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Conserved domains on  [gi|1907067839|ref|XP_036018688|]
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receptor-type tyrosine-protein phosphatase-like N isoform X2 [Mus musculus]

Protein Classification

Receptor_IA-2 and R-PTP-N domain-containing protein( domain architecture ID 13134033)

protein containing domains RESP18, PHA03247, 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 ...
 657-937 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: 656.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 657 HMILAYMEDHLRNRDRLAKEWQALCAYQAEPNTCAAAQDESNIKKNRHPDFLPYDHARIKLKVESSPSRSDYINASPIIE 736
Cdd:cd14609     1 HMILAYMEDHLRNRDRLAKEWQALCAYQAEPNTCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPIIE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 737 HDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHVYEVNLVSEHIWCEDFLVR 816
Cdd:cd14609    81 HDPRMPAYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHIYEVNLVSEHIWCEDFLVR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 817 SFYLKNLQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKG 896
Cdd:cd14609   161 SFYLKNVQTQETRTLTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKG 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1907067839 897 VKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAEEVNAI 937
Cdd:cd14609   241 VKEIDIAATLEHVRDQRPGMVRTKDQFEFALTAVAEEVNAI 281
Receptor_IA-2 pfam11548
Protein-tyrosine phosphatase receptor IA-2; IA-2 is a protein-tyrosine phosphatase receptor ...
 433-521 4.35e-42

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


:

Pssm-ID: 463293  Cd Length: 89  Bit Score: 148.15  E-value: 4.35e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 433 EEYGYIVTDQKPLSLVAGVRLLEILAEHVHMSSGSFINISVVGPAVTFRIRHNEQNLSLADVTQQAGLVKSELEAQTGLQ 512
Cdd:pfam11548   1 EEYGYIVTDNDPLSWEEGLRLMEKVAELLHLPMSSFADIRVLGPAVTFKVRANNKNLTAADVAKAAVDIKDKLEKETGLK 80


                  ....*....
gi 1907067839 513 ILQTGVGQR 521
Cdd:pfam11548  81 ILQAGVGDK 89
RESP18 super family cl20829
RESP18 domain; This domain is found in the glucocorticoid-responsive protein regulated ...
 58-112 3.64e-18

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


The actual alignment was detected with superfamily member pfam14948:

Pssm-ID: 464394  Cd Length: 103  Bit Score: 80.64  E-value: 3.64e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907067839  58 QGLSWHDDLTQHVISQEMERIPRLRPPEPHPRDRSGLVPRKPGPAG-------ELLTQGNPT 112
Cdd:pfam14948  34 QGLFWKDDLTQDVMTQKMEHISRLHPQDPCLKDGKAVFPTRTTGVRgkqeeklRLLFPKSPA 95
 
Name Accession Description Interval E-value
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 657-937 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: 656.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 657 HMILAYMEDHLRNRDRLAKEWQALCAYQAEPNTCAAAQDESNIKKNRHPDFLPYDHARIKLKVESSPSRSDYINASPIIE 736
Cdd:cd14609     1 HMILAYMEDHLRNRDRLAKEWQALCAYQAEPNTCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPIIE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 737 HDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHVYEVNLVSEHIWCEDFLVR 816
Cdd:cd14609    81 HDPRMPAYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHIYEVNLVSEHIWCEDFLVR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 817 SFYLKNLQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKG 896
Cdd:cd14609   161 SFYLKNVQTQETRTLTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKG 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1907067839 897 VKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAEEVNAI 937
Cdd:cd14609   241 VKEIDIAATLEHVRDQRPGMVRTKDQFEFALTAVAEEVNAI 281
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
673-932 1.93e-103

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 322.30  E-value: 1.93e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839  673 LAKEWQALCAYQAEPNTCAAAQDESNIKKNRHPDFLPYDHARIKLKVESSPSrSDYINASPI-IEHDPRmpAYIATQGPL 751
Cdd:smart00194   2 LEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEG-SDYINASYIdGPNGPK--AYIATQGPL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839  752 SHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGSSL--YHVYEVNLVSEHIwCEDFLVRSFYLKNLQTQETR 829
Cdd:smart00194  79 PSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPltYGDITVTLKSVEK-VDDYTIRTLEVTNTGCSETR 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839  830 TLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGvKEIDIAATLEHV 909
Cdd:smart00194 158 TVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAG-KEVDIFEIVKEL 236

                          250       260
                   ....*....|....*....|...
gi 1907067839  910 RDQRPGLVRSKDQFEFALTAVAE 932
Cdd:smart00194 237 RSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
698-932 2.92e-102

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 318.42  E-value: 2.92e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 698 NIKKNRHPDFLPYDHARIKLKveSSPSRSDYINASPIIEHdPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLV 777
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLT--GDPGPSDYINASYIDGY-KKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 778 EDGVKQCDRYWPD--EGSSLYHVYEVNLVSEHIWCEDFLVRSFYLKNLQTQETRTLTQFHFLSWPAEGTPASTRPLLDFR 855
Cdd:pfam00102  78 EKGREKCAQYWPEeeGESLEYGDFTVTLKKEKEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLL 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907067839 856 RKVNKCY-RGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGvKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAE 932
Cdd:pfam00102 158 RKVRKSSlDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAE-GEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
Receptor_IA-2 pfam11548
Protein-tyrosine phosphatase receptor IA-2; IA-2 is a protein-tyrosine phosphatase receptor ...
 433-521 4.35e-42

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


Pssm-ID: 463293  Cd Length: 89  Bit Score: 148.15  E-value: 4.35e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 433 EEYGYIVTDQKPLSLVAGVRLLEILAEHVHMSSGSFINISVVGPAVTFRIRHNEQNLSLADVTQQAGLVKSELEAQTGLQ 512
Cdd:pfam11548   1 EEYGYIVTDNDPLSWEEGLRLMEKVAELLHLPMSSFADIRVLGPAVTFKVRANNKNLTAADVAKAAVDIKDKLEKETGLK 80


                  ....*....
gi 1907067839 513 ILQTGVGQR 521
Cdd:pfam11548  81 ILQAGVGDK 89
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 689-925 2.10e-39

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 148.61  E-value: 2.10e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 689 TCAAAQDESNIKKNRHPDFLPYDHARIKLKVESSpSRSDYINASPI--IEHDPRmpaYIATQGPLSHTIADFWQMVWESG 766
Cdd:PHA02747   42 LIANFEKPENQPKNRYWDIPCWDHNRVILDSGGG-STSDYIHANWIdgFEDDKK---FIATQGPFAETCADFWKAVWQEH 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 767 CTVIVMLTPL-VEDGVKQCDRYW-PDEGSSL----YHVYEVNLVsehiwcedflVRSFYLKNL------QTQETRTLTQF 834
Cdd:PHA02747  118 CSIIVMLTPTkGTNGEEKCYQYWcLNEDGNIdmedFRIETLKTS----------VRAKYILTLieitdkILKDSRKISHF 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 835 HFLSWPAEGTPASTRPLLDF-------RRKVNKCYRGRS---CPIIVHCSDGAGRTGTYILIDMVLNRMAKgVKEIDIAA 904
Cdd:PHA02747  188 QCSEWFEDETPSDHPDFIKFikiidinRKKSGKLFNPKDallCPIVVHCSDGVGKTGIFCAVDICLNQLVK-RKAICLAK 266

                         250       260
                  ....*....|....*....|.
gi 1907067839 905 TLEHVRDQRPGLVRSKDQFEF 925
Cdd:PHA02747  267 TAEKIREQRHAGIMNFDDYLF 287
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
656-938 3.77e-33

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 129.83  E-value: 3.77e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 656 GHMILAYMEDHLRNRdrLAKEWQALcAYQAEPNTcaAAQDESNIKKNRHPDFLPYDHARIklkvesspsRSD--YINASP 733
Cdd:COG5599     5 NPIAIKSEEEKINSR--LSTLTNEL-APSHNDPQ--YLQNINGSPLNRFRDIQPYKETAL---------RANlgYLNANY 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 734 IIEHDPRMpaYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGV--KQCDRYWPDEGSslYHVYEV-NLVSEHIWC 810
Cdd:COG5599    71 IQVIGNHR--YIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEISKpkVKMPVYFRQDGE--YGKYEVsSELTESIQL 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 811 ED-FLVRSFYLKNLQT-QETRTLTQFHFLSWPAEGTPAST--RPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILI 886
Cdd:COG5599   147 RDgIEARTYVLTIKGTgQKKIEIPVLHVKNWPDHGAISAEalKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIAC 226

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907067839 887 dMVLNRMAKGVKEIDIAA--TLEHVRDQR-PGLVRSKDQFEFaLTAVAEEVNAIL 938
Cdd:COG5599   227 -LALSKSINALVQITLSVeeIVIDMRTSRnGGMVQTSEQLDV-LVKLAEQQIRPL 279
RESP18 pfam14948
RESP18 domain; This domain is found in the glucocorticoid-responsive protein regulated ...
 58-112 3.64e-18

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: 80.64  E-value: 3.64e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907067839  58 QGLSWHDDLTQHVISQEMERIPRLRPPEPHPRDRSGLVPRKPGPAG-------ELLTQGNPT 112
Cdd:pfam14948  34 QGLFWKDDLTQDVMTQKMEHISRLHPQDPCLKDGKAVFPTRTTGVRgkqeeklRLLFPKSPA 95
 
Name Accession Description Interval E-value
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 657-937 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: 656.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 657 HMILAYMEDHLRNRDRLAKEWQALCAYQAEPNTCAAAQDESNIKKNRHPDFLPYDHARIKLKVESSPSRSDYINASPIIE 736
Cdd:cd14609     1 HMILAYMEDHLRNRDRLAKEWQALCAYQAEPNTCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPIIE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 737 HDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHVYEVNLVSEHIWCEDFLVR 816
Cdd:cd14609    81 HDPRMPAYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHIYEVNLVSEHIWCEDFLVR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 817 SFYLKNLQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKG 896
Cdd:cd14609   161 SFYLKNVQTQETRTLTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKG 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1907067839 897 VKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAEEVNAI 937
Cdd:cd14609   241 VKEIDIAATLEHVRDQRPGMVRTKDQFEFALTAVAEEVNAI 281
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 655-937 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: 568.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 655 TGHMILAYMEDHLRNRDRLAKEWQALCAYQAEPNTCAAAQDESNIKKNRHPDFLPYDHARIKLKVESSPSRSDYINASPI 734
Cdd:cd14610     1 TGHMILSYMEDHLKNKNRLEKEWEALCAYQAEPNATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 735 IEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHVYEVNLVSEHIWCEDFL 814
Cdd:cd14610    81 MDHDPRNPAYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSNLYHIYEVNLVSEHIWCEDFL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 815 VRSFYLKNLQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMA 894
Cdd:cd14610   161 VRSFYLKNLQTNETRTVTQFHFLSWNDQGVPASTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMA 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1907067839 895 KGVKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAEEVNAI 937
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 ...
 728-935 1.15e-158

PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type tyrosine-protein phosphatase-like N (PTPRN) and N2 (PTPRN2) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). They consist of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. They are mainly expressed in neuropeptidergic neurons and peptide-secreting endocrine cells, including insulin-producing pancreatic beta-cells, and are involved in involved in the generation, cargo storage, traffic, exocytosis and recycling of insulin secretory granules, as well as in beta-cell proliferation. They also are major autoantigens in type 1 diabetes and are involved in the regulation of insulin secretion.


