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SRC (v-src sarcoma (Schmidt-Ruppin A-2) viral oncogene homolog (avian))

Written2009-04Stephen Hiscox
Welsh School of Pharmacy, Redwood Building, Cardiff University, Cardiff, UK

(Note : for Links provided by Atlas : click)

Identity

Alias_namesSRC1
v-src avian sarcoma (Schmidt-Ruppin A-2) viral oncogene homolog
Alias_symbol (synonym)ASV
c-src
Other aliasASV (Avian Sarcoma Virus)
c-SRC
p60-Src
pp60c-Src
HGNC (Hugo) SRC
LocusID (NCBI) 6714
Atlas_Id 448
Location 20q11.23  [Link to chromosome band 20q11]
Location_base_pair Starts at 37346128 and ends at 37405432 bp from pter ( according to hg19-Feb_2009)  [Mapping SRC.png]
Fusion genes
(updated 2017)		Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
SPIRE2 (16q24.3) / SRC (20q11.23)SRC (20q11.23) / GPR160 (3q26.2)SRC (20q11.23) / PSMB2 (1p34.3)
SRC (20q11.23) / REPIN1 (7q36.1)TMEM259 (19p13.3) / SRC (20q11.23)ZNF586 (19q13.43) / SRC (20q11.23)
ZNF587 (19q13.43) / SRC (20q11.23)
Note The Src kinase proto-oncogene has a high degree of similarity to the v-src gene of Rous sarcoma virus, although the C-terminal domain of v-Src is truncated and lacks the regulatory Tyr527 and therefore is not subjected to downregulation by Csk. Src kinase is implicated in the regulation of embryonic development, cell differentiation and proliferation. Src has been suggested to play a key role in cancer, where it may facilitate tumour spread through promotion of tumour cell invasion.

DNA/RNA

Note The gene consists of 14 exons. Two isoforms have been described differing in their 5' UTRs. Variant 1 represents the longer transcript although both isoforms 1 and 2 encode the same protein.
Description Size: 61.33 Kb, 14 exons.
mRNA: 4145 bases.

Protein

Note Src can be phosphorylated on Tyr-530 by CSK (c-Src kinase). The phosphorylated form is termed pp60c-src. Phosphorylation of this tyrosine allows facilitates interaction between the C-terminal tail and the SH2 domain, maintaining Src in an inactive formation.

Protein Translation:
MGSNKSKPKDASQRRRSLEPAENVHGAGGGAFPASQTPSKPASADGHRGPSAAFAPAAAEPKLFGGFNSSDTVTSPQRA
GPLAGGVTTFVALYDYESRTETDLSFKKGERLQIVNNTEGDWWLAHSLSTGQTGYIPSNYVAPSDSIQAEEWYFGKITRRE
GQGCFGEVWMGTWNGTTRVAIKTLKPGTMSPEAFLQEAQVMKKLRHEKLVQLYAVVSEEPIYIVTEYMSKGSLLDFLKGET
GKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLIEDNEYTARQGAKFPIKWTAPEAAL
YGRFTIKSDVWSFGILLTELTTKGRVPYPGMVNREVLDQVERGYRMPCPPECPESLHDLMCQCWRKEPEERPTFEYLQA
FLEDYFTSTEPQYQPGENL
Note: This variant (isoform 1) represents the longer Src transcript although both isoforms 1 and 2 encode the same protein as the difference is in the 5' UTR.

 
  Linear representation of the protein structure of human Src family members, showing the six distinct domains. N and C denote N- and C-termini respectively. Location of major regulatory phosphorylation sites and the myristolation signal sequence are shown.
Description Size: 536 amino acids; 59.835 KDa.
Src is 59.6KDa in size and has a domain structure comprised of six distinct functional regions (see figure above). These include an N-terminal SH4 domain that contains a lipid-modification sequence allowing targeting of Src to cellular membranes, and an adjacent, poorly-conserved region thus being unique to each Src family member. SH3 and SH2 domains adjacent to the N-terminus facilitate protein-protein interactions between Src and its interacting proteins whilst the SH1 domain allows ATP and substrate binding and has tyrosine kinase activity; autophosphorylation of Y419 within this domain is required for the maximum kinase activity of Src. The negative regulatory tail of Src contains a tyrosine at 530, the phosphorylation of which promotes a conformational change to produce an inactive Src molecule. Sequences within the C-terminus of Src have been recently identified to facilitate protein-protein interactions have been shown to regulate Src function in addition to its kinase activity.
Expression Ubiquitously expressed but with particularly high levels in brain tissue, osteoclasts and platelets.
Localisation Predominantly cytoplasmic and/or plasma membrane, the latter due to myristolation of the N-terminus. Activated Src has also been reported in the cell nucleus in some tumour tissues.
Function Src can interact with a diverse array of cellular factors allowing it to regulate a variety of normal and oncogenic processes that ultimately result in cell proliferation, differentiation, survival, adhesion, motility, invasion and angiogenesis (Thomas and Brugge, 1997; Summy and Gallick, 2003). Such interacting partners include receptor tyrosine kinases (e.g. the EGF receptor family (Biscardi et al., 1998)), integrins (Galliher and Schiemann, 2006; Huveneers et al., 2007), cell-cell adhesion molecules (Giehl and Menke, 2008), in addition to STATs (Silva, 2004), FAK (Brunton and Frame, 2008), the adaptor protein p130Cas (Chang et al., 2008) and GPCRs (McGarrigle and Huang, 2007). Importantly, Src can also interact with the oestrogen receptor (Weatherman, 2008), where it has been shown to be pivotal in both non-genomic ER activation of signalling pathways and gene transcription events. The ability of Src to function as both an effector and regulator of receptor-induced signalling allows it to mediate cross-talk between normally distinct signalling pathways and thus regulate a wide variety of both normal and oncogenic processes, including proliferation, differentiation, survival, adhesion, motility, invasion and angiogenesis.
Homology c-Src is the prototypic member of a family of nine non-receptor tyrosine kinases which share the same domain structure (Src, Fyn, Yes, Lyn, Lck, Hck, Blk, Fgr and Frk) (Erpel and Courtneidge, 1995) and are expressed in vertebrates. All Src family members have the same basic structure of an N-terminal, unique domain containing a myristylation site and frequently a palmitoylation site; regulatory SH3 and SH2 domains; a catalytic domain that has its active site wedged between the two lobes of the molecule, and a C-terminal regulatory tail that contains the hallmark regulatory tyrosine residue (Tyr527 in Src). The activity of Src family kinases is suppressed upon phosphorylation of Tyr527, allowing binding of the C-terminal domain to the SH2 domain. The SH2 and SH3 domains bind phosphotyrosine and proline-rich peptides, respectively; through these interactions, they participate in intra- and intermolecular regulation of kinase activity, as well as localization and substrate recognition. Differences in the SH2 linker sequences within Src family kinases correlate with the division of the Src kinase family into two separate subfamilies: Group A: Src, Fyn, Yes, Fgr and Group B: Lyn, Hck, Lck and Blk. Frk forms a separate but linked subfamily but with homologues also found in invertebrates. Src family members, with the exception of Src, Fyn and Yes, exhibit tissue-restricted distribution, being found primarily in cells of a haematopoietic nature. Below is a table constructed from Src homology analysis performed by CluSTr:

Src family member
% identity*
% similarity**
Fyn
75
10
Yes
73
9
Fgr
66
11
Lck
60
17
Lyn
60
17
Hck
57
17
Blk
62
13

*Percent identity between Src and protein; defined as: (Same AAs/Length of Protein 1) X100%
**Percent similarity between Src and protein; defined as: (Sim. AAs/Length of Protein 1) X100%

Mutations

Somatic The SRC family of kinases is rarely mutated in primary human tumours, although apparently scarce, a truncating and activating mutation in Src (at aa 531) has been described for a small subset of advanced-stage colorectal cancers (Irby et al., 1999).

Implicated in

Note
  
Entity Cancer
Note Elevated Src expression and/or activity has been reported in many different cancer types, where it may associate with poor clinical prognosis (Irby and Yeatman, 2000). Increased Src kinase activity in cancer is likely to arise from the deregulation of Src expression and/or activation mechanisms rather than the presence of activating mutations, since genetic mutations of this kind are rarely reported for Src (see above). Whereas constitutively activated forms of Src are transforming, wild-type Src has a relatively low transformation potential suggesting that Src may act to facilitate intracellular signalling through regulation, either directly or indirectly, of other signalling proteins.
  
  
Entity Colorectal cancer
Disease Increased Src activity has been widely described in colorectal tumour tissue compared with normal epithelia and within colon polyps, particularly those displaying a malignant phenotype (DeSeau et al., 1987; Cartwright et al., 1994). In colorectal cancer tissue studies, elevated Src kinase activity is associated with a poor clinical outcome (Aligayer et al., 2002). In vitro studies suggest that in colon cancer, Src may contribute more to disease spread than to increased proliferation (Jones et al., 2002).
  
  
Entity Breast cancer
Disease Src kinase activity is increased in breast cancer tissue compared to normal tissues (Verbeek et al., 1996). In vivo animal models suggest that Src activity is elevated in breast tumours overexpressing HER2 and interaction between Src and erbB family members may promote the development of a more aggressive disease clinically (Biscardi et al., 2000; Tan et al., 2005). Physical interactions between Src and growth factor receptors are reported in breast cancer tissues and cells, particularly with receptor tyrosine kinases of the EGFR family allowing Src to regulate signalling pathways that may contribute to aggressive breast cancer cell behaviour. Src is also intimately involved with Her2 pathway signalling in breast cancer, the result of which is the promotion of an invasive phenotype (Vadlamudi et al., 2003; Tan et al., 2005).
Oestrogenic signalling plays a critical role in promoting breast cancer cell growth where ligand-induced activation of oestrogen receptors (ERs) results in gene transcription mediated by the ER, in complex with various co-activators/co-repressor molecules. In such cases, Src is able to potentiate ER-mediated, AF-1 dependent gene transcription through indirect phosphorylation of nuclear ER via ERK1/ ERK2 (Feng et al., 2001) and Akt (Campbell et al., 2001; Shah et al., 2005) and through regulation of FAK-p130CAS-JNK signalling pathway activity and the subsequent activation of co-activator molecules including CBP ( PAG1) and GRIP1 ( NCOA2). Furthermore, Src appears to mediate non-genomic ER signalling through ERK and Akt pathways (Castoria et al., 2001; Wessler et al., 2006) to regulate cellular proliferation and survival (Castoria et al., 1999; Migliaccio et al., 2000). That Src is involved in both EGFR/Her2 and ER signalling has led to Src being implicated in growth factor-ER cross talk mechanisms in breast cancer and the development of endocrine resistance (Arpino et al., 2008; Massarweh and Schiff, 2006; Hiscox et al., 2006; Hiscox et al., 2009).
  
  
Entity Hematopoietic cancers
Disease The majority of Src family kinases are highly expressed in cells of a hematopoietic origin where they are suggested to regulate growth and proliferation. Src itself is, along with related family kinase members, are implicated in imatinib-resistant, BCR-ABL-expressing CML (Li, 2008).
  
  
Entity Other tumour types
Disease Src protein and activity have been identified as being increased in a number of other tumour types including gastric, pancreatic, lung and ovarian tumours compared to normal tissue suggesting a possible role for Src in these tumours.
  

