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Conserved domains on  [gi|2165490393|ref|XP_045368039|]
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receptor-type tyrosine-protein phosphatase-like N isoform X1 [Camelus bactrianus]

Protein Classification

Receptor_IA-2 and R-PTP-N domain-containing protein( domain architecture ID 13865691)

protein containing domains RESP18, Receptor_IA-2, and R-PTP-N

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 735-1015 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: 660.19  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  735 HMILAYMEDHLRNRDRLAKEWQALCAYQAEPNTCATAQGEGNIKKNRHPDFLPYDHARIKLKAESSPSRSDYINASPIIE 814
Cdd:cd14609      1 HMILAYMEDHLRNRDRLAKEWQALCAYQAEPNTCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPIIE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  815 HDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHVYEVNLVSEHIWCEDFLVR 894
Cdd:cd14609     81 HDPRMPAYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHIYEVNLVSEHIWCEDFLVR 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  895 SFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKG 974
Cdd:cd14609    161 SFYLKNVQTQETRTLTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKG 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 2165490393  975 VKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAEEVNAI 1015
Cdd:cd14609    241 VKEIDIAATLEHVRDQRPGMVRTKDQFEFALTAVAEEVNAI 281
Receptor_IA-2 pfam11548
Protein-tyrosine phosphatase receptor IA-2; IA-2 is a protein-tyrosine phosphatase receptor ...
 470-558 1.38e-40

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: 144.30  E-value: 1.38e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  470 EEYGYIVTDQKPLSLAAGVKLLEILAEHVHMSSGSFINISVVGPALTFRIRHNEQNLSLADVTQQAGLVKSELEAQTGLQ 549
Cdd:pfam11548    1 EEYGYIVTDNDPLSWEEGLRLMEKVAELLHLPMSSFADIRVLGPAVTFKVRANNKNLTAADVAKAAVDIKDKLEKETGLK 80


                   ....*....
gi 2165490393  550 ILQTGVGQQ 558
Cdd:pfam11548   81 ILQAGVGDK 89
RESP18 pfam14948
RESP18 domain; This domain is found in the glucocorticoid-responsive protein regulated ...
 60-160 2.37e-39

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: 141.12  E-value: 2.37e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393   60 GQCQVGVGQARPLLQVTSPVLQRLQGVLRQLMSQGLSWHDDLTQYVISQEMERIPRLRPPEPHPRDRSGLVPRRPGPTG- 138
Cdd:pfam14948    1 GQGQVGVGQLWPLQGFTAPVFQHLQVVLHQIVPQGLFWKDDLTQDVMTQKMEHISRLHPQDPCLKDGKAVFPTRTTGVRg 80

                           90       100
                   ....*....|....*....|....
gi 2165490393  139 --ELLLQGVPTGSaPAPQHRLPRP 160
Cdd:pfam14948   81 kqEEKLRLLFPKS-PAVKVNRDQC 103
 
Name Accession Description Interval E-value
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 735-1015 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: 660.19  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  735 HMILAYMEDHLRNRDRLAKEWQALCAYQAEPNTCATAQGEGNIKKNRHPDFLPYDHARIKLKAESSPSRSDYINASPIIE 814
Cdd:cd14609      1 HMILAYMEDHLRNRDRLAKEWQALCAYQAEPNTCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPIIE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  815 HDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHVYEVNLVSEHIWCEDFLVR 894
Cdd:cd14609     81 HDPRMPAYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHIYEVNLVSEHIWCEDFLVR 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  895 SFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKG 974
Cdd:cd14609    161 SFYLKNVQTQETRTLTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKG 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 2165490393  975 VKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAEEVNAI 1015
Cdd:cd14609    241 VKEIDIAATLEHVRDQRPGMVRTKDQFEFALTAVAEEVNAI 281
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
751-1010 2.56e-103

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 323.84  E-value: 2.56e-103
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393   751 LAKEWQALCAYQAEPNTCATAQGEGNIKKNRHPDFLPYDHARIKLKAESSPSrSDYINASPI-IEHDPRmpAYIATQGPL 829
Cdd:smart00194    2 LEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEG-SDYINASYIdGPNGPK--AYIATQGPL 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393   830 SHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGSSL--YHVYEVNLVSEHIwCEDFLVRSFYLKNVQTQETR 907
Cdd:smart00194   79 PSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPltYGDITVTLKSVEK-VDDYTIRTLEVTNTGCSETR 157

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393   908 TLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGvKEIDIAATLEHV 987
Cdd:smart00194  158 TVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAG-KEVDIFEIVKEL 236

                           250       260
                    ....*....|....*....|...
gi 2165490393   988 RDQRPGLVRSKDQFEFALTAVAE 1010
Cdd:smart00194  237 RSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
776-1010 1.17e-101

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 318.42  E-value: 1.17e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  776 NIKKNRHPDFLPYDHARIKLKaeSSPSRSDYINASPIIEHdPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLV 855
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLT--GDPGPSDYINASYIDGY-KKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  856 EDGVKQCDRYWPD--EGSSLYHVYEVNLVSEHIWCEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFR 933
Cdd:pfam00102   78 EKGREKCAQYWPEeeGESLEYGDFTVTLKKEKEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLL 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2165490393  934 RKVNKCY-RGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGvKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAE 1010
Cdd:pfam00102  158 RKVRKSSlDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAE-GEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
Receptor_IA-2 pfam11548
Protein-tyrosine phosphatase receptor IA-2; IA-2 is a protein-tyrosine phosphatase receptor ...
 470-558 1.38e-40

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: 144.30  E-value: 1.38e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  470 EEYGYIVTDQKPLSLAAGVKLLEILAEHVHMSSGSFINISVVGPALTFRIRHNEQNLSLADVTQQAGLVKSELEAQTGLQ 549
Cdd:pfam11548    1 EEYGYIVTDNDPLSWEEGLRLMEKVAELLHLPMSSFADIRVLGPAVTFKVRANNKNLTAADVAKAAVDIKDKLEKETGLK 80


                   ....*....
gi 2165490393  550 ILQTGVGQQ 558
Cdd:pfam11548   81 ILQAGVGDK 89
RESP18 pfam14948
RESP18 domain; This domain is found in the glucocorticoid-responsive protein regulated ...
 60-160 2.37e-39

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: 141.12  E-value: 2.37e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393   60 GQCQVGVGQARPLLQVTSPVLQRLQGVLRQLMSQGLSWHDDLTQYVISQEMERIPRLRPPEPHPRDRSGLVPRRPGPTG- 138
Cdd:pfam14948    1 GQGQVGVGQLWPLQGFTAPVFQHLQVVLHQIVPQGLFWKDDLTQDVMTQKMEHISRLHPQDPCLKDGKAVFPTRTTGVRg 80

                           90       100
                   ....*....|....*....|....
gi 2165490393  139 --ELLLQGVPTGSaPAPQHRLPRP 160
Cdd:pfam14948   81 kqEEKLRLLFPKS-PAVKVNRDQC 103
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 776-1003 2.85e-39

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 148.61  E-value: 2.85e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  776 NIKKNRHPDFLPYDHARIKLKAESSpSRSDYINASPI--IEHDPRmpaYIATQGPLSHTIADFWQMVWESGCTVIVMLTP 853
Cdd:PHA02747    51 NQPKNRYWDIPCWDHNRVILDSGGG-STSDYIHANWIdgFEDDKK---FIATQGPFAETCADFWKAVWQEHCSIIVMLTP 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  854 L-VEDGVKQCDRYW-PDEGSSL----YHVYEVNLVsehiwcedflVRSFYLK------NVQTQETRTLTQFHFLSWPAEG 921
Cdd:PHA02747   127 TkGTNGEEKCYQYWcLNEDGNIdmedFRIETLKTS----------VRAKYILtlieitDKILKDSRKISHFQCSEWFEDE 196

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  922 TPASTRPLLDF-------RRKVNKCYRGRS---CPIIVHCSDGAGRTGTYILIDMVLNRMAKgVKEIDIAATLEHVRDQR 991
Cdd:PHA02747   197 TPSDHPDFIKFikiidinRKKSGKLFNPKDallCPIVVHCSDGVGKTGIFCAVDICLNQLVK-RKAICLAKTAEKIREQR 275

                          250
                   ....*....|..
gi 2165490393  992 PGLVRSKDQFEF 1003
Cdd:PHA02747   276 HAGIMNFDDYLF 287
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
734-1016 2.90e-33

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 130.21  E-value: 2.90e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  734 GHMILAYMEDHLRNRdrLAKEWQALcAYQAEPNtcataQGEGNI---KKNRHPDFLPYDHARIklkaesspsRSD--YIN 808
Cdd:COG5599      5 NPIAIKSEEEKINSR--LSTLTNEL-APSHNDP-----QYLQNIngsPLNRFRDIQPYKETAL---------RANlgYLN 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  809 ASPIIEHDPRMpaYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGV--KQCDRYWPDEGSslYHVYEV-NLVSEH 885
Cdd:COG5599     68 ANYIQVIGNHR--YIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEISKpkVKMPVYFRQDGE--YGKYEVsSELTES 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  886 IWCED-FLVRSFYLKNVQT-QETRTLTQFHFLSWPAEGTPAST--RPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTY 961
Cdd:COG5599    144 IQLRDgIEARTYVLTIKGTgQKKIEIPVLHVKNWPDHGAISAEalKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTL 223

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2165490393  962 ILIdMVLNRMAKGVKEIDIAA--TLEHVRDQR-PGLVRSKDQFEFaLTAVAEEVNAIL 1016
Cdd:COG5599    224 IAC-LALSKSINALVQITLSVeeIVIDMRTSRnGGMVQTSEQLDV-LVKLAEQQIRPL 279
 
Name Accession Description Interval E-value
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 735-1015 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: 660.19  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  735 HMILAYMEDHLRNRDRLAKEWQALCAYQAEPNTCATAQGEGNIKKNRHPDFLPYDHARIKLKAESSPSRSDYINASPIIE 814
Cdd:cd14609      1 HMILAYMEDHLRNRDRLAKEWQALCAYQAEPNTCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPIIE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  815 HDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHVYEVNLVSEHIWCEDFLVR 894
Cdd:cd14609     81 HDPRMPAYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHIYEVNLVSEHIWCEDFLVR 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  895 SFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKG 974
Cdd:cd14609    161 SFYLKNVQTQETRTLTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKG 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 2165490393  975 VKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAEEVNAI 1015
Cdd:cd14609    241 VKEIDIAATLEHVRDQRPGMVRTKDQFEFALTAVAEEVNAI 281
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 733-1015 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: 568.15  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  733 TGHMILAYMEDHLRNRDRLAKEWQALCAYQAEPNTCATAQGEGNIKKNRHPDFLPYDHARIKLKAESSPSRSDYINASPI 812
Cdd:cd14610      1 TGHMILSYMEDHLKNKNRLEKEWEALCAYQAEPNATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  813 IEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHVYEVNLVSEHIWCEDFL 892
Cdd:cd14610     81 MDHDPRNPAYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSNLYHIYEVNLVSEHIWCEDFL 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  893 VRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMA 972
Cdd:cd14610    161 VRSFYLKNLQTNETRTVTQFHFLSWNDQGVPASTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMA 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 2165490393  973 KGVKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAEEVNAI 1015
Cdd:cd14610    241 KGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEVNAI 283
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 806-1013 2.11e-157