Pssm-ID: 350394 [Multi-domain]  Cd Length: 208  Bit Score: 463.84  E-value: 1.15e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 728 YINASPIIEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHVYEVNLVSEH 807
Cdd:cd14546     1 YINASTIYDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEVYHIYEVHLVSEH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 808 IWCEDFLVRSFYLKNLQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILID 887
Cdd:cd14546    81 IWCDDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSCPIVVHCSDGAGRTGTYILID 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1907067839 888 MVLNRMAKGVKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAEEVN 935
Cdd:cd14546   161 MVLNRMAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAEEVN 208
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
673-932 1.93e-103

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 322.30  E-value: 1.93e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839  673 LAKEWQALCAYQAEPNTCAAAQDESNIKKNRHPDFLPYDHARIKLKVESSPSrSDYINASPI-IEHDPRmpAYIATQGPL 751
Cdd:smart00194   2 LEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEG-SDYINASYIdGPNGPK--AYIATQGPL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839  752 SHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGSSL--YHVYEVNLVSEHIwCEDFLVRSFYLKNLQTQETR 829
Cdd:smart00194  79 PSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPltYGDITVTLKSVEK-VDDYTIRTLEVTNTGCSETR 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839  830 TLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGvKEIDIAATLEHV 909
Cdd:smart00194 158 TVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAG-KEVDIFEIVKEL 236

                          250       260
                   ....*....|....*....|...
gi 1907067839  910 RDQRPGLVRSKDQFEFALTAVAE 932
Cdd:smart00194 237 RSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
698-932 2.92e-102

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 318.42  E-value: 2.92e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 698 NIKKNRHPDFLPYDHARIKLKveSSPSRSDYINASPIIEHdPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLV 777
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLT--GDPGPSDYINASYIDGY-KKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 778 EDGVKQCDRYWPD--EGSSLYHVYEVNLVSEHIWCEDFLVRSFYLKNLQTQETRTLTQFHFLSWPAEGTPASTRPLLDFR 855
Cdd:pfam00102  78 EKGREKCAQYWPEeeGESLEYGDFTVTLKKEKEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLL 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907067839 856 RKVNKCY-RGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGvKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAE 932
Cdd:pfam00102 158 RKVRKSSlDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAE-GEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 728-925 4.48e-82

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: 4.48e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 728 YINASPIIEHDPRmPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGSS--LYHVYEVNLVS 805
Cdd:cd00047     1 YINASYIDGYRGP-KEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKplEYGDITVTLVS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 806 EHIwCEDFLVRSFYLKNLQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYIL 885
Cdd:cd00047    80 EEE-LSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTGTFIA 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1907067839 886 IDMVLNRMAKGvKEIDIAATLEHVRDQRPGLVRSKDQFEF 925
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 ...
 696-936 2.06e-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: 2.06e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 696 ESNIKKNRHPDFLPYDHARIKLK-VESSPSrSDYINASPIIEHDpRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLT 774
Cdd:cd14553     1 EVNKPKNRYANVIAYDHSRVILQpIEGVPG-SDYINANYCDGYR-KQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 775 PLVEDGVKQCDRYWPDEGSSLYHVYEVNLVsEHIWCEDFLVRSFYLKNLQTQETRTLTQFHFLSWPAEGTPASTRPLLDF 854
Cdd:cd14553    79 KLEERSRVKCDQYWPTRGTETYGLIQVTLL-DTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAF 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 855 RRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMaKGVKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAEEV 934
Cdd:cd14553   158 LRRVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERI-KHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLEAV 236


                  ..
gi 1907067839 935 NA 936
Cdd:cd14553   237 TC 238
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 698-931 3.83e-66

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: 222.34  E-value: 3.83e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 698 NIKKNRHPDFLPYDHARIKLK-VESSPSRSDYINASPII------EHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVI 770
Cdd:cd14544     1 NKGKNRYKNILPFDHTRVILKdRDPNVPGSDYINANYIRnenegpTTDENAKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 771 VMLTPLVEDGVKQCDRYWPDEGSS-LYHVYEVNLVSEHIwCEDFLVRSFYLKNL-QTQETRTLTQFHFLSWPAEGTPAST 848
Cdd:cd14544    81 VMTTKEVERGKNKCVRYWPDEGMQkQYGPYRVQNVSEHD-TTDYTLRELQVSKLdQGDPIREIWHYQYLSWPDHGVPSDP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 849 RPLLDFRRKVNKCYRGR--SCPIIVHCSDGAGRTGTYILIDMVLNRMAK-GVK-EIDIAATLEHVRDQRPGLVRSKDQFE 924
Cdd:cd14544   160 GGVLNFLEDVNQRQESLphAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRkGLDcDIDIQKTIQMVRSQRSGMVQTEAQYK 239


                  ....*..
gi 1907067839 925 FALTAVA 931
Cdd:cd14544   240 FIYVAVA 246
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 670-925 6.22e-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: 222.24  E-value: 6.22e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 670 RDRLAKEWQALCAyQAEPNTCAAAQDESNIKKNRHPDFLPYDHARIKLKVESSPSRSDYINASpIIEHDPRMPAYIATQG 749
Cdd:cd14543     2 KRGIYEEYEDIRR-EPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINAN-FMDGYKQKNAYIATQG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 750 PLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHVYEVNLVSEHIWC-EDFLVRSFYLKNLQTQET 828
Cdd:cd14543    80 PLPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSSLRYGDLTVTNLSVENkEHYKKTTLEIHNTETDES 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 829 RTLTQFHFLSWPAEGTPASTRPLLDFRRKVnKCYRGRSC--------------PIIVHCSDGAGRTGTYILIDMVLNRMA 894
Cdd:cd14543   160 RQVTHFQFTSWPDFGVPSSAAALLDFLGEV-RQQQALAVkamgdrwkghppgpPIVVHCSAGIGRTGTFCTLDICLSQLE 238

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1907067839 895 KgVKEIDIAATLEHVRDQRPGLVRSKDQFEF 925
Cdd:cd14543   239 D-VGTLNVMQTVRRMRTQRAFSIQTPDQYYF 268
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 728-925 2.64e-63

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


Pssm-ID: 350397 [Multi-domain]  Cd Length: 204  Bit Score: 212.60  E-value: 2.64e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 728 YINASPIIE-HDPRmpAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHVYEVNLVSE 806
Cdd:cd14549     1 YINANYVDGyNKAR--AYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTETYGNIQVTLLST 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 807 HIWCEdFLVRSFYLKNLQ------TQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRT 880
Cdd:cd14549    79 EVLAT-YTVRTFSLKNLKlkkvkgRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVGRT 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1907067839 881 GTYILIDMVLNRMAKgVKEIDIAATLEHVRDQRPGLVRSKDQFEF 925
Cdd:cd14549   158 GTYIVIDSMLQQIQD-KGTVNVFGFLKHIRTQRNYLVQTEEQYIF 201
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 698-929 6.05e-63

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: 6.05e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 698 NIKKNRHPDFLPYDHARIKLKVESSPSRSDYINASPIIEHDPRmPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLV 777
Cdd:cd14554     6 NKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQR-GAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKLR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 778 EDGVKQCDRYWPDEGSSLYHVYEVNLVSEHIWcEDFLVRSFYLKNLQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRK 857
Cdd:cd14554    85 EMGREKCHQYWPAERSARYQYFVVDPMAEYNM-PQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQ 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907067839 858 VNKCYR--GRSCPIIVHCSDGAGRTGTYILIDMVLNRM-AKGVkeIDIAATLEHVRDQRPGLVRSKDQFEFALTA 929
Cdd:cd14554   164 VHKTKEqfGQEGPITVHCSAGVGRTGVFITLSIVLERMrYEGV--VDVFQTVKLLRTQRPAMVQTEDQYQFCYRA 236
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 703-925 8.59e-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: 209.13  E-value: 8.59e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 703 RHPDFLPYDHARIKLKVESSPSRSDYINASPII-EHDPRmpAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGV 781
Cdd:cd14548     1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPgYNSPR--EFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 782 KQCDRYWPDEGSSLYHVY-EVNLVSEHIwCEDFLVRSFYLKnlQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVnK 860
Cdd:cd14548    79 VKCDHYWPFDQDPVYYGDiTVTMLSESV-LPDWTIREFKLE--RGDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLV-R 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907067839 861 CYRGRSC-PIIVHCSDGAGRTGTYILIDMVLNRMAKGvKEIDIAATLEHVRDQRPGLVRSKDQFEF 925
Cdd:cd14548   155 DYIKQEKgPTIVHCSAGVGRTGTFIALDRLLQQIESE-DYVDIFGIVYDLRKHRPLMVQTEAQYIF 219
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 728-925 1.63e-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: 207.87  E-value: 1.63e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 728 YINASPI-IEHDPRMpAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEG-SSLYHVYEVNLVS 805
Cdd:cd18533     1 YINASYItLPGTSSK-RYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEyEGEYGDLTVELVS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 806 EH-IWCEDFLVRSFYLKNlQTQETRTLTQFHFLSWPAEGTPASTRPLL---DFRRKVNKCYRGRScPIIVHCSDGAGRTG 881
Cdd:cd18533    80 EEeNDDGGFIVREFELSK-EDGKVKKVYHIQYKSWPDFGVPDSPEDLLtliKLKRELNDSASLDP-PIIVHCSAGVGRTG 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907067839 882 TYILIDMVLNRMAKGV-------KEID-IAATLEHVRDQRPGLVRSKDQFEF 925
Cdd:cd18533   158 TFIALDSLLDELKRGLsdsqdleDSEDpVYEIVNQLRKQRMSMVQTLRQYIF 209
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 702-925 5.49e-60