Bibliography

Activation of Src kinase in primary colorectal carcinoma: an indicator of poor clinical prognosis.
Aligayer H, Boyd DD, Heiss MM, Abdalla EK, Curley SA, Gallick GE.
Cancer. 2002 Jan 15;94(2):344-51.
PMID 11900220
 
Crosstalk between the estrogen receptor and the HER tyrosine kinase receptor family: molecular mechanism and clinical implications for endocrine therapy resistance.
Arpino G, Wiechmann L, Osborne CK, Schiff R.
Endocr Rev. 2008 Apr;29(2):217-33. Epub 2008 Jan 23. (REVIEW)
PMID 18216219
 
Tyrosine kinase signalling in breast cancer: epidermal growth factor receptor and c-Src interactions in breast cancer.
Biscardi JS, Ishizawar RC, Silva CM, Parsons SJ.
Breast Cancer Res. 2000;2(3):203-10. Epub 2000 Mar 7. (REVIEW)
PMID 11250711
 
Src and focal adhesion kinase as therapeutic targets in cancer.
Brunton VG, Frame MC.
Curr Opin Pharmacol. 2008 Aug;8(4):427-32. Epub 2008 Jul 22. (REVIEW)
PMID 18625340
 
Phosphatidylinositol 3-kinase/AKT-mediated activation of estrogen receptor alpha: a new model for anti-estrogen resistance.
Campbell RA, Bhat-Nakshatri P, Patel NM, Constantinidou D, Ali S, Nakshatri H.
J Biol Chem. 2001 Mar 30;276(13):9817-24. Epub 2001 Jan 3.
PMID 11139588
 
Elevated c-Src tyrosine kinase activity in premalignant epithelia of ulcerative colitis.
Cartwright CA, Coad CA, Egbert BM.
J Clin Invest. 1994 Feb;93(2):509-15.
PMID 7509341
 
PI3-kinase in concert with Src promotes the S-phase entry of oestradiol-stimulated MCF-7 cells.
Castoria G, Migliaccio A, Bilancio A, Di Domenico M, de Falco A, Lombardi M, Fiorentino R, Varricchio L, Barone MV, Auricchio F.
EMBO J. 2001 Nov 1;20(21):6050-9.
PMID 11689445
 
Src family kinase oncogenic potential and pathways in prostate cancer as revealed by AZD0530.
Chang YM, Bai L, Liu S, Yang JC, Kung HJ, Evans CP.
Oncogene. 2008 Oct 23;27(49):6365-75. Epub 2008 Aug 4.
PMID 18679417
 
Analysis of pp60c-src tyrosine kinase activity and phosphotyrosyl phosphatase activity in human colon carcinoma and normal human colon mucosal cells.
DeSeau V, Rosen N, Bolen JB.
J Cell Biochem. 1987 Oct;35(2):113-28.
PMID 2448318
 
Src family protein tyrosine kinases and cellular signal transduction pathways.
Erpel T, Courtneidge SA.
Curr Opin Cell Biol. 1995 Apr;7(2):176-82. (REVIEW)
PMID 7612268
 
Potentiation of estrogen receptor activation function 1 (AF-1) by Src/JNK through a serine 118-independent pathway.
Feng W, Webb P, Nguyen P, Liu X, Li J, Karin M, Kushner PJ.
Mol Endocrinol. 2001 Jan;15(1):32-45.
PMID 11145737
 
Beta3 integrin and Src facilitate transforming growth factor-beta mediated induction of epithelial-mesenchymal transition in mammary epithelial cells.
Galliher AJ, Schiemann WP.
Breast Cancer Res. 2006;8(4):R42.
PMID 16859511
 
Microenvironmental regulation of E-cadherin-mediated adherens junctions.
Giehl K, Menke A.
Front Biosci. 2008 May 1;13:3975-85. (REVIEW)
PMID 18508491
 
Dual targeting of Src and ER prevents acquired antihormone resistance in breast cancer cells.
Hiscox S, Jordan NJ, Smith C, James M, Morgan L, Taylor KM, Green TP, Nicholson RI.
Breast Cancer Res Treat. 2009 May;115(1):57-67. Epub 2008 May 21.
PMID 18493848
 
Src as a therapeutic target in anti-hormone/anti-growth factor-resistant breast cancer.
Hiscox S, Morgan L, Green T, Nicholson RI.
Endocr Relat Cancer. 2006 Dec;13 Suppl 1:S53-9. (REVIEW)
PMID 17259559
 
Integrin alpha v beta 3 controls activity and oncogenic potential of primed c-Src.
Huveneers S, van den Bout I, Sonneveld P, Sancho A, Sonnenberg A, Danen EH.
Cancer Res. 2007 Mar 15;67(6):2693-700.
PMID 17363590
 
Activating SRC mutation in a subset of advanced human colon cancers.
Irby RB, Mao W, Coppola D, Kang J, Loubeau JM, Trudeau W, Karl R, Fujita DJ, Jove R, Yeatman TJ.
Nat Genet. 1999 Feb;21(2):187-90.
PMID 9988270
 
Role of Src expression and activation in human cancer.
Irby RB, Yeatman TJ.
Oncogene. 2000 Nov 20;19(49):5636-42. (REVIEW)
PMID 11114744
 
Elevated c-Src is linked to altered cell-matrix adhesion rather than proliferation in KM12C human colorectal cancer cells.
Jones RJ, Avizienyte E, Wyke AW, Owens DW, Brunton VG, Frame MC.
Br J Cancer. 2002 Nov 4;87(10):1128-35.
PMID 12402152
 
Src-family kinases in the development and therapy of Philadelphia chromosome-positive chronic myeloid leukemia and acute lymphoblastic leukemia.
Li S.
Leuk Lymphoma. 2008 Jan;49(1):19-26. (REVIEW)
PMID 18203007
 
