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

2009-04-01   Stephen Hiscox 

Welsh School of Pharmacy, Redwood Building, Cardiff University, Cardiff, UK





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.


Size: 61.33 Kb, 14 exons.
mRNA: 4145 bases.



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:
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.

Atlas Image
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.


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.


Ubiquitously expressed but with particularly high levels in brain tissue, osteoclasts and platelets.


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.


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.


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**

*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%



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

Entity name
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 name
Colorectal cancer
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 name
Breast cancer
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 name
Hematopoietic cancers
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 name
Other tumour types
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.


Pubmed IDLast YearTitleAuthors
119002202002Activation of Src kinase in primary colorectal carcinoma: an indicator of poor clinical prognosis.Aligayer H et al
182162192008Crosstalk between the estrogen receptor and the HER tyrosine kinase receptor family: molecular mechanism and clinical implications for endocrine therapy resistance.Arpino G et al
112507112000Tyrosine kinase signalling in breast cancer: epidermal growth factor receptor and c-Src interactions in breast cancer.Biscardi JS et al
186253402008Src and focal adhesion kinase as therapeutic targets in cancer.Brunton VG et al
111395882001Phosphatidylinositol 3-kinase/AKT-mediated activation of estrogen receptor alpha: a new model for anti-estrogen resistance.Campbell RA et al
75093411994Elevated c-Src tyrosine kinase activity in premalignant epithelia of ulcerative colitis.Cartwright CA et al
116894452001PI3-kinase in concert with Src promotes the S-phase entry of oestradiol-stimulated MCF-7 cells.Castoria G et al
186794172008Src family kinase oncogenic potential and pathways in prostate cancer as revealed by AZD0530.Chang YM et al
24483181987Analysis of pp60c-src tyrosine kinase activity and phosphotyrosyl phosphatase activity in human colon carcinoma and normal human colon mucosal cells.DeSeau V et al
76122681995Src family protein tyrosine kinases and cellular signal transduction pathways.Erpel T et al
111457372001Potentiation of estrogen receptor activation function 1 (AF-1) by Src/JNK through a serine 118-independent pathway.Feng W et al
168595112006Beta3 integrin and Src facilitate transforming growth factor-beta mediated induction of epithelial-mesenchymal transition in mammary epithelial cells.Galliher AJ et al
185084912008Microenvironmental regulation of E-cadherin-mediated adherens junctions.Giehl K et al
184938482009Dual targeting of Src and ER prevents acquired antihormone resistance in breast cancer cells.Hiscox S et al
172595592006Src as a therapeutic target in anti-hormone/anti-growth factor-resistant breast cancer.Hiscox S et al
173635902007Integrin alpha v beta 3 controls activity and oncogenic potential of primed c-Src.Huveneers S et al
99882701999Activating SRC mutation in a subset of advanced human colon cancers.Irby RB et al
111147442000Role of Src expression and activation in human cancer.Irby RB et al
124021522002Elevated c-Src is linked to altered cell-matrix adhesion rather than proliferation in KM12C human colorectal cancer cells.Jones RJ et al
182030072008Src-family kinases in the development and therapy of Philadelphia chromosome-positive chronic myeloid leukemia and acute lymphoblastic leukemia.Li S et al
172595542006Resistance to endocrine therapy in breast cancer: exploiting estrogen receptor/growth factor signaling crosstalk.Massarweh S et al
175952212007GPCRs signaling directly through Src-family kinases.McGarrigle D et al
110328082000Steroid-induced androgen receptor-oestradiol receptor beta-Src complex triggers prostate cancer cell proliferation.Migliaccio A et al
155282702005The 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 et al
154899192004Role of STATs as downstream signal transducers in Src family kinase-mediated tumorigenesis.Silva CM et al
128849102003Src family kinases in tumor progression and metastasis.Summy JM et al
157533842005ErbB2 promotes Src synthesis and stability: novel mechanisms of Src activation that confer breast cancer metastasis.Tan M et al
94428821997Cellular functions regulated by Src family kinases.Thomas SM et al
127539092003Heregulin and HER2 signaling selectively activates c-Src phosphorylation at tyrosine 215.Vadlamudi RK et al
90148581996c-Src protein expression is increased in human breast cancer. An immunohistochemical and biochemical analysis.Verbeek BS et al
185703532008Sensing estrogen's many pathways.Weatherman RV et al
162031302006Identification of estrogen receptor ligands leading to activation of non-genomic signaling pathways while exhibiting only weak transcriptional activity.Wessler S et al

