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Protein

Tyrosine-protein kinase ZAP-70

Gene

ZAP70

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

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>

<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

Tyrosine kinase that plays an essential role in regulation of the adaptive immune response. Regulates motility, adhesion and cytokine expression of mature T-cells, as well as thymocyte development. Contributes also to the development and activation of primary B-lymphocytes. When antigen presenting cells (APC) activate T-cell receptor (TCR), a serie of phosphorylations lead to the recruitment of ZAP70 to the doubly phosphorylated TCR component CD247/CD3Z through ITAM motif at the plasma membrane. This recruitment serves to localization to the stimulated TCR and to relieve its autoinhibited conformation. Release of ZAP70 active conformation is further stabilized by phosphorylation mediated by LCK. Subsequently, ZAP70 phosphorylates at least 2 essential adapter proteins: LAT and LCP2. In turn, a large number of signaling molecules are recruited and ultimately lead to lymphokine production, T-cell proliferation and differentiation. Furthermore, ZAP70 controls cytoskeleton modifications, adhesion and mobility of T-lymphocytes, thus ensuring correct delivery of effectors to the APC. ZAP70 is also required for TCR-CD247/CD3Z internalization and degradation through interaction with the E3 ubiquitin-protein ligase CBL and adapter proteins SLA and SLA2. Thus, ZAP70 regulates both T-cell activation switch on and switch off by modulating TCR expression at the T-cell surface. During thymocyte development, ZAP70 promotes survival and cell-cycle progression of developing thymocytes before positive selection (when cells are still CD4/CD8 double negative). Additionally, ZAP70-dependent signaling pathway may also contribute to primary B-cells formation and activation through B-cell receptor (BCR).8 Publications

<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. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Activated by phosphorylation at Tyr-493 in the activation loop. Inhibited by staurosporine.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei369ATP1
<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 sitei461Proton acceptorPROSITE-ProRule annotation2 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi345 – 352ATP8

<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

  • ATP binding Source: UniProtKB
  • non-membrane spanning protein tyrosine kinase activity Source: UniProtKB
  • phosphotyrosine residue binding Source: UniProtKB
  • protein tyrosine kinase activity Source: UniProtKB

GO - Biological processi

<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 functionKinase, Transferase, Tyrosine-protein kinase
Biological processAdaptive immunity, Immunity
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

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BRENDAi
2.7.10.2 2681

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-202430 Translocation of ZAP-70 to Immunological synapse
R-HSA-202433 Generation of second messenger molecules

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
P43403

SIGNOR Signaling Network Open Resource

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SIGNORi
P43403

<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 kinase ZAP-70 (EC:2.7.10.2)
Alternative name(s):
70 kDa zeta-chain associated protein
Syk-related tyrosine kinase
<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:ZAP70
Synonyms:SRK
<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>OrganismiHomo 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 identifieri9606 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 2

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000115085.13

Human Gene Nomenclature Database

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HGNCi
HGNC:12858 ZAP70

Online Mendelian Inheritance in Man (OMIM)

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MIMi
176947 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P43403

<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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

