Src Rous sarcoma oncogene [Mus musculus] - Gene

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Summary

Official Symbol: Srcprovided by MGI
Official Full Name: Rous sarcoma oncogeneprovided by MGI
Primary source: MGI:98397
Locus tag: RP23-169M4.1
See related: Ensembl:ENSMUSG00000027646; Vega:OTTMUSG00000016179
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus; Mus
Also known as: AW259666; pp60c-src

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Genomic context

Location :: 2 H1; 2 89.0 cM

Sequence :: Chromosome: 2; NC_000068.7 (157424293..157471838)

See Src in Epigenomics, MapViewer

Chromosome 2 - NC_000068.7 Genomic Context describing neighboring genes

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Genomic regions, transcripts, and products

Genomic Sequence

Go to nucleotideGraphics FASTA GenBank

Go to reference sequence details

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Bibliography

GeneRIFs: Gene References Into Functions What's a GeneRIF?

Cinnamomum cassia extract exerts strong anti-inflammatory activity by suppressing macrophage Src/Syk-mediated NF-kappaB activation.
Title: The ability of an ethanol extract of Cinnamomum cassia to inhibit Src and spleen tyrosine kinase activity contributes to its anti-inflammatory action.
Data indicate that interaction between Cav1 and Rho-GTPases (most likely RhoC but not RhoA) promotes metastasis by stimulating alpha5-integrin expression and regulating the Src-dependent activation of Ras/Erk1/2 signaling cascades.
Title: The interaction between caveolin-1 and Rho-GTPases promotes metastasis by controlling the expression of alpha5-integrin and the activation of Src, Ras and Erk.
Fibronectin induces endothelial cell migration through beta1 integrin and Src-dependent phosphorylation of fibroblast growth factor receptor-1 at tyrosines 653/654 and 766.
Title: Fibronectin induces endothelial cell migration through β1 integrin and Src-dependent phosphorylation of fibroblast growth factor receptor-1 at tyrosines 653/654 and 766.
c-Src has essential and unique functions in proliferation and tumor progression.
Title: Mammary epithelial-specific disruption of c-Src impairs cell cycle progression and tumorigenesis.
The results demonstrate that SFKs are expressed during preimplantation development and that SFK activity is required for blastocyst formation and is an important mediator of trophectoderm tight junction permeability.
Title: Ouabain stimulates a Na+/K+-ATPase-mediated SFK-activated signalling pathway that regulates tight junction function in the mouse blastocyst.
These findings demonstrate a critical role of Src kinases in mediating proximal renal tubular cell dedifferentiation through activation of the EGFR/PI3K signaling pathway.
Title: Src family kinases regulate renal epithelial dedifferentiation through activation of EGFR/PI3K signaling.
Src was constitutively active in BaF3 cells expressing exogenous FGFR1 chimeric kinases cultured in vitro as well as in T-cell or B-cell lymphomas they induced in vivo.
Title: Src activation plays an important key role in lymphomagenesis induced by FGFR1 fusion kinases.
Inhibition of autophagy results in restoration of active Src at peripheral adhesions.
Title: Autophagic targeting of Src promotes cancer cell survival following reduced FAK signalling.
Data show that the phosphoprotein associated with glycosphigolipid-enriched microdomains (PAG)/Csk binding protein (Cbp) modulates SFK activity in the brain.
Title: Phosphoprotein associated with glycosphingolipid-enriched microdomains differentially modulates SRC kinase activity in brain maturation.
Data show that Grb14 inhibits the activity of PTP1B in retina in a phosphorylation-regulated manner, and that rhodopsin-regulated Src kinase activation in retina leads to the phosphorylation of Grb14.
Title: Phosphorylated Grb14 is an endogenous inhibitor of retinal protein tyrosine phosphatase 1B, and light-dependent activation of Src phosphorylates Grb14.

