UniProtKB - Q9Y2R2 (PTN22_HUMAN)
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- BLAST>sp|Q9Y2R2|PTN22_HUMAN Tyrosine-protein phosphatase non-receptor type 22 OS=Homo sapiens OX=9606 GN=PTPN22 PE=1 SV=2 MDQREILQKFLDEAQSKKITKEEFANEFLKLKRQSTKYKADKTYPTTVAEKPKNIKKNRY KDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEY SVLIIVMACMEYEMGKKKCERYWAEPGEMQLEFGPFSVSCEAEKRKSDYIIRTLKVKFNS ETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAI DYTWMLLKDGIIPENFSVFSLIREMRTQRPSLVQTQEQYELVYNAVLELFKRQMDVIRDK HSGTESQAKHCIPEKNHTLQADSYSPNLPKSTTKAAKMMNQQRTKMEIKESSSFDFRTSE ISAKEELVLHPAKSSTSFDFLELNYSFDKNADTTMKWQTKAFPIVGEPLQKHQSLDLGSL LFEGCSNSKPVNAAGRYFNSKVPITRTKSTPFELIQQRETKEVDSKENFSYLESQPHDSC FVEMQAQKVMHVSSAELNYSLPYDSKHQIRNASNVKHHDSSALGVYSYIPLVENPYFSSW PPSGTSSKMSLDLPEKQDGTVFPSSLLPTSSTSLFSYYNSHDSLSLNSPTNISSLLNQES AVLATAPRIDDEIPPPLPVRTPESFIVVEEAGEFSPNVPKSLSSAVKVKIGTSLEWGGTS EPKKFDDSVILRPSKSVKLRSPKSELHQDRSSPPPPLPERTLESFFLADEDCMQAQSIET YSTSYPDTMENSTSSKQTLKTPGKSFTRSKSLKILRNMKKSICNSCPPNKPAESVQSNNS SSFLNFGFANRFSKPKGPRNPPPTWNI
- Align
Tyrosine-protein phosphatase non-receptor type 22
PTPN22
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
6 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.9"Identification of substrates of human protein-tyrosine phosphatase PTPN22."
Wu J., Katrekar A., Honigberg L.A., Smith A.M., Conn M.T., Tang J., Jeffery D., Mortara K., Sampang J., Williams S.R., Buggy J., Clark J.M.
J. Biol. Chem. 281:11002-11010(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION. - Ref.12"The autoimmunity-associated gene PTPN22 potentiates toll-like receptor-driven, type 1 interferon-dependent immunity."
Wang Y., Shaked I., Stanford S.M., Zhou W., Curtsinger J.M., Mikulski Z., Shaheen Z.R., Cheng G., Sawatzke K., Campbell A.M., Auger J.L., Bilgic H., Shoyama F.M., Schmeling D.O., Balfour H.H. Jr., Hasegawa K., Chan A.C., Corbett J.A. , Binstadt B.A., Mescher M.F., Ley K., Bottini N., Peterson E.J.
Immunity 39:111-122(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH TRAF3. - Ref.14"Protein tyrosine phosphatase non-receptor type 22 modulates NOD2-induced cytokine release and autophagy."
Spalinger M.R., Lang S., Vavricka S.R., Fried M., Rogler G., Scharl M.
PLoS ONE 8:E72384-E72384(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION. - Ref.15"Structure, inhibitor, and regulatory mechanism of Lyp, a lymphoid-specific tyrosine phosphatase implicated in autoimmune diseases."
Yu X., Sun J.P., He Y., Guo X., Liu S., Zhou B., Hudmon A., Zhang Z.Y.
Proc. Natl. Acad. Sci. U.S.A. 104:19767-19772(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-294 IN COMPLEX WITH INHIBITOR, FUNCTION, PHOSPHORYLATION AT SER-35, MUTAGENESIS OF SER-35 AND THR-36. - Ref.17"Large-scale structural analysis of the classical human protein tyrosine phosphatome."
Barr A.J., Ugochukwu E., Lee W.H., King O.N.F., Filippakopoulos P., Alfano I., Savitsky P., Burgess-Brown N.A., Mueller S., Knapp S.
Cell 136:352-363(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-302, FUNCTION. - Ref.20"Substrate specificity of lymphoid-specific tyrosine phosphatase (Lyp) and identification of Src kinase-associated protein of 55 kDa homolog (SKAP-HOM) as a Lyp substrate."
Yu X., Chen M., Zhang S., Yu Z.H., Sun J.P., Wang L., Liu S., Imasaki T., Takagi Y., Zhang Z.Y.
J. Biol. Chem. 286:30526-30534(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-294 OF MUTANT SER-227 ALONE AND IN COMPLEX WITH SKAP2 PEPTIDE, SUBSTRATE SPECIFICITY, FUNCTION.
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. the chemical reaction it catalyzes. This information usually correlates with the presence of an EC (Enzyme Commission) number in the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi
1 Publication<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.20"Substrate specificity of lymphoid-specific tyrosine phosphatase (Lyp) and identification of Src kinase-associated protein of 55 kDa homolog (SKAP-HOM) as a Lyp substrate."
Yu X., Chen M., Zhang S., Yu Z.H., Sun J.P., Wang L., Liu S., Imasaki T., Takagi Y., Zhang Z.Y.
J. Biol. Chem. 286:30526-30534(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-294 OF MUTANT SER-227 ALONE AND IN COMPLEX WITH SKAP2 PEPTIDE, SUBSTRATE SPECIFICITY, FUNCTION.