<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

Immunodeficiency 48 (IMD48)5 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of severe immunodeficiency characterized by a selective absence of CD8+ T-cells.
See also OMIM:269840
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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_065623337L → R in IMD48. 1 Publication1
Natural variantiVAR_065624465R → C in IMD48. 1 PublicationCorresponds to variant dbSNP:rs113994174EnsemblClinVar.1
Natural variantiVAR_015538465R → H in IMD48. 1 PublicationCorresponds to variant dbSNP:rs137853201EnsemblClinVar.1
Natural variantiVAR_065625507A → V in IMD48. 1 Publication1
Natural variantiVAR_006351518S → R in IMD48. 1 PublicationCorresponds to variant dbSNP:rs104893674EnsemblClinVar.1
Natural variantiVAR_038688541K → KLEQ in IMD48. 1 Publication1
Natural variantiVAR_065626564C → R in IMD48. 1 Publication1
Autoimmune disease, multisystem, infantile-onset, 2 (ADMIO2)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive, autoimmune disorder characterized by systemic manifestations including blistering skin disease, uncontrollable bullous pemphigoid, inflammatory colitis, autoimmune hypothyroidism, proteinuria and nephrotic syndrome.
See also OMIM:617006
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_077137192R → W in ADMIO2; decreases interaction with phosphorylated CD247; decreases ZAP70 phosphorylation; no effect on subcellular localization of CD69 at the cell surface. 1 PublicationCorresponds to variant dbSNP:rs199840952EnsemblClinVar.1
Natural variantiVAR_077138360R → P in ADMIO2; no effect on interaction with phosphorylated CD247; increases TCR-induced Y-319 and Y-493 phosphorylation of ZAP70 and phosphorylation of LAT and LCP2; increases subcellular localization of CD69 at the cell surface; weakly decreases autoinhibition conformation. 1 PublicationCorresponds to variant dbSNP:rs869025224EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Mutagenesisi37R → K: Decreases interaction with phosphorylated CD247; when associated with K-190. 1 Publication1
Mutagenesisi131W → A: Increased constitutive kinase activity. 1 Publication1
Mutagenesisi133L → A: Increased constitutive kinase activity. 1 Publication1
Mutagenesisi141A → E: Increased constitutive kinase activity. 1 Publication1
Mutagenesisi144S → A: Increased kinase activity after activation by LCK. 1 Publication1
Mutagenesisi145Q → A: Increased kinase activity after activation by LCK. 1 Publication1
Mutagenesisi147P → A: Increased kinase activity after activation by LCK. 1 Publication1
Mutagenesisi190R → K: Decreases interaction with phosphorylated CD247; when associated with K-37. 1 Publication1
Mutagenesisi292Y → F: Induces constitutive TCR stimulation-independent NFAT induction. 1 Publication1
Mutagenesisi304K → R: No effect on ubiquitination. 1 Publication1
Mutagenesisi314V → A: Increased constitutive kinase activity. 1
Mutagenesisi315 – 319YESPY → AESPA: Increases strongly constitutive kinase activity on LAT phosphorylation. 1 Publication5
Mutagenesisi315Y → A: Increased constitutive kinase activity; when associated with F-319. 4 Publications1
Mutagenesisi315Y → F: Increased constitutive kinase activity; when associated with F-319. About 75% loss of CD247/CD3Z-binding in stimulated TCR and complete loss of VAV1 interaction. 4 Publications1
Mutagenesisi319Y → A: Increased constitutive kinase activity; when associated with F-315. 2 Publications1
Mutagenesisi319Y → F: Increased constitutive kinase activity; when associated with F-315. About 80% loss of TCR-induced NFAT activation. 2 Publications1
Mutagenesisi327D → P: Increases constitutive kinase activity on LAT phosphorylation, strongly increases subcellular localization of CD69 at the cell surface and decreases autoinhibition conformation. 1 Publication1
Mutagenesisi362K → E: Increases constitutive kinase activity on LAT phosphorylation, strongly increases subcellular localization of CD69 at the cell surface and decreases autoinhibition conformation. 1 Publication1
Mutagenesisi461D → N: Abolishes kinase activity. 1 Publication1
Mutagenesisi479D → N: Abolishes kinase activity. 1 Publication1
Mutagenesisi492Y → F: Increases kinase activity. 1 Publication1
Mutagenesisi493Y → F: Impairs kinase activity. 1 Publication1
Mutagenesisi538K → R: No effect on ubiquitination. 1 Publication1
Mutagenesisi544K → R: Strongly decreased ubiquitination. 1 Publication1
Mutagenesisi597Y → A: Increased kinase activity after activation by LCK. 1 Publication1
Mutagenesisi598Y → A: Increased kinase activity after activation by LCK. 1 Publication1

Keywords - Diseasei

Disease mutation, SCID

Organism-specific databases

DisGeNET

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DisGeNETi
7535

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

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GeneReviewsi
ZAP70

MalaCards human disease database

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MalaCardsi
ZAP70
MIMi269840 phenotype
617006 phenotype

Open Targets

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OpenTargetsi
ENSG00000115085

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
911 Combined immunodeficiency due to ZAP70 deficiency

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA37447

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL2803

Drug and drug target database

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DrugBanki
DB02010 Staurosporine

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
2285

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
ZAP70

Domain mapping of disease mutations (DMDM)

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DMDMi
1177044

<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 keyPosition(s)DescriptionActionsGraphical viewLength
<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_00000881681 – 619Tyrosine-protein kinase ZAP-70Add BLAST619