Other Information

Locus ID:

NCBI: 6714
MIM: 190090
HGNC: 11283
Ensembl: ENSG00000197122


dbSNP: 6714
ClinVar: 6714
TCGA: ENSG00000197122


Gene IDTranscript IDUniprot

Expression (GTEx)



PathwaySourceExternal ID
ErbB signaling pathwayKEGGko04012
Axon guidanceKEGGko04360
VEGF signaling pathwayKEGGko04370
Focal adhesionKEGGko04510
Adherens junctionKEGGko04520
Tight junctionKEGGko04530
Gap junctionKEGGko04540
Regulation of actin cytoskeletonKEGGko04810
GnRH signaling pathwayKEGGko04912
Epithelial cell signaling in Helicobacter pylori infectionKEGGko05120
Bladder cancerKEGGko05219
ErbB signaling pathwayKEGGhsa04012
Axon guidanceKEGGhsa04360
VEGF signaling pathwayKEGGhsa04370
Focal adhesionKEGGhsa04510
Adherens junctionKEGGhsa04520
Tight junctionKEGGhsa04530
Gap junctionKEGGhsa04540
Regulation of actin cytoskeletonKEGGhsa04810
GnRH signaling pathwayKEGGhsa04912
Epithelial cell signaling in Helicobacter pylori infectionKEGGhsa05120
Bladder cancerKEGGhsa05219
Chemokine signaling pathwayKEGGko04062
Chemokine signaling pathwayKEGGhsa04062
Bacterial invasion of epithelial cellsKEGGko05100
Bacterial invasion of epithelial cellsKEGGhsa05100
GABAergic synapseKEGGko04727
GABAergic synapseKEGGhsa04727
Viral carcinogenesisKEGGhsa05203
Viral carcinogenesisKEGGko05203
Hepatitis BKEGGhsa05161
Proteoglycans in cancerKEGGhsa05205
Proteoglycans in cancerKEGGko05205
Estrogen signaling pathwayKEGGhsa04915
Estrogen signaling pathwayKEGGko04915
Prolactin signaling pathwayKEGGhsa04917
Prolactin signaling pathwayKEGGko04917
Rap1 signaling pathwayKEGGhsa04015
Rap1 signaling pathwayKEGGko04015
Thyroid hormone signaling pathwayKEGGhsa04919
Inflammatory mediator regulation of TRP channelsKEGGhsa04750
Inflammatory mediator regulation of TRP channelsKEGGko04750
Platelet activationKEGGhsa04611
Oxytocin signaling pathwayKEGGhsa04921
Oxytocin signaling pathwayKEGGko04921
Diseases of signal transductionREACTOMER-HSA-5663202
Infectious diseaseREACTOMER-HSA-5663205
Immune SystemREACTOMER-HSA-168256
Adaptive Immune SystemREACTOMER-HSA-1280218
Costimulation by the CD28 familyREACTOMER-HSA-388841
CD28 co-stimulationREACTOMER-HSA-389356
CTLA4 inhibitory signalingREACTOMER-HSA-389513
Signaling by the B Cell Receptor (BCR)REACTOMER-HSA-983705
Downstream signaling events of B Cell Receptor (BCR)REACTOMER-HSA-1168372
PIP3 activates AKT signalingREACTOMER-HSA-1257604
Negative regulation of the PI3K/AKT networkREACTOMER-HSA-199418
Innate Immune SystemREACTOMER-HSA-168249
Fcgamma receptor (FCGR) dependent phagocytosisREACTOMER-HSA-2029480
FCGR activationREACTOMER-HSA-2029481
DAP12 interactionsREACTOMER-HSA-2172127
DAP12 signalingREACTOMER-HSA-2424491
RAF/MAP kinase cascadeREACTOMER-HSA-5673001
RAF activationREACTOMER-HSA-5673000
MAP2K and MAPK activationREACTOMER-HSA-5674135
Fc epsilon receptor (FCERI) signalingREACTOMER-HSA-2454202
FCERI mediated MAPK activationREACTOMER-HSA-2871796
Role of LAT2/NTAL/LAB on calcium mobilizationREACTOMER-HSA-2730905
C-type lectin receptors (CLRs)REACTOMER-HSA-5621481
CLEC7A (Dectin-1) signalingREACTOMER-HSA-5607764
Cytokine Signaling in Immune systemREACTOMER-HSA-1280215
Signaling by InterleukinsREACTOMER-HSA-449147
Interleukin-2 signalingREACTOMER-HSA-451927
Interleukin receptor SHC signalingREACTOMER-HSA-912526
Interleukin-3, 5 and GM-CSF signalingREACTOMER-HSA-512988
Platelet activation, signaling and aggregationREACTOMER-HSA-76002
GP1b-IX-V activation signallingREACTOMER-HSA-430116
Signal amplificationREACTOMER-HSA-392518
ADP signalling through P2Y purinoceptor 1REACTOMER-HSA-418592
Thrombin signalling through proteinase activated receptors (PARs)REACTOMER-HSA-456926
Platelet Aggregation (Plug Formation)REACTOMER-HSA-76009
Integrin alphaIIb beta3 signalingREACTOMER-HSA-354192
GRB2:SOS provides linkage to MAPK signaling for IntegrinsREACTOMER-HSA-354194
p130Cas linkage to MAPK signaling for integrinsREACTOMER-HSA-372708
Cell surface interactions at the vascular wallREACTOMER-HSA-202733
PECAM1 interactionsREACTOMER-HSA-210990
Signal TransductionREACTOMER-HSA-162582
Signaling by EGFRREACTOMER-HSA-177929
GRB2 events in EGFR signalingREACTOMER-HSA-179812
SHC1 events in EGFR signalingREACTOMER-HSA-180336