Resistance to endocrine therapy in breast cancer: exploiting estrogen receptor/growth factor signaling crosstalk.
Massarweh S, Schiff R.
Endocr Relat Cancer. 2006 Dec;13 Suppl 1:S15-24. (REVIEW)
PMID 17259554
 
GPCRs signaling directly through Src-family kinases.
McGarrigle D, Huang XY.
Sci STKE. 2007 Jun 26;2007(392):pe35. (REVIEW)
PMID 17595221
 
Steroid-induced androgen receptor-oestradiol receptor beta-Src complex triggers prostate cancer cell proliferation.
Migliaccio A, Castoria G, Di Domenico M, de Falco A, Bilancio A, Lombardi M, Barone MV, Ametrano D, Zannini MS, Abbondanza C, Auricchio F.
EMBO J. 2000 Oct 16;19(20):5406-17.
PMID 11032808
 
The Src kinase pathway promotes tamoxifen agonist action in Ishikawa endometrial cells through phosphorylation-dependent stabilization of estrogen receptor (alpha) promoter interaction and elevated steroid receptor coactivator 1 activity.
Shah YM, Rowan BG.
Mol Endocrinol. 2005 Mar;19(3):732-48. Epub 2004 Nov 4.
PMID 15528270
 
Role of STATs as downstream signal transducers in Src family kinase-mediated tumorigenesis.
Silva CM.
Oncogene. 2004 Oct 18;23(48):8017-23. (REVIEW)
PMID 15489919
 
Src family kinases in tumor progression and metastasis.
Summy JM, Gallick GE.
Cancer Metastasis Rev. 2003 Dec;22(4):337-58. (REVIEW)
PMID 12884910
 
ErbB2 promotes Src synthesis and stability: novel mechanisms of Src activation that confer breast cancer metastasis.
Tan M, Li P, Klos KS, Lu J, Lan KH, Nagata Y, Fang D, Jing T, Yu D.
Cancer Res. 2005 Mar 1;65(5):1858-67.
PMID 15753384
 
Cellular functions regulated by Src family kinases.
Thomas SM, Brugge JS.
Annu Rev Cell Dev Biol. 1997;13:513-609. (REVIEW)
PMID 9442882
 
Heregulin and HER2 signaling selectively activates c-Src phosphorylation at tyrosine 215.
Vadlamudi RK, Sahin AA, Adam L, Wang RA, Kumar R.
FEBS Lett. 2003 May 22;543(1-3):76-80.
PMID 12753909
 
c-Src protein expression is increased in human breast cancer. An immunohistochemical and biochemical analysis.
Verbeek BS, Vroom TM, Adriaansen-Slot SS, Ottenhoff-Kalff AE, Geertzema JG, Hennipman A, Rijksen G.
J Pathol. 1996 Dec;180(4):383-8.
PMID 9014858
 
Sensing estrogen's many pathways.
Weatherman RV.
ACS Chem Biol. 2008 Jun 20;3(6):338-40.
PMID 18570353
 
Identification of estrogen receptor ligands leading to activation of non-genomic signaling pathways while exhibiting only weak transcriptional activity.
Wessler S, Otto C, Wilck N, Stangl V, Fritzemeier KH.
J Steroid Biochem Mol Biol. 2006 Jan;98(1):25-35. Epub 2005 Oct 3.
PMID 16203130
 

Citation

This paper should be referenced as such :
Hiscox, S
SRC (v-src sarcoma (Schmidt-Ruppin A-2) viral oncogene homolog (avian))
Atlas Genet Cytogenet Oncol Haematol. 2010;14(3):301-304.
Free journal version : [ pdf ]   [ DOI ]
On line version : http://AtlasGeneticsOncology.org/Genes/SRCID448ch20q11.html

Other Solid tumors implicated (Data extracted from papers in the Atlas) [ 3 ]
  Breast: Ductal carcinoma
t(19;20)(q13;q11) ZNF586/SRC
t(19;20)(q13;q11) ZNF587/SRC

