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Entry version 192 (17 Jun 2020)
Sequence version 4 (13 Nov 2013)
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Protein

Proto-oncogene tyrosine-protein kinase Src

Gene

Src

Organism
Rattus norvegicus (Rat)
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 protein tyrosine kinase which is activated following engagement of many different classes of cellular receptors including immune response receptors, integrins and other adhesion receptors, receptor protein tyrosine kinases, G protein-coupled receptors as well as cytokine receptors. Participates in signaling pathways that control a diverse spectrum of biological activities including gene transcription, immune response, cell adhesion, cell cycle progression, apoptosis, migration, and transformation. Due to functional redundancy between members of the SRC kinase family, identification of the specific role of each SRC kinase is very difficult. SRC appears to be one of the primary kinases activated following engagement of receptors and plays a role in the activation of other protein tyrosine kinase (PTK) families. Receptor clustering or dimerization leads to recruitment of SRC to the receptor complexes where it phosphorylates the tyrosine residues within the receptor cytoplasmic domains. Plays an important role in the regulation of cytoskeletal organization through phosphorylation of specific substrates such as AFAP1. Phosphorylation of AFAP1 allows the SRC SH2 domain to bind AFAP1 and to localize to actin filaments. Cytoskeletal reorganization is also controlled through the phosphorylation of cortactin (CTTN) (Probable). When cells adhere via focal adhesions to the extracellular matrix, signals are transmitted by integrins into the cell resulting in tyrosine phosphorylation of a number of focal adhesion proteins, including PTK2/FAK1 and paxillin (PXN) (By similarity). In addition to phosphorylating focal adhesion proteins, SRC is also active at the sites of cell-cell contact adherens junctions and phosphorylates substrates such as beta-catenin (CTNNB1), delta-catenin (CTNND1), and plakoglobin (JUP). Another type of cell-cell junction, the gap junction, is also a target for SRC, which phosphorylates connexin-43 (GJA1). SRC is implicated in regulation of pre-mRNA-processing and phosphorylates RNA-binding proteins such as KHDRBS1 (Probable). Also plays a role in PDGF-mediated tyrosine phosphorylation of both STAT1 and STAT3, leading to increased DNA binding activity of these transcription factors (By similarity). Involved in the RAS pathway through phosphorylation of RASA1 and RASGRF1. Plays a role in EGF-mediated calcium-activated chloride channel activation (By similarity). Required for epidermal growth factor receptor (EGFR) internalization through phosphorylation of clathrin heavy chain (CLTC and CLTCL1) at 'Tyr-1477'. Involved in beta-arrestin (ARRB1 and ARRB2) desensitization through phosphorylation and activation of GRK2, leading to beta-arrestin phosphorylation and internalization. Has a critical role in the stimulation of the CDK20/MAPK3 mitogen-activated protein kinase cascade by epidermal growth factor (Probable). Might be involved not only in mediating the transduction of mitogenic signals at the level of the plasma membrane but also in controlling progression through the cell cycle via interaction with regulatory proteins in the nucleus. Plays an important role in osteoclastic bone resorption in conjunction with PTK2B/PYK2. Both the formation of a SRC-PTK2B/PYK2 complex and SRC kinase activity are necessary for this function. Recruited to activated integrins by PTK2B/PYK2, thereby phosphorylating CBL, which in turn induces the activation and recruitment of phosphatidylinositol 3-kinase to the cell membrane in a signaling pathway that is critical for osteoclast function. Promotes energy production in osteoclasts by activating mitochondrial cytochrome C oxidase (By similarity). Phosphorylates DDR2 on tyrosine residues, thereby promoting its subsequent autophosphorylation (PubMed:16186108). Phosphorylates RUNX3 and COX2 on tyrosine residues, TNK2 on 'Tyr-284' and CBL on 'Tyr-738'. Enhances DDX58/RIG-I-elicited antiviral signaling. Phosphorylates PDPK1 at 'Tyr-9', 'Tyr-373' and 'Tyr-376'. Phosphorylates BCAR1 at 'Tyr-226'. Phosphorylates CBLC at multiple tyrosine residues, phosphorylation at 'Tyr-341' activates CBLC E3 activity. Involved in anchorage-independent cell growth (By similarity). Required for podosome formation (By similarity).By similarityCurated1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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