<p>This subsection of the ‘Function’ section describes an enzyme regulatory mechanism and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/enzyme_regulation' target='_top'>More...</a></p>Enzyme regulationi
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 195 | SubstrateBy similarity | 1 | |
| <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 227 | Phosphocysteine intermediatePROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi | 1 | |
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 274 | Substrate1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- kinase binding Source: BHF-UCL
- phosphatase activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- protein tyrosine phosphatase activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- SH3 domain binding Source: BHF-UCL
- ubiquitin protein ligase binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi
- autophagy Source: UniProtKB-KW
- cellular response to muramyl dipeptide Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- lipopolysaccharide-mediated signaling pathway Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- negative regulation of autophagy Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- negative regulation of gene expression Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- negative regulation of interleukin-6 secretion Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- negative regulation of interleukin-8 secretion Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- negative regulation of JUN kinase activity Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- negative regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- negative regulation of p38MAPK cascade Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- negative regulation of T cell activation Source: BHF-UCL <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- negative regulation of T cell receptor signaling pathway Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- negative regulation of tumor necrosis factor production Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- phosphoanandamide dephosphorylation Source: BHF-UCL
- positive regulation of ERK1 and ERK2 cascade Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- positive regulation of gene expression Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- positive regulation of interferon-gamma secretion Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- positive regulation of protein K63-linked ubiquitination Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- positive regulation of toll-like receptor 3 signaling pathway Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- positive regulation of toll-like receptor 4 signaling pathway Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- positive regulation of type I interferon production Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- protein dephosphorylation Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- regulation of B cell receptor signaling pathway Source: BHF-UCL <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p> Non-traceable author statementi
- regulation of innate immune response Source: BHF-UCL <p>Inferred by Curator</p> <p>Used for cases where an annotation is not supported by any evidence but can be reasonably inferred by a curator from other GO annotations for which evidence <br />is available.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ic">GO evidence code guide</a></p> Inferred by curatori
- regulation of natural killer cell proliferation Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- regulation of NIK/NF-kappaB signaling Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- response to lipopolysaccharide Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- T cell differentiation Source: BHF-UCL
- T cell receptor signaling pathway Source: Reactome
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | Hydrolase, Protein phosphatase |
| Biological process | Autophagy, Immunity |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 3.1.3.48 2681 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-202427 Phosphorylation of CD3 and TCR zeta chains R-HSA-202430 Translocation of ZAP-70 to Immunological synapse |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | Q9Y2R2 |
SIGNOR Signaling Network Open Resource More...SIGNORi | Q9Y2R2 |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Tyrosine-protein phosphatase non-receptor type 22 (EC:3.1.3.481 Publication<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
Alternative name(s): Hematopoietic cell protein-tyrosine phosphatase 70Z-PEP Lymphoid phosphatase Short name: LyP PEST-domain phosphatase Short name: PEP |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:PTPN22 Synonyms:PTPN8 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Homo sapiens (Human) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 9606 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000134242.15 |
Human Gene Nomenclature Database More...HGNCi | HGNC:9652 PTPN22 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 600716 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q9Y2R2 |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Other locations
- Cytoplasm By similarity
Cytosol
- cytosol Source: Reactome
Nucleus
- nucleus Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
Plasma Membrane
- cytoplasmic side of plasma membrane Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
Other locations
- cytoplasm Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- perinuclear region of cytoplasm Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti
Cytoplasm<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei
Systemic lupus erythematosus (SLE)1 Publication
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More...</a></p>
Manual assertion based on experiment ini
- Ref.22"Genetic association of the R620W polymorphism of protein tyrosine phosphatase PTPN22 with human SLE."
Kyogoku C., Langefeld C.D., Ortmann W.A., Lee A., Selby S., Carlton V.E.H., Chang M., Ramos P., Baechler E.C., Batliwalla F.M., Novitzke J., Williams A.H., Gillett C., Rodine P., Graham R.R., Ardlie K.G., Gaffney P.M., Moser K.L. , Petri M., Begovich A.B., Gregersen P.K., Behrens T.W.
Am. J. Hum. Genet. 75:504-507(2004) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT SLE TRP-620.
Kyogoku C., Langefeld C.D., Ortmann W.A., Lee A., Selby S., Carlton V.E.H., Chang M., Ramos P., Baechler E.C., Batliwalla F.M., Novitzke J., Williams A.H., Gillett C., Rodine P., Graham R.R., Ardlie K.G., Gaffney P.M., Moser K.L. , Petri M., Begovich A.B., Gregersen P.K., Behrens T.W.
Am. J. Hum. Genet. 75:504-507(2004) [PubMed] [Europe PMC] [Abstract]
Diabetes mellitus, insulin-dependent (IDDM)1 Publication
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More...</a></p>
Manual assertion based on experiment ini
- Ref.23"A functional variant of lymphoid tyrosine phosphatase is associated with type I diabetes."
Bottini N., Musumeci L., Alonso A., Rahmouni S., Nika K., Rostamkhani M., MacMurray J., Meloni G.F., Lucarelli P., Pellecchia M., Eisenbarth G.S., Comings D., Mustelin T.
Nat. Genet. 36:337-338(2004) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT IDDM TRP-620, CHARACTERIZATION OF VARIANT IDDM TRP-620.
Bottini N., Musumeci L., Alonso A., Rahmouni S., Nika K., Rostamkhani M., MacMurray J., Meloni G.F., Lucarelli P., Pellecchia M., Eisenbarth G.S., Comings D., Mustelin T.
Nat. Genet. 36:337-338(2004) [PubMed] [Europe PMC] [Abstract]
Rheumatoid arthritis (RA)1 Publication
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More...</a></p>
Manual assertion based on experiment ini
- Ref.21"A missense single-nucleotide polymorphism in a gene encoding a protein tyrosine phosphatase (PTPN22) is associated with rheumatoid arthritis."
Begovich A.B., Carlton V.E., Honigberg L.A., Schrodi S.J., Chokkalingam A.P., Alexander H.C., Ardlie K.G., Huang Q., Smith A.M., Spoerke J.M., Conn M.T., Chang M., Chang S.Y., Saiki R.K., Catanese J.J., Leong D.U., Garcia V.E., McAllister L.B. , Jeffery D.A., Lee A.T., Batliwalla F., Remmers E., Criswell L.A., Seldin M.F., Kastner D.L., Amos C.I., Sninsky J.J., Gregersen P.K.