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: 462.68  E-value: 2.11e-157
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  806 YINASPIIEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHVYEVNLVSEH 885
Cdd:cd14546      1 YINASTIYDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEVYHIYEVHLVSEH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  886 IWCEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILID 965
Cdd:cd14546     81 IWCDDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSCPIVVHCSDGAGRTGTYILID 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2165490393  966 MVLNRMAKGVKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAEEVN 1013
Cdd:cd14546    161 MVLNRMAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAEEVN 208
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
751-1010 2.56e-103

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 323.84  E-value: 2.56e-103
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393   751 LAKEWQALCAYQAEPNTCATAQGEGNIKKNRHPDFLPYDHARIKLKAESSPSrSDYINASPI-IEHDPRmpAYIATQGPL 829
Cdd:smart00194    2 LEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEG-SDYINASYIdGPNGPK--AYIATQGPL 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393   830 SHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGSSL--YHVYEVNLVSEHIwCEDFLVRSFYLKNVQTQETR 907
Cdd:smart00194   79 PSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPltYGDITVTLKSVEK-VDDYTIRTLEVTNTGCSETR 157

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393   908 TLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGvKEIDIAATLEHV 987
Cdd:smart00194  158 TVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAG-KEVDIFEIVKEL 236

                           250       260
                    ....*....|....*....|...
gi 2165490393   988 RDQRPGLVRSKDQFEFALTAVAE 1010
Cdd:smart00194  237 RSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
776-1010 1.17e-101

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 318.42  E-value: 1.17e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  776 NIKKNRHPDFLPYDHARIKLKaeSSPSRSDYINASPIIEHdPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLV 855
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLT--GDPGPSDYINASYIDGY-KKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  856 EDGVKQCDRYWPD--EGSSLYHVYEVNLVSEHIWCEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFR 933
Cdd:pfam00102   78 EKGREKCAQYWPEeeGESLEYGDFTVTLKKEKEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLL 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2165490393  934 RKVNKCY-RGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGvKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAE 1010
Cdd:pfam00102  158 RKVRKSSlDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAE-GEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 806-1003 1.03e-81

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: 263.38  E-value: 1.03e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  806 YINASPIIEHDPRmPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGSS--LYHVYEVNLVS 883
Cdd:cd00047      1 YINASYIDGYRGP-KEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKplEYGDITVTLVS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  884 EHIwCEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYIL 963
Cdd:cd00047     80 EEE-LSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTGTFIA 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 2165490393  964 IDMVLNRMAKGvKEIDIAATLEHVRDQRPGLVRSKDQFEF 1003
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 ...
 774-1014 3.85e-67

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: 224.97  E-value: 3.85e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  774 EGNIKKNRHPDFLPYDHARIKLKAESSPSRSDYINASPIIEHDpRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTP 853
Cdd:cd14553      1 EVNKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYR-KQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  854 LVEDGVKQCDRYWPDEGSSLYHVYEVNLVsEHIWCEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFR 933
Cdd:cd14553     80 LEERSRVKCDQYWPTRGTETYGLIQVTLL-DTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFL 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  934 RKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMaKGVKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAEEVN 1013
Cdd:cd14553    159 RRVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERI-KHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLEAVT 237


                   .
gi 2165490393 1014 A 1014
Cdd:cd14553    238 C 238
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 748-1003 5.99e-66

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: 223.01  E-value: 5.99e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  748 RDRLAKEWQALCAyQAEPNTCATAQGEGNIKKNRHPDFLPYDHARIKLKAESSPSRSDYINASpIIEHDPRMPAYIATQG 827
Cdd:cd14543      2 KRGIYEEYEDIRR-EPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINAN-FMDGYKQKNAYIATQG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  828 PLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHVYEVNLVSEHIWC-EDFLVRSFYLKNVQTQET 906
Cdd:cd14543     80 PLPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSSLRYGDLTVTNLSVENkEHYKKTTLEIHNTETDES 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  907 RTLTQFHFLSWPAEGTPASTRPLLDFRRKVnKCYRGRSC--------------PIIVHCSDGAGRTGTYILIDMVLNRMA 972
Cdd:cd14543    160 RQVTHFQFTSWPDFGVPSSAAALLDFLGEV-RQQQALAVkamgdrwkghppgpPIVVHCSAGIGRTGTFCTLDICLSQLE 238

                          250       260       270
                   ....*....|....*....|....*....|.
gi 2165490393  973 KgVKEIDIAATLEHVRDQRPGLVRSKDQFEF 1003
Cdd:cd14543    239 D-VGTLNVMQTVRRMRTQRAFSIQTPDQYYF 268
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 776-1009 2.00e-65

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: 220.80  E-value: 2.00e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  776 NIKKNRHPDFLPYDHARIKLK-AESSPSRSDYINASPII------EHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVI 848
Cdd:cd14544      1 NKGKNRYKNILPFDHTRVILKdRDPNVPGSDYINANYIRnenegpTTDENAKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  849 VMLTPLVEDGVKQCDRYWPDEGSS-LYHVYEVNLVSEHIwCEDFLVRSFYLKNV-QTQETRTLTQFHFLSWPAEGTPAST 926
Cdd:cd14544     81 VMTTKEVERGKNKCVRYWPDEGMQkQYGPYRVQNVSEHD-TTDYTLRELQVSKLdQGDPIREIWHYQYLSWPDHGVPSDP 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  927 RPLLDFRRKVNKCYRGR--SCPIIVHCSDGAGRTGTYILIDMVLNRMAK-GVK-EIDIAATLEHVRDQRPGLVRSKDQFE 1002
Cdd:cd14544    160 GGVLNFLEDVNQRQESLphAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRkGLDcDIDIQKTIQMVRSQRSGMVQTEAQYK 239


                   ....*..
gi 2165490393 1003 FALTAVA 1009
Cdd:cd14544    240 FIYVAVA 246
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 776-1007 1.07e-62

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: 212.77  E-value: 1.07e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  776 NIKKNRHPDFLPYDHARIKLKAESSPSRSDYINASPIIEHDPRmPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLV 855
Cdd:cd14554      6 NKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQR-GAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKLR 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  856 EDGVKQCDRYWPDEGSSLYHVYEVNLVSEHIWcEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRK 935
Cdd:cd14554     85 EMGREKCHQYWPAERSARYQYFVVDPMAEYNM-PQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQ 163

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2165490393  936 VNKCYR--GRSCPIIVHCSDGAGRTGTYILIDMVLNRM-AKGVkeIDIAATLEHVRDQRPGLVRSKDQFEFALTA 1007
Cdd:cd14554    164 VHKTKEqfGQEGPITVHCSAGVGRTGVFITLSIVLERMrYEGV--VDVFQTVKLLRTQRPAMVQTEDQYQFCYRA 236
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 806-1003 1.38e-62

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: 211.06  E-value: 1.38e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  806 YINASPIIE-HDPRmpAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHVYEVNLVSE 884
Cdd:cd14549      1 YINANYVDGyNKAR--AYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTETYGNIQVTLLST 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  885 HIWCEdFLVRSFYLKNVQ------TQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRT 958
Cdd:cd14549     79 EVLAT-YTVRTFSLKNLKlkkvkgRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVGRT 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2165490393  959 GTYILIDMVLNRMAKgVKEIDIAATLEHVRDQRPGLVRSKDQFEF 1003
Cdd:cd14549    158 GTYIVIDSMLQQIQD-KGTVNVFGFLKHIRTQRNYLVQTEEQYIF 201
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 781-1003 6.48e-62

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: 209.90  E-value: 6.48e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  781 RHPDFLPYDHARIKLKAESSPSRSDYINASPII-EHDPRmpAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGV 859
Cdd:cd14548      1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPgYNSPR--EFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGR 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  860 KQCDRYWPDEGSSLYHVY-EVNLVSEHIwCEDFLVRSFYLKNVqtQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVnK 938
Cdd:cd14548     79 VKCDHYWPFDQDPVYYGDiTVTMLSESV-LPDWTIREFKLERG--DEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLV-R 154

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2165490393  939 CYRGRSC-PIIVHCSDGAGRTGTYILIDMVLNRMAKGvKEIDIAATLEHVRDQRPGLVRSKDQFEF 1003
Cdd:cd14548    155 DYIKQEKgPTIVHCSAGVGRTGTFIALDRLLQQIESE-DYVDIFGIVYDLRKHRPLMVQTEAQYIF 219
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 806-1003 1.76e-61

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


Pssm-ID: 350509 [Multi-domain]  Cd Length: 212  Bit Score: 208.26  E-value: 1.76e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  806 YINASPI-IEHDPRMpAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEG-SSLYHVYEVNLVS 883
Cdd:cd18533      1 YINASYItLPGTSSK-RYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEyEGEYGDLTVELVS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  884 EH-IWCEDFLVRSFYLKnVQTQETRTLTQFHFLSWPAEGTPASTRPLL---DFRRKVNKCYRGRScPIIVHCSDGAGRTG 959
Cdd:cd18533     80 EEeNDDGGFIVREFELS-KEDGKVKKVYHIQYKSWPDFGVPDSPEDLLtliKLKRELNDSASLDP-PIIVHCSAGVGRTG 157

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2165490393  960 TYILIDMVLNRMAKGV-------KEID-IAATLEHVRDQRPGLVRSKDQFEF 1003
Cdd:cd18533    158 TFIALDSLLDELKRGLsdsqdleDSEDpVYEIVNQLRKQRMSMVQTLRQYIF 209
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 780-1003 1.37e-59

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


Pssm-ID: 350463 [Multi-domain]  Cd Length: 229  Bit Score: 203.51  E-value: 1.37e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  780 NRHPDFLPYDHARIKLKAESSPSrSDYINASpiiehdpRMPAY------IATQGPLSHTIADFWQMVWESGCTVIVMLTP 853
Cdd:cd14615      1 NRYNNVLPYDISRVKLSVQSHST-DDYINAN-------YMPGYnskkefIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTK 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  854 LVEDGVKQCDRYWPDEGSSLYHVYEVNLVSEhIWCEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFR 933
Cdd:cd14615     73 CVEQGRTKCEEYWPSKQKKDYGDITVTMTSE-IVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFR 151

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2165490393  934 RKVNKCYRG--RSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGvKEIDIAATLEHVRDQRPGLVRSKDQFEF 1003
Cdd:cd14615    152 HLVREYMKQnpPNSPILVHCSAGVGRTGTFIAIDRLIYQIENE-NVVDVYGIVYDLRMHRPLMVQTEDQYVF 222
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 805-1018 4.84e-58

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: 198.71  E-value: 4.84e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  805 DYINASPIIEHDPRMPA---YIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEG-SSLYHVYEVN 880
Cdd:cd14541      1 DYINANYVNMEIPGSGIvnrYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGeTMQFGNLQIT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  881 LVSEHIwCEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGT 960
Cdd:cd14541     81 CVSEEV-TPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCSAGIGRTGV 159

