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Protein

Tyrosine-protein kinase SYK

Gene

SYK

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

Non-receptor tyrosine kinase which mediates signal transduction downstream of a variety of transmembrane receptors including classical immunoreceptors like the B-cell receptor (BCR). Regulates several biological processes including innate and adaptive immunity, cell adhesion, osteoclast maturation, platelet activation and vascular development. Assembles into signaling complexes with activated receptors at the plasma membrane via interaction between its SH2 domains and the receptor tyrosine-phosphorylated ITAM domains. The association with the receptor can also be indirect and mediated by adapter proteins containing ITAM or partial hemITAM domains. The phosphorylation of the ITAM domains is generally mediated by SRC subfamily kinases upon engagement of the receptor. More rarely signal transduction via SYK could be ITAM-independent. Direct downstream effectors phosphorylated by SYK include VAV1, PLCG1, PI-3-kinase, LCP2 and BLNK. Initially identified as essential in B-cell receptor (BCR) signaling, it is necessary for the maturation of B-cells most probably at the pro-B to pre-B transition. Activated upon BCR engagement, it phosphorylates and activates BLNK an adapter linking the activated BCR to downstream signaling adapters and effectors. It also phosphorylates and activates PLCG1 and the PKC signaling pathway. It also phosphorylates BTK and regulates its activity in B-cell antigen receptor (BCR)-coupled signaling. In addition to its function downstream of BCR plays also a role in T-cell receptor signaling. Plays also a crucial role in the innate immune response to fungal, bacterial and viral pathogens. It is for instance activated by the membrane lectin CLEC7A. Upon stimulation by fungal proteins, CLEC7A together with SYK activates immune cells inducing the production of ROS. Also activates the inflammasome and NF-kappa-B-mediated transcription of chemokines and cytokines in presence of pathogens. Regulates neutrophil degranulation and phagocytosis through activation of the MAPK signaling cascade. Also mediates the activation of dendritic cells by cell necrosis stimuli. Also involved in mast cells activation. Involved in interleukin-3/IL3-mediated signaling pathway in basophils (By similarity). Also functions downstream of receptors mediating cell adhesion. Relays for instance, integrin-mediated neutrophils and macrophages activation and P-selectin receptor/SELPG-mediated recruitment of leukocytes to inflammatory loci. Plays also a role in non-immune processes. It is for instance involved in vascular development where it may regulate blood and lymphatic vascular separation. It is also required for osteoclast development and function. Functions in the activation of platelets by collagen, mediating PLCG2 phosphorylation and activation. May be coupled to the collagen receptor by the ITAM domain-containing FCER1G. Also activated by the membrane lectin CLEC1B that is required for activation of platelets by PDPN/podoplanin. Involved in platelet adhesion being activated by ITGB3 engaged by fibrinogen. Together with CEACAM20, enhances production of the cytokine CXCL8/IL-8 via the NFKB pathway and may thus have a role in the intestinal immune response (By similarity).By similarity6 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

Autoinhibited. Intramolecular binding of the interdomains A and B (also called linker region) to parts of the catalytic domain keep the catalytic center in an inactive conformation. The phosphorylation of the interdomains or the binding of the SH2 domains with dually phosphorylated ITAM domains on transmembrane proteins disrupt those intramolecular interactions allowing the kinase domain to adopt an active conformation. The phosphorylation of SYK and of the ITAM domains which is responsible for SYK activation is essentially mediated by SRC subfamily kinases, like LYN, upon transmembrane receptors engagement. May also be negatively regulated by PTPN6 through dephosphorylation. Downstream signaling adapters and intermediates like BLNK or RHOH may mediate positive and/or negative feedback regulation. Negatively regulated by CBL and CBLB through ubiquitination and probable degradation. Phosphorylates SH3BP2 which in turn may regulate SYK through LYN (By similarity).By similarity

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 sitei402ATPPROSITE-ProRule annotation1
<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 sitei494Proton acceptorPROSITE-ProRule annotation1

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 bindingi377 – 385ATPPROSITE-ProRule annotation9