Am. J. Hum. Genet. 75:330-337(2004) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT RA TRP-620, INTERACTION WITH CSK, TISSUE SPECIFICITY.
Begovich A.B., Carlton V.E., Honigberg L.A., Schrodi S.J., Chokkalingam A.P., Alexander H.C., Ardlie K.G., Huang Q., Smith A.M., Spoerke J.M., Conn M.T., Chang M., Chang S.Y., Saiki R.K., Catanese J.J., Leong D.U., Garcia V.E., McAllister L.B. , Jeffery D.A., Lee A.T., Batliwalla F., Remmers E., Criswell L.A., Seldin M.F., Kastner D.L., Amos C.I., Sninsky J.J., Gregersen P.K.
Am. J. Hum. Genet. 75:330-337(2004) [PubMed] [Europe PMC] [Abstract]
Vitiligo (VTLG)1 Publication
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More...</a></p>
Manual assertion based on experiment ini
- Ref.26"A single-nucleotide polymorphism in the gene encoding lymphoid protein tyrosine phosphatase (PTPN22) confers susceptibility to generalised vitiligo."
Canton I., Akhtar S., Gavalas N.G., Gawkrodger D.J., Blomhoff A., Watson P.F., Weetman A.P., Kemp E.H.
Genes Immun. 6:584-587(2005) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT VTLG TRP-620.
Canton I., Akhtar S., Gavalas N.G., Gawkrodger D.J., Blomhoff A., Watson P.F., Weetman A.P., Kemp E.H.
Genes Immun. 6:584-587(2005) [PubMed] [Europe PMC] [Abstract]
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 35 | S → E: Loss of phosphorylation by PKC/PRKCD. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 36 | T → E: No effect on phosphorylation by PKC/PRKCD. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 129 | C → S: Decreases activity 2 fold. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 231 | C → S: Decreases activity 7 fold. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Diseasei
Diabetes mellitus, Disease mutation, Systemic lupus erythematosusOrganism-specific databases
DisGeNET More...DisGeNETi | 26191 |
MalaCards human disease database More...MalaCardsi | PTPN22 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 152700 phenotype 180300 phenotype 193200 phenotype 222100 phenotype |
Open Targets More...OpenTargetsi | ENSG00000134242 |
Orphanet; a database dedicated to information on rare diseases and orphan drugs More...Orphaneti | 397 Giant cell arteritis 900 Granulomatosis with polyangiitis 85408 Juvenile rheumatoid factor-negative polyarthritis 85410 Oligoarticular juvenile arthritis 93552 Pediatric systemic lupus erythematosus 536 Systemic lupus erythematosus 3437 Vogt-Koyanagi-Harada disease |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA33995 |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL2889 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | PTPN22 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 20139861 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000094775 | 1 – 807 | Tyrosine-protein phosphatase non-receptor type 22Add BLAST | 807 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 35 | Phosphoserine; by PKC/PRKCD1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 129 ↔ 227 | 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 449 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 635 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 684 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 692 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 |
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.15"Structure, inhibitor, and regulatory mechanism of Lyp, a lymphoid-specific tyrosine phosphatase implicated in autoimmune diseases."
Yu X., Sun J.P., He Y., Guo X., Liu S., Zhou B., Hudmon A., Zhang Z.Y.
Proc. Natl. Acad. Sci. U.S.A. 104:19767-19772(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-294 IN COMPLEX WITH INHIBITOR, FUNCTION, PHOSPHORYLATION AT SER-35, MUTAGENESIS OF SER-35 AND THR-36.
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - PTMi
Disulfide bond, PhosphoproteinProteomic databases
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q9Y2R2 |
PeptideAtlas More...PeptideAtlasi | Q9Y2R2 |
PRoteomics IDEntifications database More...PRIDEi | Q9Y2R2 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 85874 85875 [Q9Y2R2-2] 85876 [Q9Y2R2-3] 85877 [Q9Y2R2-4] 85878 [Q9Y2R2-5] |
PTM databases
DEPOD human dephosphorylation database More...DEPODi | Q9Y2R2 |
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q9Y2R2 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q9Y2R2 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.21"A missense single-nucleotide polymorphism in a gene encoding a protein tyrosine phosphatase (PTPN22) is associated with rheumatoid arthritis."
Begovich A.B., Carlton V.E., Honigberg L.A., Schrodi S.J., Chokkalingam A.P., Alexander H.C., Ardlie K.G., Huang Q., Smith A.M., Spoerke J.M., Conn M.T., Chang M., Chang S.Y., Saiki R.K., Catanese J.J., Leong D.U., Garcia V.E., McAllister L.B. , Jeffery D.A., Lee A.T., Batliwalla F., Remmers E., Criswell L.A., Seldin M.F., Kastner D.L., Amos C.I., Sninsky J.J., Gregersen P.K.
Am. J. Hum. Genet. 75:330-337(2004) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT RA TRP-620, INTERACTION WITH CSK, TISSUE SPECIFICITY.
<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.14"Protein tyrosine phosphatase non-receptor type 22 modulates NOD2-induced cytokine release and autophagy."
Spalinger M.R., Lang S., Vavricka S.R., Fried M., Rogler G., Scharl M.
PLoS ONE 8:E72384-E72384(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000134242 |
CleanEx database of gene expression profiles More...CleanExi | HS_PTPN22 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q9Y2R2 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q9Y2R2 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | CAB012209 HPA004912 HPA013350 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
6 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"Cloning and characterization of a lymphoid-specific, inducible human protein tyrosine phosphatase, Lyp."
Cohen S., Dadi H., Shaoul E., Sharfe N., Roifman C.M.
Blood 93:2013-2024(1999) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), INTERACTION WITH CBL. - Ref.12"The autoimmunity-associated gene PTPN22 potentiates toll-like receptor-driven, type 1 interferon-dependent immunity."