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  961 YILID--MVLNRMAKGVKEIDIAATLehvRDQRPGLVRSKDQFEFaltaVAEevnAILKA 1018
Cdd:cd14541    160 LITMEtaMCLIEANEPVYPLDIVRTM---RDQRAMLIQTPSQYRF----VCE---AILRV 209
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 779-1003 6.88e-57

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: 196.07  E-value: 6.88e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  779 KNRHPDFLPYDHARIKLKAESSpsRSDYINASpIIEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDG 858
Cdd:cd14545      1 LNRYRDRDPYDHDRSRVKLKQG--DNDYINAS-LVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  859 VKQCDRYWP---DEGSSLYHV-YEVNLVSEHIWcEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRR 934
Cdd:cd14545     78 QIKCAQYWPqgeGNAMIFEDTgLKVTLLSEEDK-SYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQ 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2165490393  935 KVNK--CYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKG-VKEIDIAATLEHVRDQRPGLVRSKDQFEF 1003
Cdd:cd14545    157 KVREsgSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGnPSSVDVKKVLLEMRKYRMGLIQTPDQLRF 228
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 740-1010 1.60e-56

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: 197.46  E-value: 1.60e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  740 YMEDHLRNRdRLAKEWQALCAYQAepntcATAQGEGNIKKNRHPDFLPYDHARIKLKAESSPSRSDYINASPIIE-HDPR 818
Cdd:cd14604     27 FASDFMRLR-RLSTKYRTEKIYPT-----ATGEKEENVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGvYGPK 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  819 mpAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPdegssLYHVYEVNLVSEHIWCE------DFL 892
Cdd:cd14604    101 --AYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWP-----LYGEEPMTFGPFRISCEaeqartDYF 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  893 VRSFYLKNvqTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMA 972
Cdd:cd14604    174 IRTLLLEF--QNETRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLK 251

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 2165490393  973 KGV--KEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAE 1010
Cdd:cd14604    252 AGKipEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQ 291
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 776-1012 1.78e-56

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: 196.80  E-value: 1.78e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  776 NIKKNRHPDFLPYDHARIKLK--AESSPSRSDYINASPIIEHDpRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTP 853
Cdd:cd17667     27 NKHKNRYINILAYDHSRVKLRplPGKDSKHSDYINANYVDGYN-KAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITN 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  854 LVEDGVKQCDRYWPDEGSSLYHVYEVNLVSEHIW-CedFLVRSFYLKNVQT-----------QETRTLTQFHFLSWPAEG 921
Cdd:cd17667    106 LVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHaC--YTVRRFSIRNTKVkkgqkgnpkgrQNERTVIQYHYTQWPDMG 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  922 TPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMaKGVKEIDIAATLEHVRDQRPGLVRSKDQF 1001
Cdd:cd17667    184 VPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQI-KDKSTVNVLGFLKHIRTQRNYLVQTEEQY 262

                          250
                   ....*....|.
gi 2165490393 1002 EFALTAVAEEV 1012
Cdd:cd17667    263 IFIHDALLEAI 273
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 774-1012 1.95e-56

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: 196.41  E-value: 1.95e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  774 EGNIKKNRHPDFLPYDHARIKLKAESSPSRSDYINASpIIEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTP 853
Cdd:cd14626     39 EVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINAN-YIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTR 117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  854 LVEDGVKQCDRYWPDEGSSLYHVYEVNLVsEHIWCEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFR 933
Cdd:cd14626    118 LEEKSRVKCDQYWPIRGTETYGMIQVTLL-DTVELATYSVRTFALYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFL 196

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2165490393  934 RKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMaKGVKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAEEV 1012
Cdd:cd14626    197 RRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERM-KHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLEAA 274
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 806-1010 2.09e-56

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: 193.74  E-value: 2.09e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  806 YINASPIiehdpRMPA------YIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPD---EGSSLYHV 876
Cdd:cd14538      1 YINASHI-----RIPVggdtyhYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDslnKPLICGGR 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  877 YEVNLVSEHIWcEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYrgRSCPIIVHCSDGAG 956
Cdd:cd14538     76 LEVSLEKYQSL-QDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIH--NSGPIVVHCSAGIG 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2165490393  957 RTGTYILIDMVLNRMAKGvKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAE 1010
Cdd:cd14538    153 RTGVLITIDVALGLIERD-LPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLE 205
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 776-1003 3.63e-55

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: 191.20  E-value: 3.63e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  776 NIKKNRHPDFLPYDHARIKLKAESspsrsDYINASPIiehdpRMPA------YIATQGPLSHTIADFWQMVWESGCTVIV 849
Cdd:cd14597      3 NRKKNRYKNILPYDTTRVPLGDEG-----GYINASFI-----KMPVgdeefvYIACQGPLPTTVADFWQMVWEQKSTVIA 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  850 MLTPLVEDGVKQCDRYWPDEGSSLYHVYE---VNLVS-EHIwcEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPAS 925
Cdd:cd14597     73 MMTQEVEGGKIKCQRYWPEILGKTTMVDNrlqLTLVRmQQL--KNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQ 150

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2165490393  926 TRPLLDFRRKVNKCYrgRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGVkEIDIAATLEHVRDQRPGLVRSKDQFEF 1003
Cdd:cd14597    151 PEQLLTFISYMRHIH--KSGPIITHCSAGIGRSGTLICIDVVLGLISKDL-DFDISDIVRTMRLQRHGMVQTEDQYIF 225
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 754-1010 7.75e-55

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: 192.64  E-value: 7.75e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  754 EWQALCAYQAEPNTCATAQGEGNIKKNRHPDFLPYDHARIKLKAESSPSRSDYINASpIIEHDPRMPAYIATQGPLSHTI 833
Cdd:cd14628     30 EFKRLASSKAHTSRFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINAS-FIDGYRQQKAYIATQGPLAETT 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  834 ADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHVYEVNLVSEHIWCEdFLVRSFYLKNVQTQETRTLTQFH 913
Cdd:cd14628    109 EDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQ-YILREFKVTDARDGQSRTVRQFQ 187

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  914 FLSWPAEGTPASTRPLLDFRRKVNKCYR--GRSCPIIVHCSDGAGRTGTYILIDMVLNRMA-KGVkeIDIAATLEHVRDQ 990
Cdd:cd14628    188 FTDWPEQGVPKSGEGFIDFIGQVHKTKEqfGQDGPISVHCSAGVGRTGVFITLSIVLERMRyEGV--VDIFQTVKMLRTQ 265

                          250       260
                   ....*....|....*....|
gi 2165490393  991 RPGLVRSKDQFEFALTAVAE 1010
Cdd:cd14628    266 RPAMVQTEDQYQFCYRAALE 285
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 780-1003 2.68e-54

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: 188.94  E-value: 2.68e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  780 NRHPDFLPYDHARIKLKAESSPSRSDYINASpiiehdpRMPAY------IATQGPLSHTIADFWQMVWESGCTVIVMLTP 853
Cdd:cd14619      1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINAN-------YMPGYwssqefIATQGPLPQTVGDFWRMIWEQQSSTIVMLTN 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  854 LVEDGVKQCDRYWP-DEGSSLYHVYEVNLVSEHIwCEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDF 932
Cdd:cd14619     74 CMEAGRVKCEHYWPlDYTPCTYGHLRVTVVSEEV-MENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAF 152

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2165490393  933 RRKVNKCYRGR--SCPIIVHCSDGAGRTGTYILIDMVLNRMAKGvKEIDIAATLEHVRDQRPGLVRSKDQFEF 1003
Cdd:cd14619    153 RRLLRQWLDQTmsGGPTVVHCSAGVGRTGTLIALDVLLQQLQSE-GLLGPFSFVQKMRENRPLMVQTESQYVF 224
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 738-1012 2.88e-54

catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type tyrosine-protein phosphatase S (PTPRS), also known as receptor-type tyrosine-protein phosphatase sigma (R-PTP-sigma), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRS is a receptor for glycosaminoglycans, including heparan sulfate proteoglycan and neural chondroitin sulfate proteoglycans (CSPGs), which present a barrier to axon regeneration. It also plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2. PTPRS contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350473 [Multi-domain]  Cd Length: 282  Bit Score: 190.69  E-value: 2.88e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  738 LAYMEDHLRNRD--RLAKEWQALCAYQAepNTCATAQGEGNIKKNRHPDFLPYDHARIKLKAESSPSRSDYINASpIIEH 815
Cdd:cd14625      9 LAEHTERLKANDnlKLSQEYESIDPGQQ--FTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINAN-YIDG 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  816 DPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHVYEVNLVsEHIWCEDFLVRS 895
Cdd:cd14625     86 YRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRGTETYGMIQVTLL-DTIELATFCVRT 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  896 FYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMaKGV 975
Cdd:cd14625    165 FSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVIDAMLERI-KHE 243

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 2165490393  976 KEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAEEV 1012
Cdd:cd14625    244 KTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAV 280
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 754-1010 3.19e-54

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: 190.04  E-value: 3.19e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  754 EWQALCAYQAEPNTCATAQG--EGNIKKNRHPDFLPYDHARIKLKAESSPSRSDYINASPIIEHDpRMPAYIATQGPLSH 831
Cdd:cd14603      6 EIRACSAAFKADYVCSTVAGgrKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVD-GSRAYIATQGPLSH 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  832 TIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWP-DEGSSLYHVYEVNLVSEHIWCEDFLVRSfyLKNVQTQETRTLT 910
Cdd:cd14603     85 TVLDFWRMIWQYGVKVILMACREIEMGKKKCERYWAqEQEPLQTGPFTITLVKEKRLNEEVILRT--LKVTFQKESRSVS 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  911 QFHFLSWPAEGTPASTRPLLDFRRKVNKcYRGRS-CPIIVHCSDGAGRTGTYILIDMVLNRMAKGVKEIDIA---ATLEh 986
Cdd:cd14603    163 HFQYMAWPDHGIPDSPDCMLAMIELARR-LQGSGpEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPDFSifdVVLE- 240

                          250       260
                   ....*....|....*....|....
gi 2165490393  987 VRDQRPGLVRSKDQFEFALTAVAE 1010
Cdd:cd14603    241 MRKQRPAAVQTEEQYEFLYHTVAQ 264
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 780-1003 4.40e-54

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: 187.99  E-value: 4.40e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  780 NRHPDFLPYDHARIKLKAESSPSRSDYINASPIIEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGV 859
Cdd:cd14547      1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYDGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAKE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  860 KqCDRYWPDEGSSLYHVYEVnLVSEHIWCEDFLVRSFYLKNVqtQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKC 939
Cdd:cd14547     81 K-CAQYWPEEENETYGDFEV-TVQSVKETDGYTVRKLTLKYG--GEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEEA 156