<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

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, Angiogenesis, Host-virus interaction, Immunity, Innate 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-114604 GPVI-mediated activation cascade
R-HSA-2029481 FCGR activation
R-HSA-2029482 Regulation of actin dynamics for phagocytic cup formation
R-HSA-2029485 Role of phospholipids in phagocytosis
R-HSA-2424491 DAP12 signaling
R-HSA-2454202 Fc epsilon receptor (FCERI) signaling
R-HSA-2730905 Role of LAT2/NTAL/LAB on calcium mobilization
R-HSA-2871796 FCERI mediated MAPK activation
R-HSA-2871809 FCERI mediated Ca+2 mobilization
R-HSA-354192 Integrin alphaIIb beta3 signaling
R-HSA-5607764 CLEC7A (Dectin-1) signaling
R-HSA-5621480 Dectin-2 family
R-HSA-9020558 Interleukin-2 signaling
R-HSA-912631 Regulation of signaling by CBL
R-HSA-983695 Antigen activates B Cell Receptor (BCR) leading to generation of second messengers

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

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SignaLinki
P43405

SIGNOR Signaling Network Open Resource

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SIGNORi
P43405

Protein family/group databases

MoonDB Database of extreme multifunctional and moonlighting proteins

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MoonDBi
P43405 Predicted

<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 SYK (EC:2.7.10.2)
Alternative name(s):
Spleen tyrosine kinase
p72-Syk
<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:SYK
<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 9

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000165025.14

Human Gene Nomenclature Database

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HGNCi
HGNC:11491 SYK

Online Mendelian Inheritance in Man (OMIM)

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MIMi
600085 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P43405

<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

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>Mutagenesisi297S → A: Abolishes YWHAG binding. 1 Publication1
Mutagenesisi630Y → F: Loss of interaction with BLNK. 1 Publication1

Organism-specific databases

DisGeNET

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DisGeNETi
6850

Open Targets

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OpenTargetsi
ENSG00000165025

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA36273

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL2599

Drug and drug target database

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DrugBanki
DB08846 Ellagic Acid
DB02010 Staurosporine

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
2230

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
SYK

Domain mapping of disease mutations (DMDM)

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DMDMi
1174527

<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_00000881651 – 635Tyrosine-protein kinase SYKAdd BLAST635

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 residuei28PhosphotyrosineCombined sources1 Publication1
Modified residuei44Phosphoserine1 Publication1
Modified residuei47Phosphotyrosine1 Publication1
Modified residuei131Phosphotyrosine1 Publication1
Modified residuei202Phosphoserine1 Publication1
Modified residuei256Phosphothreonine1 Publication1
Modified residuei295Phosphoserine1 Publication1
Modified residuei296Phosphotyrosine1 Publication1
Modified residuei297Phosphoserine1 Publication1
Modified residuei316Phosphoserine1 Publication1
Modified residuei317Phosphothreonine1 Publication1
Modified residuei319Phosphoserine1 Publication1
Modified residuei323Phosphotyrosine; by LYNCombined sources1 Publication1
Modified residuei345Phosphothreonine1 Publication1
Modified residuei348Phosphotyrosine1 Publication1
Modified residuei350Phosphoserine1 Publication1
Modified residuei352Phosphotyrosine1 Publication1
Modified residuei364Phosphotyrosine1 Publication1
Modified residuei379Phosphoserine1 Publication1
Modified residuei384Phosphothreonine1 Publication1
Modified residuei484Phosphotyrosine1 Publication1
Modified residuei507Phosphotyrosine1 Publication1
Modified residuei525Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei526Phosphotyrosine1 Publication1
Modified residuei530Phosphothreonine1 Publication1
Modified residuei546PhosphotyrosineBy similarity1
Modified residuei579Phosphoserine1 Publication1
Modified residuei582Phosphothreonine1 Publication1
Modified residuei629Phosphotyrosine1 Publication1
Modified residuei630Phosphotyrosine2 Publications1
Modified residuei631Phosphotyrosine1 Publication1