External links

Nomenclature
HGNC (Hugo)SRC   11283
LRG (Locus Reference Genomic)LRG_1018
Cards
AtlasSRCID448ch20q11
Entrez_Gene (NCBI)SRC  6714  SRC proto-oncogene, non-receptor tyrosine kinase
AliasesASV; SRC1; THC6; c-SRC; 
p60-Src
GeneCards (Weizmann)SRC
Ensembl hg19 (Hinxton)ENSG00000197122 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000197122 [Gene_View]  ENSG00000197122 [Sequence]  chr20:37346128-37405432 [Contig_View]  SRC [Vega]
ICGC DataPortalENSG00000197122
TCGA cBioPortalSRC
AceView (NCBI)SRC
Genatlas (Paris)SRC
WikiGenes6714
SOURCE (Princeton)SRC
Genetics Home Reference (NIH)SRC
Genomic and cartography
GoldenPath hg38 (UCSC)SRC  -     chr20:37346128-37405432 +  20q11.23   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)SRC  -     20q11.23   [Description]    (hg19-Feb_2009)
GoldenPathSRC - 20q11.23 [CytoView hg19]  SRC - 20q11.23 [CytoView hg38]
ImmunoBaseENSG00000197122
Mapping of homologs : NCBISRC [Mapview hg19]  SRC [Mapview hg38]
OMIM114500   190090   616937   
Gene and transcription
Genbank (Entrez)AF272982 AK024281 AK091756 AW135290 BC011566
RefSeq transcript (Entrez)NM_005417 NM_198291
RefSeq genomic (Entrez)
Consensus coding sequences : CCDS (NCBI)SRC
Cluster EST : UnigeneHs.195659 [ NCBI ]
CGAP (NCI)Hs.195659
Alternative Splicing GalleryENSG00000197122
Gene ExpressionSRC [ NCBI-GEO ]   SRC [ EBI - ARRAY_EXPRESS ]   SRC [ SEEK ]   SRC [ MEM ]
Gene Expression Viewer (FireBrowse)SRC [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevestigatorExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)6714
GTEX Portal (Tissue expression)SRC
Human Protein AtlasENSG00000197122-SRC [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtP12931   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtP12931  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProP12931
Splice isoforms : SwissVarP12931
PhosPhoSitePlusP12931
Domaine pattern : Prosite (Expaxy)PROTEIN_KINASE_ATP (PS00107)    PROTEIN_KINASE_DOM (PS50011)    PROTEIN_KINASE_TYR (PS00109)    SH2 (PS50001)    SH3 (PS50002)   
Domains : Interpro (EBI)Kinase-like_dom_sf    Prot_kinase_dom    Protein_kinase_ATP_BS    Ser-Thr/Tyr_kinase_cat_dom    SH2    SH2_dom_sf    SH3-like_dom_sf    SH3_domain    Tyr_kinase_AS    Tyr_kinase_cat_dom   
Domain families : Pfam (Sanger)Pkinase_Tyr (PF07714)    SH2 (PF00017)    SH3_1 (PF00018)   
Domain families : Pfam (NCBI)pfam07714    pfam00017    pfam00018   
Domain families : Smart (EMBL)SH2 (SM00252)  SH3 (SM00326)  TyrKc (SM00219)  
Conserved Domain (NCBI)SRC
DMDM Disease mutations6714
Blocks (Seattle)SRC
PDB (RSDB)1A07    1A08    1A09    1A1A    1A1B    1A1C    1A1E    1FMK    1HCS    1HCT    1KSW    1O41    1O42    1O43    1O44    1O45    1O46    1O47    1O48    1O49    1O4A    1O4B    1O4C    1O4D    1O4E    1O4F    1O4G    1O4H    1O4I    1O4J    1O4K    1O4L    1O4M    1O4N    1O4O    1O4P    1O4Q    1O4R    1SHD    1Y57    1YI6    1YOJ    1YOL    1YOM    2BDF    2BDJ    2H8H    2SRC    3VRO    3ZMP    3ZMQ    4F59    4F5A    4F5B    4HXJ    4K11    4MXO    4MXX    4MXY    4MXZ   
PDB Europe1A07    1A08    1A09    1A1A    1A1B    1A1C    1A1E    1FMK    1HCS    1HCT    1KSW    1O41    1O42    1O43    1O44    1O45    1O46    1O47    1O48    1O49    1O4A    1O4B    1O4C    1O4D    1O4E    1O4F    1O4G    1O4H    1O4I    1O4J    1O4K    1O4L    1O4M    1O4N    1O4O    1O4P    1O4Q    1O4R    1SHD    1Y57    1YI6    1YOJ    1YOL    1YOM    2BDF    2BDJ    2H8H    2SRC    3VRO    3ZMP    3ZMQ    4F59    4F5A    4F5B    4HXJ    4K11    4MXO    4MXX    4MXY    4MXZ   
PDB (PDBSum)1A07    1A08    1A09    1A1A    1A1B    1A1C    1A1E    1FMK    1HCS    1HCT    1KSW    1O41    1O42    1O43    1O44    1O45    1O46    1O47    1O48    1O49    1O4A    1O4B    1O4C    1O4D    1O4E    1O4F    1O4G    1O4H    1O4I    1O4J    1O4K    1O4L    1O4M    1O4N    1O4O    1O4P    1O4Q    1O4R    1SHD    1Y57    1YI6    1YOJ    1YOL    1YOM    2BDF    2BDJ    2H8H    2SRC    3VRO    3ZMP    3ZMQ    4F59    4F5A    4F5B    4HXJ    4K11    4MXO    4MXX    4MXY    4MXZ   
PDB (IMB)1A07    1A08    1A09    1A1A    1A1B    1A1C    1A1E    1FMK    1HCS    1HCT    1KSW    1O41    1O42    1O43    1O44    1O45    1O46    1O47    1O48    1O49    1O4A    1O4B    1O4C    1O4D    1O4E    1O4F    1O4G    1O4H    1O4I    1O4J    1O4K    1O4L    1O4M    1O4N    1O4O    1O4P    1O4Q    1O4R    1SHD    1Y57    1YI6    1YOJ    1YOL    1YOM    2BDF    2BDJ    2H8H    2SRC    3VRO    3ZMP    3ZMQ    4F59    4F5A    4F5B    4HXJ    4K11    4MXO    4MXX    4MXY    4MXZ   
Structural Biology KnowledgeBase1A07    1A08    1A09    1A1A    1A1B    1A1C    1A1E    1FMK    1HCS    1HCT    1KSW    1O41    1O42    1O43    1O44    1O45    1O46    1O47    1O48    1O49    1O4A    1O4B    1O4C    1O4D    1O4E    1O4F    1O4G    1O4H    1O4I    1O4J    1O4K    1O4L    1O4M    1O4N    1O4O    1O4P    1O4Q    1O4R    1SHD    1Y57    1YI6    1YOJ    1YOL    1YOM    2BDF    2BDJ    2H8H    2SRC    3VRO    3ZMP    3ZMQ    4F59    4F5A    4F5B    4HXJ    4K11    4MXO    4MXX    4MXY    4MXZ   
SCOP (Structural Classification of Proteins)1A07    1A08    1A09    1A1A    1A1B    1A1C    1A1E    1FMK    1HCS    1HCT    1KSW    1O41    1O42    1O43    1O44    1O45    1O46    1O47    1O48    1O49    1O4A    1O4B    1O4C    1O4D    1O4E    1O4F    1O4G    1O4H    1O4I    1O4J    1O4K    1O4L    1O4M    1O4N    1O4O    1O4P    1O4Q    1O4R    1SHD    1Y57    1YI6    1YOJ    1YOL    1YOM    2BDF    2BDJ    2H8H    2SRC    3VRO    3ZMP    3ZMQ    4F59    4F5A    4F5B    4HXJ    4K11    4MXO    4MXX    4MXY    4MXZ   
CATH (Classification of proteins structures)1A07    1A08    1A09    1A1A    1A1B    1A1C    1A1E    1FMK    1HCS    1HCT    1KSW    1O41    1O42    1O43    1O44    1O45    1O46    1O47    1O48    1O49    1O4A    1O4B    1O4C    1O4D    1O4E    1O4F    1O4G    1O4H    1O4I    1O4J    1O4K    1O4L    1O4M    1O4N    1O4O    1O4P    1O4Q    1O4R    1SHD    1Y57    1YI6    1YOJ    1YOL    1YOM    2BDF    2BDJ    2H8H    2SRC    3VRO    3ZMP    3ZMQ    4F59    4F5A    4F5B    4HXJ    4K11    4MXO    4MXX    4MXY    4MXZ   
SuperfamilyP12931
Human Protein Atlas [tissue]ENSG00000197122-SRC [tissue]
Peptide AtlasP12931
HPRD01819
IPIIPI00641230   IPI00328867   
Protein Interaction databases
DIP (DOE-UCLA)P12931
IntAct (EBI)P12931
FunCoupENSG00000197122
BioGRIDSRC
STRING (EMBL)SRC
ZODIACSRC
Ontologies - Pathways
QuickGOP12931
Ontology : AmiGOprimary ovarian follicle growth  podosome  stimulatory C-type lectin receptor signaling pathway  protein kinase activity  protein kinase activity  protein tyrosine kinase activity  protein tyrosine kinase activity  protein tyrosine kinase activity  protein tyrosine kinase activity  protein tyrosine kinase activity  non-membrane spanning protein tyrosine kinase activity  non-membrane spanning protein tyrosine kinase activity  non-membrane spanning protein tyrosine kinase activity  SH3/SH2 adaptor activity  protein kinase C binding  signaling receptor binding  signaling receptor binding  insulin receptor binding  integrin binding  integrin binding  protein binding  ATP binding  nucleus  cytoplasm  mitochondrion  mitochondrial inner membrane  lysosome  late endosome  cytosol  cytosol  actin filament  plasma membrane  plasma membrane  caveola  cell cycle  signal transduction  transmembrane receptor protein tyrosine kinase signaling pathway  signal complex assembly  epidermal growth factor receptor signaling pathway  epidermal growth factor receptor signaling pathway  transforming growth factor beta receptor signaling pathway  G protein-coupled receptor signaling pathway  integrin-mediated signaling pathway  axon guidance  protein C-terminus binding  cell proliferation  response to mechanical stimulus  response to virus  response to acidic pH  regulation of epithelial cell migration  positive regulation of epithelial cell migration  positive regulation of glucose metabolic process  positive regulation of protein processing  positive regulation of phosphatidylinositol 3-kinase signaling  postsynaptic density  positive regulation of smooth muscle cell migration  viral process  macroautophagy  kinase activity  peptidyl-serine phosphorylation  peptidyl-tyrosine phosphorylation  peptidyl-tyrosine phosphorylation  peptidyl-tyrosine phosphorylation  enzyme binding  kinase binding  heme binding  regulation of cell-cell adhesion  cell differentiation  platelet activation  estrogen receptor binding  forebrain development  extrinsic component of cytoplasmic side of plasma membrane  T cell costimulation  ubiquitin protein ligase binding  protein destabilization  response to nutrient levels  positive regulation of protein autophosphorylation  activation of protein kinase B activity  negative regulation of telomere maintenance via telomerase  negative regulation of protein homooligomerization  ruffle membrane  cellular response to insulin stimulus  regulation of intracellular estrogen receptor signaling pathway  positive regulation of integrin activation  adherens junction organization  substrate adhesion-dependent cell spreading  positive regulation of dephosphorylation  intracellular signal transduction  entry of bacterium into host cell  osteoclast development  cellular response to platelet-derived growth factor stimulus  peptidyl-tyrosine autophosphorylation  Fc-gamma receptor signaling pathway involved in phagocytosis  ERBB2 signaling pathway  SH2 domain binding  odontogenesis  neuron projection  positive regulation of apoptotic process  negative regulation of apoptotic process  regulation of vascular permeability  stress fiber assembly  negative regulation of cysteine-type endopeptidase activity involved in apoptotic process  regulation of protein binding  positive regulation of MAP kinase activity  positive regulation of phosphatidylinositol 3-kinase activity  ion channel binding  transcytosis  regulation of bone resorption  cadherin binding  bone resorption  bone resorption  positive regulation of cyclin-dependent protein serine/threonine kinase activity  negative regulation of transcription, DNA-templated  positive regulation of transcription, DNA-templated  positive regulation of insulin receptor signaling pathway  protein autophosphorylation  ephrin receptor binding  vascular endothelial growth factor receptor signaling pathway  neurotrophin TRK receptor signaling pathway  ephrin receptor signaling pathway  perinuclear region of cytoplasm  oogenesis  positive regulation of cytokine secretion  positive regulation of peptidyl-tyrosine phosphorylation  positive regulation of peptidyl-tyrosine phosphorylation  progesterone receptor signaling pathway  progesterone receptor signaling pathway  leukocyte migration  positive regulation of small GTPase mediated signal transduction  phosphoprotein binding  response to mineralocorticoid  response to electrical stimulus  negative regulation of focal adhesion assembly  positive regulation of protein kinase B signaling  positive regulation of protein kinase B signaling  negative regulation of mitochondrial depolarization  negative regulation of telomerase activity  uterus development  branching involved in mammary gland duct morphogenesis  regulation of cell projection assembly  extracellular exosome  cellular response to hydrogen peroxide  positive regulation of ERK1 and ERK2 cascade  response to interleukin-1  BMP receptor binding  