LITMETAMCLI-EANEPVYPLDIVRTMRDQRAMLIQTPSQYRF----VCE---AILRV 209
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 759-983 4.69e-61

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: 207.63  E-value: 4.69e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  759 KNRSLAVLTYDHSRILLKSQNshGSSDYINASPI-MDHDPRNpaYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSEN 837
Cdd:cd14545     1 LNRYRDRDPYDHDRSRVKLKQ--GDNDYINASLVeVEEAKRS--YILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  838 GVRQCHHYWP---DEGSNLYHV-YEVNLVSEHIWcQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFR 913
Cdd:cd14545    77 GQIKCAQYWPqgeGNAMIFEDTgLKVTLLSEEDK-SYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFL 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 226052731  914 RKVNK--CYRGRSCPIIVHCSDGAGRSGTYVLIDMVLNKMAKG-AKEIDIAATLEHLRDQRPGMVQTKEQFEF 983
Cdd:cd14545   156 QKVREsgSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGnPSSVDVKKVLLEMRKYRMGLIQTPDQLRF 228
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 760-983 9.15e-61

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


Pssm-ID: 350463 [Multi-domain]  Cd Length: 229  Bit Score: 206.98  E-value: 9.15e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  760 NRSLAVLTYDHSRILLKSQNsHGSSDYINASPIMDHDpRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGV 839
Cdd:cd14615     1 NRYNNVLPYDISRVKLSVQS-HSTDDYINANYMPGYN-SKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  840 RQCHHYWPDEGSNLYHVYEVNLVSEhIWCQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKC 919
Cdd:cd14615    79 TKCEEYWPSKQKKDYGDITVTMTSE-IVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVREY 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 226052731  920 YRG--RSCPIIVHCSDGAGRSGTYVLIDMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQFEF 983
Cdd:cd14615   158 MKQnpPNSPILVHCSAGVGRTGTFIAIDRLIYQI-ENENVVDVYGIVYDLRMHRPLMVQTEDQYVF 222
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 760-983 1.03e-59

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: 203.97  E-value: 1.03e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  760 NRSLAVLTYDHSRILLKSQNSHGSSDYINASpIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGV 839
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINAN-YMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  840 RQCHHYWP-DEGSNLYHVYEVNLVSEHIwCQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNK 918
Cdd:cd14619    80 VKCEHYWPlDYTPCTYGHLRVTVVSEEV-MENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRQ 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226052731  919 CYRGR--SCPIIVHCSDGAGRSGTYVLIDMVLNKMAKgAKEIDIAATLEHLRDQRPGMVQTKEQFEF 983
Cdd:cd14619   159 WLDQTmsGGPTVVHCSAGVGRTGTLIALDVLLQQLQS-EGLLGPFSFVQKMRENRPLMVQTESQYVF 224
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 786-990 1.47e-59

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: 202.60  E-value: 1.47e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  786 YINASPI-MDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPD---EGSNLYHVYEVNL 861
Cdd:cd14538     1 YINASHIrIPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDslnKPLICGGRLEVSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  862 VSEHIWcQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYrgRSCPIIVHCSDGAGRSGTY 941
Cdd:cd14538    81 EKYQSL-QDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIH--NSGPIVVHCSAGIGRTGVL 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 226052731  942 VLIDMVLNKMAKGaKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAE 990
Cdd:cd14538   158 ITIDVALGLIERD-LPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLE 205
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 718-992 2.48e-58

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: 202.25  E-value: 2.48e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  718 LAYMEDHLKNKN--RLEKEWEALcayqaEPNSSLVAQR---EENAPKNRSLAVLTYDHSRILLKSQNSHGSSDYINASPI 792
Cdd:cd14625     9 LAEHTERLKANDnlKLSQEYESI-----DPGQQFTWEHsnlEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINANYI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  793 mDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNLYHVYEVNLVsEHIWCQDFL 872
Cdd:cd14625    84 -DGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRGTETYGMIQVTLL-DTIELATFC 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  873 VRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYVLIDMVLNKMa 952
Cdd:cd14625   162 VRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVIDAMLERI- 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 226052731  953 KGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEV 992
Cdd:cd14625   241 KHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAV 280
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 746-990 5.77e-57

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


Pssm-ID: 350454 [Multi-domain]  Cd Length: 266  Bit Score: 197.41  E-value: 5.77e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  746 NSSLVAQREENAPKNRSLAVLTYDHSRILLKSQNSH-GSSDYINASPIMDH--DPRNPA--YIATQGPLPATVADFWQMV 820
Cdd:cd14606     8 HQRLEGQRPENKSKNRYKNILPFDHSRVILQGRDSNiPGSDYINANYVKNQllGPDENAktYIASQGCLEATVNDFWQMA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  821 WESGCAVIVMLTPLSENGVRQCHHYWPDEGSN-LYHVYEVNLVSEHIwCQDFLVRSFYLKNLQTNET-RTVTQFHFLSWY 898
Cdd:cd14606    88 WQENSRVIVMTTREVEKGRNKCVPYWPEVGMQrAYGPYSVTNCGEHD-TTEYKLRTLQVSPLDNGELiREIWHYQYLSWP 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  899 DQGVPSSTRSLLDFRRKVNKCYRG--RSCPIIVHCSDGAGRSGTYVLIDMVLNKM-AKGAK-EIDIAATLEHLRDQRPGM 974
Cdd:cd14606   167 DHGVPSEPGGVLSFLDQINQRQESlpHAGPIIVHCSAGIGRTGTIIVIDMLMENIsTKGLDcDIDIQKTIQMVRAQRSGM 246

                         250
                  ....*....|....*.
gi 226052731  975 VQTKEQFEFALTAVAE 990
Cdd:cd14606   247 VQTEAQYKFIYVAIAQ 262
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 726-990 6.37e-57

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: 198.42  E-value: 6.37e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  726 KNKNRLEKEWEALCAYQAEPNSSLVAQREENAPKNRSLAVLTYDHSRILLKSQNSHGSSDYINASpIMDHDPRNPAYIAT 805
Cdd:cd14628    22 ENVTGMELEFKRLASSKAHTSRFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINAS-FIDGYRQQKAYIAT 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  806 QGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNLYHVYEVNLVSEHIWCQdFLVRSFYLKNLQTNE 885
Cdd:cd14628   101 QGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQ-YILREFKVTDARDGQ 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  886 TRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYR--GRSCPIIVHCSDGAGRSGTYVLIDMVLNKMaKGAKEIDIAAT 963
Cdd:cd14628   180 SRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEqfGQDGPISVHCSAGVGRTGVFITLSIVLERM-RYEGVVDIFQT 258

                         250       260
                  ....*....|....*....|....*..
gi 226052731  964 LEHLRDQRPGMVQTKEQFEFALTAVAE 990
Cdd:cd14628   259 VKMLRTQRPAMVQTEDQYQFCYRAALE 285
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 765-990 5.86e-56

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: 193.23  E-value: 5.86e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  765 VLTYDHSRILLKSQNSHGSSDYINASPIMDHDPRNpAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHH 844
Cdd:cd14620     4 ILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKN-KFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKCYQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  845 YWPDEGSNLYHVYEVNlVSEHIWCQDFLVRSFYLKNLQTNET---RTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYR 921
Cdd:cd14620    83 YWPDQGCWTYGNIRVA-VEDCVVLVDYTIRKFCIQPQLPDGCkapRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVKSVNP 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 226052731  922 GRSCPIIVHCSDGAGRSGTYVLIDMVLNkMAKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAE 990
Cdd:cd14620   162 VHAGPIVVHCSAGVGRTGTFIVIDAMID-MMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 786-983 8.66e-56

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: 191.84  E-value: 8.66e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  786 YINASPIMD-HDPRnpAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNlYHVYEVNLVSE 864
Cdd:cd14558     1 YINASFIDGyWGPK--SLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKT-YGDIEVELKDT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  865 HIwCQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKV------NKCYRGRSCPIIVHCSDGAGRS 938
Cdd:cd14558    78 EK-SPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIkqklpyKNSKHGRSVPIVVHCSDGSSRT 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 226052731  939 GTYVLIdmvLNKMAKGAKE--IDIAATLEHLRDQRPGMVQTKEQFEF 983
Cdd:cd14558   157 GIFCAL---WNLLESAETEkvVDVFQVVKALRKQRPGMVSTLEQYQF 200
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 731-990 8.69e-56

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: 195.34  E-value: 8.69e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  731 LEKEWEALCAYQAEPNSSLVAQREENAPKNRSLAVLTYDHSRILLKSQNSHGSSDYINASpIMDHDPRNPAYIATQGPLP 810
Cdd:cd14627    28 MELEFKRLANSKAHTSRFISANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINAS-FIDGYRQQKAYIATQGPLA 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  811 ATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNLYHVYEVNLVSEHIWCQdFLVRSFYLKNLQTNETRTVT 890
Cdd:cd14627   107 ETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQ-YILREFKVTDARDGQSRTVR 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  891 QFHFLSWYDQGVPSSTRSLLDFRRKVNKCYR--GRSCPIIVHCSDGAGRSGTYVLIDMVLNKMaKGAKEIDIAATLEHLR 968
Cdd:cd14627   186 QFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEqfGQDGPISVHCSAGVGRTGVFITLSIVLERM-RYEGVVDIFQTVKMLR 264