<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

Ubiquitinated by CBLB after BCR activation; which promotes proteasomal degradation.By similarity
Autophosphorylated. Phosphorylated on tyrosine residues by LYN following receptors engagement. Phosphorylation on Tyr-323 creates a binding site for CBL, an adapter protein that serves as a negative regulator of BCR-stimulated calcium ion signaling. Phosphorylation at Tyr-348 creates a binding site for VAV1. Phosphorylation on Tyr-348 and Tyr-352 enhances the phosphorylation and activation of phospholipase C-gamma and the early phase of calcium ion mobilization via a phosphoinositide 3-kinase-independent pathway (By similarity). Phosphorylation on Ser-297 is very common, it peaks 5 minutes after BCR stimulation, and creates a binding site for YWHAG. Phosphorylation at Tyr-630 creates a binding site for BLNK. Dephosphorylated by PTPN6.By similarity3 Publications

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P43405

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P43405

MaxQB - The MaxQuant DataBase

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MaxQBi
P43405

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

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PaxDbi
P43405

PeptideAtlas

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PeptideAtlasi
P43405

PRoteomics IDEntifications database

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PRIDEi
P43405

ProteomicsDB human proteome resource

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ProteomicsDBi
55634
55635 [P43405-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P43405

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

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PhosphoSitePlusi
P43405

<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

Widely expressed in hematopoietic cells (at protein level). Within the B-cells compartment it is for instance expressed for pro-B-cells to plasma cells.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000165025 Expressed in 185 organ(s), highest expression level in leukocyte

CleanEx database of gene expression profiles

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CleanExi
HS_SYK

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P43405 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P43405 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB007773
HPA001384

<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 LYN; phosphorylates SYK (By similarity). Interacts with RHOH (phosphorylated); regulates mast cells activation (By similarity). Interacts with NFAM1 (phosphorylated); probably involved in BCR signaling (By similarity). Interacts with VAV1 (via SH2 domain); phosphorylates VAV1 upon BCR activation. Interacts with GAB2 (phosphorylated); probably involved in IgE Fc receptor signaling (By similarity). Interacts (via its SH2 domains) with CD79A (via its phosphorylated ITAM domain); the interaction stimulates SYK autophosphorylation and activation (By similarity). Interacts with FCRL3 (PubMed:19843936, PubMed:11162587). Interacts (via SH2 domains) with FCER1G (via ITAM domain); activates SYK and mediates neutrophils and macrophages integrin-mediated activation (By similarity). Interaction with FCER1G in basophils triggers IL3-induced IL4 production (By similarity). Interacts with ITGB2 and FGR; involved in ITGB2 downstream signaling (By similarity). Interacts with ITGB3; upon activation by ITGB3 promotes platelet adhesion. Interacts (via SH2 domains) with TYROBP (via ITAM domain); involved in neutrophils and macrophages integrin-mediated activation (By similarity). Interacts with MSN and SELPLG; mediates the selectin-dependent activation of SYK by SELPLG. Interacts with BLNK (via SH2 domain). Interacts (via the second SH2 domain) with USP25 (via C-terminus); phosphorylates USP25 and regulates USP25 intracellular levels. Interacts (via SH2 domains) with CLEC1B (dimer). Interacts with CLEC7A; participates in leukocyte activation in presence of fungal pathogens. Interacts (phosphorylated) with SLA; may regulate SYK through CBL recruitment. Interacts with YWHAG; attenuates BCR-induced membrane translocation and activation of SYK. Interacts (via SH2 domains) with GCSAM; the interaction increases after B-cell receptor stimulation, resulting in enhanced SYK autophosphorylation and activity. Interacts with TNS2; leading to the phosphorylation of SYK (PubMed:22019427). Interacts with FLNA (via filamin repeat 5); docks SYK to the plasma membrane (PubMed:20713593). Interacts with CEACAM1; lipopolysaccharide activated neutrophils induce phosphorylation of SYK resulting in the formation of a complex including TLR4 and the phosphorylated form of SYK and CEACAM1, which in turn, recruits PTPN6 that dephosphorylates SYK, reducing the production of reactive oxygen species (ROS) and lysosome disruption, leading to a reduction of the inflammasome activity (By similarity). Interacts (via SH2 domains) with CEACAM20 (phosphorylated form); the interaction further enhances CEACAM20 phosphorylation (By similarity).By similarity17 Publications
(Microbial infection) Interacts with Epstein-Barr virus LMP2A.1 Publication

<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
112717, 111 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P43405