growth factor receptor binding  growth factor receptor binding  cellular response to lipopolysaccharide  connexin binding  cellular response to peptide hormone stimulus  cellular response to progesterone stimulus  cellular response to fatty acid  cellular response to hypoxia  cellular response to fluid shear stress  positive regulation of podosome assembly  positive regulation of protein serine/threonine kinase activity  angiotensin-activated signaling pathway involved in heart process  positive regulation of canonical Wnt signaling pathway  scaffold protein binding  cell-cell adhesion  regulation of postsynaptic neurotransmitter receptor activity  glutamatergic synapse  postsynaptic specialization, intracellular component  positive regulation of protein localization to nucleus  positive regulation of non-membrane spanning protein tyrosine kinase activity  positive regulation of ovarian follicle development  positive regulation of lamellipodium morphogenesis  positive regulation of DNA biosynthetic process  positive regulation of platelet-derived growth factor receptor-beta signaling pathway  regulation of early endosome to late endosome transport  negative regulation of anoikis  negative regulation of extrinsic apoptotic signaling pathway  negative regulation of extrinsic apoptotic signaling pathway  negative regulation of intrinsic apoptotic signaling pathway  negative regulation of intrinsic apoptotic signaling pathway  regulation of caveolin-mediated endocytosis  
Ontology : EGO-EBIprimary ovarian follicle growth  podosome  stimulatory C-type lectin receptor signaling pathway  protein kinase activity  protein kinase activity  protein tyrosine kinase activity  protein tyrosine kinase activity  protein tyrosine kinase activity  protein tyrosine kinase activity  protein tyrosine kinase activity  non-membrane spanning protein tyrosine kinase activity  non-membrane spanning protein tyrosine kinase activity  non-membrane spanning protein tyrosine kinase activity  SH3/SH2 adaptor activity  protein kinase C binding  signaling receptor binding  signaling receptor binding  insulin receptor binding  integrin binding  integrin binding  protein binding  ATP binding  nucleus  cytoplasm  mitochondrion  mitochondrial inner membrane  lysosome  late endosome  cytosol  cytosol  actin filament  plasma membrane  plasma membrane  caveola  cell cycle  signal transduction  transmembrane receptor protein tyrosine kinase signaling pathway  signal complex assembly  epidermal growth factor receptor signaling pathway  epidermal growth factor receptor signaling pathway  transforming growth factor beta receptor signaling pathway  G protein-coupled receptor signaling pathway  integrin-mediated signaling pathway  axon guidance  protein C-terminus binding  cell proliferation  response to mechanical stimulus  response to virus  response to acidic pH  regulation of epithelial cell migration  positive regulation of epithelial cell migration  positive regulation of glucose metabolic process  positive regulation of protein processing  positive regulation of phosphatidylinositol 3-kinase signaling  postsynaptic density  positive regulation of smooth muscle cell migration  viral process  macroautophagy  kinase activity  peptidyl-serine phosphorylation  peptidyl-tyrosine phosphorylation  peptidyl-tyrosine phosphorylation  peptidyl-tyrosine phosphorylation  enzyme binding  kinase binding  heme binding  regulation of cell-cell adhesion  cell differentiation  platelet activation  estrogen receptor binding  forebrain development  extrinsic component of cytoplasmic side of plasma membrane  T cell costimulation  ubiquitin protein ligase binding  protein destabilization  response to nutrient levels  positive regulation of protein autophosphorylation  activation of protein kinase B activity  negative regulation of telomere maintenance via telomerase  negative regulation of protein homooligomerization  ruffle membrane  cellular response to insulin stimulus  regulation of intracellular estrogen receptor signaling pathway  positive regulation of integrin activation  adherens junction organization  substrate adhesion-dependent cell spreading  positive regulation of dephosphorylation  intracellular signal transduction  entry of bacterium into host cell  osteoclast development  cellular response to platelet-derived growth factor stimulus  peptidyl-tyrosine autophosphorylation  Fc-gamma receptor signaling pathway involved in phagocytosis  ERBB2 signaling pathway  SH2 domain binding  odontogenesis  neuron projection  positive regulation of apoptotic process  negative regulation of apoptotic process  regulation of vascular permeability  stress fiber assembly  negative regulation of cysteine-type endopeptidase activity involved in apoptotic process  regulation of protein binding  positive regulation of MAP kinase activity  positive regulation of phosphatidylinositol 3-kinase activity  ion channel binding  transcytosis  regulation of bone resorption  cadherin binding  bone resorption  bone resorption  positive regulation of cyclin-dependent protein serine/threonine kinase activity  negative regulation of transcription, DNA-templated  positive regulation of transcription, DNA-templated  positive regulation of insulin receptor signaling pathway  protein autophosphorylation  ephrin receptor binding  vascular endothelial growth factor receptor signaling pathway  neurotrophin TRK receptor signaling pathway  ephrin receptor signaling pathway  perinuclear region of cytoplasm  oogenesis  positive regulation of cytokine secretion  positive regulation of peptidyl-tyrosine phosphorylation  positive regulation of peptidyl-tyrosine phosphorylation  