                         250       260
                  ....*....|....*....|..
gi 226052731  969 DQRPGMVQTKEQFEFALTAVAE 990
Cdd:cd14627   265 TQRPAMVQTEDEYQFCYQAALE 286
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 750-990 3.35e-55

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: 193.61  E-value: 3.35e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  750 VAQREENAPKNRSLAVLTYDHSRILLKSQNSHGSSDYINASPIMD-HDPRnpAYIATQGPLPATVADFWQMVWESGCAVI 828
Cdd:cd14604    51 TGEKEENVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGvYGPK--AYIATQGPLANTVIDFWRMIWEYNVAII 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  829 VMLTPLSENGVRQCHHYWPdegsnLYHVYEVNLVSEHIWCQ------DFLVRSFYLKnLQtNETRTVTQFHFLSWYDQGV 902
Cdd:cd14604   129 VMACREFEMGRKKCERYWP-----LYGEEPMTFGPFRISCEaeqartDYFIRTLLLE-FQ-NETRRLYQFHYVNWPDHDV 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  903 PSSTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYVLIDMVLN--KMAKGAKEIDIAATLEHLRDQRPGMVQTKEQ 980
Cdd:cd14604   202 PSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNllKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQ 281

                         250
                  ....*....|
gi 226052731  981 FEFALTAVAE 990
Cdd:cd14604   282 YELVHRAIAQ 291
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 760-983 4.81e-55

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: 190.69  E-value: 4.81e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  760 NRSLAVLTYDHSRILLKSQNSHGSSDYINASPIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGV 839
Cdd:cd14547     1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYDGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  840 RqCHHYWPDEGSNLYHVYEVnLVSEHIWCQDFLVRSFYLKNlqTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKC 919
Cdd:cd14547    81 K-CAQYWPEEENETYGDFEV-TVQSVKETDGYTVRKLTLKY--GGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEEA 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 226052731  920 -YRGRSC-PIIVHCSDGAGRSGTYVLIDMVLNKMAKGAKeIDIAATLEHLRDQRPGMVQTKEQFEF 983
Cdd:cd14547   157 rQTEPHRgPIVVHCSAGIGRTGCFIATSIGCQQLREEGV-VDVLGIVCQLRLDRGGMVQTAEQYEF 221
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 755-992 6.69e-55

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


Pssm-ID: 350505 [Multi-domain]  Cd Length: 274  Bit Score: 192.17  E-value: 6.69e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  755 ENAPKNRSLAVLTYDHSRILLKSQNSHGS--SDYINASPIMDHDpRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLT 832
Cdd:cd17667    26 DNKHKNRYINILAYDHSRVKLRPLPGKDSkhSDYINANYVDGYN-KAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMIT 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  833 PLSENGVRQCHHYWPDEGSNLYHVYEVNLVSEHIW-CqdFLVRSFYLKNLQT------------NEtRTVTQFHFLSWYD 899
Cdd:cd17667   105 NLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHaC--YTVRRFSIRNTKVkkgqkgnpkgrqNE-RTVIQYHYTQWPD 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  900 QGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYVLIDMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKE 979
Cdd:cd17667   182 MGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQI-KDKSTVNVLGFLKHIRTQRNYLVQTEE 260

                         250
                  ....*....|...
gi 226052731  980 QFEFALTAVAEEV 992
Cdd:cd17667   261 QYIFIHDALLEAI 273
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 786-983 7.46e-55

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: 189.17  E-value: 7.46e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  786 YINASPIMDHDpRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNL--YHVYEVNLVS 863
Cdd:cd14542     1 YINANFIKGVS-GSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQlqFGPFKISLEK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  864 EHIWCQDFLVRSfyLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYVL 943
Cdd:cd14542    80 EKRVGPDFLIRT--LKVTFQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGCGRTGTICA 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 226052731  944 IDMVLNKMAKGA--KEIDIAATLEHLRDQRPGMVQTKEQFEF 983
Cdd:cd14542   158 IDYVWNLLKTGKipEEFSLFDLVREMRKQRPAMVQTKEQYEL 199
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 721-992 4.25e-54

catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type tyrosine-protein phosphatase D (PTPRD), also known as receptor-type tyrosine-protein phosphatase delta (R-PTP-delta), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules that play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. PTPRD is involved in pre-synaptic differentiation through interaction with SLITRK2. It contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350472 [Multi-domain]  Cd Length: 284  Bit Score: 190.33  E-value: 4.25e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  721 MEDHLK----NKN-RLEKEWEALcayqaEPNSSLVAQR---EENAPKNRSLAVLTYDHSRILLKSQNSHGSSDYINASPI 792
Cdd:cd14624     9 LADHIErlkaNDNlKFSQEYESI-----DPGQQFTWEHsnlEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINANYI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  793 MDHDPRNpAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNLYHVYEVNLVsEHIWCQDFL 872
Cdd:cd14624    84 DGYRKQN-AYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRGTETYGLIQVTLL-DTVELATYC 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  873 VRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYVLIDMVLNKMa 952
Cdd:cd14624   162 VRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERI- 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 226052731  953 KGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEV 992
Cdd:cd14624   241 KHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAV 280
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 731-990 5.81e-54

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: 189.94  E-value: 5.81e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  731 LEKEWEALCAYQAEPNSSLVAQREENAPKNRSLAVLTYDHSRILLKSQNSHGSSDYINASpIMDHDPRNPAYIATQGPLP 810
Cdd:cd14629    28 MELEFKLLANSKAHTSRFISANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINAS-FIDGYRQQKAYIATQGPLA 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  811 ATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNLYHVYEVNLVSEHIWCQdFLVRSFYLKNLQTNETRTVT 890
Cdd:cd14629   107 ETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQ-YILREFKVTDARDGQSRTIR 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  891 QFHFLSWYDQGVPSSTRSLLDFRRKVNKCYR--GRSCPIIVHCSDGAGRSGTYVLIDMVLNKMaKGAKEIDIAATLEHLR 968
Cdd:cd14629   186 QFQFTDWPEQGVPKTGEGFIDFIGQVHKTKEqfGQDGPITVHCSAGVGRTGVFITLSIVLERM-RYEGVVDMFQTVKTLR 264

                         250       260
                  ....*....|....*....|..
gi 226052731  969 DQRPGMVQTKEQFEFALTAVAE 990
Cdd:cd14629   265 TQRPAMVQTEDQYQLCYRAALE 286
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 754-983 6.29e-54

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: 187.73  E-value: 6.29e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  754 EENAPKNRSLAVLTYDHSRILLKSQNshgssDYINASPI-MDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLT 832
Cdd:cd14597     1 KENRKKNRYKNILPYDTTRVPLGDEG-----GYINASFIkMPVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  833 PLSENGVRQCHHYWPDE-GSNLYHVYEVNLVSEHIWCQD-FLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLL 910
Cdd:cd14597    76 QEVEGGKIKCQRYWPEIlGKTTMVDNRLQLTLVRMQQLKnFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPEQLL 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 226052731  911 DFRRKVNKCYrgRSCPIIVHCSDGAGRSGTYVLIDMVLNKMAKGAkEIDIAATLEHLRDQRPGMVQTKEQFEF 983
Cdd:cd14597   156 TFISYMRHIH--KSGPIITHCSAGIGRSGTLICIDVVLGLISKDL-DFDISDIVRTMRLQRHGMVQTEDQYIF 225
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 754-990 6.32e-54

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: 187.93  E-value: 6.32e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  754 EENAPKNRSLAVLTYDHSRILLKSQNSHGSSDYINASPIMD-HDPRNpaYIATQGPLPATVADFWQMVWESGCAVIVMLT 832
Cdd:cd14630     1 DENRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGyHRPRH--YIATQGPMQETVKDFWRMIWQENSASVVMVT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  833 PLSENGVRQCHHYWPDEgSNLYHVYEVNLVsEHIWCQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDF 912
Cdd:cd14630    79 NLVEVGRVKCVRYWPDD-TEVYGDIKVTLI-ETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGF 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 226052731  913 RRKVNKCYRGRSCPIIVHCSDGAGRSGTYVLIDMVLNkMAKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAE 990
Cdd:cd14630   157 VRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLD-MAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILE 233
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 755-988 9.27e-54

catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11), also called SH2 domain-containing tyrosine phosphatase 2 (SHP-2 or SHP2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 promotes the activation of the RAS/Mitogen-Activated Protein Kinases (MAPK) Extracellular-Regulated Kinases 1/2 (ERK1/2) pathway, a canonical signaling cascade that plays key roles in various cellular processes, including proliferation, survival, differentiation, migration, or metabolism. It also regulates the phosphoinositide 3-kinase (PI3K)/AKT pathway, a fundamental cascade that functions in cell survival, proliferation, migration, morphogenesis, and metabolism. PTPN11 dysregulation is associated with several developmental diseases and malignancies, such as Noonan syndrome and juvenile myelomonocytic leukemia. It contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.