Phosphorylation by CSK at Tyr-530 inhibits kinase activity. Inhibitory phosphorylation at Tyr-530 is enhanced by heme. Further phosphorylation by CDK1 partially reactivates CSK-inactivated SRC and facilitates complete reactivation by protein tyrosine phosphatase PTPRC. Integrin engagement stimulates kinase activity. Phosphorylation by PTK2/FAK1 enhances kinase activity. Butein and pseudosubstrate-based peptide inhibitors like CIYKYYF act as inhibitors (By similarity). Phosphorylation at Tyr-419 increases kinase activity.By similarity1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei298ATPPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei389Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 bindingi276 – 284ATPPROSITE-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 processCell adhesion, Cell cycle, Immunity
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.10.2 5301

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-1227986 Signaling by ERBB2
R-RNO-1251985 Nuclear signaling by ERBB4
R-RNO-1253288 Downregulation of ERBB4 signaling
R-RNO-1257604 PIP3 activates AKT signaling
R-RNO-1295596 Spry regulation of FGF signaling
R-RNO-1433557 Signaling by SCF-KIT
R-RNO-1433559 Regulation of KIT signaling
R-RNO-177929 Signaling by EGFR
R-RNO-180292 GAB1 signalosome
R-RNO-186763 Downstream signal transduction
R-RNO-191650 Regulation of gap junction activity
R-RNO-2029481 FCGR activation
R-RNO-210990 PECAM1 interactions
R-RNO-354192 Integrin signaling
R-RNO-354194 GRB2:SOS provides linkage to MAPK signaling for Integrins
R-RNO-372708 p130Cas linkage to MAPK signaling for integrins
R-RNO-389356 CD28 co-stimulation
R-RNO-389513 CTLA4 inhibitory signaling
R-RNO-3928662 EPHB-mediated forward signaling
R-RNO-3928663 EPHA-mediated growth cone collapse
R-RNO-3928664 Ephrin signaling
R-RNO-3928665 EPH-ephrin mediated repulsion of cells
R-RNO-418592 ADP signalling through P2Y purinoceptor 1
R-RNO-418594 G alpha (i) signalling events
R-RNO-418885 DCC mediated attractive signaling
R-RNO-430116 GP1b-IX-V activation signalling
R-RNO-437239 Recycling pathway of L1
R-RNO-4420097 VEGFA-VEGFR2 Pathway
R-RNO-456926 Thrombin signalling through proteinase activated receptors (PARs)
R-RNO-5218921 VEGFR2 mediated cell proliferation
R-RNO-5607764 CLEC7A (Dectin-1) signaling
R-RNO-5663220 RHO GTPases Activate Formins
R-RNO-5673000 RAF activation
R-RNO-5674135 MAP2K and MAPK activation
R-RNO-6811558 PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
R-RNO-69231 Cyclin D associated events in G1
R-RNO-8853659 RET signaling
R-RNO-8874081 MET activates PTK2 signaling
R-RNO-8934903 Receptor Mediated Mitophagy
R-RNO-8941858 Regulation of RUNX3 expression and activity
R-RNO-9009391 Extra-nuclear estrogen signaling
R-RNO-9603381 Activated NTRK3 signals through PI3K

<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%5Fand%5Ftaxonomy%5Fsection">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:
Proto-oncogene tyrosine-protein kinase Src (EC:2.7.10.21 Publication)
Alternative name(s):
Proto-oncogene c-Src
pp60c-src
Short name:
p60-Src
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:Src
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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 3
  • UP000234681 Componentsi: Chromosome 3, Unassembled WGS sequence

Organism-specific databases

Rat genome database

More...
RGDi
620795 Src

<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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Mitochondrion, Mitochondrion inner membrane, Nucleus

<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

Keywords - Diseasei

Proto-oncogene

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3014

<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 <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedBy similarity
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000881432 – 536Proto-oncogene tyrosine-protein kinase SrcAdd BLAST535