Submit: New GeneRIF Correction See all (144)

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Alleles

Alleles of this type are documented at Mouse Genome Informatics (MGI)

Targeted (Floxed/Frt) (1) 1 citation
Targeted (knock-out) (1) 1 citation

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Products	Interactant	Other Gene	Source	Pubs	Description
NP_033297.1	NP_031426.1	Adam12	BIND	PubMed	Meltrin-alpha interacts with the SH3 domain of Src and is phosphorylated by v-Src.
NP_033297.1	NP_033744.1	Adam15	BIND	PubMed	ADAM15v1 cytoplasmic domain interacts with Src
NP_033297.1	O88839	Adam15	BIND	PubMed	ADAM15v2 cytoplasmic domain interacts with Src
NP_033297.1	NP_034084.2	Bcar1	BIND	PubMed	Cas interacts with c-Src.
NP_033297.1	NP_034084.2	Bcar1	BIND	PubMed	CAS interacts with c-Src.
NP_033297.1	NP_034084.2	Bcar1	BIND	PubMed	CAS interacts with c-Src.
NP_033297.1	NP_031857.1	Dcc	BIND	PubMed	Src interacts with and phosphorylates DCC.
NP_033297.1	NP_034240.1	Efnb1	BIND	PubMed	v-Src phosphorylates Elk-L. This interaction was modeled on a demonstrated interaction between v-Src from unspecified species and Elk-L from human.
NP_033297.1	NP_034241.2	Efnb2	BIND	PubMed	v-Src phosphorylates Htk-L. This interaction was modeled on a demonstrated interaction between v-Src from unspecified species and Htk-L from human.
NP_033297.1	AAC52863.1	Enah	BIND	PubMed	Mena interacts with Src. This interaction was modelled on a demonstrated interaction between mouse Mena and Src from an unspecified species.
NP_033297.1	NP_031991.2	Evl	BIND	PubMed	EVL interacts with nSrc SH3 domain. This interaction was modeled on a demonstrated interaction between mouse EVL and nSrc from an unspecified species.
NP_033297.1	NP_579933.1	Grid2ip	BIND	PubMed	Delphilin interacts with n-Src.
NP_033297.1	TVVPMH	HpVgp2	BIND	PubMed	Src SH2 domain interacts with hmT.
NP_033297.1	NP_035447.2	Khdrbs1	BIND	PubMed	C-Src phosphorylates Sam68. This interaction was modelled on a demonstrated interaction between c-Src from an unspecified source and mouse Sam68.
NP_033297.1	NP_063920.1	Ngef	BIND	PubMed	Src phosphorylates Ngef (ephexin). This interaction was modelled on a demonstrated interaction between Src from unspecified species and mouse ephexin.
NP_033297.1	NP_056919.1	P/V/C	BIND	PubMed	Mouse Src (c-Src) interacts with and phosphorylates P from measles virus (MV).
NP_033297.1	NP_035182.1	Pdcd6ip	BIND	PubMed	Alix interacts with Src. This interaction was modeled on a demonstrated interaction between mouse Alix and human Src.
NP_033297.1	NP_032835.1	Pdgfrb	BIND	PubMed	PDGF-beta receptor phosphorylates c-Src.
NP_033297.1	NP_032008.1	Ptk2	BIND	PubMed	Src interacts with FAK. This interaction was modeled on a demonstrated interaction between Src from an unspecified species and mouse FAK.
NP_033297.1	NP_032008.1	Ptk2	BIND	PubMed	Src (c-Src) interacts with and phosphorylates Ptk2 (FAK).
NP_033297.1	NP_032008.1	Ptk2	BIND	PubMed	Ptk2 (FAK) interacts with Src (c-Src).
NP_033297.1	NP_032008.1	Ptk2	BIND	PubMed	FAK interacts with c-Src.
NP_033297.1	NP_032008.1	Ptk2	BIND	PubMed	FAK interacts with Src.
NP_033297.1	NP_032008.1	Ptk2	BIND	PubMed	FAK interacts with c-Src.
NP_033297.1	NP_035353.1	Pxn	BIND	PubMed	Src phosphorylates Paxillin
NP_033297.1	NP_033190.1	Sh3bp1	BIND	PubMed	3BP1 interacts with pp60c-src. This interaction was modelled on a demonstrated interaction between mouse 3BP1 and chicken pp60c-src.
NP_033297.1	NP_035498.2	Shc1	BIND	PubMed	Src phosphorylates Shc. This interaction was modeled on a demonstrated interaction between mouse Src and human Shc.
NP_033297.1	NP_033257.1	Sos1	BIND	PubMed	mSos1 interacts with pp60c-src. This interaction was modelled on a demonstrated interaction between mouse mSos1 and chicken pp60c-src.
NP_033297.1	NP_033297.1	Src	BIND	PubMed	Src (c-Src) autophosphorylates.
NP_033297.1	NP_033297.1	Src	BIND	PubMed	c-Src autophosphorylates.
NP_033297.1	NP_033297.1	Src	BIND	PubMed	c-Src autophosphorylates.
NP_033297.1		Stat3	BIND	PubMed	Src phosphorylates an unspecified isoform of Stat3. This interaction was modeled on a demonstrated interaction between Src and Stat3, both from an unspecified species.
NP_033297.1			BIND	PubMed	Cyclin B/Cdc2 complex phosphorylates c-Src. This interaction was modeled on a demonstrated interaction between Cyclin B/Cdc2 complex from an unspecified species and mouse c-Src.
BioGRID:203491	BioGRID:199343	Dvl2	BioGRID	PubMed	Affinity Capture-Western; Biochemical Activity
BioGRID:203491	BioGRID:202198	Prkce	BioGRID	PubMed	Affinity Capture-Western; Reconstituted Complex
	NP_032008.1	Ptk2	BIND	PubMed	c-Src interacts with and phosphorylates FAK. This interaction was modelled on a demonstrated interaction between mouse c-Src and FAK from an unspecified species.
	NP_766086.1	Ptk2b	BIND	PubMed	Pyk2 interacts with c-Src.
BioGRID:203491	BioGRID:205208	Skp2	BioGRID	PubMed	Affinity Capture-Western
BioGRID:203491	BioGRID:113164	UBC	BioGRID	PubMed	Affinity Capture-Western