Pssm-ID: 350453 [Multi-domain]  Cd Length: 253  Bit Score: 187.92  E-value: 9.27e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  755 ENAPKNRSLAVLTYDHSRILLKSQN-SHGSSDYINASPIM-DHD-PRNPA-----YIATQGPLPATVADFWQMVWESGCA 826
Cdd:cd14605     1 ENKNKNRYKNILPFDHTRVVLHDGDpNEPVSDYINANIIMpEFEtKCNNSkpkksYIATQGCLQNTVNDFWRMVFQENSR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  827 VIVMLTPLSENGVRQCHHYWPDEGS-NLYHVYEVNLVSEHIwCQDFLVRSFYLKNL-QTNETRTVTQFHFLSWYDQGVPS 904
Cdd:cd14605    81 VIVMTTKEVERGKSKCVKYWPDEYAlKEYGVMRVRNVKESA-AHDYILRELKLSKVgQGNTERTVWQYHFRTWPDHGVPS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  905 STRSLLDFRRKVNKCYRG--RSCPIIVHCSDGAGRSGTYVLIDMVLNKM-AKGAK-EIDIAATLEHLRDQRPGMVQTKEQ 980
Cdd:cd14605   160 DPGGVLDFLEEVHHKQESimDAGPVVVHCSAGIGRTGTFIVIDILIDIIrEKGVDcDIDVPKTIQMVRSQRSGMVQTEAQ 239


                  ....*...
gi 226052731  981 FEFALTAV 988
Cdd:cd14605   240 YRFIYMAV 247
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 731-990 1.16e-53

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: 188.33  E-value: 1.16e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  731 LEKEWEALCAYQAEPNSSlvAQREENAPKNRSLAVLTYDHSRILLKSQNSHGSSDYINASPImDHDPRNPAYIATQGPLP 810
Cdd:cd14633    17 FKEEYESFFEGQSAPWDS--AKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYI-DGYHRPNHYIATQGPMQ 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  811 ATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEgSNLYHVYEVNLVSEHIwCQDFLVRSFYLKNLQTNETRTVT 890
Cdd:cd14633    94 ETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDD-TEIYKDIKVTLIETEL-LAEYVIRTFAVEKRGVHEIREIR 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  891 QFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYVLIDMVLNkMAKGAKEIDIAATLEHLRDQ 970
Cdd:cd14633   172 QFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLD-MAEREGVVDIYNCVRELRSR 250

                         250       260
                  ....*....|....*....|
gi 226052731  971 RPGMVQTKEQFEFALTAVAE 990
Cdd:cd14633   251 RVNMVQTEEQYVFIHDAILE 270
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 721-990 1.76e-53

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: 188.69  E-value: 1.76e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  721 MEDHLKNKNRL-EKEWEAL--CAYQAepnSSLVAQREENAPKNRSLAVLTYDHSRILLKSQNSHGSSDYINASPIMDHDP 797
Cdd:cd14621    17 INRRMADDNKLfREEFNALpaCPIQA---TCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINASFINGYQE 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  798 RNpAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNLYHVYEVNlVSEHIWCQDFLVRSFY 877
Cdd:cd14621    94 KN-KFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGCWTYGNIRVS-VEDVTVLVDYTVRKFC 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  878 LKNL----QTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYVLIDMVLNkMAK 953
Cdd:cd14621   172 IQQVgdvtNKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVIDAMLD-MMH 250

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 226052731  954 GAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAE 990
Cdd:cd14621   251 AERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLE 287
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 786-990 5.79e-53

catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization.


Pssm-ID: 350444 [Multi-domain]  Cd Length: 207  Bit Score: 184.18  E-value: 5.79e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  786 YINASPI-MDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNLYHV--YEVNLV 862
Cdd:cd14596     1 YINASYItMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELenYQLRLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  863 SEHIwCQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYrgRSCPIIVHCSDGAGRSGTYV 942
Cdd:cd14596    81 NYQA-LQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVH--NTGPIVVHCSAGIGRAGVLI 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 226052731  943 LIDMVLNKMAKGAkEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAE 990
Cdd:cd14596   158 CVDVLLSLIEKDL-SFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLE 204
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 747-990 9.48e-53

catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein phosphatase non-receptor type 18 (PTPN18), also called brain-derived phosphatase, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN18 regulates HER2-mediated cellular functions through defining both its phosphorylation and ubiquitination states. The N-terminal catalytic PTP domain of PTPN18 blocks lysosomal routing and delays the degradation of HER2 by dephosphorylation, and its C-terminal PEST domain promotes K48-linked HER2 ubiquitination and its destruction via the proteasome pathway.


Pssm-ID: 350451 [Multi-domain]  Cd Length: 266  Bit Score: 185.80  E-value: 9.48e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  747 SSLVAQREENAPKNRSLAVLTYDHSRILLKSQNSHGSSDYINASPIMDHDpRNPAYIATQGPLPATVADFWQMVWESGCA 826
Cdd:cd14603    21 STVAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVD-GSRAYIATQGPLSHTVLDFWRMIWQYGVK 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  827 VIVMLTPLSENGVRQCHHYWPDEGSNL-YHVYEVNLVSEHIWCQDFLVRSFYLKNLQtnETRTVTQFHFLSWYDQGVPSS 905
Cdd:cd14603   100 VILMACREIEMGKKKCERYWAQEQEPLqTGPFTITLVKEKRLNEEVILRTLKVTFQK--ESRSVSHFQYMAWPDHGIPDS 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  906 TRSLLDFRRKVNKcYRGRS-CPIIVHCSDGAGRSGTYVLIDMVLNKMAKGAKEIDIA---ATLEhLRDQRPGMVQTKEQF 981
Cdd:cd14603   178 PDCMLAMIELARR-LQGSGpEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPDFSifdVVLE-MRKQRPAAVQTEEQY 255


                  ....*....
gi 226052731  982 EFALTAVAE 990
Cdd:cd14603   256 EFLYHTVAQ 264
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 750-996 1.32e-52

catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1), also called protein-tyrosine phosphatase 1B (PTP-1B), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1/PTP-1B is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It contains an N-terminal catalytic PTP domain, followed by two tandem proline-rich motifs that mediate interaction with SH3-domain-containing proteins, and a small hydrophobic stretch that localizes the enzyme to the endoplasmic reticulum (ER). It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor.


Pssm-ID: 350456 [Multi-domain]  Cd Length: 277  Bit Score: 185.61  E-value: 1.32e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  750 VAQREENAPKNRSLAVLTYDHSRILLKsqnsHGSSDYINASPI-MDHDPRnpAYIATQGPLPATVADFWQMVWESGCAVI 828
Cdd:cd14608    19 VAKLPKNKNRNRYRDVSPFDHSRIKLH----QEDNDYINASLIkMEEAQR--SYILTQGPLPNTCGHFWEMVWEQKSRGV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  829 VMLTPLSENGVRQCHHYWPD--------EGSNLyhvyEVNLVSEHIWCQdFLVRSFYLKNLQTNETRTVTQFHFLSWYDQ 900
Cdd:cd14608    93 VMLNRVMEKGSLKCAQYWPQkeekemifEDTNL----KLTLISEDIKSY-YTVRQLELENLTTQETREILHFHYTTWPDF 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  901 GVPSSTRSLLDFRRKVNK--CYRGRSCPIIVHCSDGAGRSGTYVLIDMVLNKMA--KGAKEIDIAATLEHLRDQRPGMVQ 976
Cdd:cd14608   168 GVPESPASFLNFLFKVREsgSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDkrKDPSSVDIKKVLLEMRKFRMGLIQ 247

                         250       260
                  ....*....|....*....|
gi 226052731  977 TKEQFEFALTAVAEEVNAIL 996
Cdd:cd14608   248 TADQLRFSYLAVIEGAKFIM 267
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 786-988 5.05e-52

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: 181.31  E-value: 5.05e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  786 YINASPIMDHDPRNpAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNLYHVYEVNLVSEH 865
Cdd:cd14552     1 YINASFIDGYRQKD-AYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGSVSSGDITVELKDQT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  866 IwCQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGR-SCPIIVHCSDGAGRSGTYVLI 944
Cdd:cd14552    80 D-YEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSgNHPITVHCSAGAGRTGTFCAL 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 226052731  945 DMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAV 988
Cdd:cd14552   159 STVLERV-KAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 786-983 4.57e-51

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type tyrosine-protein phosphatase Z (PTPRZ), also called receptor-type tyrosine-protein phosphatase zeta (R-PTP-zeta), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Three isoforms are generated by alternative splicing from a single PTPRZ gene: two transmembrane isoforms, PTPRZ-A and PTPRZ-B, and one secretory isoform, PTPRZ-S (also known as phosphacan); all are preferentially expressed in the central nervous system (CNS) as chondroitin sulfate (CS) proteoglycans. PTPRZ isoforms play important roles in maintaining oligodendrocyte precursor cells in an undifferentiated state. PTPRZ is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350506 [Multi-domain]  Cd Length: 209  Bit Score: 178.63  E-value: 4.57e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  786 YINASpIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNLYHVYEVNLVSEH 865
Cdd:cd17668     1 YINAN-YVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  866 IWCQdFLVRSFYLKNLQTNE--------TRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGR 937
Cdd:cd17668    80 VLAY-YTVRNFTLRNTKIKKgsqkgrpsGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSAGVGR 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 226052731  938 SGTYVLIDMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQFEF 983
Cdd:cd17668   159 TGTYIVLDSMLQQI-QHEGTVNIFGFLKHIRSQRNYLVQTEEQYVF 203
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 741-988 6.34e-51