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi2N-myristoyl glycineBy similarity1
<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 residuei17PhosphoserineCombined sources1
Modified residuei75Phosphoserine; by CDK5By similarity1
Modified residuei187PhosphotyrosineBy similarity1
Modified residuei419Phosphotyrosine; by FAK21 Publication1
Modified residuei420Phosphothreonine; by autocatalysisBy similarity1
Modified residuei530Phosphotyrosine; by CSKBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

Myristoylated at Gly-2, and this is essential for targeting to membranes.By similarity
Dephosphorylated at Tyr-530 by PTPRJ. Phosphorylated on Tyr-530 by c-Src kinase (CSK). The phosphorylated form is termed pp60c-src (By similarity). Dephosphorylated by PTPRJ at Tyr-419. Normally maintained in an inactive conformation with the SH2 domain engaged with Tyr-530, the SH3 domain engaged with the SH2-kinase linker, and Tyr-419 dephosphorylated. Dephosphorylation of Tyr-530 as a result of protein tyrosine phosphatase (PTP) action disrupts the intramolecular interaction between the SH2 domain and Tyr-530, Tyr-419 can then become autophosphorylated, resulting in SRX activation. Phosphorylation of Tyr-530 by CSK allows this interaction to reform, resulting in SRC inactivation. CDK5-mediated phosphorylation at Ser-75 targets SRC to ubiquitin-dependent degradation and thus leads to cytoskeletal reorganization. Phosphorylated by PTK2/FAK1; this enhances kinase activity (By similarity). Phosphorylated by PTK2B/PYK2; this enhances kinase activity.By similarity2 Publications
S-nitrosylation is important for activation of its kinase activity.By similarity
Ubiquitinated in response to CDK5-mediated phosphorylation. Ubiquitination mediated by CBLC requires SRC autophosphorylation at Tyr-419 and may lead to lysosomal degradation (By similarity).By similarity

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein, Ubl conjugation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q9WUD9

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

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PaxDbi
Q9WUD9

PeptideAtlas

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PeptideAtlasi
Q9WUD9

PRoteomics IDEntifications database

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PRIDEi
Q9WUD9

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q9WUD9

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

More...
PhosphoSitePlusi
Q9WUD9

<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

Isoform 2 is expressed in the brain with highest expression in the pyramidal layers of the hippocampus and the granular layer of the dentate gyrus and moderate expression in cortical regions, with higher levels in the superficial layers than in the deep layers. Isoform 2 may be neuron-specific. Isoform 1 is expressed at very low levels in the forebrain.1 Publication

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Up-regulated by MK-801, an uncompetitive N-methyl-d-aspartate (NMDA) receptor antagonist, mostly in the superficial layers of the parietal, temporal, occipital and frontal cortices.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSRNOG00000009495 Expressed in brain and 9 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q9WUD9 RN

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Part of a complex comprised of PTPRA, BCAR1, BCAR3 (via SH2 domain) and SRC; the formation of the complex is dependent on integrin mediated-tyrosine phosphorylation of PTPRA (By similarity).

Interacts with DDEF1/ASAP1; via the SH3 domain (By similarity).

Interacts with CCPG1 (By similarity).

Identified in a complex containing FGFR4, NCAM1, CDH2, PLCG1, FRS2, SRC, SHC1, GAP43 and CTTN (By similarity).

Interacts with ERBB2, STAT1 and PNN (By similarity).

Interacts with CDCP1, PELP1, TGFB1I1 and TOM1L2 (By similarity).

Interacts with the cytoplasmic domain of MUC1, phosphorylates it and increases binding of MUC1 with beta-catenin (By similarity).

Interacts with RALGPS1; via the SH3 domain (By similarity).

Interacts with CAV2 (tyrosine phosphorylated form) (By similarity).

Interacts (via the SH3 domain and the protein kinase domain) with ARRB1; the interaction is independent of the phosphorylation state of SRC C-terminus (PubMed:10995467).