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: 204.28  E-value: 5.49e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 702 NRHPDFLPYDHARIKLKVESSPSrSDYINASpiiehdpRMPAY------IATQGPLSHTIADFWQMVWESGCTVIVMLTP 775
Cdd:cd14615     1 NRYNNVLPYDISRVKLSVQSHST-DDYINAN-------YMPGYnskkefIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTK 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 776 LVEDGVKQCDRYWPDEGSSLYHVYEVNLVSEhIWCEDFLVRSFYLKNLQTQETRTLTQFHFLSWPAEGTPASTRPLLDFR 855
Cdd:cd14615    73 CVEQGRTKCEEYWPSKQKKDYGDITVTMTSE-IVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFR 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907067839 856 RKVNKCYRG--RSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGvKEIDIAATLEHVRDQRPGLVRSKDQFEF 925
Cdd:cd14615   152 HLVREYMKQnpPNSPILVHCSAGVGRTGTFIAIDRLIYQIENE-NVVDVYGIVYDLRMHRPLMVQTEDQYVF 222
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 727-940 3.71e-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: 3.71e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 727 DYINASPIIEHDPRMPA---YIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEG-SSLYHVYEVN 802
Cdd:cd14541     1 DYINANYVNMEIPGSGIvnrYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGeTMQFGNLQIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 803 LVSEHIwCEDFLVRSFYLKNLQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGT 882
Cdd:cd14541    81 CVSEEV-TPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCSAGIGRTGV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 883 YILID--MVLNRMAKGVKEIDIAATLehvRDQRPGLVRSKDQFEFaltaVAEevnAILKA 940
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; ...
 701-925 5.80e-58

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: 198.77  E-value: 5.80e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 701 KNRHPDFLPYDHARIKLKVESSpsRSDYINASpIIEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDG 780
Cdd:cd14545     1 LNRYRDRDPYDHDRSRVKLKQG--DNDYINAS-LVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 781 VKQCDRYWP---DEGSSLYHV-YEVNLVSEHIWcEDFLVRSFYLKNLQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRR 856
Cdd:cd14545    78 QIKCAQYWPqgeGNAMIFEDTgLKVTLLSEEDK-SYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQ 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907067839 857 KVNK--CYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKG-VKEIDIAATLEHVRDQRPGLVRSKDQFEF 925
Cdd:cd14545   157 KVREsgSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGnPSSVDVKKVLLEMRKYRMGLIQTPDQLRF 228
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 662-932 7.99e-57

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: 197.85  E-value: 7.99e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 662 YMEDHLRNRdRLAKEWQALCAYQAepntcAAAQDESNIKKNRHPDFLPYDHARIKLKVESSPSRSDYINASPIIE-HDPR 740
Cdd:cd14604    27 FASDFMRLR-RLSTKYRTEKIYPT-----ATGEKEENVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGvYGPK 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 741 mpAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPdegssLYHVYEVNLVSEHIWCE------DFL 814
Cdd:cd14604   101 --AYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWP-----LYGEEPMTFGPFRISCEaeqartDYF 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 815 VRSFYLKnLQtQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMA 894
Cdd:cd14604   174 IRTLLLE-FQ-NETRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLK 251

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1907067839 895 KGV--KEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAE 932
Cdd:cd14604   252 AGKipEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQ 291
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 728-932 8.27e-57

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: 194.52  E-value: 8.27e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 728 YINASPIiehdpRMPA------YIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPD---EGSSLYHV 798
Cdd:cd14538     1 YINASHI-----RIPVggdtyhYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDslnKPLICGGR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 799 YEVNLVSEHIWcEDFLVRSFYLKNLQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYrgRSCPIIVHCSDGAG 878
Cdd:cd14538    76 LEVSLEKYQSL-QDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIH--NSGPIVVHCSAGIG 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907067839 879 RTGTYILIDMVLNRMAKGvKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAE 932
Cdd:cd14538   153 RTGVLITIDVALGLIERD-LPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLE 205
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 696-934 2.42e-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: 196.02  E-value: 2.42e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 696 ESNIKKNRHPDFLPYDHARIKL-KVESSPSrSDYINASpIIEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLT 774
Cdd:cd14626    39 EVNKPKNRYANVIAYDHSRVILtSVDGVPG-SDYINAN-YIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMT 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 775 PLVEDGVKQCDRYWPDEGSSLYHVYEVNLVsEHIWCEDFLVRSFYLKNLQTQETRTLTQFHFLSWPAEGTPASTRPLLDF 854
Cdd:cd14626   117 RLEEKSRVKCDQYWPIRGTETYGMIQVTLL-DTVELATYSVRTFALYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAF 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 855 RRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMaKGVKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAEEV 934
Cdd:cd14626   196 LRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERM-KHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLEAA 274
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 698-934 1.12e-55

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


Pssm-ID: 350505 [Multi-domain]  Cd Length: 274  Bit Score: 194.10  E-value: 1.12e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 698 NIKKNRHPDFLPYDHARIKLK--VESSPSRSDYINASPIIEHDpRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTP 775
Cdd:cd17667    27 NKHKNRYINILAYDHSRVKLRplPGKDSKHSDYINANYVDGYN-KAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITN 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 776 LVEDGVKQCDRYWPDEGSSLYHVYEVNLVSEHIW-CedFLVRSFYLKNLQT-----------QETRTLTQFHFLSWPAEG 843
Cdd:cd17667   106 LVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHaC--YTVRRFSIRNTKVkkgqkgnpkgrQNERTVIQYHYTQWPDMG 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 844 TPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMaKGVKEIDIAATLEHVRDQRPGLVRSKDQF 923
Cdd:cd17667   184 VPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQI-KDKSTVNVLGFLKHIRTQRNYLVQTEEQY 262

                         250
                  ....*....|.
gi 1907067839 924 EFALTAVAEEV 934
Cdd:cd17667   263 IFIHDALLEAI 273
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 676-932 5.72e-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: 5.72e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 676 EWQALCAYQAEPNTCAAAQDESNIKKNRHPDFLPYDHARIKLKVESSPSRSDYINASpIIEHDPRMPAYIATQGPLSHTI 755
Cdd:cd14628    30 EFKRLASSKAHTSRFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINAS-FIDGYRQQKAYIATQGPLAETT 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 756 ADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHVYEVNLVSEHIWCEdFLVRSFYLKNLQTQETRTLTQFH 835
Cdd:cd14628   109 EDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQ-YILREFKVTDARDGQSRTVRQFQ 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 836 FLSWPAEGTPASTRPLLDFRRKVNKCYR--GRSCPIIVHCSDGAGRTGTYILIDMVLNRMA-KGVkeIDIAATLEHVRDQ 912
Cdd:cd14628   188 FTDWPEQGVPKSGEGFIDFIGQVHKTKEqfGQDGPISVHCSAGVGRTGVFITLSIVLERMRyEGV--VDIFQTVKMLRTQ 265

                         250       260
                  ....*....|....*....|
gi 1907067839 913 RPGLVRSKDQFEFALTAVAE 932
Cdd:cd14628   266 RPAMVQTEDQYQFCYRAALE 285
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 698-925 8.11e-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: 190.04  E-value: 8.11e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 698 NIKKNRHPDFLPYDHARIKLKVESspsrsDYINASPIiehdpRMPA------YIATQGPLSHTIADFWQMVWESGCTVIV 771
Cdd:cd14597     3 NRKKNRYKNILPYDTTRVPLGDEG-----GYINASFI-----KMPVgdeefvYIACQGPLPTTVADFWQMVWEQKSTVIA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 772 MLTPLVEDGVKQCDRYWPDEGSSLYHVYE---VNLVS-EHIwcEDFLVRSFYLKNLQTQETRTLTQFHFLSWPAEGTPAS 847
Cdd:cd14597    73 MMTQEVEGGKIKCQRYWPEILGKTTMVDNrlqLTLVRmQQL--KNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQ 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907067839 848 TRPLLDFRRKVNKCYrgRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGVkEIDIAATLEHVRDQRPGLVRSKDQFEF 925
Cdd:cd14597   151 PEQLLTFISYMRHIH--KSGPIITHCSAGIGRSGTLICIDVVLGLISKDL-DFDISDIVRTMRLQRHGMVQTEDQYIF 225
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 660-934 1.36e-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: 191.07  E-value: 1.36e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 660 LAYMEDHLRNRD--RLAKEWQALCAYQAepNTCAAAQDESNIKKNRHPDFLPYDHARIKLKVESSPSRSDYINASpIIEH 737
Cdd:cd14625     9 LAEHTERLKANDnlKLSQEYESIDPGQQ--FTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINAN-YIDG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 738 DPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHVYEVNLVsEHIWCEDFLVRS 817
Cdd:cd14625    86 YRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRGTETYGMIQVTLL-DTIELATFCVRT 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 818 FYLKNLQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMaKGV 897
Cdd:cd14625   165 FSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVIDAMLERI-KHE 243

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1907067839 898 KEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAEEV 934
Cdd:cd14625   244 KTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAV 280
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 702-925 1.71e-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: 1.71e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 702 NRHPDFLPYDHARIKLKVESSPSRSDYINASpiiehdpRMPAY------IATQGPLSHTIADFWQMVWESGCTVIVMLTP 775
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINAN-------YMPGYwssqefIATQGPLPQTVGDFWRMIWEQQSSTIVMLTN 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 776 LVEDGVKQCDRYWP-DEGSSLYHVYEVNLVSEHIwCEDFLVRSFYLKNLQTQETRTLTQFHFLSWPAEGTPASTRPLLDF 854
Cdd:cd14619    74 CMEAGRVKCEHYWPlDYTPCTYGHLRVTVVSEEV-MENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAF 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907067839 855 RRKVNKCYRGR--SCPIIVHCSDGAGRTGTYILIDMVLNRMAKGvKEIDIAATLEHVRDQRPGLVRSKDQFEF 925
Cdd:cd14619   153 RRLLRQWLDQTmsGGPTVVHCSAGVGRTGTLIALDVLLQQLQSE-GLLGPFSFVQKMRENRPLMVQTESQYVF 224
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 702-925 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: 187.60  E-value: 4.40e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 702 NRHPDFLPYDHARIKLKVESSPSRSDYINASPIIEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGV 781
Cdd:cd14547     1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYDGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 782 KqCDRYWPDEGSSLYHVYEVnLVSEHIWCEDFLVRSFYLKNlqTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKC 861
Cdd:cd14547    81 K-CAQYWPEEENETYGDFEV-TVQSVKETDGYTVRKLTLKY--GGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEEA 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907067839 862 -YRGRSC-PIIVHCSDGAGRTGTYILIDMVLNRMAKGVKeIDIAATLEHVRDQRPGLVRSKDQFEF 925
Cdd:cd14547   157 rQTEPHRgPIVVHCSAGIGRTGCFIATSIGCQQLREEGV-VDVLGIVCQLRLDRGGMVQTAEQYEF 221
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 676-932 6.30e-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: 6.30e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 676 EWQALCAYQAEPNTCAAAQDESNIKKNRHPDFLPYDHARIKLKVESSPSRSDYINASpIIEHDPRMPAYIATQGPLSHTI 755
Cdd:cd14627    31 EFKRLANSKAHTSRFISANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINAS-FIDGYRQQKAYIATQGPLAETT 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 756 ADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHVYEVNLVSEHIWCEdFLVRSFYLKNLQTQETRTLTQFH 835
Cdd:cd14627   110 EDFWRMLWENNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQ-YILREFKVTDARDGQSRTVRQFQ 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 836 FLSWPAEGTPASTRPLLDFRRKVNKCYR--GRSCPIIVHCSDGAGRTGTYILIDMVLNRMA-KGVkeIDIAATLEHVRDQ 912
Cdd:cd14627   189 FTDWPEQGVPKSGEGFIDFIGQVHKTKEqfGQDGPISVHCSAGVGRTGVFITLSIVLERMRyEGV--VDIFQTVKMLRTQ 266

                         250       260
                  ....*....|....*....|
gi 1907067839 913 RPGLVRSKDQFEFALTAVAE 932
Cdd:cd14627   267 RPAMVQTEDEYQFCYQAALE 286
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 696-932 8.42e-54

catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350478 [Multi-domain]  Cd Length: 237  Bit Score: 187.16  E-value: 8.42e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 696 ESNIKKNRHPDFLPYDHARIKLKVESSPSRSDYINASPII-EHDPRMpaYIATQGPLSHTIADFWQMVWESGCTVIVMLT 774
Cdd:cd14630     1 DENRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDgYHRPRH--YIATQGPMQETVKDFWRMIWQENSASVVMVT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 775 PLVEDGVKQCDRYWPDEgSSLYHVYEVNLVSEHIWCEdFLVRSFYLKNLQTQETRTLTQFHFLSWPAEGTPASTRPLLDF 854
Cdd:cd14630    79 NLVEVGRVKCVRYWPDD-TEVYGDIKVTLIETEPLAE-YVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGF 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907067839 855 RRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNrMAKGVKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAE 932
Cdd:cd14630   157 VRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLD-MAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILE 233
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 676-932 1.28e-53

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


Pssm-ID: 350451 [Multi-domain]  Cd Length: 266  Bit Score: 187.73  E-value: 1.28e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 676 EWQALCAYQAEPNTCA--AAQDESNIKKNRHPDFLPYDHARIKLKVESSPSRSDYINASPIIEHDpRMPAYIATQGPLSH 753
Cdd:cd14603     6 EIRACSAAFKADYVCStvAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVD-GSRAYIATQGPLSH 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 754 TIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWP-DEGSSLYHVYEVNLVSEHIWCEDFLVRSFYLKnlQTQETRTLT 832
Cdd:cd14603    85 TVLDFWRMIWQYGVKVILMACREIEMGKKKCERYWAqEQEPLQTGPFTITLVKEKRLNEEVILRTLKVT--FQKESRSVS 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 833 QFHFLSWPAEGTPASTRPLLDFRRKVNKcYRGRS-CPIIVHCSDGAGRTGTYILIDMVLNRMAKGVKEIDIA---ATLEh 908
Cdd:cd14603   163 HFQYMAWPDHGIPDSPDCMLAMIELARR-LQGSGpEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPDFSifdVVLE- 240

                         250       260
                  ....*....|....*....|....
gi 1907067839 909 VRDQRPGLVRSKDQFEFALTAVAE 932
Cdd:cd14603   241 MRKQRPAAVQTEEQYEFLYHTVAQ 264
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 698-930 2.90e-53

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: 186.38  E-value: 2.90e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 698 NIKKNRHPDFLPYDHARIKLKvESSPSR--SDYINASPI-----IEHDPRMP--AYIATQGPLSHTIADFWQMVWESGCT 768
Cdd:cd14605     2 NKNKNRYKNILPFDHTRVVLH-DGDPNEpvSDYINANIImpefeTKCNNSKPkkSYIATQGCLQNTVNDFWRMVFQENSR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 769 VIVMLTPLVEDGVKQCDRYWPDEGS-SLYHVYEVNLVSEHIwCEDFLVRSFYLKNL-QTQETRTLTQFHFLSWPAEGTPA 846
Cdd:cd14605    81 VIVMTTKEVERGKSKCVKYWPDEYAlKEYGVMRVRNVKESA-AHDYILRELKLSKVgQGNTERTVWQYHFRTWPDHGVPS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 847 STRPLLDFRRKVNKCYRG--RSCPIIVHCSDGAGRTGTYILIDMVLNRM-AKGVK-EIDIAATLEHVRDQRPGLVRSKDQ 922
Cdd:cd14605   160 DPGGVLDFLEEVHHKQESimDAGPVVVHCSAGIGRTGTFIVIDILIDIIrEKGVDcDIDVPKTIQMVRSQRSGMVQTEAQ 239


                  ....*...
gi 1907067839 923 FEFALTAV 930
Cdd:cd14605   240 YRFIYMAV 247
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 701-932 2.90e-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: 185.81  E-value: 2.90e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 701 KNRHPDFLPYDHARIKLKVESSPSRSDYINASPIIE-HDPRmpAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVED 779
Cdd:cd14602     1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGvYGPR--AYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 780 GVKQCDRYWPDEGSSLYHVYEVNLVsehiwCE------DFLVRSfyLKNLQTQETRTLTQFHFLSWPAEGTPASTRPLLD 853
Cdd:cd14602    79 GKKKCERYWAEPGEMQLEFGPFSVT-----CEaekrksDYIIRT--LKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILE 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 854 FRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGV--KEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVA 931
Cdd:cd14602   152 LIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIipENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAVI 231


                  .
gi 1907067839 932 E 932
Cdd:cd14602   232 E 232
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 694-932 5.65e-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: 5.65e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 694 QDESNIKKNRHPDFLPYDHARIKLK-VESSPSRSDYINASPIIEH--DPRMPA--YIATQGPLSHTIADFWQMVWESGCT 768
Cdd:cd14606    14 QRPENKSKNRYKNILPFDHSRVILQgRDSNIPGSDYINANYVKNQllGPDENAktYIASQGCLEATVNDFWQMAWQENSR 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 769 VIVMLTPLVEDGVKQCDRYWPDEGSS-LYHVYEVNLVSEHIwCEDFLVRSFYLKNLQTQET-RTLTQFHFLSWPAEGTPA 846
Cdd:cd14606    94 VIVMTTREVEKGRNKCVPYWPEVGMQrAYGPYSVTNCGEHD-TTEYKLRTLQVSPLDNGELiREIWHYQYLSWPDHGVPS 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 847 STRPLLDFRRKVNKCYRG--RSCPIIVHCSDGAGRTGTYILIDMVLNRM-AKGVK-EIDIAATLEHVRDQRPGLVRSKDQ 922
Cdd:cd14606   173 EPGGVLSFLDQINQRQESlpHAGPIIVHCSAGIGRTGTIIVIDMLMENIsTKGLDcDIDIQKTIQMVRAQRSGMVQTEAQ 252

                         250
                  ....*....|
gi 1907067839 923 FEFALTAVAE 932
Cdd:cd14606   253 YKFIYVAIAQ 262
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 683-938 9.55e-53

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


Pssm-ID: 350456 [Multi-domain]  Cd Length: 277  Bit Score: 185.61  E-value: 9.55e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 683 YQAEPNTCAAAQDESNIKKNRHPDFLPYDHARIKLKVESSpsrsDYINASpIIEHDPRMPAYIATQGPLSHTIADFWQMV 762
Cdd:cd14608    10 HEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDN----DYINAS-LIKMEEAQRSYILTQGPLPNTCGHFWEMV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 763 WESGCTVIVMLTPLVEDGVKQCDRYWP--DEGSSLYH--VYEVNLVSEHIWCEdFLVRSFYLKNLQTQETRTLTQFHFLS 838
Cdd:cd14608    85 WEQKSRGVVMLNRVMEKGSLKCAQYWPqkEEKEMIFEdtNLKLTLISEDIKSY-YTVRQLELENLTTQETREILHFHYTT 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 839 WPAEGTPASTRPLLDFRRKVNK--CYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMA--KGVKEIDIAATLEHVRDQRP 914
Cdd:cd14608   164 WPDFGVPESPASFLNFLFKVREsgSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDkrKDPSSVDIKKVLLEMRKFRM 243

                         250       260
                  ....*....|....*....|....
gi 1907067839 915 GLVRSKDQFEFALTAVAEEVNAIL 938
Cdd:cd14608   244 GLIQTADQLRFSYLAVIEGAKFIM 267
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 728-925 2.98e-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: 181.47  E-value: 2.98e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 728 YINASpIIEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGSSL--YHVYEVNLVS 805
Cdd:cd14542     1 YINAN-FIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQlqFGPFKISLEK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 806 EHIWCEDFLVRSfyLKNLQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYIL 885
Cdd:cd14542    80 EKRVGPDFLIRT--LKVTFQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGCGRTGTICA 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1907067839 886 IDMVLNRMAKGV--KEIDIAATLEHVRDQRPGLVRSKDQFEF 925
Cdd:cd14542   158 IDYVWNLLKTGKipEEFSLFDLVREMRKQRPAMVQTKEQYEL 199
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 675-932 6.81e-52

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: 184.07  E-value: 6.81e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 675 KEWQAL--CAYQAepnTCAAAQDESNIKKNRHPDFLPYDHARIKLK-VESSPSrSDYINASPIIEHDPRmPAYIATQGPL 751
Cdd:cd14621    30 EEFNALpaCPIQA---TCEAASKEENKEKNRYVNILPYDHSRVHLTpVEGVPD-SDYINASFINGYQEK-NKFIAAQGPK 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 752 SHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHVYEVNlVSEHIWCEDFLVRSFYLKNL----QTQE 827
Cdd:cd14621   105 EETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGCWTYGNIRVS-VEDVTVLVDYTVRKFCIQQVgdvtNKKP 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 828 TRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNrMAKGVKEIDIAATLE 907
Cdd:cd14621   184 QRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVIDAMLD-MMHAERKVDVYGFVS 262

                         250       260
                  ....*....|....*....|....*
gi 1907067839 908 HVRDQRPGLVRSKDQFEFALTAVAE 932
Cdd:cd14621   263 RIRAQRCQMVQTDMQYVFIYQALLE 287
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 676-932 1.37e-51

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


Pssm-ID: 350477 [Multi-domain]  Cd Length: 291  Bit Score: 183.00  E-value: 1.37e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 676 EWQALCAYQAEPNTCAAAQDESNIKKNRHPDFLPYDHARIKLKVESSPSRSDYINASpIIEHDPRMPAYIATQGPLSHTI 755
Cdd:cd14629    31 EFKLLANSKAHTSRFISANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINAS-FIDGYRQQKAYIATQGPLAETT 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 756 ADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHVYEVNLVSEHIWCEdFLVRSFYLKNLQTQETRTLTQFH 835
Cdd:cd14629   110 EDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQ-YILREFKVTDARDGQSRTIRQFQ 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 836 FLSWPAEGTPASTRPLLDFRRKVNKCYR--GRSCPIIVHCSDGAGRTGTYILIDMVLNRMA-KGVkeIDIAATLEHVRDQ 912
Cdd:cd14629   189 FTDWPEQGVPKTGEGFIDFIGQVHKTKEqfGQDGPITVHCSAGVGRTGVFITLSIVLERMRyEGV--VDMFQTVKTLRTQ 266

                         250       260
                  ....*....|....*....|
gi 1907067839 913 RPGLVRSKDQFEFALTAVAE 932
Cdd:cd14629   267 RPAMVQTEDQYQLCYRAALE 286
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 728-925 2.62e-51