Database of interacting proteins

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DIPi
DIP-253N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
P43405

Protein interaction database and analysis system

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IntActi
P43405, 46 interactors

Molecular INTeraction database

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MINTi
P43405

STRING: functional protein association networks

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STRINGi
9606.ENSP00000364898

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P43405

<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

1635
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
1A81X-ray3.00A/C/E/G/I/K9-262[»]
1CSYNMR-A163-265[»]
1CSZNMR-A163-265[»]
1XBAX-ray2.00A356-635[»]
1XBBX-ray1.57A356-635[»]
1XBCX-ray2.00A356-635[»]
3BUWX-ray1.45A/C317-329[»]
3EMGX-ray2.60A349-635[»]
3FQEX-ray2.50A356-635[»]
3FQHX-ray2.26A/B356-635[»]
3FQSX-ray2.10A356-635[»]
3SRVX-ray1.95A/B360-635[»]
3TUBX-ray2.23A343-635[»]
3TUCX-ray2.10A343-635[»]
3TUDX-ray2.33A343-635[»]
3VF8X-ray2.08A343-635[»]
3VF9X-ray2.30A343-635[»]
4DFLX-ray1.98A363-635[»]
4DFNX-ray2.48A363-635[»]
4F4PX-ray2.37A365-635[»]
4FL1X-ray1.79A356-635[»]
4FL2X-ray2.19A1-635[»]
4FL3X-ray1.90A1-635[»]
4FYNX-ray2.32A356-635[»]
4FYOX-ray1.40A356-635[»]
4FZ6X-ray1.85A356-635[»]
4FZ7X-ray1.75A356-635[»]
4GFGX-ray2.35A356-635[»]
4I0RX-ray2.10A356-635[»]
4I0SX-ray1.98A356-635[»]
4I0TX-ray1.70A356-635[»]
4PUZX-ray2.08A/B356-635[»]
4PV0X-ray2.00A363-635[»]
4PX6X-ray1.60A356-635[»]
4RSSX-ray1.83A356-635[»]
4RX7X-ray1.80A356-635[»]
4RX8X-ray1.59A356-635[»]
4RX9X-ray1.75A356-635[»]
4WNMX-ray2.50A343-635[»]
4XG2X-ray2.21A356-635[»]
4XG3X-ray2.30A/B356-635[»]
4XG4X-ray2.30A356-635[»]
4XG6X-ray2.40A356-635[»]
4XG7X-ray1.76A356-635[»]
4XG8X-ray2.40A/C356-635[»]
4XG9X-ray2.91A/B356-635[»]
4YJOX-ray1.60A355-635[»]
4YJPX-ray1.83A355-635[»]
4YJQX-ray1.34A355-635[»]
4YJRX-ray1.32A355-635[»]
4YJSX-ray2.22A355-635[»]
4YJTX-ray1.52A355-635[»]
4YJUX-ray1.67A355-635[»]
4YJVX-ray1.65A355-635[»]
5C26X-ray1.95A343-635[»]
5C27X-ray2.15A343-635[»]
5CXHX-ray1.90A356-635[»]
5CXZX-ray1.70A356-635[»]
5CY3X-ray1.76A356-635[»]
5GHVX-ray2.80A/B356-635[»]
5LMAX-ray1.43A360-635[»]
5LMBX-ray1.95A/B360-635[»]
5T68X-ray2.93A/B356-635[»]
5TIUX-ray1.49A356-635[»]
5TR6X-ray1.93A356-635[»]
5TT7X-ray1.77A356-635[»]
5Y5TX-ray1.80A356-635[»]
5Y5UX-ray2.14A/B356-635[»]
6HM6X-ray2.10A360-635[»]
6HM7X-ray1.64A360-635[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P43405

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

More...
SMRi
P43405

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
P43405

<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>Domaini15 – 107SH2 1PROSITE-ProRule annotationAdd BLAST93
Domaini168 – 259SH2 2PROSITE-ProRule annotationAdd BLAST92
Domaini371 – 631Protein kinasePROSITE-ProRule annotationAdd BLAST261

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>Regioni108 – 167Interdomain AAdd BLAST60
Regioni260 – 370Interdomain BAdd BLAST111

<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

The SH2 domains mediate the interaction of SYK with the phosphorylated ITAM domains of transmembrane proteins. Some proteins like CLEC1B have a partial ITAM domain (also called hemITAM) containing a single YxxL motif. The interaction with SYK requires CLEC1B homodimerization.