Interacts with ARRB1 and ARRB2 (PubMed:10995467) (By similarity).

Interacts with SRCIN1 (By similarity).

Interacts with NDFIP2 and more weakly with NDFIP1 (By similarity).

Interacts with PIK3CA and/or PIK3C2B, PTK2/FAK1 and ESR1 (dimethylated on arginine) (PubMed:8849729).

Interacts with FASLG (By similarity).

Interacts (via SH2 domain) with the 'Tyr-402' phosphorylated form of PTK2B/PYK2 (PubMed:8849729).

Interacts (via SH2 domain) with FLT3 (tyrosine phosphorylated) (By similarity).

Interacts (via SH2 and SH3 domain) with TNK2 (By similarity).

Interacts (via protein kinase domain) with the tyrosine phosphorylated form of RUNX3 (via runt domain) (By similarity).

Interacts with TRAF3 (via RING-type zinc finger domain) (By similarity).

Interacts with DDX58, MAVS and TBK1 (By similarity).

Interacts (via SH2 domain) with RACK1; the interaction is enhanced by tyrosine phosphorylation of RACK1 and inhibits SRC activity (By similarity).

Interacts with EPHB1; activates the MAPK/ERK cascade to regulate cell migration (By similarity).

Interacts with FCAMR (By similarity).

Interacts with PDGFRA (tyrosine phosphorylated) (By similarity).

Interacts with CSF1R (By similarity).

Interacts with DDR1 (By similarity).

Interacts (via SH2 domain) with the 'Tyr-9' phosphorylated form of PDPK1 (By similarity).

Interacts with AMOTL2; this interaction promotes the translocation of phosphorylated SRC to peripheral cell-matrix adhesion sites (By similarity).

Interacts with DDR2 and DAB2 (PubMed:11884411, PubMed:12473651, PubMed:16186108).

Interacts with TRAP1 (By similarity).

Interacts with CBLC; the interaction is enhanced when SRC is phosphorylated at Tyr-419 (By similarity).

Interacts with ARHGEF5 (By similarity).

Interacts (via cytoplasmic domain) with CEACAM1 (via SH2 domain); this interaction is regulated by trans-homophilic cell adhesion (PubMed:19948503).

Interacts with MPP2 (By similarity).

Interacts with PRR7 (By similarity).

Interacts (via kinase domain and to a lesser extent the SH2 domain) directly with PDLIM4; this interaction results in PTPN13-mediated dephosphorylation of this protein leading to its inactivation (By similarity).

Interacts with P85 (PIK3R1 or PIK3R2) (By similarity).

Interacts with HNRNPA2B1 (By similarity).

By similarity6 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

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BioGRIDi
249840, 16 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q9WUD9

Database of interacting proteins

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DIPi
DIP-42731N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
Q9WUD9

Protein interaction database and analysis system

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IntActi
Q9WUD9, 33 interactors

Molecular INTeraction database

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MINTi
Q9WUD9

STRING: functional protein association networks

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STRINGi
10116.ENSRNOP00000012739

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
Q9WUD9

<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

3D structure databases

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

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SMRi
Q9WUD9

Database of comparative protein structure models

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ModBasei
Search...

<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%5Fand%5Fdomains%5Fsection">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>Domaini84 – 145SH3PROSITE-ProRule annotationAdd BLAST62
Domaini151 – 248SH2PROSITE-ProRule annotationAdd BLAST98
Domaini270 – 523Protein kinasePROSITE-ProRule annotationAdd BLAST254

<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. SRC subfamily.PROSITE-ProRule annotation

Keywords - Domaini

SH2 domain, SH3 domain

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0197 Eukaryota
COG0515 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000158250

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_000288_7_2_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q9WUD9

KEGG Orthology (KO)

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KOi
K05704

Identification of Orthologs from Complete Genome Data

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OMAi
XIASGMA

Database of Orthologous Groups

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OrthoDBi
539311at2759

TreeFam database of animal gene trees

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TreeFami
TF351634

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.30.505.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR000980 SH2
IPR036860 SH2_dom_sf
IPR036028 SH3-like_dom_sf
IPR001452 SH3_domain
IPR008266 Tyr_kinase_AS
IPR020635 Tyr_kinase_cat_dom