Wang Y., Shaked I., Stanford S.M., Zhou W., Curtsinger J.M., Mikulski Z., Shaheen Z.R., Cheng G., Sawatzke K., Campbell A.M., Auger J.L., Bilgic H., Shoyama F.M., Schmeling D.O., Balfour H.H. Jr., Hasegawa K., Chan A.C., Corbett J.A. , Binstadt B.A., Mescher M.F., Ley K., Bottini N., Peterson E.J.
Immunity 39:111-122(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH TRAF3. - Ref.15"Structure, inhibitor, and regulatory mechanism of Lyp, a lymphoid-specific tyrosine phosphatase implicated in autoimmune diseases."
Yu X., Sun J.P., He Y., Guo X., Liu S., Zhou B., Hudmon A., Zhang Z.Y.
Proc. Natl. Acad. Sci. U.S.A. 104:19767-19772(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-294 IN COMPLEX WITH INHIBITOR, FUNCTION, PHOSPHORYLATION AT SER-35, MUTAGENESIS OF SER-35 AND THR-36. - Ref.19"Lyp/PTPN22 phosphatase domain: substrate recognition and specificity for Src family kinases."
Seidel R.D., Love J., Piserchio A., Cowburn D.
Submitted (DEC-2009) to the PDB data bankCited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-310 IN COMPLEX WITH SUBSTRATE. - Ref.20"Substrate specificity of lymphoid-specific tyrosine phosphatase (Lyp) and identification of Src kinase-associated protein of 55 kDa homolog (SKAP-HOM) as a Lyp substrate."
Yu X., Chen M., Zhang S., Yu Z.H., Sun J.P., Wang L., Liu S., Imasaki T., Takagi Y., Zhang Z.Y.
J. Biol. Chem. 286:30526-30534(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-294 OF MUTANT SER-227 ALONE AND IN COMPLEX WITH SKAP2 PEPTIDE, SUBSTRATE SPECIFICITY, FUNCTION. - Ref.21"A missense single-nucleotide polymorphism in a gene encoding a protein tyrosine phosphatase (PTPN22) is associated with rheumatoid arthritis."
Begovich A.B., Carlton V.E., Honigberg L.A., Schrodi S.J., Chokkalingam A.P., Alexander H.C., Ardlie K.G., Huang Q., Smith A.M., Spoerke J.M., Conn M.T., Chang M., Chang S.Y., Saiki R.K., Catanese J.J., Leong D.U., Garcia V.E., McAllister L.B. , Jeffery D.A., Lee A.T., Batliwalla F., Remmers E., Criswell L.A., Seldin M.F., Kastner D.L., Amos C.I., Sninsky J.J., Gregersen P.K.
Am. J. Hum. Genet. 75:330-337(2004) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT RA TRP-620, INTERACTION WITH CSK, TISSUE SPECIFICITY.
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
| With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| CD247 | P20963 | 4 | EBI-1211241,EBI-1165705 | |
| EGFR | P00533 | 2 | EBI-1211241,EBI-297353 | |
| GRB2 | P62993 | 2 | EBI-1211241,EBI-401755 | |
| LCK | P06239 | 6 | EBI-1211241,EBI-1348 | |
| PSTPIP1 | O43586 | 6 | EBI-1211241,EBI-1050964 | |
| SKAP2 | O75563 | 3 | EBI-1211241,EBI-2483161 | |
| Skap2 | Q3UND0 | 2 | EBI-1211241,EBI-642769 | From Mus musculus. |
| TRAF3 | Q13114 | 2 | EBI-1211241,EBI-357631 | |
| Traf3 | Q60803 | 5 | EBI-1211241,EBI-520135 | From Mus musculus. |
| ZAP70 | P43403 | 4 | EBI-1211241,EBI-1211276 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- kinase binding Source: BHF-UCL
- SH3 domain binding Source: BHF-UCL
- ubiquitin protein ligase binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 117604, 46 interactors |
Database of interacting proteins More...DIPi | DIP-29953N |
Protein interaction database and analysis system More...IntActi | Q9Y2R2, 24 interactors |
Molecular INTeraction database More...MINTi | Q9Y2R2 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000352833 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | Q9Y2R2 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 3 – 16 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 14 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 21 – 40 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 20 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 47 – 50 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 52 – 55 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 59 – 62 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 67 – 69 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 70 – 72 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 80 – 83 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 86 – 92 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 95 – 102 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 107 – 109 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 110 – 119 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 124 – 127 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 131 – 133 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 135 – 137 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 146 – 148 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 151 – 153 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 156 – 165 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 167 – 178 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 181 – 190 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 195 – 197 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 199 – 202 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 203 – 215 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 218 – 221 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 223 – 226 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 228 – 232 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 233 – 248 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 16 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 258 – 266 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 276 – 301 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 26 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 2P6X | X-ray | 1.90 | A/B | 1-302 | [»] | |