progesterone receptor signaling pathway  progesterone receptor signaling pathway  leukocyte migration  positive regulation of small GTPase mediated signal transduction  phosphoprotein binding  response to mineralocorticoid  response to electrical stimulus  negative regulation of focal adhesion assembly  positive regulation of protein kinase B signaling  positive regulation of protein kinase B signaling  negative regulation of mitochondrial depolarization  negative regulation of telomerase activity  uterus development  branching involved in mammary gland duct morphogenesis  regulation of cell projection assembly  extracellular exosome  cellular response to hydrogen peroxide  positive regulation of ERK1 and ERK2 cascade  response to interleukin-1  BMP receptor binding  growth factor receptor binding  growth factor receptor binding  cellular response to lipopolysaccharide  connexin binding  cellular response to peptide hormone stimulus  cellular response to progesterone stimulus  cellular response to fatty acid  cellular response to hypoxia  cellular response to fluid shear stress  positive regulation of podosome assembly  positive regulation of protein serine/threonine kinase activity  angiotensin-activated signaling pathway involved in heart process  positive regulation of canonical Wnt signaling pathway  scaffold protein binding  cell-cell adhesion  regulation of postsynaptic neurotransmitter receptor activity  glutamatergic synapse  postsynaptic specialization, intracellular component  positive regulation of protein localization to nucleus  positive regulation of non-membrane spanning protein tyrosine kinase activity  positive regulation of ovarian follicle development  positive regulation of lamellipodium morphogenesis  positive regulation of DNA biosynthetic process  positive regulation of platelet-derived growth factor receptor-beta signaling pathway  regulation of early endosome to late endosome transport  negative regulation of anoikis  negative regulation of extrinsic apoptotic signaling pathway  negative regulation of extrinsic apoptotic signaling pathway  negative regulation of intrinsic apoptotic signaling pathway  negative regulation of intrinsic apoptotic signaling pathway  regulation of caveolin-mediated endocytosis  
Pathways : KEGGErbB signaling pathway    Rap1 signaling pathway    Chemokine signaling pathway    Endocytosis    VEGF signaling pathway    Focal adhesion    Adherens junction    Tight junction    Gap junction    GABAergic synapse    Regulation of actin cytoskeleton    GnRH signaling pathway    Estrogen signaling pathway    Prolactin signaling pathway    Thyroid hormone signaling pathway    Bacterial invasion of epithelial cells    Epithelial cell signaling in Helicobacter pylori infection    Shigellosis    Tuberculosis    Hepatitis B    Viral carcinogenesis    Proteoglycans in cancer   
REACTOMEP12931 [protein]
REACTOME PathwaysR-HSA-9620244 [pathway]   
NDEx NetworkSRC
Atlas of Cancer Signalling NetworkSRC
Wikipedia pathwaysSRC
Orthology - Evolution
OrthoDB6714
GeneTree (enSembl)ENSG00000197122
Phylogenetic Trees/Animal Genes : TreeFamSRC
HOGENOMP12931
Homologs : HomoloGeneSRC
Homology/Alignments : Family Browser (UCSC)SRC
Gene fusions - Rearrangements
Fusion : MitelmanZNF586/SRC [19q13.43/20q11.23]  [t(19;20)(q13;q11)]  
Fusion : MitelmanZNF587/SRC [19q13.43/20q11.23]  [t(19;20)(q13;q11)]  
Fusion PortalZNF586 19q13.43 SRC 20q11.23 BRCA
Fusion PortalZNF587 19q13.43 SRC 20q11.23 BRCA
Fusion : FusionGDB17793    35722    35923    35924    35925    35926    35927    35928    43474    43477    4838   
Fusion : Fusion_HubC1ORF111--SRC    COL12A1--SRC    GABPB2--SRC    GSS--SRC    HTT--SRC    ITCH--SRC    MANBAL--SRC    P160--SRC    P47--SRC    SPIRE2--SRC    SRC--ABL1    SRC--GPR160    SRC--MANBAL    SRC--PSMB2    SRC--REPIN1   
SRC--SMC    ZNF586--SRC    ZNF587--SRC   
Fusion : QuiverSRC
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerSRC [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)SRC
dbVarSRC
ClinVarSRC
1000_GenomesSRC 
Exome Variant ServerSRC
ExAC (Exome Aggregation Consortium)ENSG00000197122
GNOMAD BrowserENSG00000197122
Varsome BrowserSRC
Genetic variants : HAPMAP6714
Genomic Variants (DGV)SRC [DGVbeta]
DECIPHERSRC [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisSRC 
Mutations
ICGC Data PortalSRC 
TCGA Data PortalSRC 
Broad Tumor PortalSRC
OASIS PortalSRC [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICSRC  [overview]  [genome browser]  [tissue]  [distribution]  
Somatic Mutations in Cancer : COSMIC3DSRC
Mutations and Diseases : HGMDSRC
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD - Leiden Open Variation Database
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
BioMutasearch SRC
DgiDB (Drug Gene Interaction Database)SRC
DoCM (Curated mutations)SRC (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)SRC (select a term)
intoGenSRC
NCG5 (London)SRC
Cancer3DSRC(select the gene name)
Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Diseases
OMIM114500    190090    616937   
Orphanet
DisGeNETSRC
MedgenSRC
Genetic Testing Registry SRC
NextProtP12931 [Medical]
TSGene6714
GENETestsSRC
Target ValidationSRC
Huge Navigator SRC [HugePedia]
snp3D : Map Gene to Disease6714
BioCentury BCIQSRC
ClinGenSRC
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD6714
Chemical/Pharm GKB GenePA36111
Clinical trialSRC
Miscellaneous
canSAR (ICR)SRC (select the gene name)
DataMed IndexSRC
Probes
Litterature
PubMed499 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
CoreMineSRC
EVEXSRC
GoPubMedSRC
iHOPSRC
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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