Pfam protein domain database

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Pfami
View protein in Pfam
PF07714 Pkinase_Tyr, 1 hit
PF00017 SH2, 1 hit
PF00018 SH3_1, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00401 SH2DOMAIN
PR00452 SH3DOMAIN
PR00109 TYRKINASE

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00252 SH2, 1 hit
SM00326 SH3, 1 hit
SM00219 TyrKc, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF50044 SSF50044, 1 hit
SSF55550 SSF55550, 1 hit
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

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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, 1 hit
PS50002 SH3, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

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. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform 1 (identifier: Q9WUD9-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
MGSNKSKPKD ASQRRRSLEP AENVHGAGGA FPASQTPSKP ASADGHRGPN
60 70 80 90 100
AAFVPPAAAE PKLFGGFNSS DTVTSPQRAG PLAGGVTTFV ALYDYESRTE
110 120 130 140 150
TDLSFKKGER LQIVNNTEGD WWLAHSLSTG QTGYIPSNYV APSDSIQAEE
160 170 180 190 200
WYFGKITRRE SERLLLNAEN PRGTFLVRES ETTKGAYCLS VSDFDNAKGL
210 220 230 240 250
NVKHYKIRKL DSGGFYITSR TQFNSLQQLV AYYSKHADGL CHRLTTVCPT
260 270 280 290 300
SKPQTQGLAK DAWEIPRESL RLEVKLGQGC FGEVWMGTWN GTTRVAIKTL
310 320 330 340 350
KPGTMSPEAF LQEAQVMKKL RHEKLVQLYA VVSEEPIYIV TEYMNKGSLL
360 370 380 390 400
DFLKGETGKY LRLPQLVDMS AQIASGMAYV ERMNYVHRDL RAANILVGEN
410 420 430 440 450
LVCKVADFGL ARLIEDNEYT ARQGAKFPIK WTAPEAALYG RFTIKSDVWS
460 470 480 490 500
FGILLTELTT KGRVPYPGMV NREVLDQVER GYRMPCPPEC PESLHDLMCQ
510 520 530
CWRKEPEERP TFEYLQAFLE DYFTSTEPQY QPGENL
Length:536
Mass (Da):59,973
Last modified:November 13, 2013 - v4
<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:i453D1E904EC660A3
GO
Isoform 2 (identifier: Q9WUD9-2) [UniParc]FASTAAdd to basket
Also known as: Neuronal Src

The sequence of this isoform differs from the canonical sequence as follows:
     117-117: T → TRKVDVR

Show »
Length:542
Mass (Da):60,727
Checksum:i6AC21D6DD66B0B39
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 conflicti143S → F in AAD24180 (Ref. 1) Curated1
Sequence conflicti143S → F in AAZ23849 (Ref. 5) Curated1
Sequence conflicti143S → F in AAZ23848 (Ref. 5) Curated1
Sequence conflicti381E → D in AAD24180 (Ref. 1) Curated1
Sequence conflicti381E → D in AAZ23849 (Ref. 5) Curated1
Sequence conflicti381E → D in AAZ23848 (Ref. 5) Curated1
Sequence conflicti528P → R in AAD24180 (Ref. 1) Curated1
Sequence conflicti528P → R in AAZ23849 (Ref. 5) Curated1
Sequence conflicti528P → R in AAZ23848 (Ref. 5) Curated1

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.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_053395117T → TRKVDVR in isoform 2. 1 Publication1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AF130457 mRNA Translation: AAD24180.1
AF157016 mRNA Translation: AAF80335.1
AABR06027223 Genomic DNA No translation available.
CH474005 Genomic DNA Translation: EDL96675.1
CH474005 Genomic DNA Translation: EDL96676.1
CH474005 Genomic DNA Translation: EDL96677.1
CH474005 Genomic DNA Translation: EDL96678.1
CH474005 Genomic DNA Translation: EDL96679.1
DQ120509 mRNA Translation: AAZ23848.1
DQ120510 mRNA Translation: AAZ23849.1