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 residuei248PhosphotyrosineCombined sources1
Modified residuei289PhosphoserineCombined sources1
Modified residuei292PhosphotyrosineCombined sources1 Publication1
Modified residuei315Phosphotyrosine; by LCK1 Publication1
Modified residuei319Phosphotyrosine1 Publication1
Modified residuei492Phosphotyrosine1 Publication1
Modified residuei493Phosphotyrosine1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki544Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei603N6-acetyllysineCombined sources1

<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

Phosphorylated on tyrosine residues upon T-cell antigen receptor (TCR) stimulation. Phosphorylation of Tyr-315 and Tyr-319 are essential for ZAP70 positive function on T-lymphocyte activation whereas Tyr-292 has a negative regulatory role. Within the C-terminal kinase domain, Tyr-492 and Tyr-493 are phosphorylated after TCR induction, Tyr-492 playing a negative regulatory role and Tyr-493 a positive. Tyr-493 is dephosphorylated by PTN22.4 Publications
Ubiquitinated in response to T cell activation. Deubiquitinated by OTUD7B.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P43403

MaxQB - The MaxQuant DataBase

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MaxQBi
P43403

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P43403

PeptideAtlas

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PeptideAtlasi
P43403

PRoteomics IDEntifications database

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PRIDEi
P43403

ProteomicsDB human proteome resource

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ProteomicsDBi
55631
55632 [P43403-2]
55633 [P43403-3]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P43403

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P43403

Miscellaneous databases

CutDB - Proteolytic event database

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PMAP-CutDBi
P43403

<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

Expressed in T- and natural killer cells. Also present in early thymocytes and pro/pre B-cells.3 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000115085 Expressed in 116 organ(s), highest expression level in small intestine Peyer's patch

CleanEx database of gene expression profiles

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CleanExi
HS_ZAP70

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P43403 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB002625
HPA003134

<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

Interacts with CD247/CD3Z; this interaction docks ZAP70 at the stimulated TCR (PubMed:1423621, PubMed:7659156, PubMed:26783323). Interacts with NFAM1 (PubMed:15143214). Interacts with adapter protein SLA; this interaction negatively regulates T-cell receptor signaling (PubMed:10449770). Interacts with FCRL3 (PubMed:12051764, PubMed:19843936). Interacts with VAV1 (PubMed:9151714). Interacts with CBL; this interaction promotes ubiquitination, internalization and subsequent degradation of CD247/CD3Z (PubMed:10449770, PubMed:10078535). Identified in a complex with CBL and UBE2L3 (PubMed:10966114). Interacts with SHB (PubMed:12084069). Interacts with adapter protein SLA2; this interaction negatively regulates T-cell receptor signaling. Interacts with CBLB. Interacts (via SH2 domains) with RHOH; this interaction regulates ZAP70 subcellular localization. Interacts with DEF6 (By similarity). Interacts (ubiquitinated form) with OTUD7B and UBASH3B (PubMed:26903241).By similarity12 Publications

<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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
113367, 52 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P43403

Database of interacting proteins

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DIPi
DIP-38781N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
P43403

Protein interaction database and analysis system

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IntActi
P43403, 24 interactors

Molecular INTeraction database

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MINTi
P43403

STRING: functional protein association networks

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STRINGi
9606.ENSP00000264972

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P43403

<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

1619
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FBVX-ray2.90B289-297[»]
1M61X-ray2.50A1-256[»]
1U59X-ray2.30A327-606[»]
2CBLX-ray2.10B286-297[»]
2OQ1X-ray1.90A3-256[»]
2OZOX-ray2.60A1-606[»]
2Y1NX-ray2.00B/D286-297[»]
3ZNIX-ray2.21B/F/J/N286-297[»]
4A4BX-ray2.79B286-297[»]
4A4CX-ray2.70B286-297[»]
4K2RX-ray3.00A1-606[»]
4XZ0X-ray2.00A1-259[»]
4XZ1X-ray2.80A1-259[»]
5O76X-ray2.47B/D286-297[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P43403

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P43403

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P43403

<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 keyPosition(s)DescriptionActionsGraphical viewLength
<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>Domaini10 – 102SH2 1PROSITE-ProRule annotationAdd BLAST93
Domaini163 – 254SH2 2PROSITE-ProRule annotationAdd BLAST92
Domaini338 – 600Protein kinasePROSITE-ProRule annotationAdd BLAST263

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Regioni103 – 162Interdomain AAdd BLAST60
Regioni255 – 337Interdomain BAdd BLAST83