GAB1 signalosomeREACTOMER-HSA-180292
Signaling by FGFRREACTOMER-HSA-190236
Signaling by FGFR1REACTOMER-HSA-5654736
Negative regulation of FGFR1 signalingREACTOMER-HSA-5654726
Spry regulation of FGF signalingREACTOMER-HSA-1295596
Signaling by FGFR2REACTOMER-HSA-5654738
Negative regulation of FGFR2 signalingREACTOMER-HSA-5654727
Signaling by FGFR3REACTOMER-HSA-5654741
Negative regulation of FGFR3 signalingREACTOMER-HSA-5654732
Signaling by FGFR4REACTOMER-HSA-5654743
Negative regulation of FGFR4 signalingREACTOMER-HSA-5654733
Signaling by Insulin receptorREACTOMER-HSA-74752
Insulin receptor signalling cascadeREACTOMER-HSA-74751
IRS-mediated signallingREACTOMER-HSA-112399
SOS-mediated signallingREACTOMER-HSA-112412
Signalling by NGFREACTOMER-HSA-166520
NGF signalling via TRKA from the plasma membraneREACTOMER-HSA-187037
Signalling to ERKsREACTOMER-HSA-187687
Signalling to RASREACTOMER-HSA-167044
p38MAPK eventsREACTOMER-HSA-171007
Signalling to p38 via RIT and RINREACTOMER-HSA-187706
Prolonged ERK activation eventsREACTOMER-HSA-169893
Frs2-mediated activationREACTOMER-HSA-170968
ARMS-mediated activationREACTOMER-HSA-170984
PI3K/AKT activationREACTOMER-HSA-198203
Signaling by PDGFREACTOMER-HSA-186797
Downstream signal transductionREACTOMER-HSA-186763
Signaling by VEGFREACTOMER-HSA-194138
VEGFR2 mediated cell proliferationREACTOMER-HSA-5218921
Signaling by SCF-KITREACTOMER-HSA-1433557
Regulation of KIT signalingREACTOMER-HSA-1433559
Signaling by ERBB2REACTOMER-HSA-1227986
MAPK family signaling cascadesREACTOMER-HSA-5683057
MAPK1/MAPK3 signalingREACTOMER-HSA-5684996
Signaling by Rho GTPasesREACTOMER-HSA-194315
RHO GTPase EffectorsREACTOMER-HSA-195258
RHO GTPases Activate ForminsREACTOMER-HSA-5663220
Signaling by GPCRREACTOMER-HSA-372790
Gastrin-CREB signalling pathway via PKC and MAPKREACTOMER-HSA-881907
Signaling by Type 1 Insulin-like Growth Factor 1 Receptor (IGF1R)REACTOMER-HSA-2404192
IGF1R signaling cascadeREACTOMER-HSA-2428924
IRS-related events triggered by IGF1RREACTOMER-HSA-2428928
Signaling by LeptinREACTOMER-HSA-2586552
Vesicle-mediated transportREACTOMER-HSA-5653656
Membrane TraffickingREACTOMER-HSA-199991
Gap junction trafficking and regulationREACTOMER-HSA-157858
Regulation of gap junction activityREACTOMER-HSA-191650
c-src mediated regulation of Cx43 function and closure of gap junctionsREACTOMER-HSA-191647
Cell-Cell communicationREACTOMER-HSA-1500931
Signal regulatory protein (SIRP) family interactionsREACTOMER-HSA-391160
Developmental BiologyREACTOMER-HSA-1266738
Axon guidanceREACTOMER-HSA-422475
NCAM signaling for neurite out-growthREACTOMER-HSA-375165
Netrin-1 signalingREACTOMER-HSA-373752
DCC mediated attractive signalingREACTOMER-HSA-418885
Netrin mediated repulsion signalsREACTOMER-HSA-418886
L1CAM interactionsREACTOMER-HSA-373760
Recycling pathway of L1REACTOMER-HSA-437239
EPH-Ephrin signalingREACTOMER-HSA-2682334
EPHA-mediated growth cone collapseREACTOMER-HSA-3928663
EPHB-mediated forward signalingREACTOMER-HSA-3928662
Ephrin signalingREACTOMER-HSA-3928664
EPH-ephrin mediated repulsion of cellsREACTOMER-HSA-3928665
PI5P, PP2A and IER3 Regulate PI3K/AKT SignalingREACTOMER-HSA-6811558
EGFR tyrosine kinase inhibitor resistanceKEGGko01521
Endocrine resistanceKEGGko01522
EGFR tyrosine kinase inhibitor resistanceKEGGhsa01521
Endocrine resistanceKEGGhsa01522
RET signalingREACTOMER-HSA-8853659
Oncogenic MAPK signalingREACTOMER-HSA-6802957
Signaling by RAS mutantsREACTOMER-HSA-6802949
Signaling by high-kinase activity BRAF mutantsREACTOMER-HSA-6802948
Signaling by moderate kinase activity BRAF mutantsREACTOMER-HSA-6802946
Paradoxical activation of RAF signaling by kinase inactive BRAFREACTOMER-HSA-6802955
Signaling by BRAF and RAF fusionsREACTOMER-HSA-6802952
Signaling by METREACTOMER-HSA-6806834
MET promotes cell motilityREACTOMER-HSA-8875878
MET activates PTK2 signalingREACTOMER-HSA-8874081
Listeria monocytogenes entry into host cellsREACTOMER-HSA-8876384
InlA-mediated entry of Listeria monocytogenes into host cellsREACTOMER-HSA-8876493
Fluid shear stress and atherosclerosisKEGGko05418
Fluid shear stress and atherosclerosisKEGGhsa05418
Mitophagy - animalKEGGko04137
Mitophagy - animalKEGGhsa04137