NCBI Reference Sequences

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RefSeqi
NP_114183.1, NM_031977.1 [Q9WUD9-2]
XP_008760609.1, XM_008762387.2 [Q9WUD9-2]
XP_008760610.1, XM_008762388.2 [Q9WUD9-2]
XP_017447554.1, XM_017592065.1 [Q9WUD9-2]
XP_017447555.1, XM_017592066.1 [Q9WUD9-2]
XP_017447556.1, XM_017592067.1 [Q9WUD9-2]
XP_017447557.1, XM_017592068.1 [Q9WUD9-2]
XP_017447558.1, XM_017592069.1 [Q9WUD9-2]
XP_017447559.1, XM_017592070.1 [Q9WUD9-2]
XP_017447560.1, XM_017592071.1 [Q9WUD9-2]
XP_017447561.1, XM_017592072.1 [Q9WUD9-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSRNOT00000012739; ENSRNOP00000012739; ENSRNOG00000009495 [Q9WUD9-1]
ENSRNOT00000080516; ENSRNOP00000071837; ENSRNOG00000009495 [Q9WUD9-2]

Database of genes from NCBI RefSeq genomes

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GeneIDi
83805

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
rno:83805

UCSC genome browser

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UCSCi
RGD:620795 rat [Q9WUD9-1]

Keywords - Coding sequence diversityi

Alternative splicing

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF130457 mRNA Translation: AAD24180.1
AF157016 mRNA Translation: AAF80335.1
AABR06027223 Genomic DNA No translation available.
CH474005 Genomic DNA Translation: EDL96675.1
CH474005 Genomic DNA Translation: EDL96676.1
CH474005 Genomic DNA Translation: EDL96677.1
CH474005 Genomic DNA Translation: EDL96678.1
CH474005 Genomic DNA Translation: EDL96679.1
DQ120509 mRNA Translation: AAZ23848.1
DQ120510 mRNA Translation: AAZ23849.1
RefSeqiNP_114183.1, NM_031977.1 [Q9WUD9-2]
XP_008760609.1, XM_008762387.2 [Q9WUD9-2]
XP_008760610.1, XM_008762388.2 [Q9WUD9-2]
XP_017447554.1, XM_017592065.1 [Q9WUD9-2]
XP_017447555.1, XM_017592066.1 [Q9WUD9-2]
XP_017447556.1, XM_017592067.1 [Q9WUD9-2]
XP_017447557.1, XM_017592068.1 [Q9WUD9-2]
XP_017447558.1, XM_017592069.1 [Q9WUD9-2]
XP_017447559.1, XM_017592070.1 [Q9WUD9-2]
XP_017447560.1, XM_017592071.1 [Q9WUD9-2]
XP_017447561.1, XM_017592072.1 [Q9WUD9-1]

3D structure databases

SMRiQ9WUD9
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi249840, 16 interactors
CORUMiQ9WUD9
DIPiDIP-42731N
ELMiQ9WUD9
IntActiQ9WUD9, 33 interactors
MINTiQ9WUD9
STRINGi10116.ENSRNOP00000012739

Chemistry databases

BindingDBiQ9WUD9
ChEMBLiCHEMBL3014

PTM databases

iPTMnetiQ9WUD9
PhosphoSitePlusiQ9WUD9

Proteomic databases

jPOSTiQ9WUD9
PaxDbiQ9WUD9
PeptideAtlasiQ9WUD9
PRIDEiQ9WUD9

Genome annotation databases

EnsembliENSRNOT00000012739; ENSRNOP00000012739; ENSRNOG00000009495 [Q9WUD9-1]
ENSRNOT00000080516; ENSRNOP00000071837; ENSRNOG00000009495 [Q9WUD9-2]
GeneIDi83805
KEGGirno:83805
UCSCiRGD:620795 rat [Q9WUD9-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
6714
RGDi620795 Src