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: 180.82  E-value: 6.34e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  741 YQAEPNSSLV-AQREENAPKNRSLAVLTYDHSRILLKsqnshGSSDYINASPIMDHDPRNP---AYIATQGPLPATVADF 816
Cdd:cd14600    24 YRKKPGLAITcAKLPQNMDKNRYKDVLPYDATRVVLQ-----GNEDYINASYVNMEIPSANivnKYIATQGPLPHTCAQF 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  817 WQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNL-YHVYEVNLVSEHiwCQ-DFLVRSFYLKNLQTNETRTVTQFHF 894
Cdd:cd14600    99 WQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDPPDVMeYGGFRVQCHSED--CTiAYVFREMLLTNTQTGEERTVTHLQY 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  895 LSWYDQGVPSSTRSLLDFRRKVnKCYRGRSCPIIVHCSDGAGRSGTYVLID--MVLNKMAKGAKEIDIAATlehLRDQRP 972
Cdd:cd14600   177 VAWPDHGVPDDSSDFLEFVNYV-RSKRVENEPVLVHCSAGIGRTGVLVTMEtaMCLTERNQPVYPLDIVRK---MRDQRA 252

                         250
                  ....*....|....*.
gi 226052731  973 GMVQTKEQFEFALTAV 988
Cdd:cd14600   253 MMVQTSSQYKFVCEAI 268
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 786-983 7.18e-51

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: 177.80  E-value: 7.18e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  786 YINASPIMDHDPRNpAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNLYHVYEVNlVSEH 865
Cdd:cd14551     1 YINASYIDGYQEKN-KFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCWTYGNLRVR-VEDT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  866 IWCQDFLVRSFYLK--NLQTNE--TRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTY 941
Cdd:cd14551    79 VVLVDYTTRKFCIQkvNRGIGEkrVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGRTGTF 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 226052731  942 VLIDMVLNkMAKGAKEIDIAATLEHLRDQRPGMVQTKEQFEF 983
Cdd:cd14551   159 IVIDAMLD-MMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVF 199
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 772-990 8.49e-51

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: 178.29  E-value: 8.49e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  772 RILLKSQNSHGSSDYINASPImDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEgS 851
Cdd:cd14631     1 RVILQPVEDDPSSDYINANYI-DGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDD-T 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  852 NLYHVYEVNLVS-EHIwcQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVH 930
Cdd:cd14631    79 EVYGDFKVTCVEmEPL--AEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVH 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  931 CSDGAGRSGTYVLIDMVLNkMAKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAE 990
Cdd:cd14631   157 CSAGAGRTGCYIVIDIMLD-MAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 761-990 2.05e-50

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: 177.54  E-value: 2.05e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  761 RSLAVLTYDHSRILLKSQNSHGSSDYINASpIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVR 840
Cdd:cd14623     1 RVLQIIPYEFNRVIIPVKRGEENTDYVNAS-FIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  841 QCHHYWPDEGSNLYHVYEVNLVSEHiWCQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCY 920
Cdd:cd14623    80 KCAQYWPSDGSVSYGDITIELKKEE-ECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQ 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226052731  921 RGR-SCPIIVHCSDGAGRSGTYVLIDMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAE 990
Cdd:cd14623   159 QQSgNHPITVHCSAGAGRTGTFCALSTVLERV-KAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 786-990 3.76e-50

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: 175.88  E-value: 3.76e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  786 YINASPImDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEgSNLYHVYEVNLVSEH 865
Cdd:cd14555     1 YINANYI-DGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDD-TEVYGDIKVTLVETE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  866 IWCQdFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYVLID 945
Cdd:cd14555    79 PLAE-YVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTGCYIVID 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 226052731  946 MVLNkMAKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAE 990
Cdd:cd14555   158 IMLD-MAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 785-990 1.21e-49

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type tyrosine-protein phosphatase E (PTPRE), also known as receptor-type tyrosine-protein phosphatase epsilon (R-PTP-epsilon), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. The PTPRE gene contains two distinct promoters that generate the two major isoforms: transmembrane (receptor type RPTPe or PTPeM) and cytoplasmic (cyt-PTPe or PTPeC). Receptor type RPTPe plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells, and may also play a role in osteoclast formation and function. It also negatively regulates PDGFRbeta-mediated signaling pathways that are crucial for the pathogenesis of atherosclerosis. cyt-PTPe acts as a negative regulator of insulin receptor signaling in skeletal muscle. It regulates insulin-induced phosphorylation of proteins downstream of the insulin receptor. Receptor type RPTPe contains a small extracellular region, a single transmembrane segment, and an intracellular region two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350470 [Multi-domain]  Cd Length: 205  Bit Score: 174.42  E-value: 1.21e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  785 DYINASPImDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNLYHVYEVNLVSE 864
Cdd:cd14622     1 DYINASFI-DGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGSVTHGEITIEIKND 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  865 HIwCQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGR-SCPIIVHCSDGAGRSGTYVL 943
Cdd:cd14622    80 TL-LETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQTgNHPIVVHCSAGAGRTGTFIA 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 226052731  944 IDMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAE 990
Cdd:cd14622   159 LSNILERV-KAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQD 204
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 760-983 1.70e-49

catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type tyrosine-protein phosphatase B (PTPRB), also known as receptor-type tyrosine-protein phosphatase beta (R-PTP-beta) or vascular endothelial protein tyrosine phosphatase(VE-PTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRB/VE-PTP is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed specifically in vascular endothelial cells and it plays an important role in blood vessel remodeling and angiogenesis.


Pssm-ID: 350465 [Multi-domain]  Cd Length: 228  Bit Score: 175.11  E-value: 1.70e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  760 NRSLAVLTYDHSRILLKSQNSHGSSDYINASPIMDHDPRNpAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGV 839
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRR-EYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  840 RQCHHYWP-DEGSNLYHVYEVNLVSEHIWcQDFLVRSFYLKNL-QTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVN 917
Cdd:cd14617    80 VKCDHYWPaDQDSLYYGDLIVQMLSESVL-PEWTIREFKICSEeQLDAPRLVRHFHYTVWPDHGVPETTQSLIQFVRTVR 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 226052731  918 KcYRGRS---CPIIVHCSDGAGRSGTYVLIDMVLNKMAKgAKEIDIAATLEHLRDQRPGMVQTKEQFEF 983
Cdd:cd14617   159 D-YINRTpgsGPTVVHCSAGVGRTGTFIALDRILQQLDS-KDSVDIYGAVHDLRLHRVHMVQTECQYVY 225
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 750-988 2.04e-49

catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein phosphatase non-receptor type 2 (PTPN2), also called T-cell protein-tyrosine phosphatase (TCPTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN2, a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner. It is deleted in 6% of all T-cell acute lymphoblastic leukemias and is associated with constitutive JAK1/STAT5 signaling and tumorigenesis.


Pssm-ID: 350455 [Multi-domain]  Cd Length: 257  Bit Score: 175.92  E-value: 2.04e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  750 VAQREENAPKNRSLAVLTYDHSRIllKSQNShgSSDYINASpIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIV 829
Cdd:cd14607    18 VAKYPENRNRNRYRDVSPYDHSRV--KLQNT--ENDYINAS-LVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  830 MLTPLSENGVRQCHHYWPDEGSNLYHVYE----VNLVSEHIWCQdFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSS 905
Cdd:cd14607    93 MLNRIVEKDSVKCAQYWPTDEEEVLSFKEtgfsVKLLSEDVKSY-YTVHLLQLENINSGETRTISHFHYTTWPDFGVPES 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  906 TRSLLDFRRKV--NKCYRGRSCPIIVHCSDGAGRSGTYVLIDMVLNKM-AKGAKEIDIAATLEHLRDQRPGMVQTKEQFE 982
Cdd:cd14607   172 PASFLNFLFKVreSGSLSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMeKKDPDSVDIKQVLLDMRKYRMGLIQTPDQLR 251


                  ....*.
gi 226052731  983 FALTAV 988
Cdd:cd14607   252 FSYMAV 257
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 759-990 4.69e-49

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: 173.87  E-value: 4.69e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  759 KNRSLAVLTYDHSRILLKSQNSHGSSDYINASPIMD-HDPRnpAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSEN 837
Cdd:cd14602     1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGvYGPR--AYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  838 GVRQCHHYWPDEGSNLYHVYEVNLVSE-HIWCQDFLVRSfyLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKV 916
Cdd:cd14602    79 GKKKCERYWAEPGEMQLEFGPFSVTCEaEKRKSDYIIRT--LKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDV 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 226052731  917 NKCYRGRSCPIIVHCSDGAGRSGTYVLIDMVLNKMAKG--AKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAE 990
Cdd:cd14602   157 RCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGiiPENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIE 232
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 760-983 8.33e-49