<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
ENSGT00940000159053

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
P43405

KEGG Orthology (KO)

More...
KOi
K05855

Identification of Orthologs from Complete Genome Data

More...
OMAi
TFNPYEP

Database of Orthologous Groups

More...
OrthoDBi
1380051at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P43405

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 (2)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 2 <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 Long (identifier: P43405-1) [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
MASSGMADSA NHLPFFFGNI TREEAEDYLV QGGMSDGLYL LRQSRNYLGG
60 70 80 90 100
FALSVAHGRK AHHYTIEREL NGTYAIAGGR THASPADLCH YHSQESDGLV
110 120 130 140 150
CLLKKPFNRP QGVQPKTGPF EDLKENLIRE YVKQTWNLQG QALEQAIISQ
160 170 180 190 200
KPQLEKLIAT TAHEKMPWFH GKISREESEQ IVLIGSKTNG KFLIRARDNN
210 220 230 240 250
GSYALCLLHE GKVLHYRIDK DKTGKLSIPE GKKFDTLWQL VEHYSYKADG
260 270 280 290 300
LLRVLTVPCQ KIGTQGNVNF GGRPQLPGSH PATWSAGGII SRIKSYSFPK
310 320 330 340 350
PGHRKSSPAQ GNRQESTVSF NPYEPELAPW AADKGPQREA LPMDTEVYES
360 370 380 390 400
PYADPEEIRP KEVYLDRKLL TLEDKELGSG NFGTVKKGYY QMKKVVKTVA
410 420 430 440 450
VKILKNEAND PALKDELLAE ANVMQQLDNP YIVRMIGICE AESWMLVMEM
460 470 480 490 500
AELGPLNKYL QQNRHVKDKN IIELVHQVSM GMKYLEESNF VHRDLAARNV
510 520 530 540 550
LLVTQHYAKI SDFGLSKALR ADENYYKAQT HGKWPVKWYA PECINYYKFS
560 570 580 590 600
SKSDVWSFGV LMWEAFSYGQ KPYRGMKGSE VTAMLEKGER MGCPAGCPRE
610 620 630
MYDLMNLCWT YDVENRPGFA AVELRLRNYY YDVVN
Length:635
Mass (Da):72,066
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:iEAA6BDE65881FC68
GO
Isoform Short (identifier: P43405-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     283-305: Missing.

Show »
Length:612
Mass (Da):69,510
Checksum:i1D4FD24C6C9F5C53
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 conflicti119P → A in CAA51970 (PubMed:8168854).Curated1
Sequence conflicti250G → P in CAA51970 (PubMed:8168854).Curated1

Natural variant

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_03383845R → H. Corresponds to variant dbSNP:rs16906862Ensembl.1

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_005010283 – 305Missing in isoform Short. 1 PublicationAdd BLAST23

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
Z29630 mRNA Translation: CAA82737.1
L28824 mRNA Translation: AAA36526.1
AL354862 Genomic DNA No translation available.
BC001645 mRNA Translation: AAH01645.1
BC011399 mRNA Translation: AAH11399.1
BC002962 mRNA Translation: AAH02962.1
X73568 mRNA Translation: CAA51970.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS47992.1 [P43405-2]
CCDS6688.1 [P43405-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
A53596

NCBI Reference Sequences

More...
RefSeqi
NP_001128524.1, NM_001135052.3 [P43405-2]
NP_001167638.1, NM_001174167.2 [P43405-1]
NP_001167639.1, NM_001174168.2 [P43405-2]
NP_003168.2, NM_003177.6 [P43405-1]
XP_005252204.1, XM_005252147.3 [P43405-1]
XP_011517248.1, XM_011518946.2 [P43405-1]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.371720

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000375746; ENSP00000364898; ENSG00000165025 [P43405-1]
ENST00000375747; ENSP00000364899; ENSG00000165025 [P43405-2]
ENST00000375751; ENSP00000364904; ENSG00000165025 [P43405-2]
ENST00000375754; ENSP00000364907; ENSG00000165025 [P43405-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
6850