Protein levels (Protein atlas)

Not detected


Entity IDNameTypeEvidenceAssociationPKPDPMIDs


Pubmed IDYearTitleCitations
198789812009An epigenetic switch involving NF-kappaB, Lin28, Let-7 MicroRNA, and IL6 links inflammation to cell transformation.594
191600182009Rho signaling, ROCK and mDia1, in transformation, metastasis and invasion.212
232428082013Inhibiting EGF receptor or SRC family kinase signaling overcomes BRAF inhibitor resistance in melanoma.143
165439522006Nephrin ectodomain engagement results in Src kinase activation, nephrin phosphorylation, Nck recruitment, and actin polymerization.136
177858442007ICAM-1-mediated, Src- and Pyk2-dependent vascular endothelial cadherin tyrosine phosphorylation is required for leukocyte transendothelial migration.134
157356822005HIF-1alpha, STAT3, CBP/p300 and Ref-1/APE are components of a transcriptional complex that regulates Src-dependent hypoxia-induced expression of VEGF in pancreatic and prostate carcinomas.130
119406072002Coordinate interactions of Csk, Src, and Syk kinases with [alpha]IIb[beta]3 initiate integrin signaling to the cytoskeleton.122
168622152006Nicotine induces cell proliferation by beta-arrestin-mediated activation of Src and Rb-Raf-1 pathways.121
212577112011An EGFR-Src-Arg-cortactin pathway mediates functional maturation of invadopodia and breast cancer cell invasion.114
119947432002v-Src's hold over actin and cell adhesions.106


Stephen Hiscox

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

Atlas Genet Cytogenet Oncol Haematol. 2009-04-01

Online version: