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Conserved domains on  [gi|13928818|ref|NP_113788|]
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receptor-type tyrosine-protein phosphatase N2 precursor [Rattus norvegicus]

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 PAP2 domain with similarity to yeast inositol phosphorylceramide synthase (AUR1) that catalyzes the addition of inositol phosphate to ceramide, an essential step in sphingolipid synthesis

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 ...
 716-998 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: 643.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  716 TGHMILAYMEDHLKNKNRLEKEWEALCAYQAEPDSSLVAQREENAPKNRSLAVLTYDHSRILLKSENSHSNSDYINASPI 795
Cdd:cd14610    1 TGHMILSYMEDHLKNKNRLEKEWEALCAYQAEPNATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  796 MDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNVYHVYEVNLVSEHIWCQDFL 875
Cdd:cd14610   81 MDHDPRNPAYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSNLYHIYEVNLVSEHIWCEDFL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  876 VRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYVLIDMVLNKMA 955
Cdd:cd14610  161 VRSFYLKNLQTNETRTVTQFHFLSWNDQGVPASTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMA 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 13928818  956 KGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEVNAI 998
Cdd:cd14610  241 KGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEVNAI 283
Receptor_IA-2 pfam11548
Protein-tyrosine phosphatase receptor IA-2; IA-2 is a protein-tyrosine phosphatase receptor ...
 498-586 6.57e-42

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: 147.77  E-value: 6.57e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818    498 EQQGYILTGNNPLSPEKGKQLMDEVAHLLRVPSSFFADVKVLGPAVIFKVSANIQNMTTADVTKAAVDNKDELEKATGLT 577
Cdd:pfam11548    1 EEYGYIVTDNDPLSWEEGLRLMEKVAELLHLPMSSFADIRVLGPAVTFKVRANNKNLTAADVAKAAVDIKDKLEKETGLK 80


                   ....*....
gi 13928818    578 ILQSGIRPK 586
Cdd:pfam11548   81 ILQAGVGDK 89
RESP18 super family cl20829
RESP18 domain; This domain is found in the glucocorticoid-responsive protein regulated ...
 80-126 1.40e-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: 39.04  E-value: 1.40e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 13928818     80 HLRIILQKLSRTGFTWQDDYTQRVIAQELSNLPK-----AYLWHEEASSPAR 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 ...
 716-998 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: 643.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  716 TGHMILAYMEDHLKNKNRLEKEWEALCAYQAEPDSSLVAQREENAPKNRSLAVLTYDHSRILLKSENSHSNSDYINASPI 795
Cdd:cd14610    1 TGHMILSYMEDHLKNKNRLEKEWEALCAYQAEPNATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  796 MDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNVYHVYEVNLVSEHIWCQDFL 875
Cdd:cd14610   81 MDHDPRNPAYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSNLYHIYEVNLVSEHIWCEDFL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  876 VRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYVLIDMVLNKMA 955
Cdd:cd14610  161 VRSFYLKNLQTNETRTVTQFHFLSWNDQGVPASTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMA 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 13928818  956 KGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEVNAI 998
Cdd:cd14610  241 KGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEVNAI 283
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
734-993 2.51e-108

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 336.55  E-value: 2.51e-108
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818     734 LEKEWEALCAYQAEPDSSLVAQREENAPKNRSLAVLTYDHSRILLKSENsHSNSDYINASPIMDHDPRNpAYIATQGPLP 813
Cdd:smart00194    2 LEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPP-GEGSDYINASYIDGPNGPK-AYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818     814 ATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEG--SNVYHVYEVNLVSEHIwCQDFLVRSFYLKNLQTNETRT 891
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEgePLTYGDITVTLKSVEK-VDDYTIRTLEVTNTGCSETRT 158

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818     892 VTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYVLIDMVLNKMAKGaKEIDIAATLEHLR 971
Cdd:smart00194  159 VTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAG-KEVDIFEIVKELR 237

                           250       260
                    ....*....|....*....|..
gi 13928818     972 DQRPGMVQTKEQFEFALTAVAE 993
Cdd:smart00194  238 SQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
759-993 1.71e-103

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 323.04  E-value: 1.71e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818    759 NAPKNRSLAVLTYDHSRILLKSENSHSnsDYINASPIMDHdPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLS 838
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGPS--DYINASYIDGY-KKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818    839 ENGVRQCHHYWPD--EGSNVYHVYEVNLVSEHIWCQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFR 916
Cdd:pfam00102   78 EKGREKCAQYWPEeeGESLEYGDFTVTLKKEKEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLL 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13928818    917 RKVNKCY-RGRSCPIIVHCSDGAGRSGTYVLIDMVLNKMAKGaKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAE 993
Cdd:pfam00102  158 RKVRKSSlDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAE-GEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
Receptor_IA-2 pfam11548
Protein-tyrosine phosphatase receptor IA-2; IA-2 is a protein-tyrosine phosphatase receptor ...
 498-586 6.57e-42

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: 147.77  E-value: 6.57e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818    498 EQQGYILTGNNPLSPEKGKQLMDEVAHLLRVPSSFFADVKVLGPAVIFKVSANIQNMTTADVTKAAVDNKDELEKATGLT 577
Cdd:pfam11548    1 EEYGYIVTDNDPLSWEEGLRLMEKVAELLHLPMSSFADIRVLGPAVTFKVRANNKNLTAADVAKAAVDIKDKLEKETGLK 80


                   ....*....
gi 13928818    578 ILQSGIRPK 586
Cdd:pfam11548   81 ILQAGVGDK 89
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 755-986 2.60e-41

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 154.39  E-value: 2.60e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818   755 QREENAPKNRSLAVLTYDHSRILLKSeNSHSNSDYINASPImDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVML 834
Cdd:PHA02747   47 EKPENQPKNRYWDIPCWDHNRVILDS-GGGSTSDYIHANWI-DGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVML 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818   835 TPLSE-NGVRQCHHYW-PDEGSNV----YHVYEVNLVsehiwcqdflVRSFYLKNL------QTNETRTVTQFHFLSWYD 902
Cdd:PHA02747  125 TPTKGtNGEEKCYQYWcLNEDGNIdmedFRIETLKTS----------VRAKYILTLieitdkILKDSRKISHFQCSEWFE 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818   903 QGVPSSTRSLLDF-------RRKVNKCYRGRS---CPIIVHCSDGAGRSGTYVLIDMVLNKMAKgAKEIDIAATLEHLRD 972
Cdd:PHA02747  195 DETPSDHPDFIKFikiidinRKKSGKLFNPKDallCPIVVHCSDGVGKTGIFCAVDICLNQLVK-RKAICLAKTAEKIRE 273

                         250
                  ....*....|....
gi 13928818   973 QRPGMVQTKEQFEF 986
Cdd:PHA02747  274 QRHAGIMNFDDYLF 287
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
732-999 6.47e-37

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 140.61  E-value: 6.47e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  732 NRLEKEWEALcAYQAEPDSSLvaQREENAPKNRSLAVLTYDHSRIllksensHSNSDYINASPIMDHDPRNpaYIATQGP 811
Cdd:COG5599   18 SRLSTLTNEL-APSHNDPQYL--QNINGSPLNRFRDIQPYKETAL-------RANLGYLNANYIQVIGNHR--YIATQYP 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  812 LPATVADFWQMVWESGCAVIVMLTPLSENGVRQ--CHHYWPDEGSnvYHVYEV-NLVSEHIWCQD-FLVRSFYLKNLQTN 887
Cdd:COG5599   86 LEEQLEDFFQMLFDNNTPVLVVLASDDEISKPKvkMPVYFRQDGE--YGKYEVsSELTESIQLRDgIEARTYVLTIKGTG 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  888 -ETRTVTQFHFLSWYDQGVPSST--RSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYVLIdMVLNKMAKGAKEIDIA 964
Cdd:COG5599  164 qKKIEIPVLHVKNWPDHGAISAEalKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIAC-LALSKSINALVQITLS 242

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 13928818  965 A--TLEHLRDQR-PGMVQTKEQFEFaLTAVAEEVNAIL 999
Cdd:COG5599  243 VeeIVIDMRTSRnGGMVQTSEQLDV-LVKLAEQQIRPL 279
RESP18 pfam14948
RESP18 domain; This domain is found in the glucocorticoid-responsive protein regulated ...
 80-126 1.40e-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: 39.04  E-value: 1.40e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 13928818     80 HLRIILQKLSRTGFTWQDDYTQRVIAQELSNLPK-----AYLWHEEASSPAR 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 ...
 716-998 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: 643.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  716 TGHMILAYMEDHLKNKNRLEKEWEALCAYQAEPDSSLVAQREENAPKNRSLAVLTYDHSRILLKSENSHSNSDYINASPI 795
Cdd:cd14610    1 TGHMILSYMEDHLKNKNRLEKEWEALCAYQAEPNATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  796 MDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNVYHVYEVNLVSEHIWCQDFL 875
Cdd:cd14610   81 MDHDPRNPAYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSNLYHIYEVNLVSEHIWCEDFL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  876 VRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYVLIDMVLNKMA 955
Cdd:cd14610  161 VRSFYLKNLQTNETRTVTQFHFLSWNDQGVPASTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMA 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 13928818  956 KGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEVNAI 998
Cdd:cd14610  241 KGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEVNAI 283
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 718-998 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 13928818  718 HMILAYMEDHLKNKNRLEKEWEALCAYQAEPDSSLVAQREENAPKNRSLAVLTYDHSRILLKSENSHSNSDYINASPIMD 797
Cdd:cd14609    1 HMILAYMEDHLRNRDRLAKEWQALCAYQAEPNTCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPIIE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  798 HDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNVYHVYEVNLVSEHIWCQDFLVR 877
Cdd:cd14609   81 HDPRMPAYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHIYEVNLVSEHIWCEDFLVR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  878 SFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYVLIDMVLNKMAKG 957
Cdd:cd14609  161 SFYLKNVQTQETRTLTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKG 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 13928818  958 AKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEVNAI 998
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 ...
 789-996 1.70e-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: 1.70e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  789 YINASPIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNVYHVYEVNLVSEH 868
Cdd:cd14546    1 YINASTIYDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEVYHIYEVHLVSEH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  869 IWCQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYVLID 948
Cdd:cd14546   81 IWCDDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSCPIVVHCSDGAGRTGTYILID 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 13928818  949 MVLNKMAKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEVN 996
Cdd:cd14546  161 MVLNRMAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAEEVN 208
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
734-993 2.51e-108