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2165490393  940 -YRGRSC-PIIVHCSDGAGRTGTYILIDMVLNRMAKGVKeIDIAATLEHVRDQRPGLVRSKDQFEF 1003
Cdd:cd14547    157 rQTEPHRgPIVVHCSAGIGRTGCFIATSIGCQQLREEGV-VDVLGIVCQLRLDRGGMVQTAEQYEF 221
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 776-1008 7.78e-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: 188.30  E-value: 7.78e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  776 NIKKNRHPDFLPYDHARIKL-KAESSPSRSDYINASPI-----IEHDPRMP--AYIATQGPLSHTIADFWQMVWESGCTV 847
Cdd:cd14605      2 NKNKNRYKNILPFDHTRVVLhDGDPNEPVSDYINANIImpefeTKCNNSKPkkSYIATQGCLQNTVNDFWRMVFQENSRV 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  848 IVMLTPLVEDGVKQCDRYWPDEGS-SLYHVYEVNLVSEHIwCEDFLVRSFYLKNV-QTQETRTLTQFHFLSWPAEGTPAS 925
Cdd:cd14605     82 IVMTTKEVERGKSKCVKYWPDEYAlKEYGVMRVRNVKESA-AHDYILRELKLSKVgQGNTERTVWQYHFRTWPDHGVPSD 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  926 TRPLLDFRRKVNKCYRG--RSCPIIVHCSDGAGRTGTYILIDMVLNRM-AKGVK-EIDIAATLEHVRDQRPGLVRSKDQF 1001
Cdd:cd14605    161 PGGVLDFLEEVHHKQESimDAGPVVVHCSAGIGRTGTFIVIDILIDIIrEKGVDcDIDVPKTIQMVRSQRSGMVQTEAQY 240


                   ....*..
gi 2165490393 1002 EFALTAV 1008
Cdd:cd14605    241 RFIYMAV 247
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 754-1010 9.92e-54

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: 189.56  E-value: 9.92e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  754 EWQALCAYQAEPNTCATAQGEGNIKKNRHPDFLPYDHARIKLKAESSPSRSDYINASpIIEHDPRMPAYIATQGPLSHTI 833
Cdd:cd14627     31 EFKRLANSKAHTSRFISANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINAS-FIDGYRQQKAYIATQGPLAETT 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  834 ADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHVYEVNLVSEHIWCEdFLVRSFYLKNVQTQETRTLTQFH 913
Cdd:cd14627    110 EDFWRMLWENNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQ-YILREFKVTDARDGQSRTVRQFQ 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  914 FLSWPAEGTPASTRPLLDFRRKVNKCYR--GRSCPIIVHCSDGAGRTGTYILIDMVLNRMA-KGVkeIDIAATLEHVRDQ 990
Cdd:cd14627    189 FTDWPEQGVPKSGEGFIDFIGQVHKTKEqfGQDGPISVHCSAGVGRTGVFITLSIVLERMRyEGV--VDIFQTVKMLRTQ 266

                          250       260
                   ....*....|....*....|
gi 2165490393  991 RPGLVRSKDQFEFALTAVAE 1010
Cdd:cd14627    267 RPAMVQTEDEYQFCYQAALE 286
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 776-1010 3.51e-53

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: 186.00  E-value: 3.51e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  776 NIKKNRHPDFLPYDHARIKLKAESSPSRSDYINASPII-EHDPRMpaYIATQGPLSHTIADFWQMVWESGCTVIVMLTPL 854
Cdd:cd14630      3 NRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDgYHRPRH--YIATQGPMQETVKDFWRMIWQENSASVVMVTNL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  855 VEDGVKQCDRYWPDEgSSLYHVYEVNLVSEHIWCEdFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRR 934
Cdd:cd14630     81 VEVGRVKCVRYWPDD-TEVYGDIKVTLIETEPLAE-YVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGFVR 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2165490393  935 KVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNrMAKGVKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAE 1010
Cdd:cd14630    159 QVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLD-MAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILE 233
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 779-1010 5.93e-53

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: 185.04  E-value: 5.93e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  779 KNRHPDFLPYDHARIKLKAESSPSRSDYINASPIIE-HDPRmpAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVED 857
Cdd:cd14602      1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGvYGPR--AYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEM 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  858 GVKQCDRYWPDEGSSLYHVYEVNLVsehiwCE------DFLVRSfyLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLD 931
Cdd:cd14602     79 GKKKCERYWAEPGEMQLEFGPFSVT-----CEaekrksDYIIRT--LKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILE 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  932 FRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGV--KEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVA 1009
Cdd:cd14602    152 LIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIipENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAVI 231


                   .
gi 2165490393 1010 E 1010
Cdd:cd14602    232 E 232
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 776-1010 8.83e-53

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


Pssm-ID: 350454 [Multi-domain]  Cd Length: 266  Bit Score: 185.85  E-value: 8.83e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  776 NIKKNRHPDFLPYDHARIKLK-AESSPSRSDYINASPIIEH--DPRMPA--YIATQGPLSHTIADFWQMVWESGCTVIVM 850
Cdd:cd14606     18 NKSKNRYKNILPFDHSRVILQgRDSNIPGSDYINANYVKNQllGPDENAktYIASQGCLEATVNDFWQMAWQENSRVIVM 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  851 LTPLVEDGVKQCDRYWPDEGSS-LYHVYEVNLVSEHIwCEDFLVRSFYLKNVQTQET-RTLTQFHFLSWPAEGTPASTRP 928
Cdd:cd14606     98 TTREVEKGRNKCVPYWPEVGMQrAYGPYSVTNCGEHD-TTEYKLRTLQVSPLDNGELiREIWHYQYLSWPDHGVPSEPGG 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  929 LLDFRRKVNKCYRG--RSCPIIVHCSDGAGRTGTYILIDMVLNRM-AKGVK-EIDIAATLEHVRDQRPGLVRSKDQFEFA 1004
Cdd:cd14606    177 VLSFLDQINQRQESlpHAGPIIVHCSAGIGRTGTIIVIDMLMENIsTKGLDcDIDIQKTIQMVRAQRSGMVQTEAQYKFI 256


                   ....*.
gi 2165490393 1005 LTAVAE 1010
Cdd:cd14606    257 YVAIAQ 262
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 806-1003 3.02e-52

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: 181.85  E-value: 3.02e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  806 YINASpIIEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGSSL--YHVYEVNLVS 883
Cdd:cd14542      1 YINAN-FIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQlqFGPFKISLEK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  884 EHIWCEDFLVRSfyLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYIL 963
Cdd:cd14542     80 EKRVGPDFLIRT--LKVTFQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGCGRTGTICA 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2165490393  964 IDMVLNRMAKGV--KEIDIAATLEHVRDQRPGLVRSKDQFEF 1003
Cdd:cd14542    158 IDYVWNLLKTGKipEEFSLFDLVREMRKQRPAMVQTKEQYEL 199
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 761-1016 1.19e-51

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: 182.92  E-value: 1.19e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  761 YQAEPNTCATAQGEGNIKKNRHPDFLPYDHARIKLKAESSpsrsDYINASpIIEHDPRMPAYIATQGPLSHTIADFWQMV 840
Cdd:cd14608     10 HEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDN----DYINAS-LIKMEEAQRSYILTQGPLPNTCGHFWEMV 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  841 WESGCTVIVMLTPLVEDGVKQCDRYWP--DEGSSLYH--VYEVNLVSEHIWCEdFLVRSFYLKNVQTQETRTLTQFHFLS 916
Cdd:cd14608     85 WEQKSRGVVMLNRVMEKGSLKCAQYWPqkEEKEMIFEdtNLKLTLISEDIKSY-YTVRQLELENLTTQETREILHFHYTT 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  917 WPAEGTPASTRPLLDFRRKVNK--CYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMA--KGVKEIDIAATLEHVRDQRP 992
Cdd:cd14608    164 WPDFGVPESPASFLNFLFKVREsgSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDkrKDPSSVDIKKVLLEMRKFRM 243

                          250       260
                   ....*....|....*....|....
gi 2165490393  993 GLVRSKDQFEFALTAVAEEVNAIL 1016
Cdd:cd14608    244 GLIQTADQLRFSYLAVIEGAKFIM 267
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 806-1003 1.34e-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: 180.17  E-value: 1.34e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  806 YINASPIIEHDpRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHVYEVNLVSEH 885
Cdd:cd17668      1 YINANYVDGYN-KPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  886 IWCEdFLVRSFYLKNVQT--------QETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGR 957
Cdd:cd17668     80 VLAY-YTVRNFTLRNTKIkkgsqkgrPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSAGVGR 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2165490393  958 TGTYILIDMVLNRMaKGVKEIDIAATLEHVRDQRPGLVRSKDQFEF 1003
Cdd:cd17668    159 TGTYIVLDSMLQQI-QHEGTVNIFGFLKHIRSQRNYLVQTEEQYVF 203
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 754-1010 2.40e-51

PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type tyrosine-protein phosphatase F (PTPRF), also known as leukocyte common antigen related (LAR), is the prototypical member of the LAR family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRF/LAR plays a role for LAR in cadherin complexes where it associates with and dephosphorylates beta-catenin, a pathway which may be critical for cadherin complex stability and cell-cell association. It also regulates focal adhesions through cyclin-dependent kinase-1 and is involved in axon guidance in the developing nervous system. It also functions in regulating insulin signaling. PTPRF contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350477 [Multi-domain]  Cd Length: 291  Bit Score: 182.62  E-value: 2.40e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  754 EWQALCAYQAEPNTCATAQGEGNIKKNRHPDFLPYDHARIKLKAESSPSRSDYINASpIIEHDPRMPAYIATQGPLSHTI 833
Cdd:cd14629     31 EFKLLANSKAHTSRFISANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINAS-FIDGYRQQKAYIATQGPLAETT 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  834 ADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHVYEVNLVSEHIWCEdFLVRSFYLKNVQTQETRTLTQFH 913
Cdd:cd14629    110 EDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQ-YILREFKVTDARDGQSRTIRQFQ 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  914 FLSWPAEGTPASTRPLLDFRRKVNKCYR--GRSCPIIVHCSDGAGRTGTYILIDMVLNRMA-KGVkeIDIAATLEHVRDQ 990
Cdd:cd14629    189 FTDWPEQGVPKTGEGFIDFIGQVHKTKEqfGQDGPITVHCSAGVGRTGVFITLSIVLERMRyEGV--VDMFQTVKTLRTQ 266

                          250       260
                   ....*....|....*....|
gi 2165490393  991 RPGLVRSKDQFEFALTAVAE 1010
Cdd:cd14629    267 RPAMVQTEDQYQLCYRAALE 286
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 806-1008 2.82e-51

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: 179.00  E-value: 2.82e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  806 YINASpIIEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHVYEVNLVSEH 885
Cdd:cd14552      1 YINAS-FIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGSVSSGDITVELKDQT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  886 IwCEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGR-SCPIIVHCSDGAGRTGTYILI 964
Cdd:cd14552     80 D-YEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSgNHPITVHCSAGAGRTGTFCAL 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2165490393  965 DMVLNRM-AKGVkeIDIAATLEHVRDQRPGLVRSKDQFEFALTAV 1008
Cdd:cd14552    159 STVLERVkAEGV--LDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 753-1010 6.36e-51

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: 181.76  E-value: 6.36e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  753 KEWQAL--CAYQAepnTCATAQGEGNIKKNRHPDFLPYDHARIKLKAESSPSRSDYINASPIIEHDPRmPAYIATQGPLS 830
Cdd:cd14621     30 EEFNALpaCPIQA---TCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINASFINGYQEK-NKFIAAQGPKE 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  831 HTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHVYEVNlVSEHIWCEDFLVRSFYLKNV----QTQET 906
Cdd:cd14621    106 ETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGCWTYGNIRVS-VEDVTVLVDYTVRKFCIQQVgdvtNKKPQ 184

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  907 RTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNrMAKGVKEIDIAATLEH 986
Cdd:cd14621    185 RLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVIDAMLD-MMHAERKVDVYGFVSR 263

                          250       260
                   ....*....|....*....|....
gi 2165490393  987 VRDQRPGLVRSKDQFEFALTAVAE 1010
Cdd:cd14621    264 IRAQRCQMVQTDMQYVFIYQALLE 287
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 782-1010 1.67e-50

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: 177.83  E-value: 1.67e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  782 HPDFLPYDHARIKLKAESSPSRSDYINASPIIEHDPRmPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQ 861
Cdd:cd14620      1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEK-NKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  862 CDRYWPDEGSSLYHVYEVNlVSEHIWCEDFLVRSFYLKNVQT---QETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNK 938
Cdd:cd14620     80 CYQYWPDQGCWTYGNIRVA-VEDCVVLVDYTIRKFCIQPQLPdgcKAPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVKS 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2165490393  939 CYRGRSCPIIVHCSDGAGRTGTYILIDMVLNrMAKGVKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAE 1010
Cdd:cd14620    159 VNPVHAGPIVVHCSAGVGRTGTFIVIDAMID-MMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 753-1010 2.80e-50

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: 179.08  E-value: 2.80e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  753 KEWQALCAYQAEPntCATAQGEGNIKKNRHPDFLPYDHARIKLKAESSPSRSDYINASpIIEHDPRMPAYIATQGPLSHT 832
Cdd:cd14633     19 EEYESFFEGQSAP--WDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGN-YIDGYHRPNHYIATQGPMQET 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  833 IADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEgSSLYHVYEVNLVSEHIWCEdFLVRSFYLKNVQTQETRTLTQF 912
Cdd:cd14633     96 IYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDD-TEIYKDIKVTLIETELLAE-YVIRTFAVEKRGVHEIREIRQF 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  913 HFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNrMAKGVKEIDIAATLEHVRDQRP 992
Cdd:cd14633    174 HFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLD-MAEREGVVDIYNCVRELRSRRV 252

                          250
                   ....*....|....*...
gi 2165490393  993 GLVRSKDQFEFALTAVAE 1010
Cdd:cd14633    253 NMVQTEEQYVFIHDAILE 270
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 806-1010 3.51e-50

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: 176.09  E-value: 3.51e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  806 YINASPIiehdpRMPA------YIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHV--Y 877
Cdd:cd14596      1 YINASYI-----TMPVgeeelfYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELenY 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  878 EVNLVSEHIwCEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYrgRSCPIIVHCSDGAGR 957
Cdd:cd14596     76 QLRLENYQA-LQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVH--NTGPIVVHCSAGIGR 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2165490393  958 TGTYILIDMVLNRMAKGVkEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAE 1010
Cdd:cd14596    153 AGVLICVDVLLSLIEKDL-SFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLE 204
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 774-1012 5.52e-50

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: 178.39  E-value: 5.52e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  774 EGNIKKNRHPDFLPYDHARIKLKAESSPSRSDYINASpIIEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTP 853
Cdd:cd14624     45 EVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINAN-YIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTK 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  854 LVEDGVKQCDRYWPDEGSSLYHVYEVNLVsEHIWCEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFR 933
Cdd:cd14624    124 LEERSRVKCDQYWPSRGTETYGLIQVTLL-DTVELATYCVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFL 202

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2165490393  934 RKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMaKGVKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAEEV 1012
Cdd:cd14624    203 RRVKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERI-KHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAV 280
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 806-1003 1.47e-49

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: 174.12  E-value: 1.47e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  806 YINASPIIE-HDPRmpAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGSSlYHVYEVNLVSE 884
Cdd:cd14558      1 YINASFIDGyWGPK--SLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKT-YGDIEVELKDT 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  885 HIwCEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKV------NKCYRGRSCPIIVHCSDGAGRT 958
Cdd:cd14558     78 EK-SPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIkqklpyKNSKHGRSVPIVVHCSDGSSRT 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2165490393  959 GTYILIdmvLNRMAKGVKE--IDIAATLEHVRDQRPGLVRSKDQFEF 1003
Cdd:cd14558    157 GIFCAL---WNLLESAETEkvVDVFQVVKALRKQRPGMVSTLEQYQF 200
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 805-1010 7.13e-49

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


Pssm-ID: 350470 [Multi-domain]  Cd Length: 205  Bit Score: 172.50  E-value: 7.13e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  805 DYINASpIIEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHVYEVNLVSE 884
Cdd:cd14622      1 DYINAS-FIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGSVTHGEITIEIKND 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  885 HIwCEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGR-SCPIIVHCSDGAGRTGTYIL 963
Cdd:cd14622     80 TL-LETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQTgNHPIVVHCSAGAGRTGTFIA 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2165490393  964 IDMVLNRM-AKGVkeIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAE 1010
Cdd:cd14622    159 LSNILERVkAEGL--LDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQD 204
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 786-1010 1.04e-48

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


Pssm-ID: 350471 [Multi-domain]  Cd Length: 228  Bit Score: 172.92  E-value: 1.04e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  786 LPYDHARIKLKAESSPSRSDYINASpIIEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRY 865
Cdd:cd14623      6 IPYEFNRVIIPVKRGEENTDYVNAS-FIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEKCAQY 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  866 WPDEGSSLYHVYEVNLVSEHiWCEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGR-S 944
Cdd:cd14623     85 WPSDGSVSYGDITIELKKEE-ECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQQQSgN 163

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2165490393  945 CPIIVHCSDGAGRTGTYILIDMVLNRM-AKGVkeIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAE 1010
Cdd:cd14623    164 HPITVHCSAGAGRTGTFCALSTVLERVkAEGI--LDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 776-1008 6.15e-48

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: 171.69  E-value: 6.15e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  776 NIKKNRHPDFLPYDHARIKLKAesspSRSDYINASPI-IEHDPRmpAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPL 854
Cdd:cd14607     24 NRNRNRYRDVSPYDHSRVKLQN----TENDYINASLVvIEEAQR--SYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRI 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  855 VEDGVKQCDRYWPDEGSSLYHVYE----VNLVSEHIWCEdFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLL 930
Cdd:cd14607     98 VEKDSVKCAQYWPTDEEEVLSFKEtgfsVKLLSEDVKSY-YTVHLLQLENINSGETRTISHFHYTTWPDFGVPESPASFL 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  931 DFRRKV--NKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGVK-EIDIAATLEHVRDQRPGLVRSKDQFEFALTA 1007
Cdd:cd14607    177 NFLFKVreSGSLSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDPdSVDIKQVLLDMRKYRMGLIQTPDQLRFSYMA 256


                   .
gi 2165490393 1008 V 1008
Cdd:cd14607    257 V 257
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 761-1008 6.96e-48

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: 171.96  E-value: 6.96e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  761 YQAEPN---TCATaQGEgNIKKNRHPDFLPYDHARIKLKAESspsrsDYINASPIIEHDPRMP---AYIATQGPLSHTIA 834
Cdd:cd14600     24 YRKKPGlaiTCAK-LPQ-NMDKNRYKDVLPYDATRVVLQGNE-----DYINASYVNMEIPSANivnKYIATQGPLPHTCA 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  835 DFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGSSL-YHVYEVNLVSEHiwCE-DFLVRSFYLKNVQTQETRTLTQF 912
Cdd:cd14600     97 QFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDPPDVMeYGGFRVQCHSED--CTiAYVFREMLLTNTQTGEERTVTHL 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  913 HFLSWPAEGTPASTRPLLDFRRKVnKCYRGRSCPIIVHCSDGAGRTGTYILID--MVLNRMAKGVKEIDIAATLehvRDQ 990
Cdd:cd14600    175 QYVAWPDHGVPDDSSDFLEFVNYV-RSKRVENEPVLVHCSAGIGRTGVLVTMEtaMCLTERNQPVYPLDIVRKM---RDQ 250

                          250
                   ....*....|....*...
gi 2165490393  991 RPGLVRSKDQFEFALTAV 1008
Cdd:cd14600    251 RAMMVQTSSQYKFVCEAI 268
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 780-1003 2.64e-47

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: 168.97  E-value: 2.64e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  780 NRHPDFLPYDHARIKLKAESSPSRSDYINASpiiehdpRMPAY------IATQGPLSHTIADFWQMVWESGCTVIVMLTP 853
Cdd:cd14618      1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINAN-------FIPGYtspqefIATQGPLKKTIEDFWRLVWEQQVCNIIMLTV 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  854 LVEDGVKQCDRYWPDEGSSLYHVY-EVNLVSEHIwCEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDF 932
Cdd:cd14618     74 GMENGRVLCDHYWPSESTPVSYGHiTVHLLAQSS-EDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAF 152

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2165490393  933 RRKVN---KCYRGRScPIIVHCSDGAGRTGTYILIDMVLNRMaKGVKEIDIAATLEHVRDQRPGLVRSKDQFEF 1003
Cdd:cd14618    153 RELVRehvQATKGKG-PTLVHCSAGVGRSGTFIALDRLLRQL-KEEKVVDVFNTVYILRMHRYLMIQTLSQYIF 224
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 780-1003 4.88e-47

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: 168.17  E-value: 4.88e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  780 NRHPDFLPYDHARIKLKAESSPSRSDYINASPIIEHDPRMpAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGV 859
Cdd:cd14617      1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRR-EYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGR 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  860 KQCDRYWPDEGSSLYHV-YEVNLVSEHIWCEdFLVRSFYLKNV-QTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVN 937
Cdd:cd14617     80 VKCDHYWPADQDSLYYGdLIVQMLSESVLPE-WTIREFKICSEeQLDAPRLVRHFHYTVWPDHGVPETTQSLIQFVRTVR 158

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2165490393  938 KcYRGRS---CPIIVHCSDGAGRTGTYILIDMVLNRMAKgVKEIDIAATLEHVRDQRPGLVRSKDQFEF 1003
Cdd:cd14617    159 D-YINRTpgsGPTVVHCSAGVGRTGTFIALDRILQQLDS-KDSVDIYGAVHDLRLHRVHMVQTECQYVY 225
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 806-1010 8.17e-47

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: 166.63  E-value: 8.17e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  806 YINASPII-EHDPRMpaYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEgSSLYHVYEVNLVSE 884
Cdd:cd14555      1 YINANYIDgYHRPNH--YIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDD-TEVYGDIKVTLVET 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  885 HIWCEdFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILI 964
Cdd:cd14555     78 EPLAE-YVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTGCYIVI 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2165490393  965 DMVLNrMAKGVKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAE 1010
Cdd:cd14555    157 DIMLD-MAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 806-1003 7.65e-46

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; Receptor-type tyrosine-protein phosphatase A (PTPRA) and E (PTPRE) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA and PTPRE share several functions including regulation of Src family kinases and voltage-gated potassium (Kv) channels. They both contain a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the first catalytic PTP domain (repeat 1).


Pssm-ID: 350399 [Multi-domain]  Cd Length: 202  Bit Score: 163.54  E-value: 7.65e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  806 YINASPIIEHDPRmPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHVYEVNlVSEH 885
Cdd:cd14551      1 YINASYIDGYQEK-NKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCWTYGNLRVR-VEDT 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  886 IWCEDFLVRSFYLKNVQ----TQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTY 961
Cdd:cd14551     79 VVLVDYTTRKFCIQKVNrgigEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGRTGTF 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2165490393  962 ILIDMVLNrMAKGVKEIDIAATLEHVRDQRPGLVRSKDQFEF 1003
Cdd:cd14551    159 IVIDAMLD-MMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVF 199
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 805-1008 2.69e-45

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: 162.42  E-value: 2.69e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  805 DYINASPI---IEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPD-EGSSLYHVYEVN 880
Cdd:cd14601      1 DYINANYInmeIPSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEpSGSSSYGGFQVT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  881 LVSEHiWCEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGT 960
Cdd:cd14601     81 CHSEE-GNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVHCSAGIGRTGV 159

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2165490393  961 YILID--MVLNRMAKGVKEIDIAATLehvRDQRPGLVRSKDQFEFALTAV 1008
Cdd:cd14601    160 LITMEtaMCLIECNQPVYPLDIVRTM---RDQRAMMIQTPSQYRFVCEAI 206
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 798-1010 3.21e-45

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: 162.50  E-value: 3.21e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  798 ESSPSrSDYINASpIIEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEgSSLYHVY 877
Cdd:cd14631      8 EDDPS-SDYINAN-YIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDD-TEVYGDF 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  878 EVNLVS-EHIwcEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAG 956
Cdd:cd14631     85 KVTCVEmEPL--AEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCSAGAG 162

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2165490393  957 RTGTYILIDMVLNrMAKGVKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAE 1010
Cdd:cd14631    163 RTGCYIVIDIMLD-MAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 775-1003 3.99e-44

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: 160.39  E-value: 3.99e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  775 GNIKKNRHPDFLPYDHARIKLK-AESSPSRSDYINASPIIEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTP 853
Cdd:cd14612     14 GHASKDRYKTILPNPQSRVCLRrAGSQEEEGSYINANYIRGYDGKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITK 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  854 LVEdGVKQCDRYWPDEGSSlYHVYE--VNLVSEhiwCEDFLVRSFYLKnvQTQETRTLTQFHFLSWPAEGTPASTRPLLD 931
Cdd:cd14612     94 LKE-KKEKCVHYWPEKEGT-YGRFEirVQDMKE---CDGYTIRDLTIQ--LEEESRSVKHYWFSSWPDHQTPESAGPLLR 166

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2165490393  932 FRRKVNKCYR--GRSCPIIVHCSDGAGRTGTYILIDMVLNRMaKGVKEIDIAATLEHVRDQRPGLVRSKDQFEF 1003
Cdd:cd14612    167 LVAEVEESRQtaASPGPIVVHCSAGIGRTGCFIATSIGCQQL-KDTGKVDILGIVCQLRLDRGGMIQTSEQYQF 239
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 775-1003 1.26e-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: 1.26e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  775 GNIKKNRHPDFLPYDHARIKLKAESSPS-RSDYINASPIIEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTP 853
Cdd:cd14613     24 GLVRKNRYKTILPNPHSRVCLTSPDQDDpLSSYINANYIRGYGGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITN 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  854 LVEDGVKqCDRYWPDEgSSLYHVYEVNlVSEHIWCEDFLVRSFYLKNvqTQETRTLTQFHFLSWPAEGTPASTRPLLDFR 933
Cdd:cd14613    104 IEEMNEK-CTEYWPEE-QVTYEGIEIT-VKQVIHADDYRLRLITLKS--GGEERGLKHYWYTSWPDQKTPDNAPPLLQLV 178

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2165490393  934 RKVN---KCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGVKeIDIAATLEHVRDQRPGLVRSKDQFEF 1003
Cdd:cd14613    179 QEVEearQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGV-VDILRTTCQLRLDRGGMIQTCEQYQF 250
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 806-1010 3.64e-43

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: 155.98  E-value: 3.64e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  806 YINASpIIEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEgSSLYHVYEVNLVSEH 885
Cdd:cd14632      1 YINAN-YIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDD-SDTYGDIKITLLKTE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  886 IWCEdFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILID 965
Cdd:cd14632     79 TLAE-YSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYIVLD 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2165490393  966 MVLNrMAKGVKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAE 1010
Cdd:cd14632    158 VMLD-MAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 806-1003 6.73e-43

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: 155.69  E-value: 6.73e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  806 YINASPI-IEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGSS----LYHVYEVN 880
Cdd:cd14540      1 YINASHItATVGGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGEhdalTFGEYKVS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  881 LVSEHIwCEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDF-------RRKVNKCYRGRS--CPIIVHC 951
Cdd:cd14540     81 TKFSVS-SGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFleeinsvRRHTNQDVAGHNrnPPTLVHC 159

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2165490393  952 SDGAGRTGTYILIDMVLNRMAKGVkEIDIAATLEHVRDQRPGLVRSKDQFEF 1003
Cdd:cd14540    160 SAGVGRTGVVILADLMLYCLDHNE-ELDIPRVLALLRHQRMLLVQTLAQYKF 210
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 806-1003 8.95e-43

protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis thaliana protein tyrosine phosphatase 1 (AtPTP1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. AtPTP1 dephosphorylates and inhibits MAP kinase 6 (MPK6) in non-oxidative stress conditions. Together with MAP kinase phosphatase 1 (MKP1) it expresses salicylic acid (SA) and camalexin biosynthesis, and therefore, modulating defense response.


Pssm-ID: 350496 [Multi-domain]  Cd Length: 206  Bit Score: 154.93  E-value: 8.95e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  806 YINASPIIEHD-PRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVeDGVK--QCDRYWPDEGSSLYHVYEVNLV 882
Cdd:cd17658      1 YINASLVETPAsESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLV-DNYStaKCADYFPAEENESREFGRISVT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  883 SEHIWCED--FLVRSFYLKNVQTQET-RTLTQFHFLSWPAEGTPASTRPLldfrRKVNKCYRG---RSCPIIVHCSDGAG 956
Cdd:cd17658     80 NKKLKHSQhsITLRVLEVQYIESEEPpLSVLHIQYPEWPDHGVPKDTRSV----RELLKRLYGippSAGPIVVHCSAGIG 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2165490393  957 RTGTYILIDMVLNRMAKG-VKEIDIAATLEHVRDQRPGLVRSKDQFEF 1003
Cdd:cd17658    156 RTGAYCTIHNTIRRILEGdMSAVDLSKTVRKFRSQRIGMVQTQDQYIF 203
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 806-1001 3.62e-42

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: 153.06  E-value: 3.62e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  806 YINASPIIEH-DPRmpAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWP--DEGSSLYHVYEVNLV 882
Cdd:cd14557      1 YINASYIDGFkEPR--KYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPsmEEGSRAFGDVVVKIN 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  883 SEHIwCEDFLVRSFYLKNVQTQET-RTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTY 961
Cdd:cd14557     79 EEKI-CPDYIIRKLNINNKKEKGSgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGTY 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 2165490393  962 ILIDMVLNRM-AKGVkeIDIAATLEHVRDQRPGLVRSKDQF 1001
Cdd:cd14557    158 IGIDAMLEGLeAEGR--VDVYGYVVKLRRQRCLMVQVEAQY 196
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 806-1004 5.65e-42

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: 152.54  E-value: 5.65e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  806 YINASPIIEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDE-GSSL-YHVYEVNLVS 883
Cdd:cd14539      1 YINASLIEDLTPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTErGQALvYGAITVSLQS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  884 EH---IWCEdflvRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCY---RGRSCPIIVHCSDGAGR 957
Cdd:cd14539     81 VRttpTHVE----RIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYlqqRSLQTPIVVHCSSGVGR 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2165490393  958 TGTYILIDMVLNRMAKGVKEIDIAATLEHVRDQRPGLVRSKDQFEFA 1004
Cdd:cd14539    157 TGAFCLLYAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFC 203
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 779-1003 9.95e-42

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: 152.76  E-value: 9.95e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  779 KNRHPDFLPYDHARIKLKAE-SSPSRSDYINASPIIEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVED 857
Cdd:cd14611      2 KNRYKTILPNPHSRVCLKPKnSNDSLSTYINANYIRGYGGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  858 GVKqCDRYWPdEGSSLYHVYE--VNLVSEhiwCEDFLVRSFYLKnvQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRK 935
Cdd:cd14611     82 NEK-CVLYWP-EKRGIYGKVEvlVNSVKE---CDNYTIRNLTLK--QGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLD 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2165490393  936 VN---KCYRGRScPIIVHCSDGAGRTGTYILIDMVLNRMA-KGVkeIDIAATLEHVRDQRPGLVRSKDQFEF 1003
Cdd:cd14611    155 VEedrLASPGRG-PVVVHCSAGIGRTGCFIATTIGCQQLKeEGV--VDVLSIVCQLRVDRGGMVQTSEQYEF 223
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 806-1003 5.47e-41

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: 149.48  E-value: 5.47e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  806 YINASPIIEHDPRmPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLvEDGVKQCDRYWPDEGSSLYHVYEVNLVSEH 885
Cdd:cd14556      1 YINAALLDSYKQP-AAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQL-DPKDQSCPQYWPDEGSGTYGPIQVEFVSTT 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  886 IwCEDFLVRSFYLKNV-QTQE-TRTLTQFHFLSWPAEG-TPASTRPLLDFRRKVNK----CYRGrscPIIVHCSDGAGRT 958
Cdd:cd14556     79 I-DEDVISRIFRLQNTtRPQEgYRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVEKwqeqSGEG---PIVVHCLNGVGRS 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2165490393  959 GTYILIDMVLNRMaKGVKEIDIAATLEHVRDQRPGLVRSKDQFEF 1003
Cdd:cd14556    155 GVFCAISSVCERI-KVENVVDVFQAVKTLRNHRPNMVETEEQYKF 198
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 780-1003 1.08e-40

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: 149.67  E-value: 1.08e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  780 NRHPDFLPYDHARIKLKAESSPSRSDYINASPIIEHdpRMP-AYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDG 858
Cdd:cd14616      1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGY--LCPnEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  859 VKQCDRYWPDEGS--SLYHVYEVNLVSEHIWcEDFLVRSfyLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKV 936
Cdd:cd14616     79 RIRCHQYWPEDNKpvTVFGDIVITKLMEDVQ-IDWTIRD--LKIERHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLV 155

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2165490393  937 NKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMaKGVKEIDIAATLEHVRDQRPGLVRSKDQFEF 1003
Cdd:cd14616    156 RASRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHI-NDHDFVDIYGLVAELRSERMCMVQNLAQYIF 221
Receptor_IA-2 pfam11548
Protein-tyrosine phosphatase receptor IA-2; IA-2 is a protein-tyrosine phosphatase receptor ...
 470-558 1.38e-40

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: 144.30  E-value: 1.38e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  470 EEYGYIVTDQKPLSLAAGVKLLEILAEHVHMSSGSFINISVVGPALTFRIRHNEQNLSLADVTQQAGLVKSELEAQTGLQ 549
Cdd:pfam11548    1 EEYGYIVTDNDPLSWEEGLRLMEKVAELLHLPMSSFADIRVLGPAVTFKVRANNKNLTAADVAKAAVDIKDKLEKETGLK 80


                   ....*....
gi 2165490393  550 ILQTGVGQQ 558
Cdd:pfam11548   81 ILQAGVGDK 89
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 776-1003 1.15e-39

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: 147.34  E-value: 1.15e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  776 NIKKNRHPDFLPYDHARIKLKAESSPSRSDYINASPIIEHD-PRmpAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPL 854
Cdd:cd14614     12 NRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNsPQ--EYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQC 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  855 VEDGVKQCDRYWP-DEGSSLYHVYEVNLVSEHiWCEDFLVRSFYLKnvQTQETRTLTQFHFLSWPAEGTPA--STRPLLD 931
Cdd:cd14614     90 NEKRRVKCDHYWPfTEEPVAYGDITVEMLSEE-EQPDWAIREFRVS--YADEVQDVMHFNYTAWPDHGVPTanAAESILQ 166

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2165490393  932 F----RRKVNKcyrgRSCPIIVHCSDGAGRTGTYILIDmvlnRMAKGVKE---IDIAATLEHVRDQRPGLVRSKDQFEF 1003
Cdd:cd14614    167 FvqmvRQQAVK----SKGPMIIHCSAGVGRTGTFIALD----RLLQHIRDhefVDILGLVSEMRSYRMSMVQTEEQYIF 237
RESP18 pfam14948
RESP18 domain; This domain is found in the glucocorticoid-responsive protein regulated ...
 60-160 2.37e-39

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: 141.12  E-value: 2.37e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393   60 GQCQVGVGQARPLLQVTSPVLQRLQGVLRQLMSQGLSWHDDLTQYVISQEMERIPRLRPPEPHPRDRSGLVPRRPGPTG- 138
Cdd:pfam14948    1 GQGQVGVGQLWPLQGFTAPVFQHLQVVLHQIVPQGLFWKDDLTQDVMTQKMEHISRLHPQDPCLKDGKAVFPTRTTGVRg 80

                           90       100
                   ....*....|....*....|....
gi 2165490393  139 --ELLLQGVPTGSaPAPQHRLPRP 160
Cdd:pfam14948   81 kqEEKLRLLFPKS-PAVKVNRDQC 103
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 776-1003 2.85e-39

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 148.61  E-value: 2.85e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  776 NIKKNRHPDFLPYDHARIKLKAESSpSRSDYINASPI--IEHDPRmpaYIATQGPLSHTIADFWQMVWESGCTVIVMLTP 853
Cdd:PHA02747    51 NQPKNRYWDIPCWDHNRVILDSGGG-STSDYIHANWIdgFEDDKK---FIATQGPFAETCADFWKAVWQEHCSIIVMLTP 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  854 L-VEDGVKQCDRYW-PDEGSSL----YHVYEVNLVsehiwcedflVRSFYLK------NVQTQETRTLTQFHFLSWPAEG 921
Cdd:PHA02747   127 TkGTNGEEKCYQYWcLNEDGNIdmedFRIETLKTS----------VRAKYILtlieitDKILKDSRKISHFQCSEWFEDE 196

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  922 TPASTRPLLDF-------RRKVNKCYRGRS---CPIIVHCSDGAGRTGTYILIDMVLNRMAKgVKEIDIAATLEHVRDQR 991
Cdd:PHA02747   197 TPSDHPDFIKFikiidinRKKSGKLFNPKDallCPIVVHCSDGVGKTGIFCAVDICLNQLVK-RKAICLAKTAEKIREQR 275

                          250
                   ....*....|..
gi 2165490393  992 PGLVRSKDQFEF 1003
Cdd:PHA02747   276 HAGIMNFDDYLF 287
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 770-1003 3.95e-37

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: 141.67  E-value: 3.95e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  770 TAQGEGNIKKNRHPDFLPYDHARIKLkAESSPSRSDYINASPI-IEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVI 848
Cdd:cd14599     32 TATLPENAERNRIREVVPYEENRVEL-VPTKENNTGYINASHIkVTVGGEEWHYIATQGPLPHTCHDFWQMVWEQGVNVI 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  849 VMLTPLVEDGVKQCDRYWPDEG----SSLYHVYEVNL-VSEHIWCedFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTP 923
Cdd:cd14599    111 AMVTAEEEGGRSKSHRYWPKLGskhsSATYGKFKVTTkFRTDSGC--YATTGLKVKHLLSGQERTVWHLQYTDWPDHGCP 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  924 ASTRPLLDF-------RRKVNKCYRG-RSC--PIIVHCSDGAGRTGTYILIDMVLNRMAKGVKeIDIAATLEHVRDQRPG 993
Cdd:cd14599    189 EEVQGFLSYleeiqsvRRHTNSMLDStKNCnpPIVVHCSAGVGRTGVVILTELMIGCLEHNEK-VEVPVMLRHLREQRMF 267

                          250
                   ....*....|
gi 2165490393  994 LVRSKDQFEF 1003
Cdd:cd14599    268 MIQTIAQYKF 277
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
908-1010 8.77e-34

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 125.16  E-value: 8.77e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393   908 TLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSC--PIIVHCSDGAGRTGTYILIDMVLNRMAKGVKEIDIAATLE 985
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESsgPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 2165490393   986 HVRDQRPGLVRSKDQFEFALTAVAE 1010
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 908-1010 8.77e-34

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


Pssm-ID: 214469 [Multi-domain]  Cd Length: 105  Bit Score: 125.16  E-value: 8.77e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393   908 TLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSC--PIIVHCSDGAGRTGTYILIDMVLNRMAKGVKEIDIAATLE 985
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESsgPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 2165490393   986 HVRDQRPGLVRSKDQFEFALTAVAE 1010
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PHA02738 PHA02738
hypothetical protein; Provisional
 776-1013 1.30e-33

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 132.36  E-value: 1.30e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  776 NIKKNRHPDFLPYDHARIKLKAESSpsRSDYINASPI--IEHDPRmpaYIATQGPLSHTIADFWQMVWESGCTVIVMLTP 853
Cdd:PHA02738    49 NRKLNRYLDAVCFDHSRVILPAERN--RGDYINANYVdgFEYKKK---FICGQAPTRQTCYDFYRMLWMEHVQIIVMLCK 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  854 LVEDGVKQCDRYWPD-EGSSL-YHVYEVNLVSehiwCEDFL--VRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPL 929
Cdd:PHA02738   124 KKENGREKCFPYWSDvEQGSIrFGKFKITTTQ----VETHPhyVKSTLLLTDGTSATQTVTHFNFTAWPDHDVPKNTSEF 199

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  930 LDFRRKVNKCY-------------RGRSCPIIVHCSDGAGRTGTYILIDMVLNRMaKGVKEIDIAATLEHVRDQRPGLVR 996
Cdd:PHA02738   200 LNFVLEVRQCQkelaqeslqighnRLQPPPIVVHCNAGLGRTPCYCVVDISISRF-DACATVSIPSIVSSIRNQRYYSLF 278

                          250
                   ....*....|....*..
gi 2165490393  997 SKDQFEFALTAVAEEVN 1013
Cdd:PHA02738   279 IPFQYFFCYRAVKRYVN 295
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 806-1003 2.75e-33

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: 127.83  E-value: 2.75e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  806 YINASPIIEHdpRMPA-YIATQGPLSHTIADFWQMVWESGCTVIVMLTPLveDGVKQCDRYWPDEGSSLYHVYEVNLVSE 884
Cdd:cd14634      1 YINAALMDSH--KQPAaFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEM--DAAQLCMQYWPEKTSCCYGPIQVEFVSA 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  885 HIwCEDFLVRSFYLKNVQTQET--RTLTQFHFLSWPA-EGTPASTRPLLDFRRKVNKC---YRGRSCPIIVHCSDGAGRT 958
Cdd:cd14634     77 DI-DEDIISRIFRICNMARPQDgyRIVQHLQYIGWPAyRDTPPSKRSILKVVRRLEKWqeqYDGREGRTVVHCLNGGGRS 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2165490393  959 GTYILIDMVlNRMAKGVKEIDIAATLEHVRDQRPGLVRSKDQFEF 1003
Cdd:cd14634    156 GTFCAICSV-CEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKF 199
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
734-1016 2.90e-33

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 130.21  E-value: 2.90e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  734 GHMILAYMEDHLRNRdrLAKEWQALcAYQAEPNtcataQGEGNI---KKNRHPDFLPYDHARIklkaesspsRSD--YIN 808
Cdd:COG5599      5 NPIAIKSEEEKINSR--LSTLTNEL-APSHNDP-----QYLQNIngsPLNRFRDIQPYKETAL---------RANlgYLN 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  809 ASPIIEHDPRMpaYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGV--KQCDRYWPDEGSslYHVYEV-NLVSEH 885
Cdd:COG5599     68 ANYIQVIGNHR--YIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEISKpkVKMPVYFRQDGE--YGKYEVsSELTES 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  886 IWCED-FLVRSFYLKNVQT-QETRTLTQFHFLSWPAEGTPAST--RPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTY 961
Cdd:COG5599    144 IQLRDgIEARTYVLTIKGTgQKKIEIPVLHVKNWPDHGAISAEalKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTL 223

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2165490393  962 ILIdMVLNRMAKGVKEIDIAA--TLEHVRDQR-PGLVRSKDQFEFaLTAVAEEVNAIL 1016
Cdd:COG5599    224 IAC-LALSKSINALVQITLSVeeIVIDMRTSRnGGMVQTSEQLDV-LVKLAEQQIRPL 279
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 806-1003 3.03e-32

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


Pssm-ID: 350398 [Multi-domain]  Cd Length: 200  Bit Score: 124.36  E-value: 3.03e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  806 YINASPIIEHDpRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGvkQCDRYWPDEGSSLYHV-YEVNLVSE 884
Cdd:cd14550      1 YINASYLQGYR-RSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWPTKEKPLECEtFKVTLSGE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  885 HIWC----EDFLVRSFYLKNvqTQETRTLT--QFHFLSWPAEGTPASTrpLLDFRRKVNKCYRGRSCPIIVHCSDGAGRT 958
Cdd:cd14550     78 DHSClsneIRLIVRDFILES--TQDDYVLEvrQFQCPSWPNPCSPIHT--VFELINTVQEWAQQRDGPIVVHDRYGGVQA 153