| 2QCJ | X-ray | 3.00 | A/B | 1-294 | [»] | |
| 2QCT | X-ray | 2.80 | A/B | 1-294 | [»] | |
| 3BRH | X-ray | 2.20 | A/B | 1-310 | [»] | |
| 3H2X | X-ray | 2.20 | A | 1-302 | [»] | |
| 3OLR | X-ray | 2.50 | A/B/C/D | 1-294 | [»] | |
| 3OMH | X-ray | 2.90 | A/B/C/D | 1-294 | [»] | |
| 4J51 | X-ray | 2.30 | A/B | 1-303 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q9Y2R2 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q9Y2R2 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q9Y2R2 |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Domains and Repeats
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 24 – 289 | Tyrosine-protein phosphatasePROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 266 |
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 227 – 233 | Substrate binding | 7 |
<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0789 Eukaryota COG5599 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00900000140785 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG103877 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q9Y2R2 |
KEGG Orthology (KO) More...KOi | K18024 |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q9Y2R2 |
TreeFam database of animal gene trees More...TreeFami | TF351977 |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.90.190.10, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR029021 Prot-tyrosine_phosphatase-like IPR000242 PTPase_domain IPR016276 PTPN22 IPR016130 Tyr_Pase_AS IPR003595 Tyr_Pase_cat IPR000387 TYR_PHOSPHATASE_dom |
Pfam protein domain database More...Pfami | View protein in Pfam PF00102 Y_phosphatase, 1 hit |
PIRSF; a whole-protein classification database More...PIRSFi | PIRSF000930 PTPN8_PTPN22, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00700 PRTYPHPHTASE |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00194 PTPc, 1 hit SM00404 PTPc_motif, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF52799 SSF52799, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00383 TYR_PHOSPHATASE_1, 1 hit PS50056 TYR_PHOSPHATASE_2, 1 hit PS50055 TYR_PHOSPHATASE_PTP, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (6)i
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
This entry describes 6 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basketAdded to basket
This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
10 20 30 40 50
MDQREILQKF LDEAQSKKIT KEEFANEFLK LKRQSTKYKA DKTYPTTVAE
60 70 80 90 100
KPKNIKKNRY KDILPYDYSR VELSLITSDE DSSYINANFI KGVYGPKAYI
110 120 130 140 150
ATQGPLSTTL LDFWRMIWEY SVLIIVMACM EYEMGKKKCE RYWAEPGEMQ
160 170 180 190 200
LEFGPFSVSC EAEKRKSDYI IRTLKVKFNS ETRTIYQFHY KNWPDHDVPS
210 220 230 240 250
SIDPILELIW DVRCYQEDDS VPICIHCSAG CGRTGVICAI DYTWMLLKDG
260 270 280 290 300
IIPENFSVFS LIREMRTQRP SLVQTQEQYE LVYNAVLELF KRQMDVIRDK
310 320 330 340 350
HSGTESQAKH CIPEKNHTLQ ADSYSPNLPK STTKAAKMMN QQRTKMEIKE
360 370 380 390 400
SSSFDFRTSE ISAKEELVLH PAKSSTSFDF LELNYSFDKN ADTTMKWQTK
410 420 430 440 450
AFPIVGEPLQ KHQSLDLGSL LFEGCSNSKP VNAAGRYFNS KVPITRTKST
460 470 480 490 500
PFELIQQRET KEVDSKENFS YLESQPHDSC FVEMQAQKVM HVSSAELNYS
510 520 530 540 550
LPYDSKHQIR NASNVKHHDS SALGVYSYIP LVENPYFSSW PPSGTSSKMS
560 570 580 590 600
LDLPEKQDGT VFPSSLLPTS STSLFSYYNS HDSLSLNSPT NISSLLNQES
610 620 630 640 650
AVLATAPRID DEIPPPLPVR TPESFIVVEE AGEFSPNVPK SLSSAVKVKI
660 670 680 690 700
GTSLEWGGTS EPKKFDDSVI LRPSKSVKLR SPKSELHQDR SSPPPPLPER
710 720 730 740 750
TLESFFLADE DCMQAQSIET YSTSYPDTME NSTSSKQTLK TPGKSFTRSK
760 770 780 790 800
SLKILRNMKK SICNSCPPNK PAESVQSNNS SSFLNFGFAN RFSKPKGPRN
PPPTWNI
The sequence of this isoform differs from the canonical sequence as follows:
685-807: ELHQDRSSPP...PRNPPPTWNI → GKNFSWL
10 20 30 40 50
MDQREILQKF LDEAQSKKIT KEEFANEFLK LKRQSTKYKA DKTYPTTVAE
60 70 80 90 100
KPKNIKKNRY KDILPYDYSR VELSLITSDE DSSYINANFI KGVYGPKAYI
110 120 130 140 150
ATQGPLSTTL LDFWRMIWEY SVLIIVMACM EYEMGKKKCE RYWAEPGEMQ
160 170 180 190 200
LEFGPFSVSC EAEKRKSDYI IRTLKVKFNS ETRTIYQFHY KNWPDHDVPS
210 220 230 240 250
SIDPILELIW DVRCYQEDDS VPICIHCSAG CGRTGVICAI DYTWMLLKDG
260 270 280 290 300
IIPENFSVFS LIREMRTQRP SLVQTQEQYE LVYNAVLELF KRQMDVIRDK
310 320 330 340 350
HSGTESQAKH CIPEKNHTLQ ADSYSPNLPK STTKAAKMMN QQRTKMEIKE
360 370 380 390 400
SSSFDFRTSE ISAKEELVLH PAKSSTSFDF LELNYSFDKN ADTTMKWQTK
410 420 430 440 450
AFPIVGEPLQ KHQSLDLGSL LFEGCSNSKP VNAAGRYFNS KVPITRTKST
460 470 480 490 500
PFELIQQRET KEVDSKENFS YLESQPHDSC FVEMQAQKVM HVSSAELNYS
510 520 530 540 550
LPYDSKHQIR NASNVKHHDS SALGVYSYIP LVENPYFSSW PPSGTSSKMS
560 570 580 590 600
LDLPEKQDGT VFPSSLLPTS STSLFSYYNS HDSLSLNSPT NISSLLNQES
610 620 630 640 650
AVLATAPRID DEIPPPLPVR TPESFIVVEE AGEFSPNVPK SLSSAVKVKI
660 670 680 690
GTSLEWGGTS EPKKFDDSVI LRPSKSVKLR SPKSGKNFSW L
The sequence of this isoform differs from the canonical sequence as follows:
251-305: Missing.
10 20 30 40 50
MDQREILQKF LDEAQSKKIT KEEFANEFLK LKRQSTKYKA DKTYPTTVAE
60 70 80 90 100
KPKNIKKNRY KDILPYDYSR VELSLITSDE DSSYINANFI KGVYGPKAYI
110 120 130 140 150
ATQGPLSTTL LDFWRMIWEY SVLIIVMACM EYEMGKKKCE RYWAEPGEMQ
160 170 180 190 200
LEFGPFSVSC EAEKRKSDYI IRTLKVKFNS ETRTIYQFHY KNWPDHDVPS
210 220 230 240 250
SIDPILELIW DVRCYQEDDS VPICIHCSAG CGRTGVICAI DYTWMLLKDG
260 270 280 290 300
SQAKHCIPEK NHTLQADSYS PNLPKSTTKA AKMMNQQRTK MEIKESSSFD
310 320 330 340 350
FRTSEISAKE ELVLHPAKSS TSFDFLELNY SFDKNADTTM KWQTKAFPIV
360 370 380 390 400
GEPLQKHQSL DLGSLLFEGC SNSKPVNAAG RYFNSKVPIT RTKSTPFELI
410 420 430 440 450
QQRETKEVDS KENFSYLESQ PHDSCFVEMQ AQKVMHVSSA ELNYSLPYDS
460 470 480 490 500
KHQIRNASNV KHHDSSALGV YSYIPLVENP YFSSWPPSGT SSKMSLDLPE
510 520 530 540 550
KQDGTVFPSS LLPTSSTSLF SYYNSHDSLS LNSPTNISSL LNQESAVLAT
560 570 580 590 600
APRIDDEIPP PLPVRTPESF IVVEEAGEFS PNVPKSLSSA VKVKIGTSLE
610 620 630 640 650
WGGTSEPKKF DDSVILRPSK SVKLRSPKSE LHQDRSSPPP PLPERTLESF
660 670 680 690 700
FLADEDCMQA QSIETYSTSY PDTMENSTSS KQTLKTPGKS FTRSKSLKIL
710 720 730 740 750
RNMKKSICNS CPPNKPAESV QSNNSSSFLN FGFANRFSKP KGPRNPPPTW
NI
The sequence of this isoform differs from the canonical sequence as follows:
647-674: Missing.
10 20 30 40 50
MDQREILQKF LDEAQSKKIT KEEFANEFLK LKRQSTKYKA DKTYPTTVAE
60 70 80 90 100
KPKNIKKNRY KDILPYDYSR VELSLITSDE DSSYINANFI KGVYGPKAYI
110 120 130 140 150
ATQGPLSTTL LDFWRMIWEY SVLIIVMACM EYEMGKKKCE RYWAEPGEMQ
160 170 180 190 200
LEFGPFSVSC EAEKRKSDYI IRTLKVKFNS ETRTIYQFHY KNWPDHDVPS
210 220 230 240 250
SIDPILELIW DVRCYQEDDS VPICIHCSAG CGRTGVICAI DYTWMLLKDG
260 270 280 290 300
IIPENFSVFS LIREMRTQRP SLVQTQEQYE LVYNAVLELF KRQMDVIRDK
310 320 330 340 350
HSGTESQAKH CIPEKNHTLQ ADSYSPNLPK STTKAAKMMN QQRTKMEIKE
360 370 380 390 400
SSSFDFRTSE ISAKEELVLH PAKSSTSFDF LELNYSFDKN ADTTMKWQTK
410 420 430 440 450
AFPIVGEPLQ KHQSLDLGSL LFEGCSNSKP VNAAGRYFNS KVPITRTKST
460 470 480 490 500
PFELIQQRET KEVDSKENFS YLESQPHDSC FVEMQAQKVM HVSSAELNYS
510 520 530 540 550
LPYDSKHQIR NASNVKHHDS SALGVYSYIP LVENPYFSSW PPSGTSSKMS
560 570 580 590 600
LDLPEKQDGT VFPSSLLPTS STSLFSYYNS HDSLSLNSPT NISSLLNQES
610 620 630 640 650
AVLATAPRID DEIPPPLPVR TPESFIVVEE AGEFSPNVPK SLSSAVKSVK
660 670 680 690 700
LRSPKSELHQ DRSSPPPPLP ERTLESFFLA DEDCMQAQSI ETYSTSYPDT
710 720 730 740 750
MENSTSSKQT LKTPGKSFTR SKSLKILRNM KKSICNSCPP NKPAESVQSN
760 770
NSSSFLNFGF ANRFSKPKGP RNPPPTWNI
The sequence of this isoform differs from the canonical sequence as follows:
137-160: Missing.
181-203: ETRTIYQFHYKNWPDHDVPSSID → VSVILAHQTSLQNLFSQITPAHF
204-807: Missing.
10 20 30 40 50
MDQREILQKF LDEAQSKKIT KEEFANEFLK LKRQSTKYKA DKTYPTTVAE
60 70 80 90 100
KPKNIKKNRY KDILPYDYSR VELSLITSDE DSSYINANFI KGVYGPKAYI
110 120 130 140 150
ATQGPLSTTL LDFWRMIWEY SVLIIVMACM EYEMGKEAEK RKSDYIIRTL
160 170
KVKFNSVSVI LAHQTSLQNL FSQITPAHF
The sequence of this isoform differs from the canonical sequence as follows:
124-250: Missing.