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 336.55  E-value: 2.51e-108
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818     734 LEKEWEALCAYQAEPDSSLVAQREENAPKNRSLAVLTYDHSRILLKSENsHSNSDYINASPIMDHDPRNpAYIATQGPLP 813
Cdd:smart00194    2 LEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPP-GEGSDYINASYIDGPNGPK-AYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818     814 ATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEG--SNVYHVYEVNLVSEHIwCQDFLVRSFYLKNLQTNETRT 891
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEgePLTYGDITVTLKSVEK-VDDYTIRTLEVTNTGCSETRT 158

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818     892 VTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYVLIDMVLNKMAKGaKEIDIAATLEHLR 971
Cdd:smart00194  159 VTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAG-KEVDIFEIVKELR 237

                           250       260
                    ....*....|....*....|..
gi 13928818     972 DQRPGMVQTKEQFEFALTAVAE 993
Cdd:smart00194  238 SQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
759-993 1.71e-103

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 323.04  E-value: 1.71e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818    759 NAPKNRSLAVLTYDHSRILLKSENSHSnsDYINASPIMDHdPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLS 838
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGPS--DYINASYIDGY-KKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818    839 ENGVRQCHHYWPD--EGSNVYHVYEVNLVSEHIWCQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFR 916
Cdd:pfam00102   78 EKGREKCAQYWPEeeGESLEYGDFTVTLKKEKEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLL 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13928818    917 RKVNKCY-RGRSCPIIVHCSDGAGRSGTYVLIDMVLNKMAKGaKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAE 993
Cdd:pfam00102  158 RKVRKSSlDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAE-GEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 789-986 1.95e-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: 276.09  E-value: 1.95e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  789 YINASPIMDHDPRNpAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSN--VYHVYEVNLVS 866
Cdd:cd00047    1 YINASYIDGYRGPK-EYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKplEYGDITVTLVS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  867 EHIwCQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYVL 946
Cdd:cd00047   80 EEE-LSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTGTFIA 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 13928818  947 IDMVLNKMAKGaKEIDIAATLEHLRDQRPGMVQTKEQFEF 986
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 ...
 757-997 5.11e-73

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: 241.15  E-value: 5.11e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  757 EENAPKNRSLAVLTYDHSRILLKSENSHSNSDYINASpIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTP 836
Cdd:cd14553    1 EVNKPKNRYANVIAYDHSRVILQPIEGVPGSDYINAN-YCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  837 LSENGVRQCHHYWPDEGSNVYHVYEVNLVsEHIWCQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFR 916
Cdd:cd14553   80 LEERSRVKCDQYWPTRGTETYGLIQVTLL-DTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  917 RKVNKCYRGRSCPIIVHCSDGAGRSGTYVLIDMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEVN 996
Cdd:cd14553  159 RRVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERI-KHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLEAVT 237


                 .
gi 13928818  997 A 997
Cdd:cd14553  238 C 238
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 759-986 4.45e-71

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: 237.26  E-value: 4.45e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  759 NAPKNRSLAVLTYDHSRILLKSENSHSNSDYINASpIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLS 838
Cdd:cd14543   29 NQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINAN-FMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLVIVMTTRVV 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  839 ENGVRQCHHYWPDEGSNVYHVYEVNLVSEHIWC-QDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRR 917
Cdd:cd14543  108 ERGRVKCGQYWPLEEGSSLRYGDLTVTNLSVENkEHYKKTTLEIHNTETDESRQVTHFQFTSWPDFGVPSSAAALLDFLG 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  918 KVnKCYRGRSC--------------PIIVHCSDGAGRSGTYVLIDMVLNKMAKGAKeIDIAATLEHLRDQRPGMVQTKEQ 983
Cdd:cd14543  188 EV-RQQQALAVkamgdrwkghppgpPIVVHCSAGIGRTGTFCTLDICLSQLEDVGT-LNVMQTVRRMRTQRAFSIQTPDQ 265


                 ...
gi 13928818  984 FEF 986
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 ...
 759-990 1.14e-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: 232.03  E-value: 1.14e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  759 NAPKNRSLAVLTYDHSRILLKSENSHSNSDYINASPIMDHDPRNpAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLS 838
Cdd:cd14554    6 NKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRG-AYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKLR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  839 ENGVRQCHHYWPDEGSNVYHVYEVNLVSEHIWCQdFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRK 918
Cdd:cd14554   85 EMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQ-YILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQ 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13928818  919 VNKCYR--GRSCPIIVHCSDGAGRSGTYVLIDMVLNKM-AKGAkeIDIAATLEHLRDQRPGMVQTKEQFEFALTA 990
Cdd:cd14554  164 VHKTKEqfGQEGPITVHCSAGVGRTGVFITLSIVLERMrYEGV--VDVFQTVKLLRTQRPAMVQTEDQYQFCYRA 236
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 768-986 4.77e-66

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: 221.46  E-value: 4.77e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  768 VLTYDHSRILLKSENSHSNSDYINASPIMD-HDPRNpaYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCH 846
Cdd:cd14548    5 ILPYDHSRVKLIPINEEEGSDYINANYIPGyNSPRE--FIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVKCD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  847 HYWP-DEGSNVYHVYEVNLVSEHIwCQDFLVRSFYLKNLQtnETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVnKCYRG 925
Cdd:cd14548   83 HYWPfDQDPVYYGDITVTMLSESV-LPDWTIREFKLERGD--EVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLV-RDYIK 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13928818  926 RSC-PIIVHCSDGAGRSGTYVLIDMVLNKMAKgAKEIDIAATLEHLRDQRPGMVQTKEQFEF 986
Cdd:cd14548  159 QEKgPTIVHCSAGVGRTGTFIALDRLLQQIES-EDYVDIFGIVYDLRKHRPLMVQTEAQYIF 219
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 789-986 6.97e-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: 220.58  E-value: 6.97e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  789 YINASPI-MDHDPRNpAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNVYH-VYEVNLVS 866
Cdd:cd18533    1 YINASYItLPGTSSK-RYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGEYgDLTVELVS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  867 EH-IWCQDFLVRSFYLKNlQTNETRTVTQFHFLSWYDQGVPSSTRSLL---DFRRKVNKCYRGRScPIIVHCSDGAGRSG 942
Cdd:cd18533   80 EEeNDDGGFIVREFELSK-EDGKVKKVYHIQYKSWPDFGVPDSPEDLLtliKLKRELNDSASLDP-PIIVHCSAGVGRTG 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 13928818  943 TYVLIDMVLNKMAKGA-------KEID-IAATLEHLRDQRPGMVQTKEQFEF 986
Cdd:cd18533  158 TFIALDSLLDELKRGLsdsqdleDSEDpVYEIVNQLRKQRMSMVQTLRQYIF 209
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 789-986 5.07e-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: 5.07e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  789 YINASPImDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNVYHVYEVNLVSEH 868
Cdd:cd14549    1 YINANYV-DGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTETYGNIQVTLLSTE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  869 IWCQdFLVRSFYLKNLQ------TNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSG 942
Cdd:cd14549   80 VLAT-YTVRTFSLKNLKlkkvkgRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVGRTG 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 13928818  943 TYVLIDMVLnKMAKGAKEIDIAATLEHLRDQRPGMVQTKEQFEF 986
Cdd:cd14549  159 TYIVIDSML-QQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIF 201
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 759-992 1.47e-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: 218.49  E-value: 1.47e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  759 NAPKNRSLAVLTYDHSRILLKS-ENSHSNSDYINASPIM------DHDPRNPAYIATQGPLPATVADFWQMVWESGCAVI 831
Cdd:cd14544    1 NKGKNRYKNILPFDHTRVILKDrDPNVPGSDYINANYIRnenegpTTDENAKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  832 VMLTPLSENGVRQCHHYWPDEG-SNVYHVYEVNLVSEHIwCQDFLVRSFYLKNL-QTNETRTVTQFHFLSWYDQGVPSST 909
Cdd:cd14544   81 VMTTKEVERGKNKCVRYWPDEGmQKQYGPYRVQNVSEHD-TTDYTLRELQVSKLdQGDPIREIWHYQYLSWPDHGVPSDP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  910 RSLLDFRRKVNKCYRGR--SCPIIVHCSDGAGRSGTYVLIDMVLNKMAKG--AKEIDIAATLEHLRDQRPGMVQTKEQFE 985
Cdd:cd14544  160 GGVLNFLEDVNQRQESLphAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKglDCDIDIQKTIQMVRSQRSGMVQTEAQYK 239


                 ....*..
gi 13928818  986 FALTAVA 992
Cdd:cd14544  240 FIYVAVA 246
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 757-995 6.44e-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: 6.44e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  757 EENAPKNRSLAVLTYDHSRILLKSENSHSNSDYINASPIMDHDPRNpAYIATQGPLPATVADFWQMVWESGCAVIVMLTP 836
Cdd:cd14626   39 EVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGYRKQN-AYIATQGPLPETLSDFWRMVWEQRTATIVMMTR 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  837 LSENGVRQCHHYWPDEGSNVYHVYEVNLVsEHIWCQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFR 916
Cdd:cd14626  118 LEEKSRVKCDQYWPIRGTETYGMIQVTLL-DTVELATYSVRTFALYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFL 196

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13928818  917 RKVNKCYRGRSCPIIVHCSDGAGRSGTYVLIDMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEV 995
Cdd:cd14626  197 RRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERM-KHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLEAA 274
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 788-1001 3.88e-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: 207.18  E-value: 3.88e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  788 DYINASPIMDHDPRNPA---YIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNVYH-VYEVN 863
Cdd:cd14541    1 DYINANYVNMEIPGSGIvnrYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGETMQFgNLQIT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  864 LVSEHIwCQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGT 943
Cdd:cd14541   81 CVSEEV-TPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCSAGIGRTGV 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 13928818  944 YVLIDMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFaltaVAEevnAILKA 1001
Cdd:cd14541  160 LITMETAMCLI-EANEPVYPLDIVRTMRDQRAMLIQTPSQYRF----VCE---AILRV 209
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 763-986 6.44e-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: 207.36  E-value: 6.44e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  763 NRSLAVLTYDHSRILLKSENsHSNSDYINASPIMDHDpRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGV 842
Cdd:cd14615    1 NRYNNVLPYDISRVKLSVQS-HSTDDYINANYMPGYN-SKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  843 RQCHHYWPDEGSNVYHVYEVNLVSEhIWCQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKC 922
Cdd:cd14615   79 TKCEEYWPSKQKKDYGDITVTMTSE-IVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVREY 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13928818  923 YRG--RSCPIIVHCSDGAGRSGTYVLIDMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQFEF 986
Cdd:cd14615  158 MKQnpPNSPILVHCSAGVGRTGTFIAIDRLIYQI-ENENVVDVYGIVYDLRMHRPLMVQTEDQYVF 222
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 762-986 9.44e-60

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: 204.16  E-value: 9.44e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  762 KNRSLAVLTYDHSRILLKSENShsNSDYINASPI-MDHDPRNpaYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSEN 840
Cdd:cd14545    1 LNRYRDRDPYDHDRSRVKLKQG--DNDYINASLVeVEEAKRS--YILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  841 GVRQCHHYWPDEGSNVYHV----YEVNLVSEHIWcQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFR 916
Cdd:cd14545   77 GQIKCAQYWPQGEGNAMIFedtgLKVTLLSEEDK-SYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFL 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13928818  917 RKVNK--CYRGRSCPIIVHCSDGAGRSGTYVLIDMVLNKMAKG-AKEIDIAATLEHLRDQRPGMVQTKEQFEF 986
Cdd:cd14545  156 QKVREsgSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGnPSSVDVKKVLLEMRKYRMGLIQTPDQLRF 228
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 789-993 1.26e-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: 202.99  E-value: 1.26e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  789 YINASPI-MDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPD---EGSNVYHVYEVNL 864
Cdd:cd14538    1 YINASHIrIPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDslnKPLICGGRLEVSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  865 VSEHIWcQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYrgRSCPIIVHCSDGAGRSGTY 944
Cdd:cd14538   81 EKYQSL-QDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIH--NSGPIVVHCSAGIGRTGVL 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 13928818  945 VLIDMVLNKMAKGaKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAE 993
Cdd:cd14538  158 ITIDVALGLIERD-LPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLE 205
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 763-986 9.88e-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: 201.27  E-value: 9.88e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  763 NRSLAVLTYDHSRILLKSENSHSNSDYINASpIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGV 842
Cdd:cd14619    1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINAN-YMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  843 RQCHHYWP-DEGSNVYHVYEVNLVSEHIwCQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNK 921
Cdd:cd14619   80 VKCEHYWPlDYTPCTYGHLRVTVVSEEV-MENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRQ 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13928818  922 CYRGR--SCPIIVHCSDGAGRSGTYVLIDMVLNKMAKgAKEIDIAATLEHLRDQRPGMVQTKEQFEF 986
Cdd:cd14619  159 WLDQTmsGGPTVVHCSAGVGRTGTLIALDVLLQQLQS-EGLLGPFSFVQKMRENRPLMVQTESQYVF 224
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 721-995 2.05e-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: 2.05e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  721 LAYMEDHLKNKN--RLEKEWEALcayqaEPDSSLVAQR---EENAPKNRSLAVLTYDHSRILLKSENSHSNSDYINASPI 795
Cdd:cd14625    9 LAEHTERLKANDnlKLSQEYESI-----DPGQQFTWEHsnlEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINANYI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  796 mDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNVYHVYEVNLVsEHIWCQDFL 875
Cdd:cd14625   84 -DGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRGTETYGMIQVTLL-DTIELATFC 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  876 VRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYVLIDMVLNKMa 955
Cdd:cd14625  162 VRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVIDAMLERI- 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 13928818  956 KGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEV 995
Cdd:cd14625  241 KHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAV 280
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 729-993 2.56e-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: 199.57  E-value: 2.56e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  729 KNKNRLEKEWEALCAYQAEPDSSLVAQREENAPKNRSLAVLTYDHSRILLKSENSHSNSDYINASpIMDHDPRNPAYIAT 808
Cdd:cd14628   22 ENVTGMELEFKRLASSKAHTSRFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINAS-FIDGYRQQKAYIAT 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  809 QGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNVYHVYEVNLVSEHIWCQdFLVRSFYLKNLQTNE 888
Cdd:cd14628  101 QGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQ-YILREFKVTDARDGQ 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  889 TRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYR--GRSCPIIVHCSDGAGRSGTYVLIDMVLNKMaKGAKEIDIAAT 966
Cdd:cd14628  180 SRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEqfGQDGPISVHCSAGVGRTGVFITLSIVLERM-RYEGVVDIFQT 258

                        250       260
                 ....*....|....*....|....*..
gi 13928818  967 LEHLRDQRPGMVQTKEQFEFALTAVAE 993
Cdd:cd14628  259 VKMLRTQRPAMVQTEDQYQFCYRAALE 285
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 755-993 4.94e-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: 197.80  E-value: 4.94e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  755 QREENAPKNRSLAVLTYDHSRILLKSENSHS-NSDYINASPIMDH--DPRNPA--YIATQGPLPATVADFWQMVWESGCA 829
Cdd:cd14606   14 QRPENKSKNRYKNILPFDHSRVILQGRDSNIpGSDYINANYVKNQllGPDENAktYIASQGCLEATVNDFWQMAWQENSR 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  830 VIVMLTPLSENGVRQCHHYWPDEGSN-VYHVYEVNLVSEHIwCQDFLVRSFYLKNLQTNET-RTVTQFHFLSWYDQGVPS 907
Cdd:cd14606   94 VIVMTTREVEKGRNKCVPYWPEVGMQrAYGPYSVTNCGEHD-TTEYKLRTLQVSPLDNGELiREIWHYQYLSWPDHGVPS 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  908 STRSLLDFRRKVNKCYRG--RSCPIIVHCSDGAGRSGTYVLIDMVLNKM-AKGAK-EIDIAATLEHLRDQRPGMVQTKEQ 983
Cdd:cd14606  173 EPGGVLSFLDQINQRQESlpHAGPIIVHCSAGIGRTGTIIVIDMLMENIsTKGLDcDIDIQKTIQMVRAQRSGMVQTEAQ 252

                        250
                 ....*....|
gi 13928818  984 FEFALTAVAE 993
Cdd:cd14606  253 YKFIYVAIAQ 262
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 768-993 4.63e-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: 193.62  E-value: 4.63e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  768 VLTYDHSRILLKSENSHSNSDYINASPIMDHDPRNpAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHH 847
Cdd:cd14620    4 ILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKN-KFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKCYQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  848 YWPDEGSNVYHVYEVNlVSEHIWCQDFLVRSFYLKNLQTNET---RTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYR 924
Cdd:cd14620   83 YWPDQGCWTYGNIRVA-VEDCVVLVDYTIRKFCIQPQLPDGCkapRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVKSVNP 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13928818  925 GRSCPIIVHCSDGAGRSGTYVLIDMVLNkMAKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAE 993
Cdd:cd14620  162 VHAGPIVVHCSAGVGRTGTFIVIDAMID-MMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 763-986 6.03e-56

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: 193.00  E-value: 6.03e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  763 NRSLAVLTYDHSRILLKSENSHSNSDYINASPIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGV 842
Cdd:cd14547    1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYDGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  843 RqCHHYWPDEGSNVYHVYEVnLVSEHIWCQDFLVRSFYLKNlqTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKC 922
Cdd:cd14547   81 K-CAQYWPEEENETYGDFEV-TVQSVKETDGYTVRKLTLKY--GGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEEA 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13928818  923 -YRGRSC-PIIVHCSDGAGRSGTYVLIDMVLNKMAKGAKeIDIAATLEHLRDQRPGMVQTKEQFEF 986
Cdd:cd14547  157 rQTEPHRgPIVVHCSAGIGRTGCFIATSIGCQQLREEGV-VDVLGIVCQLRLDRGGMVQTAEQYEF 221
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 734-993 6.24e-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: 195.72  E-value: 6.24e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  734 LEKEWEALCAYQAEPDSSLVAQREENAPKNRSLAVLTYDHSRILLKSENSHSNSDYINASpIMDHDPRNPAYIATQGPLP 813
Cdd:cd14627   28 MELEFKRLANSKAHTSRFISANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINAS-FIDGYRQQKAYIATQGPLA 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  814 ATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNVYHVYEVNLVSEHIWCQdFLVRSFYLKNLQTNETRTVT 893
Cdd:cd14627  107 ETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQ-YILREFKVTDARDGQSRTVR 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  894 QFHFLSWYDQGVPSSTRSLLDFRRKVNKCYR--GRSCPIIVHCSDGAGRSGTYVLIDMVLNKMaKGAKEIDIAATLEHLR 971
Cdd:cd14627  186 QFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEqfGQDGPISVHCSAGVGRTGVFITLSIVLERM-RYEGVVDIFQTVKMLR 264

                        250       260
                 ....*....|....*....|..
gi 13928818  972 DQRPGMVQTKEQFEFALTAVAE 993
Cdd:cd14627  265 TQRPAMVQTEDEYQFCYQAALE 286
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 789-986 8.75e-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: 8.75e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  789 YINASPIMD-HDPRnpAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNvYHVYEVNLVSE 867
Cdd:cd14558    1 YINASFIDGyWGPK--SLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKT-YGDIEVELKDT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  868 HIwCQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKV------NKCYRGRSCPIIVHCSDGAGRS 941
Cdd:cd14558   78 EK-SPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIkqklpyKNSKHGRSVPIVVHCSDGSSRT 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 13928818  942 GTYVLIdmvLNKMAKGAKE--IDIAATLEHLRDQRPGMVQTKEQFEF 986
Cdd:cd14558  157 GIFCAL---WNLLESAETEkvVDVFQVVKALRKQRPGMVSTLEQYQF 200
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 753-993 1.58e-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: 194.77  E-value: 1.58e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  753 VAQREENAPKNRSLAVLTYDHSRILLKSENSHSNSDYINASPIMD-HDPRnpAYIATQGPLPATVADFWQMVWESGCAVI 831
Cdd:cd14604   51 TGEKEENVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGvYGPK--AYIATQGPLANTVIDFWRMIWEYNVAII 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  832 VMLTPLSENGVRQCHHYWPDEGSNvyhvyEVNLVSEHIWCQ------DFLVRSFYLKnLQtNETRTVTQFHFLSWYDQGV 905
Cdd:cd14604  129 VMACREFEMGRKKCERYWPLYGEE-----PMTFGPFRISCEaeqartDYFIRTLLLE-FQ-NETRRLYQFHYVNWPDHDV 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  906 PSSTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYVLIDMVLN--KMAKGAKEIDIAATLEHLRDQRPGMVQTKEQ 983
Cdd:cd14604  202 PSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNllKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQ 281

                        250
                 ....*....|
gi 13928818  984 FEFALTAVAE 993
Cdd:cd14604  282 YELVHRAIAQ 291
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 789-986 3.54e-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: 189.94  E-value: 3.54e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  789 YINASPIMDHDpRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNV--YHVYEVNLVS 866
Cdd:cd14542    1 YINANFIKGVS-GSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQlqFGPFKISLEK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  867 EHIWCQDFLVRSfyLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYVL 946
Cdd:cd14542   80 EKRVGPDFLIRT--LKVTFQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGCGRTGTICA 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 13928818  947 IDMVLNKMAKGA--KEIDIAATLEHLRDQRPGMVQTKEQFEF 986
Cdd:cd14542  158 IDYVWNLLKTGKipEEFSLFDLVREMRKQRPAMVQTKEQYEL 199
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 749-995 5.56e-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: 5.56e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  749 DSSLVAQRE---ENAPKNRSLAVLTYDHSRILLK--SENSHSNSDYINASPIMDHDpRNPAYIATQGPLPATVADFWQMV 823
Cdd:cd17667   14 DMNITAEHSnhpDNKHKNRYINILAYDHSRVKLRplPGKDSKHSDYINANYVDGYN-KAKAYIATQGPLKSTFEDFWRMI 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  824 WESGCAVIVMLTPLSENGVRQCHHYWPDEGSNVYHVYEVNLVSEHIW-CqdFLVRSFYLKNLQT------------NEtR 890
Cdd:cd17667   93 WEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHaC--YTVRRFSIRNTKVkkgqkgnpkgrqNE-R 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  891 TVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYVLIDMVLNKMaKGAKEIDIAATLEHL 970
Cdd:cd17667  170 TVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQI-KDKSTVNVLGFLKHI 248

                        250       260
                 ....*....|....*....|....*
gi 13928818  971 RDQRPGMVQTKEQFEFALTAVAEEV 995
Cdd:cd17667  249 RTQRNYLVQTEEQYIFIHDALLEAI 273
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 757-993 9.96e-55

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: 190.24  E-value: 9.96e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  757 EENAPKNRSLAVLTYDHSRILLKSENSHSNSDYINASPIMD-HDPRNpaYIATQGPLPATVADFWQMVWESGCAVIVMLT 835
Cdd:cd14630    1 DENRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGyHRPRH--YIATQGPMQETVKDFWRMIWQENSASVVMVT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  836 PLSENGVRQCHHYWPDEgSNVYHVYEVNLVsEHIWCQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDF 915
Cdd:cd14630   79 NLVEVGRVKCVRYWPDD-TEVYGDIKVTLI-ETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGF 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13928818  916 RRKVNKCYRGRSCPIIVHCSDGAGRSGTYVLIDMVLNkMAKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAE 993
Cdd:cd14630  157 VRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLD-MAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILE 233
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 757-986 1.29e-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: 189.66  E-value: 1.29e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  757 EENAPKNRSLAVLTYDHSRILLKSENshsnsDYINASPI-MDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLT 835
Cdd:cd14597    1 KENRKKNRYKNILPYDTTRVPLGDEG-----GYINASFIkMPVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMT 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  836 PLSENGVRQCHHYWPDEGSNVYHVYE---VNLVS-EHIwcQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRS 911
Cdd:cd14597   76 QEVEGGKIKCQRYWPEILGKTTMVDNrlqLTLVRmQQL--KNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPEQ 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13928818  912 LLDFRRKVNKCYrgRSCPIIVHCSDGAGRSGTYVLIDMVLNKMAKGAkEIDIAATLEHLRDQRPGMVQTKEQFEF 986
Cdd:cd14597  154 LLTFISYMRHIH--KSGPIITHCSAGIGRSGTLICIDVVLGLISKDL-DFDISDIVRTMRLQRHGMVQTEDQYIF 225
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 734-993 1.48e-54

catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350481 [Multi-domain]  Cd Length: 273  Bit Score: 191.02  E-value: 1.48e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  734 LEKEWEALCAYQAEPDSSlvAQREENAPKNRSLAVLTYDHSRILLKSENSHSNSDYINASPImDHDPRNPAYIATQGPLP 813
Cdd:cd14633   17 FKEEYESFFEGQSAPWDS--AKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYI-DGYHRPNHYIATQGPMQ 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  814 ATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEgSNVYHVYEVNLVSEHIwCQDFLVRSFYLKNLQTNETRTVT 893
Cdd:cd14633   94 ETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDD-TEIYKDIKVTLIETEL-LAEYVIRTFAVEKRGVHEIREIR 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  894 QFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYVLIDMVLNkMAKGAKEIDIAATLEHLRDQ 973
Cdd:cd14633  172 QFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLD-MAEREGVVDIYNCVRELRSR 250

                        250       260
                 ....*....|....*....|
gi 13928818  974 RPGMVQTKEQFEFALTAVAE 993
Cdd:cd14633  251 RVNMVQTEEQYVFIHDAILE 270
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 724-993 2.05e-54

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: 191.39  E-value: 2.05e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  724 MEDHLKNKNRL-EKEWEAL--CAYQAEPDSslvAQREENAPKNRSLAVLTYDHSRILLKSENSHSNSDYINASPIMDHDP 800
Cdd:cd14621   17 INRRMADDNKLfREEFNALpaCPIQATCEA---ASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINASFINGYQE 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  801 RNpAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNVYHVYEVNlVSEHIWCQDFLVRSFY 880
Cdd:cd14621   94 KN-KFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGCWTYGNIRVS-VEDVTVLVDYTVRKFC 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  881 LKNL----QTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYVLIDMVLNkMAK 956
Cdd:cd14621  172 IQQVgdvtNKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVIDAMLD-MMH 250

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 13928818  957 GAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAE 993
Cdd:cd14621  251 AERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLE 287
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 757-995 3.08e-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: 190.71  E-value: 3.08e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  757 EENAPKNRSLAVLTYDHSRILLKSENSHSNSDYINASPIMDHDPRNpAYIATQGPLPATVADFWQMVWESGCAVIVMLTP 836
Cdd:cd14624   45 EVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINANYIDGYRKQN-AYIATQGALPETFGDFWRMIWEQRSATVVMMTK 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  837 LSENGVRQCHHYWPDEGSNVYHVYEVNLVsEHIWCQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFR 916
Cdd:cd14624  124 LEERSRVKCDQYWPSRGTETYGLIQVTLL-DTVELATYCVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFL 202

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13928818  917 RKVNKCYRGRSCPIIVHCSDGAGRSGTYVLIDMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEV 995
Cdd:cd14624  203 RRVKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERI-KHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAV 280
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 734-993 3.61e-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: 190.71  E-value: 3.61e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  734 LEKEWEALCAYQAEPDSSLVAQREENAPKNRSLAVLTYDHSRILLKSENSHSNSDYINASpIMDHDPRNPAYIATQGPLP 813
Cdd:cd14629   28 MELEFKLLANSKAHTSRFISANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINAS-FIDGYRQQKAYIATQGPLA 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  814 ATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNVYHVYEVNLVSEHIWCQdFLVRSFYLKNLQTNETRTVT 893
Cdd:cd14629  107 ETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQ-YILREFKVTDARDGQSRTIR 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  894 QFHFLSWYDQGVPSSTRSLLDFRRKVNKCYR--GRSCPIIVHCSDGAGRSGTYVLIDMVLNKMaKGAKEIDIAATLEHLR 971
Cdd:cd14629  186 QFQFTDWPEQGVPKTGEGFIDFIGQVHKTKEqfGQDGPITVHCSAGVGRTGVFITLSIVLERM-RYEGVVDMFQTVKTLR 264

                        250       260
                 ....*....|....*....|..
gi 13928818  972 DQRPGMVQTKEQFEFALTAVAE 993
Cdd:cd14629  265 TQRPAMVQTEDQYQLCYRAALE 286
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 758-991 6.27e-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: 188.69  E-value: 6.27e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  758 ENAPKNRSLAVLTYDHSRILLKS-ENSHSNSDYINASPIM-DHD-PRNPA-----YIATQGPLPATVADFWQMVWESGCA 829
Cdd:cd14605    1 ENKNKNRYKNILPFDHTRVVLHDgDPNEPVSDYINANIIMpEFEtKCNNSkpkksYIATQGCLQNTVNDFWRMVFQENSR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  830 VIVMLTPLSENGVRQCHHYWPDEGS-NVYHVYEVNLVSEHIwCQDFLVRSFYLKNL-QTNETRTVTQFHFLSWYDQGVPS 907
Cdd:cd14605   81 VIVMTTKEVERGKSKCVKYWPDEYAlKEYGVMRVRNVKESA-AHDYILRELKLSKVgQGNTERTVWQYHFRTWPDHGVPS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  908 STRSLLDFRRKVNKCYRG--RSCPIIVHCSDGAGRSGTYVLIDMVLNKM-AKGAK-EIDIAATLEHLRDQRPGMVQTKEQ 983
Cdd:cd14605  160 DPGGVLDFLEEVHHKQESimDAGPVVVHCSAGIGRTGTFIVIDILIDIIrEKGVDcDIDVPKTIQMVRSQRSGMVQTEAQ 239


                 ....*...
gi 13928818  984 FEFALTAV 991
Cdd:cd14605  240 YRFIYMAV 247
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 789-993 4.44e-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: 4.44e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  789 YINASPI-MDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNVYHV--YEVNLV 865
Cdd:cd14596    1 YINASYItMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELenYQLRLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  866 SEHIwCQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYrgRSCPIIVHCSDGAGRSGTYV 945
Cdd:cd14596   81 NYQA-LQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVH--NTGPIVVHCSAGIGRAGVLI 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 13928818  946 LIDMVLNKMAKGAkEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAE 993
Cdd:cd14596  158 CVDVLLSLIEKDL-SFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLE 204
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 753-999 1.65e-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: 185.23  E-value: 1.65e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  753 VAQREENAPKNRSLAVLTYDHSRILLKSENShsnsDYINASPI-MDHDPRnpAYIATQGPLPATVADFWQMVWESGCAVI 831
Cdd:cd14608   19 VAKLPKNKNRNRYRDVSPFDHSRIKLHQEDN----DYINASLIkMEEAQR--SYILTQGPLPNTCGHFWEMVWEQKSRGV 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  832 VMLTPLSENGVRQCHHYWPDEGSNVYHVYEVN----LVSEHIWCQdFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPS 907
Cdd:cd14608   93 VMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNlkltLISEDIKSY-YTVRQLELENLTTQETREILHFHYTTWPDFGVPE 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  908 STRSLLDFRRKVNK--CYRGRSCPIIVHCSDGAGRSGTYVLIDMVLNKMA--KGAKEIDIAATLEHLRDQRPGMVQTKEQ 983
Cdd:cd14608  172 SPASFLNFLFKVREsgSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDkrKDPSSVDIKKVLLEMRKFRMGLIQTADQ 251

                        250
                 ....*....|....*.
gi 13928818  984 FEFALTAVAEEVNAIL 999
Cdd:cd14608  252 LRFSYLAVIEGAKFIM 267
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 789-991 3.65e-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: 181.70  E-value: 3.65e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  789 YINASPIMDHDPRNpAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNVYHVYEVNLVSEH 868
Cdd:cd14552    1 YINASFIDGYRQKD-AYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGSVSSGDITVELKDQT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  869 IwCQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGR-SCPIIVHCSDGAGRSGTYVLI 947
Cdd:cd14552   80 D-YEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSgNHPITVHCSAGAGRTGTFCAL 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 13928818  948 DMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAV 991
Cdd:cd14552  159 STVLERV-KAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 764-993 7.70e-52

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: 181.78  E-value: 7.70e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  764 RSLAVLTYDHSRILLKSENSHSNSDYINASpIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVR 843
Cdd:cd14623    1 RVLQIIPYEFNRVIIPVKRGEENTDYVNAS-FIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  844 QCHHYWPDEGSNVYHVYEVNLVSEHiWCQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCY 923
Cdd:cd14623   80 KCAQYWPSDGSVSYGDITIELKKEE-ECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQ 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13928818  924 RGR-SCPIIVHCSDGAGRSGTYVLIDMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAE 993
Cdd:cd14623  159 QQSgNHPITVHCSAGAGRTGTFCALSTVLERV-KAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 750-993 1.14e-51

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: 182.72  E-value: 1.14e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  750 SSLVAQREENAPKNRSLAVLTYDHSRILLKSENSHSNSDYINASPIMDHDpRNPAYIATQGPLPATVADFWQMVWESGCA 829
Cdd:cd14603   21 STVAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVD-GSRAYIATQGPLSHTVLDFWRMIWQYGVK 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  830 VIVMLTPLSENGVRQCHHYWP-DEGSNVYHVYEVNLVSEHIWCQDFLVRSFYLKNLQtnETRTVTQFHFLSWYDQGVPSS 908
Cdd:cd14603  100 VILMACREIEMGKKKCERYWAqEQEPLQTGPFTITLVKEKRLNEEVILRTLKVTFQK--ESRSVSHFQYMAWPDHGIPDS 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  909 TRSLLDFRRKVNKcYRGRS-CPIIVHCSDGAGRSGTYVLIDMVLNKMAKGAKEIDIA---ATLEhLRDQRPGMVQTKEQF 984
Cdd:cd14603  178 PDCMLAMIELARR-LQGSGpEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPDFSifdVVLE-MRKQRPAAVQTEEQY 255


                 ....*....
gi 13928818  985 EFALTAVAE 993
Cdd:cd14603  256 EFLYHTVAQ 264
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 789-986 3.98e-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: 179.02  E-value: 3.98e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  789 YINASpIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNVYHVYEVNLVSEH 868
Cdd:cd17668    1 YINAN-YVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  869 IWCQdFLVRSFYLKNLQTNE--------TRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGR 940
Cdd:cd17668   80 VLAY-YTVRNFTLRNTKIKKgsqkgrpsGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSAGVGR 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 13928818  941 SGTYVLIDMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQFEF 986
Cdd:cd17668  159 TGTYIVLDSMLQQI-QHEGTVNIFGFLKHIRSQRNYLVQTEEQYVF 203
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 789-986 5.72e-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: 178.18  E-value: 5.72e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  789 YINASPIMDHDPRNpAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNVYHVYEVNlVSEH 868
Cdd:cd14551    1 YINASYIDGYQEKN-KFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCWTYGNLRVR-VEDT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  869 IWCQDFLVRSFYLK--NLQTNE--TRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTY 944
Cdd:cd14551   79 VVLVDYTTRKFCIQkvNRGIGEkrVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGRTGTF 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 13928818  945 VLIDMVLNkMAKGAKEIDIAATLEHLRDQRPGMVQTKEQFEF 986
Cdd:cd14551  159 IVIDAMLD-MMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVF 199
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 789-993 1.38e-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: 177.03  E-value: 1.38e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  789 YINASPImDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEgSNVYHVYEVNLVSEH 868
Cdd:cd14555    1 YINANYI-DGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDD-TEVYGDIKVTLVETE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  869 IWCQdFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYVLID 948
Cdd:cd14555   79 PLAE-YVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTGCYIVID 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 13928818  949 MVLNkMAKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAE 993
Cdd:cd14555  158 IMLD-MAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 775-993 3.05e-50

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: 176.75  E-value: 3.05e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  775 RILLKSENSHSNSDYINASPImDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEgS 854
Cdd:cd14631    1 RVILQPVEDDPSSDYINANYI-DGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDD-T 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  855 NVYHVYEVNLVS-EHIwcQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVH 933
Cdd:cd14631   79 EVYGDFKVTCVEmEPL--AEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVH 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  934 CSDGAGRSGTYVLIDMVLNkMAKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAE 993
Cdd:cd14631  157 CSAGAGRTGCYIVIDIMLD-MAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 754-991 3.13e-50

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: 178.89  E-value: 3.13e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  754 AQREENAPKNRSLAVLTYDHSRILLKSenshsNSDYINASPIMDHDPRNP---AYIATQGPLPATVADFWQMVWESGCAV 830
Cdd:cd14600   35 AKLPQNMDKNRYKDVLPYDATRVVLQG-----NEDYINASYVNMEIPSANivnKYIATQGPLPHTCAQFWQVVWEQKLSL 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  831 IVMLTPLSENGVRQCHHYWPDEGSNV-YHVYEVNLVSEHiwCQ-DFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSS 908
Cdd:cd14600  110 IVMLTTLTERGRTKCHQYWPDPPDVMeYGGFRVQCHSED--CTiAYVFREMLLTNTQTGEERTVTHLQYVAWPDHGVPDD 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  909 TRSLLDFRRKVnKCYRGRSCPIIVHCSDGAGRSGTYVLID--MVLNKMAKGAKEIDIAATlehLRDQRPGMVQTKEQFEF 986
Cdd:cd14600  188 SSDFLEFVNYV-RSKRVENEPVLVHCSAGIGRTGVLVTMEtaMCLTERNQPVYPLDIVRK---MRDQRAMMVQTSSQYKF 263


                 ....*
gi 13928818  987 ALTAV 991
Cdd:cd14600  264 VCEAI 268
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 788-993 8.31e-50

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


Pssm-ID: 350470 [Multi-domain]  Cd Length: 205  Bit Score: 175.19  E-value: 8.31e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  788 DYINASPImDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNVYHVYEVNLVSE 867
Cdd:cd14622    1 DYINASFI-DGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGSVTHGEITIEIKND 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  868 HIwCQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGR-SCPIIVHCSDGAGRSGTYVL 946
Cdd:cd14622   80 TL-LETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQTgNHPIVVHCSAGAGRTGTFIA 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 13928818  947 IDMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAE 993
Cdd:cd14622  159 LSNILERV-KAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQD 204
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 762-993 1.18e-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: 175.80  E-value: 1.18e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  762 KNRSLAVLTYDHSRILLKSENSHSNSDYINASPIMD-HDPRnpAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSEN 840
Cdd:cd14602    1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGvYGPR--AYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEM 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  841 GVRQCHHYWPDEGSNVYHVYEVNLVSE-HIWCQDFLVRSfyLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKV 919
Cdd:cd14602   79 GKKKCERYWAEPGEMQLEFGPFSVTCEaEKRKSDYIIRT--LKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDV 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13928818  920 NKCYRGRSCPIIVHCSDGAGRSGTYVLIDMVLNKMAKG--AKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAE 993
Cdd:cd14602  157 RCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGiiPENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIE 232
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 753-991 1.37e-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: 176.31  E-value: 1.37e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  753 VAQREENAPKNRSLAVLTYDHSRILLKSenshSNSDYINASpIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIV 832
Cdd:cd14607   18 VAKYPENRNRNRYRDVSPYDHSRVKLQN----TENDYINAS-LVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVV 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  833 MLTPLSENGVRQCHHYWPDEGSNVYHVYE----VNLVSEHIWCQdFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSS 908
Cdd:cd14607   93 MLNRIVEKDSVKCAQYWPTDEEEVLSFKEtgfsVKLLSEDVKSY-YTVHLLQLENINSGETRTISHFHYTTWPDFGVPES 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  909 TRSLLDFRRKV--NKCYRGRSCPIIVHCSDGAGRSGTYVLIDMVLNKM-AKGAKEIDIAATLEHLRDQRPGMVQTKEQFE 985
Cdd:cd14607  172 PASFLNFLFKVreSGSLSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMeKKDPDSVDIKQVLLDMRKYRMGLIQTPDQLR 251