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: 173.21  E-value: 8.33e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  760 NRSLAVLTYDHSRILLKSQNSHGSSDYINASPImdhdprnPAY------IATQGPLPATVADFWQMVWESGCAVIVMLTP 833
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFI-------PGYtspqefIATQGPLKKTIEDFWRLVWEQQVCNIIMLTV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  834 LSENGVRQCHHYWPDEGSNLYHVY-EVNLVSEHIwCQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDF 912
Cdd:cd14618    74 GMENGRVLCDHYWPSESTPVSYGHiTVHLLAQSS-EDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAF 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226052731  913 RRKVN---KCYRGRScPIIVHCSDGAGRSGTYVLIDMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQFEF 983
Cdd:cd14618   153 RELVRehvQATKGKG-PTLVHCSAGVGRSGTFIALDRLLRQL-KEEKVVDVFNTVYILRMHRYLMIQTLSQYIF 224
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 785-988 1.84e-48

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: 171.28  E-value: 1.84e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  785 DYINASPIMDHDPRNP---AYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPD-EGSNLYHVYEVN 860
Cdd:cd14601     1 DYINANYINMEIPSSSiinRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEpSGSSSYGGFQVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  861 LVSEHiWCQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGT 940
Cdd:cd14601    81 CHSEE-GNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVHCSAGIGRTGV 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 226052731  941 YVLID--MVLNKMAKGAKEIDIAATlehLRDQRPGMVQTKEQFEFALTAV 988
Cdd:cd14601   160 LITMEtaMCLIECNQPVYPLDIVRT---MRDQRAMMIQTPSQYRFVCEAI 206
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 786-983 5.72e-48

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: 170.33  E-value: 5.72e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  786 YINASPI-MDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSN----LYHVYEVN 860
Cdd:cd14540     1 YINASHItATVGGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGEhdalTFGEYKVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  861 LVSEHIwCQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDF-------RRKVNKCYRGRS--CPIIVHC 931
Cdd:cd14540    81 TKFSVS-SGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFleeinsvRRHTNQDVAGHNrnPPTLVHC 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 226052731  932 SDGAGRSGTYVLIDMVLNKMAKGaKEIDIAATLEHLRDQRPGMVQTKEQFEF 983
Cdd:cd14540   160 SAGVGRTGVVILADLMLYCLDHN-EELDIPRVLALLRHQRMLLVQTLAQYKF 210
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 786-984 2.65e-47

PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein phosphatase non-receptor type 23 (PTPN23), also called His domain-containing protein tyrosine phosphatase (HD-PTP) or protein tyrosine phosphatase TD14 (PTP-TD14), is a catalytically inactive member of the tyrosine-specific protein tyrosine phosphatase (PTP) family. Human PTPN23 may be involved in the regulation of small nuclear ribonucleoprotein assembly and pre-mRNA splicing by modifying the survival motor neuron (SMN) complex. It plays a role in ciliogenesis and is part of endosomal sorting complex required for transport (ESCRT) pathways. PTPN23 contains five domains: a BRO1-like domain that plays a role in endosomal sorting; a V-domain that interacts with Lys63-linked polyubiquitinated substrates; a central proline-rich region that might recruit SH3-containing proteins; a PTP-like domain; and a proteolytic degradation-targeting motif, also known as a PEST sequence.


Pssm-ID: 350387 [Multi-domain]  Cd Length: 205  Bit Score: 167.95  E-value: 2.65e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  786 YINASPIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDE-GSNL-YHVYEVNLVS 863
Cdd:cd14539     1 YINASLIEDLTPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTErGQALvYGAITVSLQS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  864 EHIwcQDFLV-RSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCY---RGRSCPIIVHCSDGAGRSG 939
Cdd:cd14539    81 VRT--TPTHVeRIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYlqqRSLQTPIVVHCSSGVGRTG 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 226052731  940 TYVLIDMVLNKMAKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFA 984
Cdd:cd14539   159 AFCLLYAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFC 203
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 757-983 7.50e-47

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: 168.09  E-value: 7.50e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  757 APKNRSLAVLTYDHSRILLKS-QNSHGSSDYINASPIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLS 835
Cdd:cd14612    16 ASKDRYKTILPNPQSRVCLRRaGSQEEEGSYINANYIRGYDGKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITKLK 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  836 EnGVRQCHHYWPD-EGSNLYHVYEVNLVSEhiwCQDFLVRSFYLKnlQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRR 914
Cdd:cd14612    96 E-KKEKCVHYWPEkEGTYGRFEIRVQDMKE---CDGYTIRDLTIQ--LEEESRSVKHYWFSSWPDHQTPESAGPLLRLVA 169

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226052731  915 KVNKCYR--GRSCPIIVHCSDGAGRSGTYVLIDMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQFEF 983
Cdd:cd14612   170 EVEESRQtaASPGPIVVHCSAGIGRTGCFIATSIGCQQL-KDTGKVDILGIVCQLRLDRGGMIQTSEQYQF 239
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 756-983 5.10e-46

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: 165.83  E-value: 5.10e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  756 NAPKNRSLAVLTYDHSRILLKSQNSHGSSDYINASPIMDHD-PRNpaYIATQGPLPATVADFWQMVWESGCAVIVMLTPL 834
Cdd:cd14614    12 NRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNsPQE--YIATQGPLPETRNDFWKMVLQQKSQIIVMLTQC 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  835 SENGVRQCHHYWP-DEGSNLYHVYEVNLVSEHiWCQDFLVRSFYLKnlQTNETRTVTQFHFLSWYDQGVPS--STRSLLD 911
Cdd:cd14614    90 NEKRRVKCDHYWPfTEEPVAYGDITVEMLSEE-EQPDWAIREFRVS--YADEVQDVMHFNYTAWPDHGVPTanAAESILQ 166

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 226052731  912 F----RRKVNKcyrgRSCPIIVHCSDGAGRSGTYVLIDMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQFEF 983
Cdd:cd14614   167 FvqmvRQQAVK----SKGPMIIHCSAGVGRTGTFIALDRLLQHI-RDHEFVDILGLVSEMRSYRMSMVQTEEQYIF 237
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 786-990 6.97e-46

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: 163.68  E-value: 6.97e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  786 YINASPImDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEgSNLYHVYEVNLVSEH 865
Cdd:cd14632     1 YINANYI-DGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDD-SDTYGDIKITLLKTE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  866 IWCQdFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYVLID 945
Cdd:cd14632    79 TLAE-YSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYIVLD 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 226052731  946 MVLNkMAKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAE 990
Cdd:cd14632   158 VMLD-MAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 786-983 2.20e-45

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: 162.19  E-value: 2.20e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  786 YINASpIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGvRQCHHYWPDEGSNLYHVYEVNLVSEH 865
Cdd:cd14556     1 YINAA-LLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKD-QSCPQYWPDEGSGTYGPIQVEFVSTT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  866 IWCqDFLVRSFYLKNLQ--TNETRTVTQFHFLSW-YDQGVPSSTRSLLDFRRKVNK----CYRGrscPIIVHCSDGAGRS 938
Cdd:cd14556    79 IDE-DVISRIFRLQNTTrpQEGYRMVQQFQFLGWpRDRDTPPSKRALLKLLSEVEKwqeqSGEG---PIVVHCLNGVGRS 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 226052731  939 GTYVLIDMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQFEF 983
Cdd:cd14556   155 GVFCAISSVCERI-KVENVVDVFQAVKTLRNHRPNMVETEEQYKF 198
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 786-981 3.36e-45

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: 161.53  E-value: 3.36e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  786 YINASPIMDH-DPRNpaYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWP--DEGSNLYHVYEVNLV 862
Cdd:cd14557     1 YINASYIDGFkEPRK--YIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPsmEEGSRAFGDVVVKIN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  863 SEHIwCQDFLVRSFYLKNLQTNET-RTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTY 941
Cdd:cd14557    79 EEKI-CPDYIIRKLNINNKKEKGSgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGTY 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 226052731  942 VLIDMVLNKM-AKGakEIDIAATLEHLRDQRPGMVQTKEQF 981
Cdd:cd14557   158 IGIDAMLEGLeAEG--RVDVYGYVVKLRRQRCLMVQVEAQY 196
Receptor_IA-2 pfam11548
Protein-tyrosine phosphatase receptor IA-2; IA-2 is a protein-tyrosine phosphatase receptor ...
 495-583 1.87e-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: 1.87e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731   495 EQQGYILTGNNPLSPEKGKQLMDQVAHILRVPSSFFADIKVLGPAVTFKVSANIQNMTTADVIKAAADNKDQLEKATGLT 574
Cdd:pfam11548    1 EEYGYIVTDNDPLSWEEGLRLMEKVAELLHLPMSSFADIRVLGPAVTFKVRANNKNLTAADVAKAAVDIKDKLEKETGLK 80


                   ....*....
gi 226052731   575 ILQSGIRPK 583
Cdd:pfam11548   81 ILQAGVGDK 89
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 786-983 2.41e-43