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:6850

UCSC genome browser

More...
UCSCi
uc004aqz.4 human [P43405-1]

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

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z29630 mRNA Translation: CAA82737.1
L28824 mRNA Translation: AAA36526.1
AL354862 Genomic DNA No translation available.
BC001645 mRNA Translation: AAH01645.1
BC011399 mRNA Translation: AAH11399.1
BC002962 mRNA Translation: AAH02962.1
X73568 mRNA Translation: CAA51970.1
CCDSiCCDS47992.1 [P43405-2]
CCDS6688.1 [P43405-1]
PIRiA53596
RefSeqiNP_001128524.1, NM_001135052.3 [P43405-2]
NP_001167638.1, NM_001174167.2 [P43405-1]
NP_001167639.1, NM_001174168.2 [P43405-2]
NP_003168.2, NM_003177.6 [P43405-1]
XP_005252204.1, XM_005252147.3 [P43405-1]
XP_011517248.1, XM_011518946.2 [P43405-1]
UniGeneiHs.371720

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A81X-ray3.00A/C/E/G/I/K9-262[»]
1CSYNMR-A163-265[»]
1CSZNMR-A163-265[»]
1XBAX-ray2.00A356-635[»]
1XBBX-ray1.57A356-635[»]
1XBCX-ray2.00A356-635[»]
3BUWX-ray1.45A/C317-329[»]
3EMGX-ray2.60A349-635[»]
3FQEX-ray2.50A356-635[»]
3FQHX-ray2.26A/B356-635[»]
3FQSX-ray2.10A356-635[»]
3SRVX-ray1.95A/B360-635[»]
3TUBX-ray2.23A343-635[»]
3TUCX-ray2.10A343-635[»]
3TUDX-ray2.33A343-635[»]
3VF8X-ray2.08A343-635[»]
3VF9X-ray2.30A343-635[»]
4DFLX-ray1.98A363-635[»]
4DFNX-ray2.48A363-635[»]
4F4PX-ray2.37A365-635[»]
4FL1X-ray1.79A356-635[»]
4FL2X-ray2.19A1-635[»]
4FL3X-ray1.90A1-635[»]
4FYNX-ray2.32A356-635[»]
4FYOX-ray1.40A356-635[»]
4FZ6X-ray1.85A356-635[»]
4FZ7X-ray1.75A356-635[»]
4GFGX-ray2.35A356-635[»]
4I0RX-ray2.10A356-635[»]
4I0SX-ray1.98A356-635[»]
4I0TX-ray1.70A356-635[»]
4PUZX-ray2.08A/B356-635[»]
4PV0X-ray2.00A363-635[»]
4PX6X-ray1.60A356-635[»]
4RSSX-ray1.83A356-635[»]
4RX7X-ray1.80A356-635[»]
4RX8X-ray1.59A356-635[»]
4RX9X-ray1.75A356-635[»]
4WNMX-ray2.50A343-635[»]
4XG2X-ray2.21A356-635[»]
4XG3X-ray2.30A/B356-635[»]
4XG4X-ray2.30A356-635[»]
4XG6X-ray2.40A356-635[»]
4XG7X-ray1.76A356-635[»]
4XG8X-ray2.40A/C356-635[»]
4XG9X-ray2.91A/B356-635[»]
4YJOX-ray1.60A355-635[»]
4YJPX-ray1.83A355-635[»]
4YJQX-ray1.34A355-635[»]
4YJRX-ray1.32A355-635[»]
4YJSX-ray2.22A355-635[»]
4YJTX-ray1.52A355-635[»]
4YJUX-ray1.67A355-635[»]
4YJVX-ray1.65A355-635[»]
5C26X-ray1.95A343-635[»]
5C27X-ray2.15A343-635[»]
5CXHX-ray1.90A356-635[»]
5CXZX-ray1.70A356-635[»]
5CY3X-ray1.76A356-635[»]
5GHVX-ray2.80A/B356-635[»]
5LMAX-ray1.43A360-635[»]
5LMBX-ray1.95A/B360-635[»]
5T68X-ray2.93A/B356-635[»]
5TIUX-ray1.49A356-635[»]
5TR6X-ray1.93A356-635[»]
5TT7X-ray1.77A356-635[»]
5Y5TX-ray1.80A356-635[»]
5Y5UX-ray2.14A/B356-635[»]
6HM6X-ray2.10A360-635[»]
6HM7X-ray1.64A360-635[»]
ProteinModelPortaliP43405
SMRiP43405
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112717, 111 interactors
CORUMiP43405
DIPiDIP-253N
ELMiP43405
IntActiP43405, 46 interactors
MINTiP43405
STRINGi9606.ENSP00000364898

