SRC report

I. Expression across cell types

II. Expression across tissues

sc-RNAseq data

Insufficient scRNA-seq data for expression of SRC at tissue level.

III. Associated gene sets

GO_0048013Biological processephrin receptor signaling pathway
GO_0042476Biological processodontogenesis
GO_0071498Biological processcellular response to fluid shear stress
GO_0060444Biological processbranching involved in mammary gland duct morphogenesis
GO_0014856Biological processskeletal muscle cell proliferation
GO_0001545Biological processprimary ovarian follicle growth
GO_0043114Biological processregulation of vascular permeability
GO_0045124Biological processregulation of bone resorption
GO_0031333Biological processnegative regulation of protein-containing complex assembly
GO_0051895Biological processnegative regulation of focal adhesion assembly
GO_0016236Biological processmacroautophagy
GO_0002862Biological processnegative regulation of inflammatory response to antigenic stimulus
GO_0030168Biological processplatelet activation
GO_0038128Biological processERBB2 signaling pathway
GO_0032211Biological processnegative regulation of telomere maintenance via telomerase
GO_0043066Biological processnegative regulation of apoptotic process
GO_0050900Biological processleukocyte migration
GO_0035635Biological processentry of bacterium into host cell
GO_0051057Biological processpositive regulation of small GTPase mediated signal transduction
GO_0046579Biological processpositive regulation of Ras protein signal transduction
GO_0007173Biological processepidermal growth factor receptor signaling pathway
GO_0051897Biological processpositive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
GO_0009612Biological processresponse to mechanical stimulus
GO_2001243Biological processnegative regulation of intrinsic apoptotic signaling pathway
GO_0006468Biological processprotein phosphorylation
GO_0009410Biological processresponse to xenobiotic stimulus
GO_0010632Biological processregulation of epithelial cell migration
GO_0070374Biological processpositive regulation of ERK1 and ERK2 cascade
GO_1904707Biological processpositive regulation of vascular associated smooth muscle cell proliferation
GO_0070301Biological processcellular response to hydrogen peroxide
GO_0035331Biological processnegative regulation of hippo signaling
GO_0034332Biological processadherens junction organization
GO_2000386Biological processpositive regulation of ovarian follicle development
GO_0010629Biological processnegative regulation of gene expression
GO_0048011Biological processneurotrophin TRK receptor signaling pathway
GO_0022407Biological processregulation of cell-cell adhesion
GO_0045087Biological processinnate immune response
GO_0030900Biological processforebrain development
GO_0007165Biological processsignal transduction
GO_0031295Biological processT cell costimulation
GO_0035306Biological processpositive regulation of dephosphorylation
GO_2000811Biological processnegative regulation of anoikis
GO_0007155Biological processcell adhesion
GO_0014911Biological processpositive regulation of smooth muscle cell migration
GO_0010447Biological processresponse to acidic pH
GO_0060491Biological processregulation of cell projection assembly
GO_0071897Biological processDNA biosynthetic process
GO_0007229Biological processintegrin-mediated signaling pathway
GO_0034446Biological processsubstrate adhesion-dependent cell spreading
GO_0051450Biological processmyoblast proliferation
GO_0060576Biological processintestinal epithelial cell development
GO_0071375Biological processcellular response to peptide hormone stimulus
GO_0086091Biological processregulation of heart rate by cardiac conduction
GO_0010954Biological processpositive regulation of protein processing
GO_0045453Biological processbone resorption
GO_0010907Biological processpositive regulation of glucose metabolic process
GO_0071222Biological processcellular response to lipopolysaccharide
GO_0001819Biological processpositive regulation of cytokine production
GO_0046777Biological processprotein autophosphorylation
GO_0034139Biological processregulation of toll-like receptor 3 signaling pathway
GO_0051385Biological processresponse to mineralocorticoid
GO_0036120Biological processcellular response to platelet-derived growth factor stimulus
GO_0043154Biological processnegative regulation of cysteine-type endopeptidase activity involved in apoptotic process
GO_0071803Biological processpositive regulation of podosome assembly
GO_2000394Biological processpositive regulation of lamellipodium morphogenesis
GO_0032869Biological processcellular response to insulin stimulus
GO_0051974Biological processnegative regulation of telomerase activity
GO_0090263Biological processpositive regulation of canonical Wnt signaling pathway
GO_0050847Biological processprogesterone receptor signaling pathway
GO_0031648Biological processprotein destabilization
GO_0002223Biological processstimulatory C-type lectin receptor signaling pathway
GO_0051222Biological processpositive regulation of protein transport
GO_0007172Biological processsignal complex assembly
GO_0060065Biological processuterus development