                 ....*.
gi 13928818  986 FALTAV 991
Cdd:cd14607  252 FSYMAV 257
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 763-986 2.03e-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: 174.75  E-value: 2.03e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  763 NRSLAVLTYDHSRILLKSENSHSNSDYINASPImdhdprnPAY------IATQGPLPATVADFWQMVWESGCAVIVMLTP 836
Cdd:cd14618    1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFI-------PGYtspqefIATQGPLKKTIEDFWRLVWEQQVCNIIMLTV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  837 LSENGVRQCHHYWPDEGSNVYHVY-EVNLVSEHIwCQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDF 915
Cdd:cd14618   74 GMENGRVLCDHYWPSESTPVSYGHiTVHLLAQSS-EDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAF 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13928818  916 RRKVN---KCYRGRScPIIVHCSDGAGRSGTYVLIDMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQFEF 986
Cdd:cd14618  153 RELVRehvQATKGKG-PTLVHCSAGVGRSGTFIALDRLLRQL-KEEKVVDVFNTVYILRMHRYLMIQTLSQYIF 224
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 763-986 7.50e-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: 173.18  E-value: 7.50e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  763 NRSLAVLTYDHSRILLKSENSHSNSDYINASPIMDHDPRNpAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGV 842
Cdd:cd14617    1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRR-EYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  843 RQCHHYWP-DEGSNVYHVYEVNLVSEHIWcQDFLVRSFYLKNL-QTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVN 920
Cdd:cd14617   80 VKCDHYWPaDQDSLYYGDLIVQMLSESVL-PEWTIREFKICSEeQLDAPRLVRHFHYTVWPDHGVPETTQSLIQFVRTVR 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13928818  921 KcYRGRS---CPIIVHCSDGAGRSGTYVLIDMVLNKMAKgAKEIDIAATLEHLRDQRPGMVQTKEQFEF 986
Cdd:cd14617  159 D-YINRTpgsGPTVVHCSAGVGRTGTFIALDRILQQLDS-KDSVDIYGAVHDLRLHRVHMVQTECQYVY 225
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 788-991 1.48e-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: 171.67  E-value: 1.48e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  788 DYINASPIMDHDPRNP---AYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPD-EGSNVYHVYEVN 863
Cdd:cd14601    1 DYINANYINMEIPSSSiinRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEpSGSSSYGGFQVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  864 LVSEHiWCQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGT 943
Cdd:cd14601   81 CHSEE-GNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVHCSAGIGRTGV 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 13928818  944 YVLID--MVLNKMAKGAKEIDIAATlehLRDQRPGMVQTKEQFEFALTAV 991
Cdd:cd14601  160 LITMEtaMCLIECNQPVYPLDIVRT---MRDQRAMMIQTPSQYRFVCEAI 206
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 789-986 2.06e-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: 171.49  E-value: 2.06e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  789 YINASPI-MDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSN----VYHVYEVN 863
Cdd:cd14540    1 YINASHItATVGGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGEhdalTFGEYKVS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  864 LVSEHIwCQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDF-------RRKVNKCYRGRS--CPIIVHC 934
Cdd:cd14540   81 TKFSVS-SGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFleeinsvRRHTNQDVAGHNrnPPTLVHC 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 13928818  935 SDGAGRSGTYVLIDMVLNKMAKGaKEIDIAATLEHLRDQRPGMVQTKEQFEF 986
Cdd:cd14540  160 SAGVGRTGVVILADLMLYCLDHN-EELDIPRVLALLRHQRMLLVQTLAQYKF 210
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 789-987 3.67e-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: 167.56  E-value: 3.67e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  789 YINASPIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDE-GSNV-YHVYEVNLVS 866
Cdd:cd14539    1 YINASLIEDLTPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTErGQALvYGAITVSLQS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  867 EHIwcQDFLV-RSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCY---RGRSCPIIVHCSDGAGRSG 942
Cdd:cd14539   81 VRT--TPTHVeRIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYlqqRSLQTPIVVHCSSGVGRTG 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 13928818  943 TYVLIDMVLNKMAKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFA 987
Cdd:cd14539  159 AFCLLYAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFC 203
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 760-986 4.34e-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: 168.86  E-value: 4.34e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  760 APKNRSLAVLTYDHSRILLKSE-NSHSNSDYINASPIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLS 838
Cdd:cd14612   16 ASKDRYKTILPNPQSRVCLRRAgSQEEEGSYINANYIRGYDGKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITKLK 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  839 EnGVRQCHHYWPD-EGSNVYHVYEVNLVSEhiwCQDFLVRSFYLKnlQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRR 917
Cdd:cd14612   96 E-KKEKCVHYWPEkEGTYGRFEIRVQDMKE---CDGYTIRDLTIQ--LEEESRSVKHYWFSSWPDHQTPESAGPLLRLVA 169

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13928818  918 KVNKCYR--GRSCPIIVHCSDGAGRSGTYVLIDMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQFEF 986
Cdd:cd14612  170 EVEESRQtaASPGPIVVHCSAGIGRTGCFIATSIGCQQL-KDTGKVDILGIVCQLRLDRGGMIQTSEQYQF 239
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 759-986 3.58e-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: 166.22  E-value: 3.58e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  759 NAPKNRSLAVLTYDHSRILLKSENSHSNSDYINASPIMDHD-PRNpaYIATQGPLPATVADFWQMVWESGCAVIVMLTPL 837
Cdd:cd14614   12 NRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNsPQE--YIATQGPLPETRNDFWKMVLQQKSQIIVMLTQC 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  838 SENGVRQCHHYWP-DEGSNVYHVYEVNLVSEHiWCQDFLVRSFYLKnlQTNETRTVTQFHFLSWYDQGVPS--STRSLLD 914
Cdd:cd14614   90 NEKRRVKCDHYWPfTEEPVAYGDITVEMLSEE-EQPDWAIREFRVS--YADEVQDVMHFNYTAWPDHGVPTanAAESILQ 166

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13928818  915 F----RRKVNKcyrgRSCPIIVHCSDGAGRSGTYVLIDMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQFEF 986
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 ...
 789-993 7.14e-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: 7.14e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  789 YINASPImDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEgSNVYHVYEVNLVSEH 868
Cdd:cd14632    1 YINANYI-DGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDD-SDTYGDIKITLLKTE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  869 IWCQdFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYVLID 948
Cdd:cd14632   79 TLAE-YSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYIVLD 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 13928818  949 MVLNkMAKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAE 993
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 ...
 789-986 7.76e-46

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: 163.35  E-value: 7.76e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  789 YINASpIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGvRQCHHYWPDEGSNVYHVYEVNLVSEH 868
Cdd:cd14556    1 YINAA-LLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKD-QSCPQYWPDEGSGTYGPIQVEFVSTT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  869 IWCqDFLVRSFYLKNLQ--TNETRTVTQFHFLSW-YDQGVPSSTRSLLDFRRKVNK----CYRGrscPIIVHCSDGAGRS 941
Cdd:cd14556   79 IDE-DVISRIFRLQNTTrpQEGYRMVQQFQFLGWpRDRDTPPSKRALLKLLSEVEKwqeqSGEG---PIVVHCLNGVGRS 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 13928818  942 GTYVLIDMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQFEF 986
Cdd:cd14556  155 GVFCAISSVCERI-KVENVVDVFQAVKTLRNHRPNMVETEEQYKF 198
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 789-984 1.54e-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: 162.69  E-value: 1.54e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  789 YINASPIMDH-DPRNpaYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWP--DEGSNVYHVYEVNLV 865
Cdd:cd14557    1 YINASYIDGFkEPRK--YIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPsmEEGSRAFGDVVVKIN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  866 SEHIwCQDFLVRSFYLKNLQTNET-RTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTY 944
Cdd:cd14557   79 EEKI-CPDYIIRKLNINNKKEKGSgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGTY 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 13928818  945 VLIDMVLNKM-AKGakEIDIAATLEHLRDQRPGMVQTKEQF 984
Cdd:cd14557  158 IGIDAMLEGLeAEG--RVDVYGYVVKLRRQRCLMVQVEAQY 196
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 789-986 9.95e-44

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: 157.63  E-value: 9.95e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  789 YINASPIMDHDPRN-PAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVR-QCHHYWPDE--GSNVYHVYEVNL 864
Cdd:cd17658    1 YINASLVETPASESlPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTaKCADYFPAEenESREFGRISVTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  865 VSEHIWCQDFLVRSFYLKNLQTNET-RTVTQFHFLSWYDQGVPSSTRSLldfrRKVNKCYRG---RSCPIIVHCSDGAGR 940
Cdd:cd17658   81 KKLKHSQHSITLRVLEVQYIESEEPpLSVLHIQYPEWPDHGVPKDTRSV----RELLKRLYGippSAGPIVVHCSAGIGR 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 13928818  941 SGTYVLIDMVLNKMAKGAKE-IDIAATLEHLRDQRPGMVQTKEQFEF 986
Cdd:cd17658  157 TGAYCTIHNTIRRILEGDMSaVDLSKTVRKFRSQRIGMVQTQDQYIF 203
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 762-986 1.27e-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: 159.26  E-value: 1.27e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  762 KNRSLAVLTYDHSRILLKSENSHSN-SDYINASPIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSEN 840
Cdd:cd14613   28 KNRYKTILPNPHSRVCLTSPDQDDPlSSYINANYIRGYGGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEM 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  841 GvRQCHHYWPDEgSNVYHVYEVNlVSEHIWCQDFLVRSFYLKNlqTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVN 920
Cdd:cd14613  108 N-EKCTEYWPEE-QVTYEGIEIT-VKQVIHADDYRLRLITLKS--GGEERGLKHYWYTSWPDQKTPDNAPPLLQLVQEVE 182

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13928818  921 ---KCYRGRSCPIIVHCSDGAGRSGTYVLIDMVLNKMAKGAKeIDIAATLEHLRDQRPGMVQTKEQFEF 986
Cdd:cd14613  183 earQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGV-VDILRTTCQLRLDRGGMIQTCEQYQF 250
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 762-986 6.05e-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: 6.05e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  762 KNRSLAVLTYDHSRILLKSENSH-SNSDYINASPIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSEN 840
Cdd:cd14611    2 KNRYKTILPNPHSRVCLKPKNSNdSLSTYINANYIRGYGGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  841 GvRQCHHYWPdEGSNVYHVYE--VNLVSEhiwCQDFLVRSFYLKnlQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRK 918
Cdd:cd14611   82 N-EKCVLYWP-EKRGIYGKVEvlVNSVKE---CDNYTIRNLTLK--QGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLD 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13928818  919 VN---KCYRGRScPIIVHCSDGAGRSGTYVLIDMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQFEF 986
Cdd:cd14611  155 VEedrLASPGRG-PVVVHCSAGIGRTGCFIATTIGCQQL-KEEGVVDVLSIVCQLRVDRGGMVQTSEQYEF 223
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 763-986 5.40e-42

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: 153.52  E-value: 5.40e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  763 NRSLAVLTYDHSRILLKSENSHSNSDYINASPIMDHDPRNpAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGV 842
Cdd:cd14616    1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPN-EFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  843 RQCHHYWPDEGS--NVYHVYEVNLVSEHIWcQDFLVRSfyLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVN 920
Cdd:cd14616   80 IRCHQYWPEDNKpvTVFGDIVITKLMEDVQ-IDWTIRD--LKIERHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVR 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13928818  921 KCYRGRSCPIIVHCSDGAGRSGTYVLIDMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQFEF 986
Cdd:cd14616  157 ASRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHI-NDHDFVDIYGLVAELRSERMCMVQNLAQYIF 221
Receptor_IA-2 pfam11548
Protein-tyrosine phosphatase receptor IA-2; IA-2 is a protein-tyrosine phosphatase receptor ...
 498-586 6.57e-42

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: 147.77  E-value: 6.57e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818    498 EQQGYILTGNNPLSPEKGKQLMDEVAHLLRVPSSFFADVKVLGPAVIFKVSANIQNMTTADVTKAAVDNKDELEKATGLT 577
Cdd:pfam11548    1 EEYGYIVTDNDPLSWEEGLRLMEKVAELLHLPMSSFADIRVLGPAVTFKVRANNKNLTAADVAKAAVDIKDKLEKETGLK 80


                   ....*....
gi 13928818    578 ILQSGIRPK 586
Cdd:pfam11548   81 ILQAGVGDK 89
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 758-986 1.93e-41

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: 154.00  E-value: 1.93e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  758 ENAPKNRSLAVLTYDHSRILLkSENSHSNSDYINASPI-MDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTP 836
Cdd:cd14599   37 ENAERNRIREVVPYEENRVEL-VPTKENNTGYINASHIkVTVGGEEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTA 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  837 LSENGVRQCHHYWPDEGSN----VYHVYEVNL-VSEHIWCqdFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRS 911
Cdd:cd14599  116 EEEGGRSKSHRYWPKLGSKhssaTYGKFKVTTkFRTDSGC--YATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEEVQG 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  912 LLDF-------RRKVNKCYRG-RSC--PIIVHCSDGAGRSGTYVLIDMVLNKMAKGAKeIDIAATLEHLRDQRPGMVQTK 981
Cdd:cd14599  194 FLSYleeiqsvRRHTNSMLDStKNCnpPIVVHCSAGVGRTGVVILTELMIGCLEHNEK-VEVPVMLRHLREQRMFMIQTI 272


                 ....*
gi 13928818  982 EQFEF 986
Cdd:cd14599  273 AQYKF 277
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 755-986 2.60e-41

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 154.39  E-value: 2.60e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818   755 QREENAPKNRSLAVLTYDHSRILLKSeNSHSNSDYINASPImDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVML 834
Cdd:PHA02747   47 EKPENQPKNRYWDIPCWDHNRVILDS-GGGSTSDYIHANWI-DGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVML 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818   835 TPLSE-NGVRQCHHYW-PDEGSNV----YHVYEVNLVsehiwcqdflVRSFYLKNL------QTNETRTVTQFHFLSWYD 902
Cdd:PHA02747  125 TPTKGtNGEEKCYQYWcLNEDGNIdmedFRIETLKTS----------VRAKYILTLieitdkILKDSRKISHFQCSEWFE 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818   903 QGVPSSTRSLLDF-------RRKVNKCYRGRS---CPIIVHCSDGAGRSGTYVLIDMVLNKMAKgAKEIDIAATLEHLRD 972
Cdd:PHA02747  195 DETPSDHPDFIKFikiidinRKKSGKLFNPKDallCPIVVHCSDGVGKTGIFCAVDICLNQLVK-RKAICLAKTAEKIRE 273

                         250
                  ....*....|....
gi 13928818   973 QRPGMVQTKEQFEF 986
Cdd:PHA02747  274 QRHAGIMNFDDYLF 287
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
891-993 1.39e-37

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 136.33  E-value: 1.39e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818     891 TVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSC--PIIVHCSDGAGRSGTYVLIDMVLNKMAKGAKEIDIAATLE 968
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESsgPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 13928818     969 HLRDQRPGMVQTKEQFEFALTAVAE 993
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 891-993 1.39e-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: 1.39e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818     891 TVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSC--PIIVHCSDGAGRSGTYVLIDMVLNKMAKGAKEIDIAATLE 968
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESsgPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 13928818     969 HLRDQRPGMVQTKEQFEFALTAVAE 993
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
732-999 6.47e-37

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 140.61  E-value: 6.47e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  732 NRLEKEWEALcAYQAEPDSSLvaQREENAPKNRSLAVLTYDHSRIllksensHSNSDYINASPIMDHDPRNpaYIATQGP 811
Cdd:COG5599   18 SRLSTLTNEL-APSHNDPQYL--QNINGSPLNRFRDIQPYKETAL-------RANLGYLNANYIQVIGNHR--YIATQYP 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  812 LPATVADFWQMVWESGCAVIVMLTPLSENGVRQ--CHHYWPDEGSnvYHVYEV-NLVSEHIWCQD-FLVRSFYLKNLQTN 887
Cdd:COG5599   86 LEEQLEDFFQMLFDNNTPVLVVLASDDEISKPKvkMPVYFRQDGE--YGKYEVsSELTESIQLRDgIEARTYVLTIKGTG 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  888 -ETRTVTQFHFLSWYDQGVPSST--RSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYVLIdMVLNKMAKGAKEIDIA 964
Cdd:COG5599  164 qKKIEIPVLHVKNWPDHGAISAEalKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIAC-LALSKSINALVQITLS 242

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 13928818  965 A--TLEHLRDQR-PGMVQTKEQFEFaLTAVAEEVNAIL 999
Cdd:COG5599  243 VeeIVIDMRTSRnGGMVQTSEQLDV-LVKLAEQQIRPL 279
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 789-986 7.68e-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: 135.15  E-value: 7.68e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  789 YINASpIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLseNGVRQCHHYWPDEGSNVYHVYEVNLVSEH 868
Cdd:cd14634    1 YINAA-LMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEM--DAAQLCMQYWPEKTSCCYGPIQVEFVSAD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  869 IwCQDFLVRSFYLKNLQTNET--RTVTQFHFLSW--YdQGVPSSTRSLLDFRRKVNKC---YRGRSCPIIVHCSDGAGRS 941
Cdd:cd14634   78 I-DEDIISRIFRICNMARPQDgyRIVQHLQYIGWpaY-RDTPPSKRSILKVVRRLEKWqeqYDGREGRTVVHCLNGGGRS 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 13928818  942 GTYVLIDMVlNKMAKGAKEIDIAATLEHLRDQRPGMVQTKEQFEF 986
Cdd:cd14634  156 GTFCAICSV-CEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKF 199
PHA02738 PHA02738
hypothetical protein; Provisional
 759-996 1.51e-34

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 135.05  E-value: 1.51e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818   759 NAPKNRSLAVLTYDHSRILLKSENSHSnsDYINASPImDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLS 838
Cdd:PHA02738   49 NRKLNRYLDAVCFDHSRVILPAERNRG--DYINANYV-DGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKK 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818   839 ENGVRQCHHYWPD--EGSNVYHVYEVNLVSehIWCQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFR 916
Cdd:PHA02738  126 ENGREKCFPYWSDveQGSIRFGKFKITTTQ--VETHPHYVKSTLLLTDGTSATQTVTHFNFTAWPDHDVPKNTSEFLNFV 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818   917 RKVNKCY-------------RGRSCPIIVHCSDGAGRSGTYVLIDMVLNKMaKGAKEIDIAATLEHLRDQRPGMVQTKEQ 983
Cdd:PHA02738  204 LEVRQCQkelaqeslqighnRLQPPPIVVHCNAGLGRTPCYCVVDISISRF-DACATVSIPSIVSSIRNQRYYSLFIPFQ 282

                         250
                  ....*....|...
gi 13928818   984 FEFALTAVAEEVN 996
Cdd:PHA02738  283 YFFCYRAVKRYVN 295
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 789-993 7.87e-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: 7.87e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  789 YINASpIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSE-NGVRQCHHYWPDEGSNVYHVYEVNLVSE 867
Cdd:cd14637    1 YINAA-LTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQsNSAWPCLQYWPEPGLQQYGPMEVEFVSG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  868 HIwCQDFLVRSFYLKNLQ--TNETRTVTQFHFLSWYD-QGVPSSTRSLLDFRRKVNK----CYRGRScpiIVHCSDGAGR 940
Cdd:cd14637   80 SA-DEDIVTRLFRVQNITrlQEGHLMVRHFQFLRWSAyRDTPDSKKAFLHLLASVEKwqreSGEGRT---VVHCLNGGGR 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 13928818  941 SGTYVLIDMVLnKMAKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAE 993
Cdd:cd14637  156 SGTYCASAMIL-EMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 789-993 1.21e-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: 128.60  E-value: 1.21e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  789 YINASpIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLseNGVRQCHHYWPDEGSNVYHVYEVNLVSEH 868
Cdd:cd14636    1 YINAA-LMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEV--DLAQGCPQYWPEEGMLRYGPIQVECMSCS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  869 IWCqDFLVRSFYLKNLQTNET--RTVTQFHFLSWYD-QGVPSSTRSLLDFRRKVNK----CYRGRSCPIIvHCSDGAGRS 941
Cdd:cd14636   78 MDC-DVISRIFRICNLTRPQEgyLMVQQFQYLGWAShREVPGSKRSFLKLILQVEKwqeeCDEGEGRTII-HCLNGGGRS 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 13928818  942 GTYVLIDMVLnKMAKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAE 993
Cdd:cd14636  156 GMFCAISIVC-EMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 789-986 1.03e-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: 126.63  E-value: 1.03e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  789 YINASPI------MDHDprnpaYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSN----VYH 858
Cdd:cd14598    1 YINASHIkvtvggKEWD-----YIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLGSRhntvTYG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  859 VYEVNL-VSEHIWCqdFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDF-------RRKVNKCY--RGRSC 928
Cdd:cd14598   76 RFKITTrFRTDSGC--YATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYleeiqsvRRHTNSTIdpKSPNP 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 13928818  929 PIIVHCSDGAGRSGTYVLIDMVLNKMAKGAKeIDIAATLEHLRDQRPGMVQTKEQFEF 986
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 ...
 789-986 2.19e-31

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: 122.04  E-value: 2.19e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  789 YINASPIMDHDpRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGvrQCHHYWPDEGSNVYHV-YEVNLVSE 867
Cdd:cd14550    1 YINASYLQGYR-RSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWPTKEKPLECEtFKVTLSGE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  868 HIWC----QDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTrsLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGT 943
Cdd:cd14550   78 DHSClsneIRLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPIHT--VFELINTVQEWAQQRDGPIVVHDRYGGVQAAT 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 13928818  944 YVLIdMVLNKMAKGAKEIDI--AATLEHLRdqRPGMVQTKEQFEF 986
Cdd:cd14550  156 FCAL-TTLHQQLEHESSVDVyqVAKLYHLM--RPGVFTSKEDYQF 197
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 748-986 4.39e-31