788-807: FANRFSKPKGPRNPPPTWNI → MCVILLKS
10 20 30 40 50
MDQREILQKF LDEAQSKKIT KEEFANEFLK LKRQSTKYKA DKTYPTTVAE
60 70 80 90 100
KPKNIKKNRY KDILPYDYSR VELSLITSDE DSSYINANFI KGVYGPKAYI
110 120 130 140 150
ATQGPLSTTL LDFWRMIWEY SVLIIPENFS VFSLIREMRT QRPSLVQTQE
160 170 180 190 200
QYELVYNAVL ELFKRQMDVI RDKHSGTESQ AKHCIPEKNH TLQADSYSPN
210 220 230 240 250
LPKSTTKAAK MMNQQRTKME IKESSSFDFR TSEISAKEEL VLHPAKSSTS
260 270 280 290 300
FDFLELNYSF DKNADTTMKW QTKAFPIVGE PLQKHQSLDL GSLLFEGCSN
310 320 330 340 350
SKPVNAAGRY FNSKVPITRT KSTPFELIQQ RETKEVDSKE NFSYLESQPH
360 370 380 390 400
DSCFVEMQAQ KVMHVSSAEL NYSLPYDSKH QIRNASNVKH HDSSALGVYS
410 420 430 440 450
YIPLVENPYF SSWPPSGTSS KMSLDLPEKQ DGTVFPSSLL PTSSTSLFSY
460 470 480 490 500
YNSHDSLSLN SPTNISSLLN QESAVLATAP RIDDEIPPPL PVRTPESFIV
510 520 530 540 550
VEEAGEFSPN VPKSLSSAVK VKIGTSLEWG GTSEPKKFDD SVILRPSKSV
560 570 580 590 600
KLRSPKSELH QDRSSPPPPL PERTLESFFL ADEDCMQAQS IETYSTSYPD
610 620 630 640 650
TMENSTSSKQ TLKTPGKSFT RSKSLKILRN MKKSICNSCP PNKPAESVQS
660
NNSSSFLNFG MCVILLKS
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 51 – 52 | KP → NA in AAD00904 (PubMed:10068674).Curated | 2 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 51 – 52 | KP → NA in AAD00905 (PubMed:10068674).Curated | 2 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 126 | V → G in AAD27764 (PubMed:21044313).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 147 | G → V in AAD27764 (PubMed:21044313).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 240 | I → IV in AAD00905 (PubMed:10068674).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 372 | A → V in AK310570 (PubMed:14702039).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 420 | L → P in AAD27764 (PubMed:21044313).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 742 | P → S in AAD27764 (PubMed:21044313).Curated | 1 |
Natural variant
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072629 | 201 | S → F Polymorphism; moderately reduces phosphatase activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072630 | 263 | R → Q Polymorphism; reduces risk of SLE and RA but not IDDM; associated with reduced risk of ulcerative colitis but not of Crohn disease; severely reduces phosphatase activity. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072631 | 266 | R → W Polymorphism; severely reduces phosphatase activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_022605 | 620 | R → W in IDDM, RA, SLE and VTLG; also found in patients with Graves disease, Hashimoto thyroiditis and Addison disease; associated with reduced risk of Crohn disease but not of ulcerative colitis; affects CSK kinase binding; alters B cell receptor signaling and memory B cell proliferation. 12 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Alternative sequence
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_044428 | 124 – 250 | Missing in isoform 6. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 127 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_039725 | 137 – 160 | Missing in isoform 5. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 24 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_039726 | 181 – 203 | ETRTI…PSSID → VSVILAHQTSLQNLFSQITP AHF in isoform 5. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 23 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_039727 | 204 – 807 | Missing in isoform 5. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 604 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_039728 | 251 – 305 | Missing in isoform 3. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 55 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_039729 | 647 – 674 | Missing in isoform 4. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 28 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_005134 | 685 – 807 | ELHQD…PTWNI → GKNFSWL in isoform 2. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 123 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_044429 | 788 – 807 | FANRF…PTWNI → MCVILLKS in isoform 6. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 20 |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | AF001846 mRNA Translation: AAD00904.1 AF001847 mRNA Translation: AAD00905.1 GU479452 mRNA Translation: ADD59979.1 AF077031 mRNA Translation: AAD27764.1 AK310570 mRNA No translation available. EF064714 Genomic DNA Translation: ABK41897.1 AL137856 Genomic DNA No translation available. CH471122 Genomic DNA Translation: EAW56575.1 CH471122 Genomic DNA Translation: EAW56576.1 BC017785 mRNA Translation: AAH17785.1 BC071670 mRNA Translation: AAH71670.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS863.1 [Q9Y2R2-1] CCDS864.2 [Q9Y2R2-3] |
NCBI Reference Sequences More...RefSeqi | NP_001180360.1, NM_001193431.2 [Q9Y2R2-4] NP_001295226.1, NM_001308297.1 NP_036543.4, NM_012411.5 [Q9Y2R2-3] NP_057051.3, NM_015967.6 [Q9Y2R2-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.535276 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000460620; ENSP00000433141; ENSG00000134242 [Q9Y2R2-5] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 26191 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:26191 |
UCSC genome browser More...UCSCi | uc001edt.4 human [Q9Y2R2-1] |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Coding sequence diversityi
Alternative splicing, Polymorphism<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q9Y2R2 | UPI0001A57B82 | 302 | |||
| UPI000C2A63FA | 820 | ||||
| Tyrosine-protein phosphatase | 813 | ||||
| Tyrosine-protein phosphatase | 813 | ||||
| Tyrosine-protein phosphatase | 813 | ||||
| +278 | |||||
| Q9Y2R2-4 | UPI000C2A6913 | 792 | |||
| UPI00075FB6D1 | 779 | ||||
| UPI000273CBA6 | 779 | ||||
| UPI0005F3DA96 | 779 | ||||
| UPI00027434A4 | 779 | ||||
| +67 | |||||
| Q9Y2R2-5 | Tyrosine-protein phosphatase | 179 | |||
| Tyrosine-protein phosphatase | 179 | ||||
| Tyrosine-protein phosphatase | 179 | ||||
| Tyrosine-protein phosphatase | 180 | ||||
| Tyrosine-protein phosphatase | 179 | ||||
| +29 | |||||
| Q9Y2R2-6 | Tyrosine-protein phosphatase | 693 | |||
| Protein tyrosine phosphatase, non-receptor type 22 | 679 | ||||
| Tyrosine-protein phosphatase | 671 | ||||
| Tyrosine-protein phosphatase | 668 | ||||
| Tyrosine-protein phosphatase | 668 | ||||
| +30 | |||||
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | AF001846 mRNA Translation: AAD00904.1 AF001847 mRNA Translation: AAD00905.1 GU479452 mRNA Translation: ADD59979.1 AF077031 mRNA Translation: AAD27764.1 AK310570 mRNA No translation available. EF064714 Genomic DNA Translation: ABK41897.1 AL137856 Genomic DNA No translation available. CH471122 Genomic DNA Translation: EAW56575.1 CH471122 Genomic DNA Translation: EAW56576.1 BC017785 mRNA Translation: AAH17785.1 BC071670 mRNA Translation: AAH71670.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS863.1 [Q9Y2R2-1] CCDS864.2 [Q9Y2R2-3] |