Phylogenomic databases

eggNOGiKOG0197 Eukaryota
COG0515 LUCA
GeneTreeiENSGT00940000158250
HOGENOMiCLU_000288_7_2_1
InParanoidiQ9WUD9
KOiK05704
OMAiXIASGMA
OrthoDBi539311at2759
TreeFamiTF351634

Enzyme and pathway databases

BRENDAi2.7.10.2 5301
ReactomeiR-RNO-1227986 Signaling by ERBB2
R-RNO-1251985 Nuclear signaling by ERBB4
R-RNO-1253288 Downregulation of ERBB4 signaling
R-RNO-1257604 PIP3 activates AKT signaling
R-RNO-1295596 Spry regulation of FGF signaling
R-RNO-1433557 Signaling by SCF-KIT
R-RNO-1433559 Regulation of KIT signaling
R-RNO-177929 Signaling by EGFR
R-RNO-180292 GAB1 signalosome
R-RNO-186763 Downstream signal transduction
R-RNO-191650 Regulation of gap junction activity
R-RNO-2029481 FCGR activation
R-RNO-210990 PECAM1 interactions
R-RNO-354192 Integrin signaling
R-RNO-354194 GRB2:SOS provides linkage to MAPK signaling for Integrins
R-RNO-372708 p130Cas linkage to MAPK signaling for integrins
R-RNO-389356 CD28 co-stimulation
R-RNO-389513 CTLA4 inhibitory signaling
R-RNO-3928662 EPHB-mediated forward signaling
R-RNO-3928663 EPHA-mediated growth cone collapse
R-RNO-3928664 Ephrin signaling
R-RNO-3928665 EPH-ephrin mediated repulsion of cells
R-RNO-418592 ADP signalling through P2Y purinoceptor 1
R-RNO-418594 G alpha (i) signalling events
R-RNO-418885 DCC mediated attractive signaling
R-RNO-430116 GP1b-IX-V activation signalling
R-RNO-437239 Recycling pathway of L1
R-RNO-4420097 VEGFA-VEGFR2 Pathway
R-RNO-456926 Thrombin signalling through proteinase activated receptors (PARs)
R-RNO-5218921 VEGFR2 mediated cell proliferation
R-RNO-5607764 CLEC7A (Dectin-1) signaling
R-RNO-5663220 RHO GTPases Activate Formins
R-RNO-5673000 RAF activation
R-RNO-5674135 MAP2K and MAPK activation
R-RNO-6811558 PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
R-RNO-69231 Cyclin D associated events in G1
R-RNO-8853659 RET signaling
R-RNO-8874081 MET activates PTK2 signaling
R-RNO-8934903 Receptor Mediated Mitophagy
R-RNO-8941858 Regulation of RUNX3 expression and activity
R-RNO-9009391 Extra-nuclear estrogen signaling
R-RNO-9603381 Activated NTRK3 signals through PI3K

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q9WUD9

Gene expression databases

BgeeiENSRNOG00000009495 Expressed in brain and 9 other tissues
GenevisibleiQ9WUD9 RN

Family and domain databases

Gene3Di3.30.505.10, 1 hit
InterProiView protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR000980 SH2
IPR036860 SH2_dom_sf
IPR036028 SH3-like_dom_sf
IPR001452 SH3_domain
IPR008266 Tyr_kinase_AS
IPR020635 Tyr_kinase_cat_dom
PfamiView protein in Pfam
PF07714 Pkinase_Tyr, 1 hit
PF00017 SH2, 1 hit
PF00018 SH3_1, 1 hit
PRINTSiPR00401 SH2DOMAIN
PR00452 SH3DOMAIN
PR00109 TYRKINASE
SMARTiView protein in SMART
SM00252 SH2, 1 hit
SM00326 SH3, 1 hit
SM00219 TyrKc, 1 hit
SUPFAMiSSF50044 SSF50044, 1 hit
SSF55550 SSF55550, 1 hit
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, 1 hit
PS50002 SH3, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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 nameiSRC_RAT
<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: Q9WUD9
Secondary accession number(s): G3V776, Q45QJ2, Q9JJ10
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 13, 2013
Last modified: June 17, 2020
This is version 192 of the entry and version 4 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

<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

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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