Function	Evidence Code	Pubs
ATP binding	IEA Inferred from Electronic Annotation more info
SH2 domain binding	ISO Inferred from Sequence Orthology more info
cell adhesion molecule binding	ISO Inferred from Sequence Orthology more info
enzyme binding	ISO Inferred from Sequence Orthology more info
ephrin receptor binding	IPI Inferred from Physical Interaction more info	PubMed
ephrin receptor binding	ISO Inferred from Sequence Orthology more info
estrogen receptor binding	ISO Inferred from Sequence Orthology more info
heme binding	ISO Inferred from Sequence Orthology more info
insulin receptor binding	ISO Inferred from Sequence Orthology more info
ion channel binding	ISO Inferred from Sequence Orthology more info
kinase activity	IMP Inferred from Mutant Phenotype more info	PubMed
non-membrane spanning protein tyrosine kinase activity	IEA Inferred from Electronic Annotation more info
nucleotide binding	IEA Inferred from Electronic Annotation more info
protein C-terminus binding	ISO Inferred from Sequence Orthology more info
protein binding	IPI Inferred from Physical Interaction more info	PubMed
protein complex binding	ISO Inferred from Sequence Orthology more info
protein domain specific binding	IPI Inferred from Physical Interaction more info	PubMed
protein kinase C binding	ISO Inferred from Sequence Orthology more info
protein kinase activity	IDA Inferred from Direct Assay more info	PubMed
protein kinase activity	ISO Inferred from Sequence Orthology more info
protein kinase binding	ISO Inferred from Sequence Orthology more info
protein tyrosine kinase activity	IMP Inferred from Mutant Phenotype more info	PubMed
protein tyrosine kinase activity	ISO Inferred from Sequence Orthology more info
receptor binding	ISO Inferred from Sequence Orthology more info
transferase activity	IEA Inferred from Electronic Annotation more info
transferase activity, transferring phosphorus-containing groups	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
activation of protein kinase B activity	ISO Inferred from Sequence Orthology more info
adherens junction organization	ISO Inferred from Sequence Orthology more info
bone resorption	IMP Inferred from Mutant Phenotype more info	PubMed
branching involved in mammary gland duct morphogenesis	IMP Inferred from Mutant Phenotype more info	PubMed
cell adhesion	IEA Inferred from Electronic Annotation more info
cell cycle	IEA Inferred from Electronic Annotation more info
cell migration	IMP Inferred from Mutant Phenotype more info	PubMed
cell proliferation	ISO Inferred from Sequence Orthology more info
forebrain development	IGI Inferred from Genetic Interaction more info	PubMed
intracellular protein kinase cascade	ISO Inferred from Sequence Orthology more info
negative regulation of extrinsic apoptotic signaling pathway	ISO Inferred from Sequence Orthology more info
negative regulation of intrinsic apoptotic signaling pathway	ISO Inferred from Sequence Orthology more info
negative regulation of transcription, DNA-dependent	ISO Inferred from Sequence Orthology more info
nerve growth factor receptor signaling pathway	ISO Inferred from Sequence Orthology more info
oogenesis	IMP Inferred from Mutant Phenotype more info	PubMed
peptidyl-serine phosphorylation	ISO Inferred from Sequence Orthology more info
peptidyl-tyrosine phosphorylation	IDA Inferred from Direct Assay more info	PubMed
phosphorylation	IEA Inferred from Electronic Annotation more info
positive regulation of DNA biosynthetic process	ISO Inferred from Sequence Orthology more info
positive regulation of ERK1 and ERK2 cascade	IMP Inferred from Mutant Phenotype more info	PubMed
positive regulation of ERK1 and ERK2 cascade	ISO Inferred from Sequence Orthology more info
positive regulation of MAP kinase activity	ISO Inferred from Sequence Orthology more info
positive regulation of apoptotic process	ISO Inferred from Sequence Orthology more info
positive regulation of canonical Wnt receptor signaling pathway	IGI Inferred from Genetic Interaction more info	PubMed
positive regulation of cell adhesion	ISO Inferred from Sequence Orthology more info
positive regulation of cyclin-dependent protein kinase activity	ISO Inferred from Sequence Orthology more info
positive regulation of cytokine secretion	ISO Inferred from Sequence Orthology more info
positive regulation of gene expression	ISO Inferred from Sequence Orthology more info
positive regulation of glucose metabolic process	ISO Inferred from Sequence Orthology more info
positive regulation of insulin receptor signaling pathway	ISO Inferred from Sequence Orthology more info
positive regulation of intracellular protein kinase cascade	ISO Inferred from Sequence Orthology more info
positive regulation of phosphatidylinositol 3-kinase activity	ISO Inferred from Sequence Orthology more info
positive regulation of protein autophosphorylation	ISO Inferred from Sequence Orthology more info
positive regulation of protein transport	ISO Inferred from Sequence Orthology more info
positive regulation of smooth muscle cell migration	ISO Inferred from Sequence Orthology more info
positive regulation of transcription, DNA-dependent	ISO Inferred from Sequence Orthology more info
protein autophosphorylation	ISO Inferred from Sequence Orthology more info
protein phosphorylation	IDA Inferred from Direct Assay more info	PubMed
protein phosphorylation	ISO Inferred from Sequence Orthology more info
regulation of intracellular estrogen receptor signaling pathway	IMP Inferred from Mutant Phenotype more info	PubMed
response to interleukin-1	ISO Inferred from Sequence Orthology more info
transcytosis	ISO Inferred from Sequence Orthology more info
uterus development	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
caveola	ISO Inferred from Sequence Orthology more info
cytoplasm	IEA Inferred from Electronic Annotation more info
cytoskeleton	IEA Inferred from Electronic Annotation more info
membrane	IEA Inferred from Electronic Annotation more info
mitochondrial inner membrane	ISO Inferred from Sequence Orthology more info
mitochondrion	IEA Inferred from Electronic Annotation more info
nucleus	IEA Inferred from Electronic Annotation more info
plasma membrane	ISO Inferred from Sequence Orthology more info
postsynaptic density	ISO Inferred from Sequence Orthology more info
synaptosome	ISO Inferred from Sequence Orthology more info