GO_0046628Biological processpositive regulation of insulin receptor signaling pathway
GO_0048041Biological processfocal adhesion assembly
GO_0045056Biological processtranscytosis
GO_0048010Biological processvascular endothelial growth factor receptor signaling pathway
GO_1903997Biological processpositive regulation of non-membrane spanning protein tyrosine kinase activity
GO_1904263Biological processpositive regulation of TORC1 signaling
GO_0043065Biological processpositive regulation of apoptotic process
GO_0010634Biological processpositive regulation of epithelial cell migration
GO_0036035Biological processosteoclast development
GO_0071393Biological processcellular response to progesterone stimulus
GO_0071398Biological processcellular response to fatty acid
GO_2000641Biological processregulation of early endosome to late endosome transport
GO_0007283Biological processspermatogenesis
GO_0007611Biological processlearning or memory
GO_0051602Biological processresponse to electrical stimulus
GO_0033146Biological processregulation of intracellular estrogen receptor signaling pathway
GO_1990646Biological processcellular response to prolactin
GO_0070555Biological processresponse to interleukin-1
GO_2001286Biological processregulation of caveolin-mediated endocytosis
GO_0048008Biological processplatelet-derived growth factor receptor signaling pathway
GO_0031667Biological processresponse to nutrient levels
GO_0018108Biological processpeptidyl-tyrosine phosphorylation
GO_0070102Biological processinterleukin-6-mediated signaling pathway
GO_0035556Biological processintracellular signal transduction
GO_0050731Biological processpositive regulation of peptidyl-tyrosine phosphorylation
GO_0038166Biological processangiotensin-activated signaling pathway
GO_0030154Biological processcell differentiation
GO_0051902Biological processnegative regulation of mitochondrial depolarization
GO_2001237Biological processnegative regulation of extrinsic apoptotic signaling pathway
GO_0043149Biological processstress fiber assembly
GO_0045747Biological processpositive regulation of Notch signaling pathway
GO_0098609Biological processcell-cell adhesion
GO_0007179Biological processtransforming growth factor beta receptor signaling pathway
GO_0033625Biological processpositive regulation of integrin activation
GO_0048477Biological processoogenesis
GO_0071902Biological processpositive regulation of protein serine/threonine kinase activity
GO_0045780Biological processpositive regulation of bone resorption
GO_2000256Biological processpositive regulation of male germ cell proliferation
GO_2000588Biological processpositive regulation of platelet-derived growth factor receptor-beta signaling pathway
GO_0038096Biological processFc-gamma receptor signaling pathway involved in phagocytosis
GO_1900182Biological processpositive regulation of protein localization to nucleus
GO_0071456Biological processcellular response to hypoxia
GO_0098978Cellular componentglutamatergic synapse
GO_0045121Cellular componentmembrane raft
GO_0043025Cellular componentneuronal cell body
GO_0097060Cellular componentsynaptic membrane
GO_0070062Cellular componentextracellular exosome
GO_0005654Cellular componentnucleoplasm
GO_0099091Cellular componentpostsynaptic specialization, intracellular component
GO_0005770Cellular componentlate endosome
GO_0005886Cellular componentplasma membrane
GO_0005739Cellular componentmitochondrion
GO_0005764Cellular componentlysosome
GO_0002102Cellular componentpodosome
GO_0005743Cellular componentmitochondrial inner membrane
GO_0005884Cellular componentactin filament
GO_0044294Cellular componentdendritic growth cone
GO_0005737Cellular componentcytoplasm
GO_0005901Cellular componentcaveola
GO_0032587Cellular componentruffle membrane
GO_1902737Cellular componentdendritic filopodium
GO_0048471Cellular componentperinuclear region of cytoplasm
GO_0005925Cellular componentfocal adhesion
GO_0005829Cellular componentcytosol
GO_0030054Cellular componentcell junction
GO_0016004Molecular functionphospholipase activator activity
GO_0071253Molecular functionconnexin binding
GO_0046875Molecular functionephrin receptor binding
GO_0004672Molecular functionprotein kinase activity
GO_0042169Molecular functionSH2 domain binding
GO_0097110Molecular functionscaffold protein binding
GO_0005524Molecular functionATP binding
GO_0051117Molecular functionATPase binding
GO_0005080Molecular functionprotein kinase C binding
GO_0005102Molecular functionsignaling receptor binding
GO_0070700Molecular functionBMP receptor binding
GO_0043274Molecular functionphospholipase binding
GO_0019899Molecular functionenzyme binding
GO_0004715Molecular functionnon-membrane spanning protein tyrosine kinase activity
GO_0004713Molecular functionprotein tyrosine kinase activity
GO_0030331Molecular functionnuclear estrogen receptor binding
GO_0044325Molecular functiontransmembrane transporter binding
GO_0005515Molecular functionprotein binding
GO_0005158Molecular functioninsulin receptor binding
GO_0045296Molecular functioncadherin binding
GO_0005178Molecular functionintegrin binding
GO_0020037Molecular functionheme binding
GO_0051219Molecular functionphosphoprotein binding