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


Pssm-ID: 350506 [Multi-domain]  Cd Length: 209  Bit Score: 179.40  E-value: 2.62e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 728 YINASPIIEHDpRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHVYEVNLVSEH 807
Cdd:cd17668     1 YINANYVDGYN-KPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 808 IWCEdFLVRSFYLKNLQT--------QETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGR 879
Cdd:cd17668    80 VLAY-YTVRNFTLRNTKIkkgsqkgrPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSAGVGR 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1907067839 880 TGTYILIDMVLNRMaKGVKEIDIAATLEHVRDQRPGLVRSKDQFEF 925
Cdd:cd17668   159 TGTYIVLDSMLQQI-QHEGTVNIFGFLKHIRSQRNYLVQTEEQYVF 203
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 728-930 3.10e-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: 178.62  E-value: 3.10e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 728 YINASpIIEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHVYEVNLVSEH 807
Cdd:cd14552     1 YINAS-FIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGSVSSGDITVELKDQT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 808 IwCEDFLVRSFYLKNLQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGR-SCPIIVHCSDGAGRTGTYILI 886
Cdd:cd14552    80 D-YEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSgNHPITVHCSAGAGRTGTFCAL 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1907067839 887 DMVLNRM-AKGVkeIDIAATLEHVRDQRPGLVRSKDQFEFALTAV 930
Cdd:cd14552   159 STVLERVkAEGV--LDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 675-932 1.59e-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: 179.47  E-value: 1.59e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 675 KEWQALCAYQAEPntCAAAQDESNIKKNRHPDFLPYDHARIKLKVESSPSRSDYINASpIIEHDPRMPAYIATQGPLSHT 754
Cdd:cd14633    19 EEYESFFEGQSAP--WDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGN-YIDGYHRPNHYIATQGPMQET 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 755 IADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEgSSLYHVYEVNLVSEHIWCEdFLVRSFYLKNLQTQETRTLTQF 834
Cdd:cd14633    96 IYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDD-TEIYKDIKVTLIETELLAE-YVIRTFAVEKRGVHEIREIRQF 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 835 HFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNrMAKGVKEIDIAATLEHVRDQRP 914
Cdd:cd14633   174 HFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLD-MAEREGVVDIYNCVRELRSRRV 252

                         250
                  ....*....|....*...
gi 1907067839 915 GLVRSKDQFEFALTAVAE 932
Cdd:cd14633   253 NMVQTEEQYVFIHDAILE 270
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 728-932 3.16e-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: 3.16e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 728 YINASPIiehdpRMPA------YIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHV--Y 799
Cdd:cd14596     1 YINASYI-----TMPVgeeelfYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELenY 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 800 EVNLVSEHIwCEDFLVRSFYLKNLQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYrgRSCPIIVHCSDGAGR 879
Cdd:cd14596    76 QLRLENYQA-LQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVH--NTGPIVVHCSAGIGR 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907067839 880 TGTYILIDMVLNRMAKGVkEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAE 932
Cdd:cd14596   153 AGVLICVDVLLSLIEKDL-SFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLE 204
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 728-925 3.37e-50

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: 175.66  E-value: 3.37e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 728 YINASPIIE-HDPRmpAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGSSlYHVYEVNLVSE 806
Cdd:cd14558     1 YINASFIDGyWGPK--SLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKT-YGDIEVELKDT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 807 HIwCEDFLVRSFYLKNLQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKV------NKCYRGRSCPIIVHCSDGAGRT 880
Cdd:cd14558    78 EK-SPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIkqklpyKNSKHGRSVPIVVHCSDGSSRT 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1907067839 881 GTYILIdmvLNRMAKGVKE--IDIAATLEHVRDQRPGLVRSKDQFEF 925
Cdd:cd14558   157 GIFCAL---WNLLESAETEkvVDVFQVVKALRKQRPGMVSTLEQYQF 200
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 704-932 3.69e-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: 176.67  E-value: 3.69e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 704 HPDFLPYDHARIKL-KVESSPSrSDYINASPIIEHDPRmPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVK 782
Cdd:cd14620     1 YPNILPYDHSRVILsQLDGIPC-SDYINASYIDGYKEK-NKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 783 QCDRYWPDEGSSLYHVYEVNlVSEHIWCEDFLVRSFYLKNLQT---QETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVN 859
Cdd:cd14620    79 KCYQYWPDQGCWTYGNIRVA-VEDCVVLVDYTIRKFCIQPQLPdgcKAPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVK 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907067839 860 KCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNrMAKGVKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAE 932
Cdd:cd14620   158 SVNPVHAGPIVVHCSAGVGRTGTFIVIDAMID-MMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 696-934 8.50e-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: 177.62  E-value: 8.50e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 696 ESNIKKNRHPDFLPYDHARIKLKVESSPSRSDYINASpIIEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTP 775
Cdd:cd14624    45 EVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINAN-YIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTK 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 776 LVEDGVKQCDRYWPDEGSSLYHVYEVNLVsEHIWCEDFLVRSFYLKNLQTQETRTLTQFHFLSWPAEGTPASTRPLLDFR 855
Cdd:cd14624   124 LEERSRVKCDQYWPSRGTETYGLIQVTLL-DTVELATYCVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFL 202

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907067839 856 RKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMaKGVKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAEEV 934
Cdd:cd14624   203 RRVKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERI-KHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAV 280
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 708-932 2.15e-49

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: 174.46  E-value: 2.15e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 708 LPYDHARIKLKVESSPSRSDYINASpIIEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRY 787
Cdd:cd14623     6 IPYEFNRVIIPVKRGEENTDYVNAS-FIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEKCAQY 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 788 WPDEGSSLYHVYEVNLVSEHiWCEDFLVRSFYLKNLQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGR-S 866
Cdd:cd14623    85 WPSDGSVSYGDITIELKKEE-ECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQQQSgN 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907067839 867 CPIIVHCSDGAGRTGTYILIDMVLNRM-AKGVkeIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAE 932
Cdd:cd14623   164 HPITVHCSAGAGRTGTFCALSTVLERVkAEGI--LDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 727-932 8.20e-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: 172.11  E-value: 8.20e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 727 DYINASpIIEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHVYEVNLVSE 806
Cdd:cd14622     1 DYINAS-FIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGSVTHGEITIEIKND 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 807 HIwCEDFLVRSFYLKNLQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGR-SCPIIVHCSDGAGRTGTYIL 885
Cdd:cd14622    80 TL-LETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQTgNHPIVVHCSAGAGRTGTFIA 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1907067839 886 IDMVLNRM-AKGVkeIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAE 932
Cdd:cd14622   159 LSNILERVkAEGL--LDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQD 204
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 693-930 3.98e-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: 172.07  E-value: 3.98e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 693 AQDESNIKKNRHPDFLPYDHARIKLKvessPSRSDYINASPI-IEHDPRmpAYIATQGPLSHTIADFWQMVWESGCTVIV 771
Cdd:cd14607    19 AKYPENRNRNRYRDVSPYDHSRVKLQ----NTENDYINASLVvIEEAQR--SYILTQGPLPNTCCHFWLMVWQQKTKAVV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 772 MLTPLVEDGVKQCDRYWPDEGSSLYHVYE----VNLVSEHIWCEdFLVRSFYLKNLQTQETRTLTQFHFLSWPAEGTPAS 847
Cdd:cd14607    93 MLNRIVEKDSVKCAQYWPTDEEEVLSFKEtgfsVKLLSEDVKSY-YTVHLLQLENINSGETRTISHFHYTTWPDFGVPES 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 848 TRPLLDFRRKV--NKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGVK-EIDIAATLEHVRDQRPGLVRSKDQFE 924
Cdd:cd14607   172 PASFLNFLFKVreSGSLSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDPdSVDIKQVLLDMRKYRMGLIQTPDQLR 251


                  ....*.
gi 1907067839 925 FALTAV 930
Cdd:cd14607   252 FSYMAV 257
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 683-930 6.62e-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: 6.62e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 683 YQAEPN---TCAaaQDESNIKKNRHPDFLPYDHARIKLKVESspsrsDYINASPIIEHDPRMP---AYIATQGPLSHTIA 756
Cdd:cd14600    24 YRKKPGlaiTCA--KLPQNMDKNRYKDVLPYDATRVVLQGNE-----DYINASYVNMEIPSANivnKYIATQGPLPHTCA 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 757 DFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGSSL-YHVYEVNLVSEHiwCE-DFLVRSFYLKNLQTQETRTLTQF 834
Cdd:cd14600    97 QFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDPPDVMeYGGFRVQCHSED--CTiAYVFREMLLTNTQTGEERTVTHL 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 835 HFLSWPAEGTPASTRPLLDFRRKVnKCYRGRSCPIIVHCSDGAGRTGTYILID--MVLNRMAKGVKEIDIAATLehvRDQ 912
Cdd:cd14600   175 QYVAWPDHGVPDDSSDFLEFVNYV-RSKRVENEPVLVHCSAGIGRTGVLVTMEtaMCLTERNQPVYPLDIVRKM---RDQ 250

                         250
                  ....*....|....*...
gi 1907067839 913 RPGLVRSKDQFEFALTAV 930
Cdd:cd14600   251 RAMMVQTSSQYKFVCEAI 268
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 702-925 4.20e-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: 168.20  E-value: 4.20e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 702 NRHPDFLPYDHARIKLKVESSPSRSDYINASpiiehdpRMPAY------IATQGPLSHTIADFWQMVWESGCTVIVMLTP 775
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINAN-------FIPGYtspqefIATQGPLKKTIEDFWRLVWEQQVCNIIMLTV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 776 LVEDGVKQCDRYWPDEGSSLYHVY-EVNLVSEHIwCEDFLVRSFYLKNLQTQETRTLTQFHFLSWPAEGTPASTRPLLDF 854
Cdd:cd14618    74 GMENGRVLCDHYWPSESTPVSYGHiTVHLLAQSS-EDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAF 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907067839 855 RRKVN---KCYRGRScPIIVHCSDGAGRTGTYILIDMVLNRMaKGVKEIDIAATLEHVRDQRPGLVRSKDQFEF 925
Cdd:cd14618   153 RELVRehvQATKGKG-PTLVHCSAGVGRSGTFIALDRLLRQL-KEEKVVDVFNTVYILRMHRYLMIQTLSQYIF 224
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 702-925 5.60e-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: 167.79  E-value: 5.60e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 702 NRHPDFLPYDHARIKLKVESSPSRSDYINASPIIEHDPRMpAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGV 781
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRR-EYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 782 KQCDRYWPDEGSSLYHV-YEVNLVSEHIWCEdFLVRSFYLKNL-QTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVN 859
Cdd:cd14617    80 VKCDHYWPADQDSLYYGdLIVQMLSESVLPE-WTIREFKICSEeQLDAPRLVRHFHYTVWPDHGVPETTQSLIQFVRTVR 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907067839 860 KcYRGRS---CPIIVHCSDGAGRTGTYILIDMVLNRMAKgVKEIDIAATLEHVRDQRPGLVRSKDQFEF 925
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, ...
 728-932 6.60e-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: 6.60e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 728 YINASPII-EHDPRMpaYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEgSSLYHVYEVNLVSE 806
Cdd:cd14555     1 YINANYIDgYHRPNH--YIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDD-TEVYGDIKVTLVET 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 807 HIWCEdFLVRSFYLKNLQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILI 886
Cdd:cd14555    78 EPLAE-YVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTGCYIVI 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1907067839 887 DMVLNrMAKGVKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAE 932
Cdd:cd14555   157 DIMLD-MAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 727-930 5.23e-46