General protein information

Preferred Names: neuronal proto-oncogene tyrosine-protein kinase Src

Names: neuronal proto-oncogene tyrosine-protein kinase Src; p60-Src; proto-oncogene c-Src

NP_001020566.1

EC 2.7.10.2

NP_033297.2

EC 2.7.10.2

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NCBI Reference Sequences (RefSeq)

RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_001025395.2 → NP_001020566.1 neuronal proto-oncogene tyrosine-protein kinase Src isoform 2

Status: VALIDATED

Source sequence(s)

AL672259, CD355175, CX218263, M17031

Consensus CDS

CCDS16978.1

UniProtKB/Swiss-Prot

P05480

UniProtKB/TrEMBL

Q80XU2

Related

ENSMUSP00000029175, OTTMUSP00000017316, ENSMUST00000029175, OTTMUST00000038724

Conserved Domains (4) summary

cd00174
Location:87 – 141
Blast Score: 172

SH3; Src homology 3 domains; SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of ...

cd05034
Location:262 – 521
Blast Score: 1501

PTKc_Src_like; Catalytic domain of Src kinase-like Protein Tyrosine Kinases

cd10365
Location:146 – 246
Blast Score: 545

SH2_Src_Src; Src homology 2 (SH2) domain found in tyrosine kinase sarcoma (Src)

pfam07714
Location:269 – 518
Blast Score: 1046

Pkinase_Tyr; Protein tyrosine kinase
NM_009271.3 → NP_033297.2 neuronal proto-oncogene tyrosine-protein kinase Src isoform 1

Status: VALIDATED

Source sequence(s)

AL672259, CD355175, CX218263, M17031

Consensus CDS

CCDS38305.1

UniProtKB/Swiss-Prot

P05480

Related

ENSMUSP00000090237, ENSMUST00000092576

Conserved Domains (4) summary

cd00174
Location:87 – 147
Blast Score: 155

SH3; Src homology 3 domains; SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of ...

cd05034
Location:268 – 527
Blast Score: 1502

PTKc_Src_like; Catalytic domain of Src kinase-like Protein Tyrosine Kinases

cd10365
Location:152 – 252
Blast Score: 544

SH2_Src_Src; Src homology 2 (SH2) domain found in tyrosine kinase sarcoma (Src)

pfam07714
Location:275 – 524
Blast Score: 1046

Pkinase_Tyr; Protein tyrosine kinase

RefSeqs of Annotated Genomes: Build 38.1

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCm38 C57BL/6J

Genomic

NC_000068.7 Reference GRCm38 C57BL/6J

Range

157424293..157471838

Download

GenBank, FASTA, Sequence Viewer (Graphics)

Alternate Mm_Celera

Genomic

AC_000024.1 Alternate Mm_Celera

Range

163383913..163416616

Download

GenBank, FASTA, Sequence Viewer (Graphics)

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Related Sequences

Nucleotide		Protein	Strain
Heading	Accession and Version	Protein	Strain
genomic	AJ312258.1	None	BALB/c
genomic	AJ312259.1	None	BALB/c
genomic	AJ312260.1	None	BALB/c
genomic	AJ312261.1	None	BALB/c
genomic	AJ312262.1	None	BALB/c
genomic	AJ312263.1	None	BALB/c
genomic	AJ312264.1	None	BALB/c
genomic	AJ313104.1	None	BALB/c
genomic	AJ313176.1	None	BALB/c
genomic	AJ313177.1	None	BALB/c
genomic	AL672259.9	CAM16140.1
		CAM16141.1
genomic	AY902331.1	AAX90616.1	CAST/EiJ
genomic	CH466551.1	EDL06234.1	mixed
mRNA	AK017629.1	None	C57BL/6J
mRNA	AK146056.1	BAE26865.1	C57BL/6J
mRNA	AK182969.1	None
mRNA	AK189521.1	None
mRNA	AK190301.1	None
mRNA	AK192339.1	None
mRNA	AK201096.1	None
mRNA	AK208623.1	None
mRNA	AK216314.1	None
mRNA	BC039953.1	AAH39953.1	FVB/N
mRNA	CD355175.1	None	C57BL/6
mRNA	CX218263.1	None	C57BL/6
mRNA	M17031.1	AAA40135.1

Protein Accession	Links
Protein Accession	GenPept Link	UniProtKB Link
P05480.4	GenPept	UniProtKB/Swiss-Prot:P05480
Q3UKD6	GenPept	UniProtKB/TrEMBL:Q3UKD6
Q80XU2	GenPept	UniProtKB/TrEMBL:Q80XU2