Chemistry databases

BindingDBiP43405
ChEMBLiCHEMBL2599
DrugBankiDB08846 Ellagic Acid
DB02010 Staurosporine
GuidetoPHARMACOLOGYi2230

Protein family/group databases

MoonDBiP43405 Predicted

PTM databases

iPTMnetiP43405
PhosphoSitePlusiP43405

Polymorphism and mutation databases

BioMutaiSYK
DMDMi1174527

Proteomic databases

EPDiP43405
jPOSTiP43405
MaxQBiP43405
PaxDbiP43405
PeptideAtlasiP43405
PRIDEiP43405
ProteomicsDBi55634
55635 [P43405-2]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
6850
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000375746; ENSP00000364898; ENSG00000165025 [P43405-1]
ENST00000375747; ENSP00000364899; ENSG00000165025 [P43405-2]
ENST00000375751; ENSP00000364904; ENSG00000165025 [P43405-2]
ENST00000375754; ENSP00000364907; ENSG00000165025 [P43405-1]
GeneIDi6850
KEGGihsa:6850
UCSCiuc004aqz.4 human [P43405-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
6850
DisGeNETi6850
EuPathDBiHostDB:ENSG00000165025.14

GeneCards: human genes, protein and diseases

More...
GeneCardsi
SYK
HGNCiHGNC:11491 SYK
HPAiCAB007773
HPA001384
MIMi600085 gene
neXtProtiNX_P43405
OpenTargetsiENSG00000165025
PharmGKBiPA36273

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiENOG410IH0T Eukaryota
COG0515 LUCA
GeneTreeiENSGT00940000159053
HOGENOMiHOG000113264
HOVERGENiHBG001540
InParanoidiP43405
KOiK05855
OMAiTFNPYEP
OrthoDBi1380051at2759
PhylomeDBiP43405
TreeFamiTF351629

Enzyme and pathway databases

BRENDAi2.7.10.2 2681
ReactomeiR-HSA-114604 GPVI-mediated activation cascade
R-HSA-2029481 FCGR activation
R-HSA-2029482 Regulation of actin dynamics for phagocytic cup formation
R-HSA-2029485 Role of phospholipids in phagocytosis
R-HSA-2424491 DAP12 signaling
R-HSA-2454202 Fc epsilon receptor (FCERI) signaling
R-HSA-2730905 Role of LAT2/NTAL/LAB on calcium mobilization
R-HSA-2871796 FCERI mediated MAPK activation
R-HSA-2871809 FCERI mediated Ca+2 mobilization
R-HSA-354192 Integrin alphaIIb beta3 signaling
R-HSA-5607764 CLEC7A (Dectin-1) signaling
R-HSA-5621480 Dectin-2 family
R-HSA-9020558 Interleukin-2 signaling
R-HSA-912631 Regulation of signaling by CBL
R-HSA-983695 Antigen activates B Cell Receptor (BCR) leading to generation of second messengers
SignaLinkiP43405
SIGNORiP43405

Miscellaneous databases

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

More...
ChiTaRSi
SYK human
EvolutionaryTraceiP43405

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
Syk

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

More...
GenomeRNAii
6850

Protein Ontology

More...
PROi
PR:P43405

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000165025 Expressed in 185 organ(s), highest expression level in leukocyte
CleanExiHS_SYK
ExpressionAtlasiP43405 baseline and differential
GenevisibleiP43405 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 nameiKSYK_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: P43405
<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 217 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 9
    Human chromosome 9: entries, gene names and cross-references to MIM
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