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 124.34  E-value: 4.39e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818   748 PDSSLVAQREENAPKNRSLAVLTYDHSRILLKSENShsNSDYINASPIMDHDPRNpAYIATQGPLPATVADFWQMVWESG 827
Cdd:PHA02742   41 AFSCNESLELKNMKKCRYPDAPCFDRNRVILKIEDG--GDDFINASYVDGHNAKG-RFICTQAPLEETALDFWQAIFQDQ 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818   828 CAVIVMLTPLSENGVRQCHHYW-PDEGSNVYHvYEVNLVSEHIwcQDFlvRSFYLKNLQTNETRT-----VTQFHFLSWY 901
Cdd:PHA02742  118 VRVIVMITKIMEDGKEACYPYWmPHERGKATH-GEFKIKTKKI--KSF--RNYAVTNLCLTDTNTgasldIKHFAYEDWP 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818   902 DQGVPSSTRSLLDFRRKVNKC-----------YRGRSCPIIVHCSDGAGRSGTYVLIDMVLNKMAKGAKeIDIAATLEHL 970
Cdd:PHA02742  193 HGGLPRDPNKFLDFVLAVREAdlkadvdikgeNIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAI-IPLLSIVRDL 271

                         250
                  ....*....|....*.
gi 13928818   971 RDQRPGMVQTKEQFEF 986
Cdd:PHA02742  272 RKQRHNCLSLPQQYIF 287
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 748-991 8.69e-31

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 123.99  E-value: 8.69e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818   748 PDSSLVAQ--REENAPKNRSLAVLTYDHSRILLKSENSH-------------------SNSDYINASPIMDHDPRNpAYI 806
Cdd:PHA02746   38 PIRGTTNHflKKENLKKNRFHDIPCWDHSRVVINAHESLkmfdvgdsdgkkievtsedNAENYIHANFVDGFKEAN-KFI 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818   807 ATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGvRQCHHYW-PDEGSNVYHVYEVNLVSEHIWCQDFLVRSFYLKNLQ 885
Cdd:PHA02746  117 CAQGPKEDTSEDFFKLISEHESQVIVSLTDIDDDD-EKCFELWtKEEDSELAFGRFVAKILDIIEELSFTKTRLMITDKI 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818   886 TNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKcYRGR-----------SCPIIVHCSDGAGRSGTYVLIDMVLNKM 954
Cdd:PHA02746  196 SDTSREIHHFWFPDWPDNGIPTGMAEFLELINKVNE-EQAElikqadndpqtLGPIVVHCSAGIGRAGTFCAIDNALEQL 274

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 13928818   955 AKgAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAV 991
Cdd:PHA02746  275 EK-EKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 789-993 1.31e-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: 1.31e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  789 YINASpIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLseNGVRQCHHYWPDEGSNVYHVYEVNLVSEH 868
Cdd:cd14635    1 YINAA-LMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDV--DPAQLCPQYWPENGVHRHGPIQVEFVSAD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  869 IWcQDFLVRSFYLKNLQTNET--RTVTQFHFLSW-YDQGVPSSTRSLLDFRRKVNKC---YRGRSCPIIVHCSDGAGRSG 942
Cdd:cd14635   78 LE-EDIISRIFRIYNAARPQDgyRMVQQFQFLGWpMYRDTPVSKRSFLKLIRQVDKWqeeYNGGEGRTVVHCLNGGGRSG 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 13928818  943 TYVLIDMVLnKMAKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAE 993
Cdd:cd14635  157 TFCAISIVC-EMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 789-991 2.54e-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: 2.54e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  789 YINASPIMDHDPRNpAYIATQGPLPATVADFWQMVWESGCAVIVMLtPLSENGVRQCHHYWP--DEGSNVyHVYEVNLVS 866
Cdd:cd17669    1 YINASYIMGYYQSN-EFIITQHPLLHTIKDFWRMIWDHNAQLIVML-PDGQNMAEDEFVYWPnkDEPINC-ETFKVTLIA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  867 EHIWC----QDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVP-SSTRSLLDFrrkVNKCYRGRSCPIIVHCSDGAGRS 941
Cdd:cd17669   78 EEHKClsneEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPiSKTFELISI---IKEEAANRDGPMIVHDEHGGVTA 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 13928818  942 GTYVLIDMVLNKMAKgAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAV 991
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 ...
 789-991 5.27e-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: 86.66  E-value: 5.27e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  789 YINASPIMDHdPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLtPLSENGVRQCHHYWP--DEGSNVyHVYEVNLVS 866
Cdd:cd17670    1 YINASYIMGY-YRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVML-PDNQGLAEDEFVYWPsrEESMNC-EAFTVTLIS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  867 EHIWC----QDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVP-SSTRSLLDFrrkVNKCYRGRSCPIIVHCSDGAGRS 941
Cdd:cd17670   78 KDRLClsneEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPiSSTFELINV---IKEEALTRDGPTIVHDEFGAVSA 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 13928818  942 GTYVLIdMVLNKMAKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAV 991
Cdd:cd17670  155 GTLCAL-TTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAM 203
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 732-1003 6.63e-13

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 70.77  E-value: 6.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818   732 NRLEKEWEALCAYQAEPDSSLVAQREENAPK-NRSLAVLTYDHSRILLKSENSHSNSDYINAspiMDHDPRnpaYIATQG 810
Cdd:PHA02740   25 SCIIKEYRAIVPEHEDEANKACAQAENKAKDeNLALHITRLLHRRIKLFNDEKVLDARFVDG---YDFEQK---FICIIN 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818   811 PLPATVADFWQMVWESGCAVIVMLTPLSEngvRQCHH-YWPDEGSNVYHVYEVNLVSEHIWCQDFLVRSFYLKNLQTNET 889
Cdd:PHA02740   99 LCEDACDKFLQALSDNKVQIIVLISRHAD---KKCFNqFWSLKEGCVITSDKFQIETLEIIIKPHFNLTLLSLTDKFGQA 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818   890 RTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYR--------GRSCPIIVHCSDGAGRSGTYVLIDMVLNKMAKGAKeI 961
Cdd:PHA02740  176 QKISHFQYTAWPADGFSHDPDAFIDFFCNIDDLCAdlekhkadGKIAPIIIDCIDGISSSAVFCVFDICATEFDKTGM-L 254

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 13928818   962 DIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEVNAILKALP 1003
Cdd:PHA02740  255 SIANALKKVRQKKYGCMNCLDDYVFCYHLIAAYLKEKFDILK 296
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 802-985 1.22e-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: 1.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  802 NPAYIATQGPLPATVADFWQMVWESGCAVIVMLTplSENGVR--QCHHYWpdEGSNVYHvyEVNLVSEHIWCQD----FL 875
Cdd:cd14559   28 KNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLA--SNKDIQrkGLPPYF--RQSGTYG--SVTVKSKKTGKDElvdgLK 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  876 VRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSS--TRSLLDF-----RRKVNKCYRGRSCPI--------IVHCSDGAGR 940
Cdd:cd14559  102 ADMYNLKITDGNKTITIPVVHVTNWPDHTAISSegLKELADLvnksaEEKRNFYKSKGSSAIndknkllpVIHCRAGVGR 181

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 13928818  941 SGTyVLIDMVlnkMAKGAKEIDIAATLEHLRDQRPG-MVQTKEQFE 985
Cdd:cd14559  182 TGQ-LAAAME---LNKSPNNLSVEDIVSDMRTSRNGkMVQKDEQLD 223
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 894-986 3.63e-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: 3.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  894 QFHFLSWYDQGVPS--STRSLLDFRRKVNKCYRgrscPIIVHCSDGAGRSGTYVLIDMVLNKMAKGAKEIDIaatlehLR 971
Cdd:cd14504   51 RYHHIPIEDYTPPTleQIDEFLDIVEEANAKNE----AVLVHCLAGKGRTGTMLACYLVKTGKISAVDAINE------IR 120

                         90
                 ....*....|....*
gi 13928818  972 DQRPGMVQTKEQFEF 986
Cdd:cd14504  121 RIRPGSIETSEQEKF 135
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
894-986 4.28e-06

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 47.27  E-value: 4.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  894 QFHFLSWYDQGVPSSTRsLLDFRRKVNKCYRgRSCPIIVHCSDGAGRSGTyVLIdMVLnkMAKGakeIDIAATLEHLRDQ 973
Cdd:COG2453   49 EYLHLPIPDFGAPDDEQ-LQEAVDFIDEALR-EGKKVLVHCRGGIGRTGT-VAA-AYL--VLLG---LSAEEALARVRAA 119

                         90
                 ....*....|...
gi 13928818  974 RPGMVQTKEQFEF 986
Cdd:COG2453  120 RPGAVETPAQRAF 132
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 913-986 3.76e-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: 3.76e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13928818  913 LDFRRKVNKCYrgrsCPIIVHCSDGAGRSGTYVLIDMVLnKMAKGAKEIdiaatLEHLRDQRPG-MVQTKEQFEF 986
Cdd:cd14494   46 LEVLDQAEKPG----EPVLVHCKAGVGRTGTLVACYLVL-LGGMSAEEA-----VRIVRLIRPGgIPQTIEQLDF 110
RESP18 pfam14948
RESP18 domain; This domain is found in the glucocorticoid-responsive protein regulated ...
 80-126 1.40e-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: 39.04  E-value: 1.40e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 13928818     80 HLRIILQKLSRTGFTWQDDYTQRVIAQELSNLPK-----AYLWHEEASSPAR 126
Cdd:pfam14948   23 HLQVVLHQIVPQGLFWKDDLTQDVMTQKMEHISRlhpqdPCLKDGKAVFPTR 74
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 867-996 2.74e-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: 2.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  867 EHIWCQDFLVRS--FY--LKNLQTNETRtvtqFHFLSWYDQGVPSSTRsLLDFRRKVNKCYR--GRscpIIVHCSDGAGR 940
Cdd:cd14506   51 EHASCGPGLEPEsgFSylPEAFMRAGIY----FYNFGWKDYGVPSLTT-ILDIVKVMAFALQegGK---VAVHCHAGLGR 122

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13928818  941 SGtyVLIDMVL---NKMAKgakeidiAATLEHLRDQRPGMVQTKEQ----FEFALTAVAEEVN 996
Cdd:cd14506  123 TG--VLIACYLvyaLRMSA-------DQAIRLVRSKRPNSIQTRGQvlcvREFAQFLLPLRNV 176
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 894-986 4.21e-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: 4.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13928818  894 QFHFLSWYDQGVPSSTRS---LLDFRRKVNKCYRGrscpIIVHCSDGAGRSGTY---VLidMVLNKMAKGAKEIDIaatl 967
Cdd:cd14505   74 TWHHLPIPDGGVPSDIAQwqeLLEELLSALENGKK----VLIHCKGGLGRTGLIaacLL--LELGDTLDPEQAIAA---- 143

                         90
                 ....*....|....*....
gi 13928818  968 ehLRDQRPGMVQTKEQFEF 986
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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