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: 164.35  E-value: 5.23e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 727 DYINASPI---IEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPD-EGSSLYHVYEVN 802
Cdd:cd14601     1 DYINANYInmeIPSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEpSGSSSYGGFQVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 803 LVSEHiWCEDFLVRSFYLKNLQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGT 882
Cdd:cd14601    81 CHSEE-GNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVHCSAGIGRTGV 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907067839 883 YILID--MVLNRMAKGVKEIDIAATLehvRDQRPGLVRSKDQFEFALTAV 930
Cdd:cd14601   160 LITMEtaMCLIECNQPVYPLDIVRTM---RDQRAMMIQTPSQYRFVCEAI 206
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 719-932 1.00e-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: 163.65  E-value: 1.00e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 719 VESSPSrSDYINASpIIEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEgSSLYHV 798
Cdd:cd14631     7 VEDDPS-SDYINAN-YIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDD-TEVYGD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 799 YEVNLVS-EHIwcEDFLVRSFYLKNLQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGA 877
Cdd:cd14631    84 FKVTCVEmEPL--AEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCSAGA 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907067839 878 GRTGTYILIDMVLNrMAKGVKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAE 932
Cdd:cd14631   162 GRTGCYIVIDIMLD-MAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 728-925 2.04e-45

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


Pssm-ID: 350399 [Multi-domain]  Cd Length: 202  Bit Score: 162.39  E-value: 2.04e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 728 YINASPIIEHDPRmPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHVYEVNlVSEH 807
Cdd:cd14551     1 YINASYIDGYQEK-NKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCWTYGNLRVR-VEDT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 808 IWCEDFLVRSFYLK----NLQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTY 883
Cdd:cd14551    79 VVLVDYTTRKFCIQkvnrGIGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGRTGTF 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1907067839 884 ILIDMVLNrMAKGVKEIDIAATLEHVRDQRPGLVRSKDQFEF 925
Cdd:cd14551   159 IVIDAMLD-MMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVF 199
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 701-925 1.46e-43

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: 158.46  E-value: 1.46e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 701 KNRHPDFLPYDHARIKLKVE-SSPSRSDYINASPIIEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEd 779
Cdd:cd14612    18 KDRYKTILPNPQSRVCLRRAgSQEEEGSYINANYIRGYDGKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITKLKE- 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 780 GVKQCDRYWPDEGSSlYHVYE--VNLVSEhiwCEDFLVRSFYLKnlQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRK 857
Cdd:cd14612    97 KKEKCVHYWPEKEGT-YGRFEirVQDMKE---CDGYTIRDLTIQ--LEEESRSVKHYWFSSWPDHQTPESAGPLLRLVAE 170

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 858 VNKCYR--GRSCPIIVHCSDGAGRTGTYILIDMVLNRMaKGVKEIDIAATLEHVRDQRPGLVRSKDQFEF 925
Cdd:cd14612   171 VEESRQtaASPGPIVVHCSAGIGRTGCFIATSIGCQQL-KDTGKVDILGIVCQLRLDRGGMIQTSEQYQF 239
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 728-932 2.86e-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: 156.36  E-value: 2.86e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 728 YINASpIIEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEgSSLYHVYEVNLVSEH 807
Cdd:cd14632     1 YINAN-YIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDD-SDTYGDIKITLLKTE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 808 IWCEdFLVRSFYLKNLQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILID 887
Cdd:cd14632    79 TLAE-YSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYIVLD 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1907067839 888 MVLNrMAKGVKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAE 932
Cdd:cd14632   158 VMLD-MAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 699-925 4.14e-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: 157.72  E-value: 4.14e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 699 IKKNRHPDFLPYDHARIKLKVESSPS-RSDYINASPIIEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLV 777
Cdd:cd14613    26 VRKNRYKTILPNPHSRVCLTSPDQDDpLSSYINANYIRGYGGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIE 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 778 EDGVKqCDRYWPDEgSSLYHVYEVNlVSEHIWCEDFLVRSFYLKNlqTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRK 857
Cdd:cd14613   106 EMNEK-CTEYWPEE-QVTYEGIEIT-VKQVIHADDYRLRLITLKS--GGEERGLKHYWYTSWPDQKTPDNAPPLLQLVQE 180

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907067839 858 VN---KCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGVKeIDIAATLEHVRDQRPGLVRSKDQFEF 925
Cdd:cd14613   181 VEearQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGV-VDILRTTCQLRLDRGGMIQTCEQYQF 250
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 728-925 4.45e-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: 156.08  E-value: 4.45e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 728 YINASPI-IEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGSS----LYHVYEVN 802
Cdd:cd14540     1 YINASHItATVGGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGEhdalTFGEYKVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 803 LVSEHIwCEDFLVRSFYLKNLQTQETRTLTQFHFLSWPAEGTPASTRPLLDF-------RRKVNKCYRGRS--CPIIVHC 873
Cdd:cd14540    81 TKFSVS-SGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFleeinsvRRHTNQDVAGHNrnPPTLVHC 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907067839 874 SDGAGRTGTYILIDMVLNRMAKGVkEIDIAATLEHVRDQRPGLVRSKDQFEF 925
Cdd:cd14540   160 SAGVGRTGVVILADLMLYCLDHNE-ELDIPRVLALLRHQRMLLVQTLAQYKF 210
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 728-926 1.31e-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: 154.08  E-value: 1.31e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 728 YINASPIIEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDE-GSSL-YHVYEVNLVS 805
Cdd:cd14539     1 YINASLIEDLTPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTErGQALvYGAITVSLQS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 806 EH---IWCEdflvRSFYLKNLQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCY---RGRSCPIIVHCSDGAGR 879
Cdd:cd14539    81 VRttpTHVE----RIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYlqqRSLQTPIVVHCSSGVGR 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1907067839 880 TGTYILIDMVLNRMAKGVKEIDIAATLEHVRDQRPGLVRSKDQFEFA 926
Cdd:cd14539   157 TGAFCLLYAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFC 203
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 728-925 2.37e-42

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: 153.39  E-value: 2.37e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 728 YINASPIIEHD-PRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVeDGVK--QCDRYWPDEGSSLYHVYEVNLV 804
Cdd:cd17658     1 YINASLVETPAsESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLV-DNYStaKCADYFPAEENESREFGRISVT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 805 SEHIWCED--FLVRSFYLKNLQTQET-RTLTQFHFLSWPAEGTPASTRPLldfrRKVNKCYRG---RSCPIIVHCSDGAG 878
Cdd:cd17658    80 NKKLKHSQhsITLRVLEVQYIESEEPpLSVLHIQYPEWPDHGVPKDTRSV----RELLKRLYGippSAGPIVVHCSAGIG 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1907067839 879 RTGTYILIDMVLNRMAKG-VKEIDIAATLEHVRDQRPGLVRSKDQFEF 925
Cdd:cd17658   156 RTGAYCTIHNTIRRILEGdMSAVDLSKTVRKFRSQRIGMVQTQDQYIF 203
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 728-923 3.87e-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: 152.67  E-value: 3.87e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 728 YINASPIIEH-DPRmpAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWP--DEGSSLYHVYEVNLV 804
Cdd:cd14557     1 YINASYIDGFkEPR--KYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPsmEEGSRAFGDVVVKIN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 805 SEHIwCEDFLVRSFYLKNLQTQET-RTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTY 883
Cdd:cd14557    79 EEKI-CPDYIIRKLNINNKKEKGSgREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGTY 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1907067839 884 ILIDMVLNRM-AKGVkeIDIAATLEHVRDQRPGLVRSKDQF 923
Cdd:cd14557   158 IGIDAMLEGLeAEGR--VDVYGYVVKLRRQRCLMVQVEAQY 196
Receptor_IA-2 pfam11548
Protein-tyrosine phosphatase receptor IA-2; IA-2 is a protein-tyrosine phosphatase receptor ...
 433-521 4.35e-42

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


Pssm-ID: 463293  Cd Length: 89  Bit Score: 148.15  E-value: 4.35e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 433 EEYGYIVTDQKPLSLVAGVRLLEILAEHVHMSSGSFINISVVGPAVTFRIRHNEQNLSLADVTQQAGLVKSELEAQTGLQ 512
Cdd:pfam11548   1 EEYGYIVTDNDPLSWEEGLRLMEKVAELLHLPMSSFADIRVLGPAVTFKVRANNKNLTAADVAKAAVDIKDKLEKETGLK 80


                  ....*....
gi 1907067839 513 ILQTGVGQR 521
Cdd:pfam11548  81 ILQAGVGDK 89
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 701-925 6.06e-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: 153.15  E-value: 6.06e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 701 KNRHPDFLPYDHARIKLKVE-SSPSRSDYINASPIIEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVED 779
Cdd:cd14611     2 KNRYKTILPNPHSRVCLKPKnSNDSLSTYINANYIRGYGGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 780 GVKqCDRYWPdEGSSLYHVYE--VNLVSEhiwCEDFLVRSFYLKnlQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRK 857
Cdd:cd14611    82 NEK-CVLYWP-EKRGIYGKVEvlVNSVKE---CDNYTIRNLTLK--QGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLD 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907067839 858 VN---KCYRGRScPIIVHCSDGAGRTGTYILIDMVLNRMA-KGVkeIDIAATLEHVRDQRPGLVRSKDQFEF 925
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 ...
 728-925 2.19e-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: 150.64  E-value: 2.19e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 728 YINASPIIEHDPRmPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLvEDGVKQCDRYWPDEGSSLYHVYEVNLVSEH 807
Cdd:cd14556     1 YINAALLDSYKQP-AAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQL-DPKDQSCPQYWPDEGSGTYGPIQVEFVSTT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 808 IwCEDFLVRSFYLKN-LQTQE-TRTLTQFHFLSWPAEG-TPASTRPLLDFRRKVNK----CYRGrscPIIVHCSDGAGRT 880
Cdd:cd14556    79 I-DEDVISRIFRLQNtTRPQEgYRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVEKwqeqSGEG---PIVVHCLNGVGRS 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1907067839 881 GTYILIDMVLNRMaKGVKEIDIAATLEHVRDQRPGLVRSKDQFEF 925
Cdd:cd14556   155 GVFCAISSVCERI-KVENVVDVFQAVKTLRNHRPNMVETEEQYKF 198
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 702-925 4.54e-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: 147.75  E-value: 4.54e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 702 NRHPDFLPYDHARIKLKVESSPSRSDYINASPIIEHdpRMP-AYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDG 780
Cdd:cd14616     1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGY--LCPnEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 781 VKQCDRYWPDEGS--SLYHVYEVNLVSEHIWcEDFLVRSfyLKNLQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKV 858
Cdd:cd14616    79 RIRCHQYWPEDNKpvTVFGDIVITKLMEDVQ-IDWTIRD--LKIERHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLV 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907067839 859 NKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMaKGVKEIDIAATLEHVRDQRPGLVRSKDQFEF 925
Cdd:cd14616   156 RASRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHI-NDHDFVDIYGLVAELRSERMCMVQNLAQYIF 221
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 692-925 6.59e-40