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Composed of 2 N-terminal SH2 domains and a C-terminal kinase domain. The tandem SH2 domains bind to the doubly phosphorylated tyrosine-based activation motif (ITAM) of CD247/CD3Z and the non-canonical phosphorylated tyrosine-based activation motif (TAM) of RHOH (By similarity). The interdomain B located between the second SH2 and the kinase domain contains 3 tyrosines (Tyr-292, Tyr-315, Tyr-319) that are phosphorylated following TCR activation. These sites have been implicated in binding to other signaling molecules including CBL or VAV1. Thus, ZAP70 can also function as a scaffold by recruiting additional factors to the stimulated TCR complex.By similarity1 Publication

<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

Belongs to the protein kinase superfamily. Tyr protein kinase family. SYK/ZAP-70 subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, SH2 domain

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410IH0T Eukaryota
COG0515 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000159185

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000113264

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG001540

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P43403

KEGG Orthology (KO)

More...
KOi
K07360

Identification of Orthologs from Complete Genome Data

More...
OMAi
ADKDEMM

Database of Orthologous Groups

More...
OrthoDBi
827472at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P43403

TreeFam database of animal gene trees

More...
TreeFami
TF351629

Family and domain databases

Conserved Domains Database

More...
CDDi
cd09938 SH2_N-SH2_Zap70_Syk_like, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.930.10, 1 hit
3.30.505.10, 2 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR023420 Kinase_SYK/ZAP-70_inter-SH2_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR000980 SH2
IPR036860 SH2_dom_sf
IPR035838 SYK/ZAP-70_N_SH2
IPR008266 Tyr_kinase_AS
IPR020635 Tyr_kinase_cat_dom
IPR012234 Tyr_kinase_non-rcpt_SYK/ZAP70

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF07714 Pkinase_Tyr, 1 hit
PF00017 SH2, 2 hits

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000604 TyrPK_SYK, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00401 SH2DOMAIN
PR00109 TYRKINASE

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00252 SH2, 2 hits
SM00219 TyrKc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF55550 SSF55550, 2 hits
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00109 PROTEIN_KINASE_TYR, 1 hit
PS50001 SH2, 2 hits

<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 (3)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 3 <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 basket
Isoform 1 (identifier: P43403-1) [UniParc]FASTAAdd 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.

« Hide
        10         20         30         40         50
MPDPAAHLPF FYGSISRAEA EEHLKLAGMA DGLFLLRQCL RSLGGYVLSL
60 70 80 90 100
VHDVRFHHFP IERQLNGTYA IAGGKAHCGP AELCEFYSRD PDGLPCNLRK
110 120 130 140 150
PCNRPSGLEP QPGVFDCLRD AMVRDYVRQT WKLEGEALEQ AIISQAPQVE
160 170 180 190 200
KLIATTAHER MPWYHSSLTR EEAERKLYSG AQTDGKFLLR PRKEQGTYAL
210 220 230 240 250
SLIYGKTVYH YLISQDKAGK YCIPEGTKFD TLWQLVEYLK LKADGLIYCL
260 270 280 290 300
KEACPNSSAS NASGAAAPTL PAHPSTLTHP QRRIDTLNSD GYTPEPARIT
310 320 330 340 350
SPDKPRPMPM DTSVYESPYS DPEELKDKKL FLKRDNLLIA DIELGCGNFG
360 370 380 390 400
SVRQGVYRMR KKQIDVAIKV LKQGTEKADT EEMMREAQIM HQLDNPYIVR
410 420 430 440 450
LIGVCQAEAL MLVMEMAGGG PLHKFLVGKR EEIPVSNVAE LLHQVSMGMK
460 470 480 490 500
YLEEKNFVHR DLAARNVLLV NRHYAKISDF GLSKALGADD SYYTARSAGK
510 520 530 540 550
WPLKWYAPEC INFRKFSSRS DVWSYGVTMW EALSYGQKPY KKMKGPEVMA
560 570 580 590 600
FIEQGKRMEC PPECPPELYA LMSDCWIYKW EDRPDFLTVE QRMRACYYSL
610
ASKVEGPPGS TQKAEAACA
Length:619
Mass (Da):69,872
Last modified:November 1, 1995 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iD1E1A8EC66FA116F
GO
Isoform 2 (identifier: P43403-2) [UniParc]FASTAAdd to basket
Also known as: TZK

The sequence of this isoform differs from the canonical sequence as follows:
     1-307: Missing.