IV. Literature review

[source]
Gene nameSRC
Protein nameSRC proto-oncogene, non-receptor tyrosine kinase
Proto-oncogene tyrosine-protein kinase Src (EC 2.7.10.2) (Proto-oncogene c-Src) (pp60c-src) (p60-Src)
Tyrosine kinase pp60c-src
SynonymsSRC1
DescriptionFUNCTION: 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) . 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 . 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 . Phosphorylates DDR2 on tyrosine residues, thereby promoting its subsequent autophosphorylation . Phosphorylates RUNX3 and COX2 on tyrosine residues, TNK2 on 'Tyr-284' and CBL on 'Tyr-731' . Enhances RIGI-elicited antiviral signaling . Phosphorylates PDPK1 at 'Tyr-9', 'Tyr-373' and 'Tyr-376' . Phosphorylates BCAR1 at 'Tyr-128' . Phosphorylates CBLC at multiple tyrosine residues, phosphorylation at 'Tyr-341' activates CBLC E3 activity . Phosphorylates synaptic vesicle protein synaptophysin (SYP) (By similarity). Involved in anchorage-independent cell growth . Required for podosome formation (By similarity). Mediates IL6 signaling by activating YAP1-NOTCH pathway to induce inflammation-induced epithelial regeneration . Phosphorylates OTUB1, promoting deubiquitination of RPTOR . Phosphorylates caspase CASP8 at 'Tyr-380' which negatively regulates CASP8 processing and activation, down-regulating CASP8 proapoptotic function . .; FUNCTION: [Isoform 1]: Non-receptor protein tyrosine kinase which phosphorylates synaptophysin with high affinity. .; FUNCTION: [Isoform 2]: Non-receptor protein tyrosine kinase which shows higher basal kinase activity than isoform 1, possibly due to weakened intramolecular interactions which enhance autophosphorylation of Tyr-419 and subsequent activation (By similarity). The SH3 domain shows reduced affinity with the linker sequence between the SH2 and kinase domains which may account for the increased basal activity (By similarity). Displays altered substrate specificity compared to isoform 1, showing weak affinity for synaptophysin and for peptide substrates containing class I or class II SH3 domain-binding motifs (By similarity). Plays a role in L1CAM-mediated neurite elongation, possibly by acting downstream of L1CAM to drive cytoskeletal rearrangements involved in neurite outgrowth (By similarity). .; FUNCTION: [Isoform 3]: Non-receptor protein tyrosine kinase which shows higher basal kinase activity than isoform 1, possibly due to weakened intramolecular interactions which enhance autophosphorylation of Tyr-419 and subsequent activation (By similarity). The SH3 domain shows reduced affinity with the linker sequence between the SH2 and kinase domains which may account for the increased basal activity (By similarity). Displays altered substrate specificity compared to isoform 1, showing weak affinity for synaptophysin and for peptide substrates containing class I or class II SH3 domain-binding motifs (By similarity). Plays a role in neurite elongation (By similarity). .

AccessionsA0A8I5KYU4
ENST00000358208.9 [P12931-3]
ENST00000373567.6 [P12931-1]
P12931
ENST00000692112.1 [P12931-1]
ENST00000709398.1 [P12931-3]
ENST00000373558.2 [P12931-2]
ENST00000709397.1 [P12931-2]
Q71UK5
ENST00000709395.1 [P12931-1]
ENST00000709396.1 [P12931-1]
ENST00000692423.1 [P12931-1]
ENST00000709394.1 [P12931-1]
ENST00000373578.7 [P12931-1]
ENST00000693012.1
ENST00000709392.1 [P12931-1]