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: 156.47  E-value: 2.41e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  786 YINASPIMDHDPRN-PAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVR-QCHHYWPDEGSNLYHVYEVNLVS 863
Cdd:cd17658     1 YINASLVETPASESlPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTaKCADYFPAEENESREFGRISVTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  864 EHIWCQD--FLVRSFYLKNLQTNET-RTVTQFHFLSWYDQGVPSSTRSLldfrRKVNKCYRG---RSCPIIVHCSDGAGR 937
Cdd:cd17658    81 KKLKHSQhsITLRVLEVQYIESEEPpLSVLHIQYPEWPDHGVPKDTRSV----RELLKRLYGippSAGPIVVHCSAGIGR 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 226052731  938 SGTYVLIDMVLNKMAKGAKE-IDIAATLEHLRDQRPGMVQTKEQFEF 983
Cdd:cd17658   157 TGAYCTIHNTIRRILEGDMSaVDLSKTVRKFRSQRIGMVQTQDQYIF 203
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 759-983 2.63e-43

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: 158.49  E-value: 2.63e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  759 KNRSLAVLTYDHSRILLKSQNSHGS-SDYINASPIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSEN 837
Cdd:cd14613    28 KNRYKTILPNPHSRVCLTSPDQDDPlSSYINANYIRGYGGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEM 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  838 GvRQCHHYWPDEgSNLYHVYEVNlVSEHIWCQDFLVRSFYLKNlqTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVN 917
Cdd:cd14613   108 N-EKCTEYWPEE-QVTYEGIEIT-VKQVIHADDYRLRLITLKS--GGEERGLKHYWYTSWPDQKTPDNAPPLLQLVQEVE 182

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 226052731  918 ---KCYRGRSCPIIVHCSDGAGRSGTYVLIDMVLNKMAKGAKeIDIAATLEHLRDQRPGMVQTKEQFEF 983
Cdd:cd14613   183 earQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGV-VDILRTTCQLRLDRGGMIQTCEQYQF 250
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 759-983 5.52e-43

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: 156.23  E-value: 5.52e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  759 KNRSLAVLTYDHSRILLKSQNSHGS-SDYINASPIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSEN 837
Cdd:cd14611     2 KNRYKTILPNPHSRVCLKPKNSNDSlSTYINANYIRGYGGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  838 GvRQCHHYWPdEGSNLYHVYE--VNLVSEhiwCQDFLVRSFYLKnlQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRK 915
Cdd:cd14611    82 N-EKCVLYWP-EKRGIYGKVEvlVNSVKE---CDNYTIRNLTLK--QGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLD 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226052731  916 VN---KCYRGRScPIIVHCSDGAGRSGTYVLIDMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQFEF 983
Cdd:cd14611   155 VEedrLASPGRG-PVVVHCSAGIGRTGCFIATTIGCQQL-KEEGVVDVLSIVCQLRVDRGGMVQTSEQYEF 223
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 752-983 3.05e-41

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 154.00  E-value: 3.05e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  752 QREENAPKNRSLAVLTYDHSRILLKSQnSHGSSDYINASPImDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVML 831
Cdd:PHA02747   47 EKPENQPKNRYWDIPCWDHNRVILDSG-GGSTSDYIHANWI-DGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVML 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  832 TPLSE-NGVRQCHHYW-PDEGSNL----YHVYEVNLVsehiwcqdflVRSFYLKNL------QTNETRTVTQFHFLSWYD 899
Cdd:PHA02747  125 TPTKGtNGEEKCYQYWcLNEDGNIdmedFRIETLKTS----------VRAKYILTLieitdkILKDSRKISHFQCSEWFE 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  900 QGVPSSTRSLLDF-------RRKVNKCYRGRS---CPIIVHCSDGAGRSGTYVLIDMVLNKMAKgAKEIDIAATLEHLRD 969
Cdd:PHA02747  195 DETPSDHPDFIKFikiidinRKKSGKLFNPKDallCPIVVHCSDGVGKTGIFCAVDICLNQLVK-RKAICLAKTAEKIRE 273

                         250
                  ....*....|....
gi 226052731  970 QRPGMVQTKEQFEF 983
Cdd:PHA02747  274 QRHAGIMNFDDYLF 287
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 760-983 8.25e-41

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: 150.06  E-value: 8.25e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  760 NRSLAVLTYDHSRILLKSQNSHGSSDYINASPIMDHDPRNpAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGV 839
Cdd:cd14616     1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPN-EFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  840 RQCHHYWPDEGS--NLYHVYEVNLVSEHIWcQDFLVRSfyLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVN 917
Cdd:cd14616    80 IRCHQYWPEDNKpvTVFGDIVITKLMEDVQ-IDWTIRD--LKIERHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVR 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 226052731  918 KCYRGRSCPIIVHCSDGAGRSGTYVLIDMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQFEF 983
Cdd:cd14616   157 ASRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHI-NDHDFVDIYGLVAELRSERMCMVQNLAQYIF 221
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 755-983 2.63e-40

catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein phosphatase non-receptor type 14 (PTPN14), also called protein-tyrosine phosphatase pez, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN14 is a potential tumor suppressor and plays a regulatory role in the Hippo and Wnt/beta-catenin signaling pathways. It contains an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350447 [Multi-domain]  Cd Length: 287  Bit Score: 150.53  E-value: 2.63e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  755 ENAPKNRSLAVLTYDHSRILL--KSQNSHGssdYINASPI-MDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVML 831
Cdd:cd14599    37 ENAERNRIREVVPYEENRVELvpTKENNTG---YINASHIkVTVGGEEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMV 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  832 TPLSENGVRQCHHYWPDEGSN----LYHVYEVNL-VSEHIWCqdFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSST 906
Cdd:cd14599   114 TAEEEGGRSKSHRYWPKLGSKhssaTYGKFKVTTkFRTDSGC--YATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEEV 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  907 RSLLDF-------RRKVNKCYRG-RSC--PIIVHCSDGAGRSGTYVLIDMVLNKMAKGAKeIDIAATLEHLRDQRPGMVQ 976
Cdd:cd14599   192 QGFLSYleeiqsvRRHTNSMLDStKNCnpPIVVHCSAGVGRTGVVILTELMIGCLEHNEK-VEVPVMLRHLREQRMFMIQ 270


                  ....*..
gi 226052731  977 TKEQFEF 983
Cdd:cd14599   271 TIAQYKF 277
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
888-990 1.38e-37

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 136.33  E-value: 1.38e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731    888 TVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSC--PIIVHCSDGAGRSGTYVLIDMVLNKMAKGAKEIDIAATLE 965
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESsgPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 226052731    966 HLRDQRPGMVQTKEQFEFALTAVAE 990
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 888-990 1.38e-37

Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine phosphatases. Homologues detected by this profile and not by those of "PTPc" or "DSPc" are predicted to be protein phosphatases with a similar fold to DSPs and PTPs, yet with unpredicted specificities.


Pssm-ID: 214469 [Multi-domain]  Cd Length: 105  Bit Score: 136.33  E-value: 1.38e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731    888 TVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSC--PIIVHCSDGAGRSGTYVLIDMVLNKMAKGAKEIDIAATLE 965
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESsgPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 226052731    966 HLRDQRPGMVQTKEQFEFALTAVAE 990
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
729-996 8.60e-37

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 140.23  E-value: 8.60e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  729 NRLEKEWEALcAYQAEPNSSLvaQREENAPKNRSLAVLTYDHSRIllksqnshGSSD-YINASPIMDHDPRNpaYIATQG 807
Cdd:COG5599    18 SRLSTLTNEL-APSHNDPQYL--QNINGSPLNRFRDIQPYKETAL--------RANLgYLNANYIQVIGNHR--YIATQY 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  808 PLPATVADFWQMVWESGCAVIVMLTPLSENGVRQ--CHHYWPDEGSNLYHVYEVNLVSEHIWCQDFLVRSFYLKNLQTN- 884
Cdd:COG5599    85 PLEEQLEDFFQMLFDNNTPVLVVLASDDEISKPKvkMPVYFRQDGEYGKYEVSSELTESIQLRDGIEARTYVLTIKGTGq 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  885 ETRTVTQFHFLSWYDQGVPSST--RSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYVLIdMVLNKMAKGAKEIDIAA 962
Cdd:COG5599   165 KKIEIPVLHVKNWPDHGAISAEalKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIAC-LALSKSINALVQITLSV 243

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 226052731  963 --TLEHLRDQR-PGMVQTKEQFEFaLTAVAEEVNAIL 996
Cdd:COG5599   244 eeIVIDMRTSRnGGMVQTSEQLDV-LVKLAEQQIRPL 279
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 786-983 8.51e-36

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: 134.76  E-value: 8.51e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  786 YINASpIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLseNGVRQCHHYWPDEGSNLYHVYEVNLVSEH 865
Cdd:cd14634     1 YINAA-LMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEM--DAAQLCMQYWPEKTSCCYGPIQVEFVSAD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  866 IwCQDFLVRSFYLKNLQTNET--RTVTQFHFLSW--YdQGVPSSTRSLLDFRRKVNKC---YRGRSCPIIVHCSDGAGRS 938
Cdd:cd14634    78 I-DEDIISRIFRICNMARPQDgyRIVQHLQYIGWpaY-RDTPPSKRSILKVVRRLEKWqeqYDGREGRTVVHCLNGGGRS 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 226052731  939 GTYVLIDMVlNKMAKGAKEIDIAATLEHLRDQRPGMVQTKEQFEF 983
Cdd:cd14634   156 GTFCAICSV-CEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKF 199
PHA02738 PHA02738
hypothetical protein; Provisional
 756-993 1.62e-34

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 135.05  E-value: 1.62e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  756 NAPKNRSLAVLTYDHSRILLKSQNSHGssDYINASPImDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLS 835
Cdd:PHA02738   49 NRKLNRYLDAVCFDHSRVILPAERNRG--DYINANYV-DGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKK 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  836 ENGVRQCHHYWPD-EGSNL----YHVYEVNlVSEHIwcqdFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLL 910
Cdd:PHA02738  126 ENGREKCFPYWSDvEQGSIrfgkFKITTTQ-VETHP----HYVKSTLLLTDGTSATQTVTHFNFTAWPDHDVPKNTSEFL 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  911 DFRRKVNKCY-------------RGRSCPIIVHCSDGAGRSGTYVLIDMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQT 977
Cdd:PHA02738  201 NFVLEVRQCQkelaqeslqighnRLQPPPIVVHCNAGLGRTPCYCVVDISISRF-DACATVSIPSIVSSIRNQRYYSLFI 279

                         250
                  ....*....|....*.
gi 226052731  978 KEQFEFALTAVAEEVN 993
Cdd:PHA02738  280 PFQYFFCYRAVKRYVN 295
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 786-990 6.98e-34

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: 129.26  E-value: 6.98e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  786 YINASpIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSE-NGVRQCHHYWPDEGSNLYHVYEVNLVSE 864
Cdd:cd14637     1 YINAA-LTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQsNSAWPCLQYWPEPGLQQYGPMEVEFVSG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  865 HIwCQDFLVRSFYLKNLQ--TNETRTVTQFHFLSWYD-QGVPSSTRSLLDFRRKVNK----CYRGRScpiIVHCSDGAGR 937
Cdd:cd14637    80 SA-DEDIVTRLFRVQNITrlQEGHLMVRHFQFLRWSAyRDTPDSKKAFLHLLASVEKwqreSGEGRT---VVHCLNGGGR 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 226052731  938 SGTYVLIDMVLnKMAKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAE 990
Cdd:cd14637   156 SGTYCASAMIL-EMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 786-990 1.07e-33

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: 128.99  E-value: 1.07e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  786 YINASpIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLseNGVRQCHHYWPDEGSNLYHVYEVNLVSEH 865
Cdd:cd14636     1 YINAA-LMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEV--DLAQGCPQYWPEEGMLRYGPIQVECMSCS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  866 IWCqDFLVRSFYLKNLQTNET--RTVTQFHFLSWYD-QGVPSSTRSLLDFRRKVNK----CYRGRSCPIIvHCSDGAGRS 938
Cdd:cd14636    78 MDC-DVISRIFRICNLTRPQEgyLMVQQFQYLGWAShREVPGSKRSFLKLILQVEKwqeeCDEGEGRTII-HCLNGGGRS 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 226052731  939 GTYVLIDMVLnKMAKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAE 990
Cdd:cd14636   156 GMFCAISIVC-EMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 786-983 1.50e-32

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: 125.86  E-value: 1.50e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  786 YINASPI------MDHDprnpaYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSN----LYH 855
Cdd:cd14598     1 YINASHIkvtvggKEWD-----YIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLGSRhntvTYG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  856 VYEVNL-VSEHIWCqdFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDF-------RRKVNKCY--RGRSC 925
Cdd:cd14598    76 RFKITTrFRTDSGC--YATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYleeiqsvRRHTNSTIdpKSPNP 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 226052731  926 PIIVHCSDGAGRSGTYVLIDMVLNKMAKGAKeIDIAATLEHLRDQRPGMVQTKEQFEF 983
Cdd:cd14598   154 PVLVHCSAGVGRTGVVILSEIMIACLEHNEM-LDIPRVLDMLRQQRMMMVQTLSQYTF 210
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 786-983 9.15e-32

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: 123.20  E-value: 9.15e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  786 YINASPIMDHDpRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGvrQCHHYWPDEGSNLYHV-YEVNLVSE 864
Cdd:cd14550     1 YINASYLQGYR-RSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWPTKEKPLECEtFKVTLSGE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  865 HIWC----QDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTrsLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGT 940
Cdd:cd14550    78 DHSClsneIRLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPIHT--VFELINTVQEWAQQRDGPIVVHDRYGGVQAAT 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 226052731  941 YVLIdMVLNKMAKGAKEIDI--AATLEHLRdqRPGMVQTKEQFEF 983
Cdd:cd14550   156 FCAL-TTLHQQLEHESSVDVyqVAKLYHLM--RPGVFTSKEDYQF 197
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 745-983 2.54e-31

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 125.11  E-value: 2.54e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  745 PNSSLVAQREENAPKNRSLAVLTYDHSRILLKSQNshGSSDYINASPIMDHDPRNpAYIATQGPLPATVADFWQMVWESG 824
Cdd:PHA02742   41 AFSCNESLELKNMKKCRYPDAPCFDRNRVILKIED--GGDDFINASYVDGHNAKG-RFICTQAPLEETALDFWQAIFQDQ 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  825 CAVIVMLTPLSENGVRQCHHYW-PDEGSNLYHvYEVNLVSEHIwcQDFlvRSFYLKNLQTNETRT-----VTQFHFLSWY 898
Cdd:PHA02742  118 VRVIVMITKIMEDGKEACYPYWmPHERGKATH-GEFKIKTKKI--KSF--RNYAVTNLCLTDTNTgasldIKHFAYEDWP 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  899 DQGVPSSTRSLLDFRRKVNKC-----------YRGRSCPIIVHCSDGAGRSGTYVLIDMVLNKMAKGAKeIDIAATLEHL 967
Cdd:PHA02742  193 HGGLPRDPNKFLDFVLAVREAdlkadvdikgeNIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAI-IPLLSIVRDL 271

                         250
                  ....*....|....*.
gi 226052731  968 RDQRPGMVQTKEQFEF 983
Cdd:PHA02742  272 RKQRHNCLSLPQQYIF 287
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 745-988 3.39e-31

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 125.14  E-value: 3.39e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  745 PNSSLVAQ--REENAPKNRSLAVLTYDHSRILLKSQNS-----HGSSD--------------YINASPIMDHDPRNpAYI 803
Cdd:PHA02746   38 PIRGTTNHflKKENLKKNRFHDIPCWDHSRVVINAHESlkmfdVGDSDgkkievtsednaenYIHANFVDGFKEAN-KFI 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  804 ATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGvRQCHHYW-PDEGSNLYHVYEVNLVSEHIWCQDFLVRSFYLKNLQ 882
Cdd:PHA02746  117 CAQGPKEDTSEDFFKLISEHESQVIVSLTDIDDDD-EKCFELWtKEEDSELAFGRFVAKILDIIEELSFTKTRLMITDKI 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  883 TNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKcYRGR-----------SCPIIVHCSDGAGRSGTYVLIDMVLNKM 951
Cdd:PHA02746  196 SDTSREIHHFWFPDWPDNGIPTGMAEFLELINKVNE-EQAElikqadndpqtLGPIVVHCSAGIGRAGTFCAIDNALEQL 274

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 226052731  952 AKgAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAV 988
Cdd:PHA02746  275 EK-EKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 786-990 1.13e-29

PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350483 [Multi-domain]  Cd Length: 206  Bit Score: 117.10  E-value: 1.13e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  786 YINASpIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLseNGVRQCHHYWPDEGSNLYHVYEVNLVSEH 865
Cdd:cd14635     1 YINAA-LMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDV--DPAQLCPQYWPENGVHRHGPIQVEFVSAD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  866 IWcQDFLVRSFYLKNLQTNET--RTVTQFHFLSW-YDQGVPSSTRSLLDFRRKVNKC---YRGRSCPIIVHCSDGAGRSG 939
Cdd:cd14635    78 LE-EDIISRIFRIYNAARPQDgyRMVQQFQFLGWpMYRDTPVSKRSFLKLIRQVDKWqeeYNGGEGRTVVHCLNGGGRSG 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 226052731  940 TYVLIDMVLnKMAKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAE 990
Cdd:cd14635   157 TFCAISIVC-EMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 786-988 2.98e-20

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type tyrosine-protein phosphatase Z (PTPRZ), also called receptor-type tyrosine-protein phosphatase zeta (R-PTP-zeta), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Three isoforms are generated by alternative splicing from a single PTPRZ gene: two transmembrane isoforms, PTPRZ-A and PTPRZ-B, and one secretory isoform, PTPRZ-S (also known as phosphacan); all are preferentially expressed in the central nervous system (CNS) as chondroitin sulfate (CS) proteoglycans. PTPRZ isoforms play important roles in maintaining oligodendrocyte precursor cells in an undifferentiated state. PTPRZ is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350507 [Multi-domain]  Cd Length: 204  Bit Score: 90.05  E-value: 2.98e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  786 YINASPIMDHDPRNpAYIATQGPLPATVADFWQMVWESGCAVIVMLtPLSENGVRQCHHYWP--DEGSNLyHVYEVNLVS 863
Cdd:cd17669     1 YINASYIMGYYQSN-EFIITQHPLLHTIKDFWRMIWDHNAQLIVML-PDGQNMAEDEFVYWPnkDEPINC-ETFKVTLIA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  864 EHIWC----QDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVP-SSTRSLLDFrrkVNKCYRGRSCPIIVHCSDGAGRS 938
Cdd:cd17669    78 EEHKClsneEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPiSKTFELISI---IKEEAANRDGPMIVHDEHGGVTA 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 226052731  939 GTYVLIDMVLNKMAKgAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAV 988
Cdd:cd17669   155 GTFCALTTLMHQLEK-ENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAI 203
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 786-988 6.18e-19