NCBI Reference Sequences More...RefSeqi | NP_001180360.1, NM_001193431.2 [Q9Y2R2-4] NP_001295226.1, NM_001308297.1 NP_036543.4, NM_012411.5 [Q9Y2R2-3] NP_057051.3, NM_015967.6 [Q9Y2R2-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.535276 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 2P6X | X-ray | 1.90 | A/B | 1-302 | [»] | |
| 2QCJ | X-ray | 3.00 | A/B | 1-294 | [»] | |
| 2QCT | X-ray | 2.80 | A/B | 1-294 | [»] | |
| 3BRH | X-ray | 2.20 | A/B | 1-310 | [»] | |
| 3H2X | X-ray | 2.20 | A | 1-302 | [»] | |
| 3OLR | X-ray | 2.50 | A/B/C/D | 1-294 | [»] | |
| 3OMH | X-ray | 2.90 | A/B/C/D | 1-294 | [»] | |
| 4J51 | X-ray | 2.30 | A/B | 1-303 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q9Y2R2 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q9Y2R2 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 117604, 46 interactors |
Database of interacting proteins More...DIPi | DIP-29953N |
Protein interaction database and analysis system More...IntActi | Q9Y2R2, 24 interactors |
Molecular INTeraction database More...MINTi | Q9Y2R2 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000352833 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | Q9Y2R2 |
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL2889 |
PTM databases
DEPOD human dephosphorylation database More...DEPODi | Q9Y2R2 |
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q9Y2R2 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q9Y2R2 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | PTPN22 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 20139861 |
Proteomic databases
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q9Y2R2 |
PeptideAtlas More...PeptideAtlasi | Q9Y2R2 |
PRoteomics IDEntifications database More...PRIDEi | Q9Y2R2 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 85874 85875 [Q9Y2R2-2] 85876 [Q9Y2R2-3] 85877 [Q9Y2R2-4] 85878 [Q9Y2R2-5] |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 26191 |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000460620; ENSP00000433141; ENSG00000134242 [Q9Y2R2-5] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 26191 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:26191 |
UCSC genome browser More...UCSCi | uc001edt.4 human [Q9Y2R2-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 26191 |
DisGeNET More...DisGeNETi | 26191 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000134242.15 |
GeneCards: human genes, protein and diseases More...GeneCardsi | PTPN22 |
Human Gene Nomenclature Database More...HGNCi | HGNC:9652 PTPN22 |
Human Protein Atlas More...HPAi | CAB012209 HPA004912 HPA013350 |
MalaCards human disease database More...MalaCardsi | PTPN22 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 152700 phenotype 180300 phenotype 193200 phenotype 222100 phenotype 600716 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q9Y2R2 |
Open Targets More...OpenTargetsi | ENSG00000134242 |
Orphanet; a database dedicated to information on rare diseases and orphan drugs More...Orphaneti | 397 Giant cell arteritis 900 Granulomatosis with polyangiitis 85408 Juvenile rheumatoid factor-negative polyarthritis 85410 Oligoarticular juvenile arthritis 93552 Pediatric systemic lupus erythematosus 536 Systemic lupus erythematosus 3437 Vogt-Koyanagi-Harada disease |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA33995 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0789 Eukaryota COG5599 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00900000140785 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG103877 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q9Y2R2 |
KEGG Orthology (KO) More...KOi | K18024 |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q9Y2R2 |
TreeFam database of animal gene trees More...TreeFami | TF351977 |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 3.1.3.48 2681 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-202427 Phosphorylation of CD3 and TCR zeta chains R-HSA-202430 Translocation of ZAP-70 to Immunological synapse |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | Q9Y2R2 |
SIGNOR Signaling Network Open Resource More...SIGNORi | Q9Y2R2 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | PTPN22 human |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q9Y2R2 |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | PTPN22 |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 26191 |
Protein Ontology More...PROi | PR:Q9Y2R2 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000134242 |
CleanEx database of gene expression profiles More...CleanExi | HS_PTPN22 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q9Y2R2 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q9Y2R2 HS |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.90.190.10, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR029021 Prot-tyrosine_phosphatase-like IPR000242 PTPase_domain IPR016276 PTPN22 IPR016130 Tyr_Pase_AS IPR003595 Tyr_Pase_cat IPR000387 TYR_PHOSPHATASE_dom |
Pfam protein domain database More...Pfami | View protein in Pfam PF00102 Y_phosphatase, 1 hit |
PIRSF; a whole-protein classification database More...PIRSFi | PIRSF000930 PTPN8_PTPN22, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00700 PRTYPHPHTASE |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00194 PTPc, 1 hit SM00404 PTPc_motif, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF52799 SSF52799, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00383 TYR_PHOSPHATASE_1, 1 hit PS50056 TYR_PHOSPHATASE_2, 1 hit PS50055 TYR_PHOSPHATASE_PTP, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | PTN22_HUMAN | |
| <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | Q9Y2R2Primary (citable) accession number: Q9Y2R2 Secondary accession number(s): A0N0K6 , B1ALC8, D4NZ71, E9PLD8, E9PPI1, O95063, O95064, Q6IPX8, Q8WVM1 | |
| <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | March 27, 2002 |
| Last sequence update: | March 27, 2002 | |
| Last modified: | June 20, 2018 | |
| This is version 162 of the entry and version 2 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | |
<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Technical termi
3D-structure, Complete proteome, Reference proteomeDocuments
- Human chromosome 1
Human chromosome 1: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations - Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