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: 148.11  E-value: 6.59e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 692 AAQDESNIKKNRHPDFLPYDHARIKLKVESSPSRSDYINASPIIEHD-PRmpAYIATQGPLSHTIADFWQMVWESGCTVI 770
Cdd:cd14614     6 AADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNsPQ--EYIATQGPLPETRNDFWKMVLQQKSQII 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 771 VMLTPLVEDGVKQCDRYWP-DEGSSLYHVYEVNLVSEHiWCEDFLVRSFYLKnlQTQETRTLTQFHFLSWPAEGTPA--S 847
Cdd:cd14614    84 VMLTQCNEKRRVKCDHYWPfTEEPVAYGDITVEMLSEE-EQPDWAIREFRVS--YADEVQDVMHFNYTAWPDHGVPTanA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 848 TRPLLDF----RRKVNKcyrgRSCPIIVHCSDGAGRTGTYILIDmvlnRMAKGVKE---IDIAATLEHVRDQRPGLVRSK 920
Cdd:cd14614   161 AESILQFvqmvRQQAVK----SKGPMIIHCSAGVGRTGTFIALD----RLLQHIRDhefVDILGLVSEMRSYRMSMVQTE 232


                  ....*
gi 1907067839 921 DQFEF 925
Cdd:cd14614   233 EQYIF 237
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 689-925 2.10e-39

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 148.61  E-value: 2.10e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 689 TCAAAQDESNIKKNRHPDFLPYDHARIKLKVESSpSRSDYINASPI--IEHDPRmpaYIATQGPLSHTIADFWQMVWESG 766
Cdd:PHA02747   42 LIANFEKPENQPKNRYWDIPCWDHNRVILDSGGG-STSDYIHANWIdgFEDDKK---FIATQGPFAETCADFWKAVWQEH 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 767 CTVIVMLTPL-VEDGVKQCDRYW-PDEGSSL----YHVYEVNLVsehiwcedflVRSFYLKNL------QTQETRTLTQF 834
Cdd:PHA02747  118 CSIIVMLTPTkGTNGEEKCYQYWcLNEDGNIdmedFRIETLKTS----------VRAKYILTLieitdkILKDSRKISHF 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 835 HFLSWPAEGTPASTRPLLDF-------RRKVNKCYRGRS---CPIIVHCSDGAGRTGTYILIDMVLNRMAKgVKEIDIAA 904
Cdd:PHA02747  188 QCSEWFEDETPSDHPDFIKFikiidinRKKSGKLFNPKDallCPIVVHCSDGVGKTGIFCAVDICLNQLVK-RKAICLAK 266

                         250       260
                  ....*....|....*....|.
gi 1907067839 905 TLEHVRDQRPGLVRSKDQFEF 925
Cdd:PHA02747  267 TAEKIREQRHAGIMNFDDYLF 287
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 698-925 2.37e-38

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: 144.75  E-value: 2.37e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 698 NIKKNRHPDFLPYDHARIKLkVESSPSRSDYINASPI-IEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPL 776
Cdd:cd14599    38 NAERNRIREVVPYEENRVEL-VPTKENNTGYINASHIkVTVGGEEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAE 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 777 VEDGVKQCDRYWPDEG----SSLYHVYEVNL-VSEHIWCedFLVRSFYLKNLQTQETRTLTQFHFLSWPAEGTPASTRPL 851
Cdd:cd14599   117 EEGGRSKSHRYWPKLGskhsSATYGKFKVTTkFRTDSGC--YATTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEEVQGF 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 852 LDF-------RRKVNKCYRG-RSC--PIIVHCSDGAGRTGTYILIDMVLNRMAKGVKeIDIAATLEHVRDQRPGLVRSKD 921
Cdd:cd14599   195 LSYleeiqsvRRHTNSMLDStKNCnpPIVVHCSAGVGRTGVVILTELMIGCLEHNEK-VEVPVMLRHLREQRMFMIQTIA 273


                  ....
gi 1907067839 922 QFEF 925
Cdd:cd14599   274 QYKF 277
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 830-932 8.07e-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: 8.07e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839  830 TLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSC--PIIVHCSDGAGRTGTYILIDMVLNRMAKGVKEIDIAATLE 907
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESsgPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGEVDIFDTVK 80

                           90       100
                   ....*....|....*....|....*
gi 1907067839  908 HVRDQRPGLVRSKDQFEFALTAVAE 932
Cdd:smart00012  81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
830-932 8.07e-34

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 125.16  E-value: 8.07e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839  830 TLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSC--PIIVHCSDGAGRTGTYILIDMVLNRMAKGVKEIDIAATLE 907
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESsgPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGEVDIFDTVK 80

                           90       100
                   ....*....|....*....|....*
gi 1907067839  908 HVRDQRPGLVRSKDQFEFALTAVAE 932
Cdd:smart00404  81 ELRSQRPGMVQTEEQYLFLYRALLE 105
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 728-925 1.59e-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: 128.22  E-value: 1.59e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 728 YINASPIIEHdpRMPA-YIATQGPLSHTIADFWQMVWESGCTVIVMLTPLveDGVKQCDRYWPDEGSSLYHVYEVNLVSE 806
Cdd:cd14634     1 YINAALMDSH--KQPAaFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEM--DAAQLCMQYWPEKTSCCYGPIQVEFVSA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 807 HIwCEDFLVRSFYLKNLQTQET--RTLTQFHFLSWPA-EGTPASTRPLLDFRRKVNKC---YRGRSCPIIVHCSDGAGRT 880
Cdd:cd14634    77 DI-DEDIISRIFRICNMARPQDgyRIVQHLQYIGWPAyRDTPPSKRSILKVVRRLEKWqeqYDGREGRTVVHCLNGGGRS 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1907067839 881 GTYILIDMVlNRMAKGVKEIDIAATLEHVRDQRPGLVRSKDQFEF 925
Cdd:cd14634   156 GTFCAICSV-CEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKF 199
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
656-938 3.77e-33

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 129.83  E-value: 3.77e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 656 GHMILAYMEDHLRNRdrLAKEWQALcAYQAEPNTcaAAQDESNIKKNRHPDFLPYDHARIklkvesspsRSD--YINASP 733
Cdd:COG5599     5 NPIAIKSEEEKINSR--LSTLTNEL-APSHNDPQ--YLQNINGSPLNRFRDIQPYKETAL---------RANlgYLNANY 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 734 IIEHDPRMpaYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGV--KQCDRYWPDEGSslYHVYEV-NLVSEHIWC 810
Cdd:COG5599    71 IQVIGNHR--YIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEISKpkVKMPVYFRQDGE--YGKYEVsSELTESIQL 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 811 ED-FLVRSFYLKNLQT-QETRTLTQFHFLSWPAEGTPAST--RPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILI 886
Cdd:COG5599   147 RDgIEARTYVLTIKGTgQKKIEIPVLHVKNWPDHGAISAEalKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIAC 226

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907067839 887 dMVLNRMAKGVKEIDIAA--TLEHVRDQR-PGLVRSKDQFEFaLTAVAEEVNAIL 938
Cdd:COG5599   227 -LALSKSINALVQITLSVeeIVIDMRTSRnGGMVQTSEQLDV-LVKLAEQQIRPL 279
PHA02738 PHA02738
hypothetical protein; Provisional
 694-935 4.08e-33

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 130.82  E-value: 4.08e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 694 QDESNIKKNRHPDFLPYDHARIKLKVESSpsRSDYINASPI--IEHDPRmpaYIATQGPLSHTIADFWQMVWESGCTVIV 771
Cdd:PHA02738   45 AEKKNRKLNRYLDAVCFDHSRVILPAERN--RGDYINANYVdgFEYKKK---FICGQAPTRQTCYDFYRMLWMEHVQIIV 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 772 MLTPLVEDGVKQCDRYWPD-EGSSL-YHVYEVNLVSehiwCEDFL--VRSFYLKNLQTQETRTLTQFHFLSWPAEGTPAS 847
Cdd:PHA02738  120 MLCKKKENGREKCFPYWSDvEQGSIrFGKFKITTTQ----VETHPhyVKSTLLLTDGTSATQTVTHFNFTAWPDHDVPKN 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 848 TRPLLDFRRKVNKCY-------------RGRSCPIIVHCSDGAGRTGTYILIDMVLNRMaKGVKEIDIAATLEHVRDQRP 914
Cdd:PHA02738  196 TSEFLNFVLEVRQCQkelaqeslqighnRLQPPPIVVHCNAGLGRTPCYCVVDISISRF-DACATVSIPSIVSSIRNQRY 274

                         250       260
                  ....*....|....*....|.
gi 1907067839 915 GLVRSKDQFEFALTAVAEEVN 935
Cdd:PHA02738  275 YSLFIPFQYFFCYRAVKRYVN 295
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 728-925 2.76e-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: 2.76e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 728 YINASPIIEHDpRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGvkQCDRYWPDEGSSLYHV-YEVNLVSE 806
Cdd:cd14550     1 YINASYLQGYR-RSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWPTKEKPLECEtFKVTLSGE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 807 HIWC----EDFLVRSFYLKNlqTQETRTLT--QFHFLSWPAEGTPASTrpLLDFRRKVNKCYRGRSCPIIVHCSDGAGRT 880
Cdd:cd14550    78 DHSClsneIRLIVRDFILES--TQDDYVLEvrQFQCPSWPNPCSPIHT--VFELINTVQEWAQQRDGPIVVHDRYGGVQA 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1907067839 881 GTYILIdMVLNRMAKGVKEIDI--AATLEHVRdqRPGLVRSKDQFEF 925
Cdd:cd14550   154 ATFCAL-TTLHQQLEHESSVDVyqVAKLYHLM--RPGVFTSKEDYQF 197
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 728-925 3.54e-31

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: 122.01  E-value: 3.54e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 728 YINASPI------IEHDprmpaYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHV-YE 800
Cdd:cd14598     1 YINASHIkvtvggKEWD-----YIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLGSRHNTVtYG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 801 VNLVSEHIWCED--FLVRSFYLKNLQTQETRTLTQFHFLSWPAEGTPASTRPLLDF-------RRKVNKCY--RGRSCPI 869
Cdd:cd14598    76 RFKITTRFRTDSgcYATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYleeiqsvRRHTNSTIdpKSPNPPV 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907067839 870 IVHCSDGAGRTGTYILIDMVL-----NRMakgvkeIDIAATLEHVRDQRPGLVRSKDQFEF 925
Cdd:cd14598   156 LVHCSAGVGRTGVVILSEIMIaclehNEM------LDIPRVLDMLRQQRMMMVQTLSQYTF 210
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 687-925 3.93e-31