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: 86.27  E-value: 6.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  786 YINASPIMDHdPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLtPLSENGVRQCHHYWP--DEGSNLyHVYEVNLVS 863
Cdd:cd17670     1 YINASYIMGY-YRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVML-PDNQGLAEDEFVYWPsrEESMNC-EAFTVTLIS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  864 EHIWC----QDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVP-SSTRSLLDFrrkVNKCYRGRSCPIIVHCSDGAGRS 938
Cdd:cd17670    78 KDRLClsneEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPiSSTFELINV---IKEEALTRDGPTIVHDEFGAVSA 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 226052731  939 GTYVLIdMVLNKMAKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAV 988
Cdd:cd17670   155 GTLCAL-TTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAM 203
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 729-1000 1.14e-12

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 70.00  E-value: 1.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  729 NRLEKEWEALCAYQAEPNSSLVAQREENAPK-NRSLAVLTYDHSRILLKSQNSHGSSDYINAspiMDHDPRnpaYIATQG 807
Cdd:PHA02740   25 SCIIKEYRAIVPEHEDEANKACAQAENKAKDeNLALHITRLLHRRIKLFNDEKVLDARFVDG---YDFEQK---FICIIN 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  808 PLPATVADFWQMVWESGCAVIVMLTPLSEngvRQCHH-YWP-DEG----SNLYHVYEVNLVSEhiwcQDFLVRSFYLKNl 881
Cdd:PHA02740   99 LCEDACDKFLQALSDNKVQIIVLISRHAD---KKCFNqFWSlKEGcvitSDKFQIETLEIIIK----PHFNLTLLSLTD- 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  882 QTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYR--------GRSCPIIVHCSDGAGRSGTYVLIDMVLNKMAK 953
Cdd:PHA02740  171 KFGQAQKISHFQYTAWPADGFSHDPDAFIDFFCNIDDLCAdlekhkadGKIAPIIIDCIDGISSSAVFCVFDICATEFDK 250

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 226052731  954 GAKeIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEVNAILKALP 1000
Cdd:PHA02740  251 TGM-LSIANALKKVRQKKYGCMNCLDDYVFCYHLIAAYLKEKFDILK 296
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 799-982 1.45e-07

YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. YopH is an essential virulence determinant of the pathogenic bacterium by dephosphorylating several focal adhesion proteins including p130Cas in human epithelial cells, resulting in the disruption of focal adhesions and cell detachment from the extracellular matrix. It contains an N-terminal domain that contains signals required for TTSS-mediated delivery of YopH into host cells and a C-terminal catalytic PTP domain.


Pssm-ID: 350407 [Multi-domain]  Cd Length: 227  Bit Score: 53.56  E-value: 1.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  799 NPAYIATQGPLPATVADFWQMVWESGCAVIVMLTplSENGVR--QCHHYWpdEGSNLYHvyEVNLVSEHIWCQD----FL 872
Cdd:cd14559    28 KNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLA--SNKDIQrkGLPPYF--RQSGTYG--SVTVKSKKTGKDElvdgLK 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  873 VRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSS--TRSLLDF-----RRKVNKCYRGRSCPI--------IVHCSDGAGR 937
Cdd:cd14559   102 ADMYNLKITDGNKTITIPVVHVTNWPDHTAISSegLKELADLvnksaEEKRNFYKSKGSSAIndknkllpVIHCRAGVGR 181

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 226052731  938 SGTyVLIDMVlnkMAKGAKEIDIAATLEHLRDQRPG-MVQTKEQFE 982
Cdd:cd14559   182 TGQ-LAAAME---LNKSPNNLSVEDIVSDMRTSRNGkMVQKDEQLD 223
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 891-983 3.62e-07

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


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 50.35  E-value: 3.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  891 QFHFLSWYDQGVPS--STRSLLDFRRKVNKCYRgrscPIIVHCSDGAGRSGTYVLIDMVLNKMAKGAKEIDIaatlehLR 968
Cdd:cd14504    51 RYHHIPIEDYTPPTleQIDEFLDIVEEANAKNE----AVLVHCLAGKGRTGTMLACYLVKTGKISAVDAINE------IR 120

                          90
                  ....*....|....*
gi 226052731  969 DQRPGMVQTKEQFEF 983
Cdd:cd14504   121 RIRPGSIETSEQEKF 135
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
891-983 2.64e-06

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 48.04  E-value: 2.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  891 QFHFLSWYDQGVPSSTRsLLDFRRKVNKCYRgRSCPIIVHCSDGAGRSGTyVLIdMVLnkMAKGakeIDIAATLEHLRDQ 970
Cdd:COG2453    49 EYLHLPIPDFGAPDDEQ-LQEAVDFIDEALR-EGKKVLVHCRGGIGRTGT-VAA-AYL--VLLG---LSAEEALARVRAA 119

                          90
                  ....*....|...
gi 226052731  971 RPGMVQTKEQFEF 983
Cdd:COG2453   120 RPGAVETPAQRAF 132
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 910-983 3.75e-04

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


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 41.18  E-value: 3.75e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 226052731  910 LDFRRKVNKCYrgrsCPIIVHCSDGAGRSGTYVLIDMVLnKMAKGAKEIdiaatLEHLRDQRPG-MVQTKEQFEF 983
Cdd:cd14494    46 LEVLDQAEKPG----EPVLVHCKAGVGRTGTLVACYLVL-LGGMSAEEA-----VRIVRLIRPGgIPQTIEQLDF 110
RESP18 pfam14948
RESP18 domain; This domain is found in the glucocorticoid-responsive protein regulated ...
 80-126 2.17e-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: 2.17e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 226052731    80 HLKVTLQKLSRTGFTWQDDYTQRVIAQELANLPK-----AYLWHGEASGPAR 126
Cdd:pfam14948   23 HLQVVLHQIVPQGLFWKDDLTQDVMTQKMEHISRlhpqdPCLKDGKAVFPTR 74
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 864-993 2.73e-03

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


Pssm-ID: 350356 [Multi-domain]  Cd Length: 206  Bit Score: 40.41  E-value: 2.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  864 EHIWCQDFLVRS--FY--LKNLQTNETRtvtqFHFLSWYDQGVPSSTRsLLDFRRKVNKCYR--GRscpIIVHCSDGAGR 937
Cdd:cd14506    51 EHASCGPGLEPEsgFSylPEAFMRAGIY----FYNFGWKDYGVPSLTT-ILDIVKVMAFALQegGK---VAVHCHAGLGR 122

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 226052731  938 SGtyVLIDMVL---NKMAKgakeidiAATLEHLRDQRPGMVQTKEQ----FEFALTAVAEEVN 993
Cdd:cd14506   123 TG--VLIACYLvyaLRMSA-------DQAIRLVRSKRPNSIQTRGQvlcvREFAQFLLPLRNV 176
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 891-983 3.64e-03

cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of eukaryotic cyclin-dependent kinase inhibitor 3 (CDKN3) and related archaeal and bacterial proteins. CDKN3 is also known as kinase-associated phosphatase (KAP), CDK2-associated dual-specificity phosphatase, cyclin-dependent kinase interactor 1 (CDI1), or cyclin-dependent kinase-interacting protein 2 (CIP2). It has been characterized as dual-specificity phosphatase, which function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and protein-tyrosine-phosphatase (EC 3.1.3.48). It dephosphorylates CDK2 at a threonine residue in a cyclin-dependent manner, resulting in the inhibition of G1/S cell cycle progression. It also interacts with CDK1 and controls progression through mitosis by dephosphorylating CDC2. CDKN3 may also function as a tumor suppressor; its loss of function was found in a variety of cancers including glioblastoma and hepatocellular carcinoma. However, it has also been found over-expressed in many cancers such as breast, cervical, lung and prostate cancers, and may also have an oncogenic function.


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 39.17  E-value: 3.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052731  891 QFHFLSWYDQGVPSSTRS---LLDFRRKVNKCYRGrscpIIVHCSDGAGRSGTY---VLidMVLNKMAKGAKEIDIaatl 964
Cdd:cd14505    74 TWHHLPIPDGGVPSDIAQwqeLLEELLSALENGKK----VLIHCKGGLGRTGLIaacLL--LELGDTLDPEQAIAA---- 143

                          90
                  ....*....|....*....
gi 226052731  965 ehLRDQRPGMVQTKEQFEF 983
Cdd:cd14505   144 --VRALRPGAIQTPKQENF 160
 
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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