Show »
Length:312
Mass (Da):35,647
Checksum:iB1D7A63A61D63215
GO
Isoform 3 (identifier: P43403-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-126: Missing.
     127-134: VRQTWKLE → MRLGPRWK

Note: No experimental confirmation available.
Show »
Length:493
Mass (Da):55,873
Checksum:i14F1841C3F898EEF
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_041846175R → L1 PublicationCorresponds to variant dbSNP:rs55964305Ensembl.1
Natural variantiVAR_041847191P → L1 PublicationCorresponds to variant dbSNP:rs56403250Ensembl.1
Natural variantiVAR_077137192R → W in ADMIO2; decreases interaction with phosphorylated CD247; decreases ZAP70 phosphorylation; no effect on subcellular localization of CD69 at the cell surface. 1 PublicationCorresponds to variant dbSNP:rs199840952EnsemblClinVar.1
Natural variantiVAR_065623337L → R in IMD48. 1 Publication1
Natural variantiVAR_077138360R → P in ADMIO2; no effect on interaction with phosphorylated CD247; increases TCR-induced Y-319 and Y-493 phosphorylation of ZAP70 and phosphorylation of LAT and LCP2; increases subcellular localization of CD69 at the cell surface; weakly decreases autoinhibition conformation. 1 PublicationCorresponds to variant dbSNP:rs869025224EnsemblClinVar.1
Natural variantiVAR_041848448G → E in a head and neck squamous cell carcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_065624465R → C in IMD48. 1 PublicationCorresponds to variant dbSNP:rs113994174EnsemblClinVar.1
Natural variantiVAR_015538465R → H in IMD48. 1 PublicationCorresponds to variant dbSNP:rs137853201EnsemblClinVar.1
Natural variantiVAR_065625507A → V in IMD48. 1 Publication1
Natural variantiVAR_006351518S → R in IMD48. 1 PublicationCorresponds to variant dbSNP:rs104893674EnsemblClinVar.1
Natural variantiVAR_041849523W → L1 PublicationCorresponds to variant dbSNP:rs56189815Ensembl.1
Natural variantiVAR_038688541K → KLEQ in IMD48. 1 Publication1
Natural variantiVAR_065626564C → R in IMD48. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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_0311561 – 307Missing in isoform 2. 1 PublicationAdd BLAST307
Alternative sequenceiVSP_0311571 – 126Missing in isoform 3. 1 PublicationAdd BLAST126
Alternative sequenceiVSP_031158127 – 134VRQTWKLE → MRLGPRWK in isoform 3. 1 Publication8

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
L05148 mRNA No translation available.
AB083211 mRNA Translation: BAC43747.1
AC016699 Genomic DNA Translation: AAX93187.1
BC039039 mRNA Translation: AAH39039.1
BC053878 mRNA Translation: AAH53878.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS33254.1 [P43403-1]
CCDS33255.1 [P43403-2]

Protein sequence database of the Protein Information Resource

More...
PIRi
A44266
A49955

NCBI Reference Sequences

More...
RefSeqi
NP_001070.2, NM_001079.3 [P43403-1]
NP_997402.1, NM_207519.1 [P43403-2]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.234569

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000264972; ENSP00000264972; ENSG00000115085 [P43403-1]
ENST00000451498; ENSP00000400475; ENSG00000115085 [P43403-2]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
7535

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:7535

UCSC genome browser

More...
UCSCi
uc002syd.2 human [P43403-1]

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

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

ZAP70base

ZAP70 mutation db

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L05148 mRNA No translation available.
AB083211 mRNA Translation: BAC43747.1
AC016699 Genomic DNA Translation: AAX93187.1
BC039039 mRNA Translation: AAH39039.1
BC053878 mRNA Translation: AAH53878.1
CCDSiCCDS33254.1 [P43403-1]
CCDS33255.1 [P43403-2]
PIRiA44266
A49955
RefSeqiNP_001070.2, NM_001079.3 [P43403-1]
NP_997402.1, NM_207519.1 [P43403-2]
UniGeneiHs.234569