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 124.34  E-value: 3.93e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 687 PNTCAAAQDESNIKKNRHPDFLPYDHARIKLKVESSpsRSDYINASPIIEHDPRMpAYIATQGPLSHTIADFWQMVWESG 766
Cdd:PHA02742   41 AFSCNESLELKNMKKCRYPDAPCFDRNRVILKIEDG--GDDFINASYVDGHNAKG-RFICTQAPLEETALDFWQAIFQDQ 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 767 CTVIVMLTPLVEDGVKQCDRYW-PDEGSSLYHvYEVNLVSEHIwcEDFlvRSFYLKNLQTQETRT-----LTQFHFLSWP 840
Cdd:PHA02742  118 VRVIVMITKIMEDGKEACYPYWmPHERGKATH-GEFKIKTKKI--KSF--RNYAVTNLCLTDTNTgasldIKHFAYEDWP 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 841 AEGTPASTRPLLDFRRKVNKC-----------YRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGVKeIDIAATLEHV 909
Cdd:PHA02742  193 HGGLPRDPNKFLDFVLAVREAdlkadvdikgeNIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAI-IPLLSIVRDL 271

                         250
                  ....*....|....*.
gi 1907067839 910 RDQRPGLVRSKDQFEF 925
Cdd:PHA02742  272 RKQRHNCLSLPQQYIF 287
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 728-932 8.18e-30

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: 117.43  E-value: 8.18e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 728 YINASPIIEHdpRMPA-YIATQGPLSHTIADFWQMVWESGCTVIVMLTPLveDGVKQCDRYWPDEGSSLYHVYEVNLVSE 806
Cdd:cd14636     1 YINAALMDSY--RQPAaFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEV--DLAQGCPQYWPEEGMLRYGPIQVECMSC 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 807 HIWCeDFLVRSFYLKNL-QTQETRTLT-QFHFLSWPA-EGTPASTRPLLDFRRKVNK----CYRGRSCPIIvHCSDGAGR 879
Cdd:cd14636    77 SMDC-DVISRIFRICNLtRPQEGYLMVqQFQYLGWAShREVPGSKRSFLKLILQVEKwqeeCDEGEGRTII-HCLNGGGR 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907067839 880 TGTYILIDMVLnRMAKGVKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAE 932
Cdd:cd14636   155 SGMFCAISIVC-EMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 728-932 3.19e-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: 115.78  E-value: 3.19e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 728 YINASpIIEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVE-DGVKQCDRYWPDEGSSLYHVYEVNLVSE 806
Cdd:cd14637     1 YINAA-LTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQsNSAWPCLQYWPEPGLQQYGPMEVEFVSG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 807 HIwCEDFLVRSFYLKNL-QTQETRTLT-QFHFLSWPA-EGTPASTRPLLDFRRKVNK----CYRGRScpiIVHCSDGAGR 879
Cdd:cd14637    80 SA-DEDIVTRLFRVQNItRLQEGHLMVrHFQFLRWSAyRDTPDSKKAFLHLLASVEKwqreSGEGRT---VVHCLNGGGR 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907067839 880 TGTYILIDMVLNrMAKGVKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAE 932
Cdd:cd14637   156 SGTYCASAMILE-MIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 728-932 4.52e-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: 4.52e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 728 YINASpIIEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLveDGVKQCDRYWPDEGSSLYHVYEVNLVSEH 807
Cdd:cd14635     1 YINAA-LMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDV--DPAQLCPQYWPENGVHRHGPIQVEFVSAD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 808 IWcEDFLVRSFYLKNLQTQET--RTLTQFHFLSWPA-EGTPASTRPLLDFRRKVNKC---YRGRSCPIIVHCSDGAGRTG 881
Cdd:cd14635    78 LE-EDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMyRDTPVSKRSFLKLIRQVDKWqeeYNGGEGRTVVHCLNGGGRSG 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907067839 882 TYILIDMVLnRMAKGVKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAE 932
Cdd:cd14635   157 TFCAISIVC-EMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 698-930 2.42e-28

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 116.67  E-value: 2.42e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 698 NIKKNRHPDFLPYDHARI-------------------KLKVESSPSRSDYINASpIIEHDPRMPAYIATQGPLSHTIADF 758
Cdd:PHA02746   51 NLKKNRFHDIPCWDHSRVvinaheslkmfdvgdsdgkKIEVTSEDNAENYIHAN-FVDGFKEANKFICAQGPKEDTSEDF 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 759 WQMVWESGCTVIVMLTPlVEDGVKQCDRYW-PDEGSSLYHVYEVNLVSEHIWCEDFLVRSFYLKNLQTQETRTLTQFHFL 837
Cdd:PHA02746  130 FKLISEHESQVIVSLTD-IDDDDEKCFELWtKEEDSELAFGRFVAKILDIIEELSFTKTRLMITDKISDTSREIHHFWFP 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 838 SWPAEGTPASTRPLLDFRRKVNKcYRGR-----------SCPIIVHCSDGAGRTGTYILIDMVLNRMAKGvKEIDIAATL 906
Cdd:PHA02746  209 DWPDNGIPTGMAEFLELINKVNE-EQAElikqadndpqtLGPIVVHCSAGIGRAGTFCAIDNALEQLEKE-KEVCLGEIV 286

                         250       260
                  ....*....|....*....|....
gi 1907067839 907 EHVRDQRPGLVRSKDQFEFALTAV 930
Cdd:PHA02746  287 LKIRKQRHSSVFLPEQYAFCYKAL 310
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 728-930 1.79e-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: 1.79e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 728 YINASPIIEHDpRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCdRYWPDEGSSLY-HVYEVNLVSE 806
Cdd:cd17669     1 YINASYIMGYY-QSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEF-VYWPNKDEPINcETFKVTLIAE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 807 HIWC----EDFLVRSFYLKNLQTQETRTLTQFHFLSWPAEGTPAS-TRPLLDFrrkVNKCYRGRSCPIIVHCSDGAGRTG 881
Cdd:cd17669    79 EHKClsneEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISkTFELISI---IKEEAANRDGPMIVHDEHGGVTAG 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1907067839 882 TYILIDMVLNRMAKGvKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAV 930
Cdd:cd17669   156 TFCALTTLMHQLEKE-NSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAI 203
RESP18 pfam14948
RESP18 domain; This domain is found in the glucocorticoid-responsive protein regulated ...
 58-112 3.64e-18

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: 80.64  E-value: 3.64e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907067839  58 QGLSWHDDLTQHVISQEMERIPRLRPPEPHPRDRSGLVPRKPGPAG-------ELLTQGNPT 112
Cdd:pfam14948  34 QGLFWKDDLTQDVMTQKMEHISRLHPQDPCLKDGKAVFPTRTTGVRgkqeeklRLLFPKSPA 95
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 728-930 5.95e-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: 83.19  E-value: 5.95e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 728 YINASPIIEHdPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVML---TPLVEDGVKqcdrYWPDEGSSLY-HVYEVNL 803
Cdd:cd17670     1 YINASYIMGY-YRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpdnQGLAEDEFV----YWPSREESMNcEAFTVTL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 804 VSEHIWC----EDFLVRSFYLKNLQTQETRTLTQFHFLSWPAEGTP-ASTRPLLDFrrkVNKCYRGRSCPIIVHCSDGAG 878
Cdd:cd17670    76 ISKDRLClsneEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPiSSTFELINV---IKEEALTRDGPTIVHDEFGAV 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907067839 879 RTGTYILIdMVLNRMAKGVKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAV 930
Cdd:cd17670   153 SAGTLCAL-TTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAM 203
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 672-942 3.36e-14

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 74.23  E-value: 3.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 672 RLAKEWQALCAYQAEPNTCAAAQDESNIKK-NRHPDFLPYDHARIKLKVESSPSRSDYINAspiIEHDPRmpaYIATQGP 750
Cdd:PHA02740   26 CIIKEYRAIVPEHEDEANKACAQAENKAKDeNLALHITRLLHRRIKLFNDEKVLDARFVDG---YDFEQK---FICIINL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 751 LSHTIADFWQMVWESGCTVIVMLTPLVEdgvKQC-DRYWP-DEGS-SLYHVYEVNLVsEHIWCEDFLVRSFYLKNLQTQE 827
Cdd:PHA02740  100 CEDACDKFLQALSDNKVQIIVLISRHAD---KKCfNQFWSlKEGCvITSDKFQIETL-EIIIKPHFNLTLLSLTDKFGQA 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067839 828 tRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYR--------GRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKgVKE 899
Cdd:PHA02740  176 -QKISHFQYTAWPADGFSHDPDAFIDFFCNIDDLCAdlekhkadGKIAPIIIDCIDGISSSAVFCVFDICATEFDK-TGM 253

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1907067839 900 IDIAATLEHVRDQRPGLVRSKDQFEFALTAVAEEVNAILKALP 942
Cdd:PHA02740  254 LSIANALKKVRQKKYGCMNCLDDYVFCYHLIAAYLKEKFDILK 296
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 868-925 2.29e-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: 2.29e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907067839 868 PIIVHCSDGAGRTGTYILIDMVLNRMAKGVKEIDIaatlehVRDQRPGLVRSKDQFEF 925
Cdd:cd14504    84 AVLVHCLAGKGRTGTMLACYLVKTGKISAVDAINE------IRRIRPGSIETSEQEKF 135
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 844-915 4.03e-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: 4.03e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907067839 844 TPASTRPLLDFRRKVNKCYrgrsCPIIVHCSDGAGRTGTYILIDMVLnRMAKGVKEIdiaatLEHVRDQRPG 915
Cdd:cd14494    38 TLAMVDRFLEVLDQAEKPG----EPVLVHCKAGVGRTGTLVACYLVL-LGGMSAEEA-----VRIVRLIRPG 99
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
868-925 2.49e-03

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 39.18  E-value: 2.49e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907067839 868 PIIVHCSDGAGRTGTyILIdMVLnrMAKGVkeiDIAATLEHVRDQRPGLVRSKDQFEF 925
Cdd:COG2453    82 KVLVHCRGGIGRTGT-VAA-AYL--VLLGL---SAEEALARVRAARPGAVETPAQRAF 132
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 742-797 2.54e-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: 2.54e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907067839 742 PAYIATQGPLSHtIADFWQMVWESGCTVIVMLT-PLVEDGVKQCDRYWPDEGSSLYH 797
Cdd:cd14494     7 LRLIAGALPLSP-LEADSRFLKQLGVTTIVDLTlAMVDRFLEVLDQAEKPGEPVLVH 62
 
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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