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2165490393  959 GTYILIdMVLNRMAKGVKEIDI--AATLEHVRdqRPGLVRSKDQFEF 1003
Cdd:cd14550    154 ATFCAL-TTLHQQLEHESSVDVyqVAKLYHLM--RPGVFTSKEDYQF 197
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 806-1003 1.41e-30

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: 120.47  E-value: 1.41e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  806 YINASPI------IEHDprmpaYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHV-YE 878
Cdd:cd14598      1 YINASHIkvtvggKEWD-----YIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLGSRHNTVtYG 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  879 VNLVSEHIWCED--FLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDF-------RRKVNKCY--RGRSCPI 947
Cdd:cd14598     76 RFKITTRFRTDSgcYATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYleeiqsvRRHTNSTIdpKSPNPPV 155

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2165490393  948 IVHCSDGAGRTGTYILIDMVL-----NRMakgvkeIDIAATLEHVRDQRPGLVRSKDQFEF 1003
Cdd:cd14598    156 LVHCSAGVGRTGVVILSEIMIaclehNEM------LDIPRVLDMLRQQRMMMVQTLSQYTF 210
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 765-1003 6.72e-30

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 120.88  E-value: 6.72e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  765 PNTCATAQGEGNIKKNRHPDFLPYDHARIKLKAESSpsRSDYINASPIIEHDPRMpAYIATQGPLSHTIADFWQMVWESG 844
Cdd:PHA02742    41 AFSCNESLELKNMKKCRYPDAPCFDRNRVILKIEDG--GDDFINASYVDGHNAKG-RFICTQAPLEETALDFWQAIFQDQ 117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  845 CTVIVMLTPLVEDGVKQCDRYW-PDEGSSLYHvYEVNLVSEHIWC-EDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGT 922
Cdd:PHA02742   118 VRVIVMITKIMEDGKEACYPYWmPHERGKATH-GEFKIKTKKIKSfRNYAVTNLCLTDTNTGASLDIKHFAYEDWPHGGL 196

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  923 PASTRPLLDFRRKVNKC-----------YRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGVKeIDIAATLEHVRDQR 991
Cdd:PHA02742   197 PRDPNKFLDFVLAVREAdlkadvdikgeNIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAI-IPLLSIVRDLRKQR 275

                          250
                   ....*....|..
gi 2165490393  992 PGLVRSKDQFEF 1003
Cdd:PHA02742   276 HNCLSLPQQYIF 287
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 806-1010 2.33e-29

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: 116.55  E-value: 2.33e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  806 YINASpIIEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVE-DGVKQCDRYWPDEGSSLYHVYEVNLVSE 884
Cdd:cd14637      1 YINAA-LTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQsNSAWPCLQYWPEPGLQQYGPMEVEFVSG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  885 HIwCEDFLVRSFYLKNV-QTQETRTLT-QFHFLSWPA-EGTPASTRPLLDFRRKVNK----CYRGRScpiIVHCSDGAGR 957
Cdd:cd14637     80 SA-DEDIVTRLFRVQNItRLQEGHLMVrHFQFLRWSAyRDTPDSKKAFLHLLASVEKwqreSGEGRT---VVHCLNGGGR 155

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2165490393  958 TGTYILIDMVLNrMAKGVKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAE 1010
Cdd:cd14637    156 SGTYCASAMILE-MIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 806-1010 5.03e-29

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: 115.51  E-value: 5.03e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  806 YINASPIIEHdpRMPA-YIATQGPLSHTIADFWQMVWESGCTVIVMLTPLveDGVKQCDRYWPDEGSSLYHVYEVNLVSE 884
Cdd:cd14636      1 YINAALMDSY--RQPAaFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEV--DLAQGCPQYWPEEGMLRYGPIQVECMSC 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  885 HIWCeDFLVRSFYLKNV-QTQETRTLT-QFHFLSWPA-EGTPASTRPLLDFRRKVNK----CYRGRSCPIIvHCSDGAGR 957
Cdd:cd14636     77 SMDC-DVISRIFRICNLtRPQEGYLMVqQFQYLGWAShREVPGSKRSFLKLILQVEKwqeeCDEGEGRTII-HCLNGGGR 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2165490393  958 TGTYILIDMVLnRMAKGVKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAE 1010
Cdd:cd14636    155 SGMFCAISIVC-EMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 806-1010 5.06e-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: 115.56  E-value: 5.06e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  806 YINASpIIEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLveDGVKQCDRYWPDEGSSLYHVYEVNLVSEH 885
Cdd:cd14635      1 YINAA-LMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDV--DPAQLCPQYWPENGVHRHGPIQVEFVSAD 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  886 IWcEDFLVRSFYLKNVQTQET--RTLTQFHFLSWPA-EGTPASTRPLLDFRRKVNKC---YRGRSCPIIVHCSDGAGRTG 959
Cdd:cd14635     78 LE-EDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMyRDTPVSKRSFLKLIRQVDKWqeeYNGGEGRTVVHCLNGGGRSG 156

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2165490393  960 TYILIDMVLnRMAKGVKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAE 1010
Cdd:cd14635    157 TFCAISIVC-EMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 776-1008 8.41e-29

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 118.21  E-value: 8.41e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  776 NIKKNRHPDFLPYDHARIKLKAESS----------PSR---------SDYINASpIIEHDPRMPAYIATQGPLSHTIADF 836
Cdd:PHA02746    51 NLKKNRFHDIPCWDHSRVVINAHESlkmfdvgdsdGKKievtsednaENYIHAN-FVDGFKEANKFICAQGPKEDTSEDF 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  837 WQMVWESGCTVIVMLTPlVEDGVKQCDRYW-PDEGSSLYHVYEVNLVSEHIWCEDFLVRSFYLKNVQTQETRTLTQFHFL 915
Cdd:PHA02746   130 FKLISEHESQVIVSLTD-IDDDDEKCFELWtKEEDSELAFGRFVAKILDIIEELSFTKTRLMITDKISDTSREIHHFWFP 208

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  916 SWPAEGTPASTRPLLDFRRKVNKcYRGR-----------SCPIIVHCSDGAGRTGTYILIDMVLNRMAKGvKEIDIAATL 984
Cdd:PHA02746   209 DWPDNGIPTGMAEFLELINKVNE-EQAElikqadndpqtLGPIVVHCSAGIGRAGTFCAIDNALEQLEKE-KEVCLGEIV 286

                          250       260
                   ....*....|....*....|....
gi 2165490393  985 EHVRDQRPGLVRSKDQFEFALTAV 1008
Cdd:PHA02746   287 LKIRKQRHSSVFLPEQYAFCYKAL 310
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 806-1008 1.89e-19

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: 87.74  E-value: 1.89e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  806 YINASPIIEHDpRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCdRYWPDEGSSLY-HVYEVNLVSE 884
Cdd:cd17669      1 YINASYIMGYY-QSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEF-VYWPNKDEPINcETFKVTLIAE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  885 HIWC----EDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPAS-TRPLLDFrrkVNKCYRGRSCPIIVHCSDGAGRTG 959
Cdd:cd17669     79 EHKClsneEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISkTFELISI---IKEEAANRDGPMIVHDEHGGVTAG 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2165490393  960 TYILIDMVLNRMAKGvKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAV 1008
Cdd:cd17669    156 TFCALTTLMHQLEKE-NSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAI 203
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 806-1008 4.37e-18

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: 83.96  E-value: 4.37e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  806 YINASPIIEHdPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVML---TPLVEDGVKqcdrYWPDEGSSLY-HVYEVNL 881
Cdd:cd17670      1 YINASYIMGY-YRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpdnQGLAEDEFV----YWPSREESMNcEAFTVTL 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  882 VSEHIWC----EDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTP-ASTRPLLDFrrkVNKCYRGRSCPIIVHCSDGAG 956
Cdd:cd17670     76 ISKDRLClsneEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPiSSTFELINV---IKEEALTRDGPTIVHDEFGAV 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2165490393  957 RTGTYILIdMVLNRMAKGVKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAV 1008
Cdd:cd17670    153 SAGTLCAL-TTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAM 203
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 750-1020 2.61e-14

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 75.00  E-value: 2.61e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  750 RLAKEWQALCAYQAEPNTCATAQGEGNIKK-NRHPDFLPYDHARIKLKAESSPSRSDYINAspiIEHDPRmpaYIATQGP 828
Cdd:PHA02740    26 CIIKEYRAIVPEHEDEANKACAQAENKAKDeNLALHITRLLHRRIKLFNDEKVLDARFVDG---YDFEQK---FICIINL 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  829 LSHTIADFWQMVWESGCTVIVMLTPLVEdgvKQC-DRYWP-DEGS-SLYHVYEVNLVsEHIWCEDFLVRSFYLKNVQTQE 905
Cdd:PHA02740   100 CEDACDKFLQALSDNKVQIIVLISRHAD---KKCfNQFWSlKEGCvITSDKFQIETL-EIIIKPHFNLTLLSLTDKFGQA 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165490393  906 tRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYR--------GRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKgVKE 977
Cdd:PHA02740   176 -QKISHFQYTAWPADGFSHDPDAFIDFFCNIDDLCAdlekhkadGKIAPIIIDCIDGISSSAVFCVFDICATEFDK-TGM 253

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 2165490393  978 IDIAATLEHVRDQRPGLVRSKDQFEFALTAVAEEVNAILKALP 1020
Cdd:PHA02740   254 LSIANALKKVRQKKYGCMNCLDDYVFCYHLIAAYLKEKFDILK 296
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 946-1003 2.36e-06

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: 48.04  E-value: 2.36e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2165490393  946 PIIVHCSDGAGRTGTYILIDMVLNRMAKGVKEIDIaatlehVRDQRPGLVRSKDQFEF 1003
Cdd:cd14504     84 AVLVHCLAGKGRTGTMLACYLVKTGKISAVDAINE------IRRIRPGSIETSEQEKF 135
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 922-993 4.65e-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: 40.80  E-value: 4.65e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2165490393  922 TPASTRPLLDFRRKVNKCYrgrsCPIIVHCSDGAGRTGTYILIDMVLnRMAKGVKEIdiaatLEHVRDQRPG 993
Cdd:cd14494     38 TLAMVDRFLEVLDQAEKPG----EPVLVHCKAGVGRTGTLVACYLVL-LGGMSAEEA-----VRIVRLIRPG 99
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 820-875 2.90e-03

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: 38.48  E-value: 2.90e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2165490393  820 PAYIATQGPLSHtIADFWQMVWESGCTVIVMLT-PLVEDGVKQCDRYWPDEGSSLYH 875
Cdd:cd14494      7 LRLIAGALPLSP-LEADSRFLKQLGVTTIVDLTlAMVDRFLEVLDQAEKPGEPVLVH 62
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
946-1003 3.28e-03

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 38.80  E-value: 3.28e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2165490393  946 PIIVHCSDGAGRTGTyILIdMVLnrMAKGVkeiDIAATLEHVRDQRPGLVRSKDQFEF 1003
Cdd:COG2453     82 KVLVHCRGGIGRTGT-VAA-AYL--VLLGL---SAEEALARVRAARPGAVETPAQRAF 132
 
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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