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FBVX-ray2.90B289-297[»]
1M61X-ray2.50A1-256[»]
1U59X-ray2.30A327-606[»]
2CBLX-ray2.10B286-297[»]
2OQ1X-ray1.90A3-256[»]
2OZOX-ray2.60A1-606[»]
2Y1NX-ray2.00B/D286-297[»]
3ZNIX-ray2.21B/F/J/N286-297[»]
4A4BX-ray2.79B286-297[»]
4A4CX-ray2.70B286-297[»]
4K2RX-ray3.00A1-606[»]
4XZ0X-ray2.00A1-259[»]
4XZ1X-ray2.80A1-259[»]
5O76X-ray2.47B/D286-297[»]
ProteinModelPortaliP43403
SMRiP43403
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113367, 52 interactors
CORUMiP43403
DIPiDIP-38781N
ELMiP43403
IntActiP43403, 24 interactors
MINTiP43403
STRINGi9606.ENSP00000264972

Chemistry databases

BindingDBiP43403
ChEMBLiCHEMBL2803
DrugBankiDB02010 Staurosporine
GuidetoPHARMACOLOGYi2285

PTM databases

iPTMnetiP43403
PhosphoSitePlusiP43403

Polymorphism and mutation databases

BioMutaiZAP70
DMDMi1177044

Proteomic databases

jPOSTiP43403
MaxQBiP43403
PaxDbiP43403
PeptideAtlasiP43403
PRIDEiP43403
ProteomicsDBi55631
55632 [P43403-2]
55633 [P43403-3]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
7535
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264972; ENSP00000264972; ENSG00000115085 [P43403-1]
ENST00000451498; ENSP00000400475; ENSG00000115085 [P43403-2]
GeneIDi7535
KEGGihsa:7535
UCSCiuc002syd.2 human [P43403-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
7535
DisGeNETi7535
EuPathDBiHostDB:ENSG00000115085.13

GeneCards: human genes, protein and diseases

More...
GeneCardsi
ZAP70
GeneReviewsiZAP70
HGNCiHGNC:12858 ZAP70
HPAiCAB002625
HPA003134
MalaCardsiZAP70
MIMi176947 gene
269840 phenotype
617006 phenotype
neXtProtiNX_P43403
OpenTargetsiENSG00000115085
Orphaneti911 Combined immunodeficiency due to ZAP70 deficiency
PharmGKBiPA37447

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiENOG410IH0T Eukaryota
COG0515 LUCA
GeneTreeiENSGT00940000159185
HOGENOMiHOG000113264
HOVERGENiHBG001540
InParanoidiP43403
KOiK07360
OMAiADKDEMM
OrthoDBi827472at2759
PhylomeDBiP43403
TreeFamiTF351629

Enzyme and pathway databases

BRENDAi2.7.10.2 2681
ReactomeiR-HSA-202430 Translocation of ZAP-70 to Immunological synapse
R-HSA-202433 Generation of second messenger molecules
SignaLinkiP43403
SIGNORiP43403

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
ZAP70 human
EvolutionaryTraceiP43403

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
ZAP70

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
7535
PMAP-CutDBiP43403

Protein Ontology

More...
PROi
PR:P43403

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000115085 Expressed in 116 organ(s), highest expression level in small intestine Peyer's patch
CleanExiHS_ZAP70
GenevisibleiP43403 HS

Family and domain databases

CDDicd09938 SH2_N-SH2_Zap70_Syk_like, 1 hit
Gene3Di1.10.930.10, 1 hit
3.30.505.10, 2 hits
InterProiView protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR023420 Kinase_SYK/ZAP-70_inter-SH2_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR000980 SH2
IPR036860 SH2_dom_sf
IPR035838 SYK/ZAP-70_N_SH2
IPR008266 Tyr_kinase_AS
IPR020635 Tyr_kinase_cat_dom
IPR012234 Tyr_kinase_non-rcpt_SYK/ZAP70
PfamiView protein in Pfam
PF07714 Pkinase_Tyr, 1 hit
PF00017 SH2, 2 hits
PIRSFiPIRSF000604 TyrPK_SYK, 1 hit
PRINTSiPR00401 SH2DOMAIN
PR00109 TYRKINASE
SMARTiView protein in SMART
SM00252 SH2, 2 hits
SM00219 TyrKc, 1 hit
SUPFAMiSSF55550 SSF55550, 2 hits
SSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00109 PROTEIN_KINASE_TYR, 1 hit
PS50001 SH2, 2 hits

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 nameiZAP70_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>AccessioniPrimary (citable) accession number: P43403
Secondary accession number(s): A6NFP4
, Q6PIA4, Q8IXD6, Q9UBS6
<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 historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: January 16, 2019
This is version 218 of the entry and version 1 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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
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