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P05480

- SRC_MOUSE

UniProt

P05480 - SRC_MOUSE

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Protein
Neuronal proto-oncogene tyrosine-protein kinase Src
Gene
Src
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Non-receptor protein tyrosine kinase which is activated following engagement of many different classes of cellular receptors including immune response receptors, integrins and other adhesion receptors, receptor protein tyrosine kinases, G protein-coupled receptors as well as cytokine receptors. Participates in signaling pathways that control a diverse spectrum of biological activities including gene transcription, immune response, cell adhesion, cell cycle progression, apoptosis, migration, and transformation. Due to functional redundancy between members of the SRC kinase family, identification of the specific role of each SRC kinase is very difficult. SRC appears to be one of the primary kinases activated following engagement of receptors and plays a role in the activation of other protein tyrosine kinase (PTK) families. Receptor clustering or dimerization leads to recruitment of SRC to the receptor complexes where it phosphorylates the tyrosine residues within the receptor cytoplasmic domains. Plays an important role in the regulation of cytoskeletal organization through phosphorylation of specific substrates such as AFAP1. Phosphorylation of AFAP1 allows the SRC SH2 domain to bind AFAP1 and to localize to actin filaments. Cytoskeletal reorganization is also controlled through the phosphorylation of cortactin (CTTN). 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. Also plays a role in PDGF-mediated tyrosine phosphorylation of both STAT1 and STAT3, leading to increased DNA binding activity of these transcription factors. 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 ADRBK1, 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. 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 DDX58/RIG-I-elicited antiviral signaling. Phosphorylates PDPK1 at 'Tyr-9', 'Tyr-373' and 'Tyr-376'. Phosphorylates BCAR1 at 'Tyr-132'. Phosphorylates CBLC at multiple tyrosine residues, phosphorylation at 'Tyr-341' activates CBLC E3 activity.4 Publications

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

Enzyme regulationi

Phosphorylation by CSK at Tyr-535 inhibits kinase activity. Inhibitory phosphorylation at Tyr-535 is enhanced by heme. Further phosphorylation by CDK1 partially reactivates CSK-inactivated SRC and facilitates complete reactivation by protein tyrosine phosphatase PTPRC. Integrin engagement stimulates kinase activity. Phosphorylation by PTK2/FAK1 enhances kinase activity. Butein and pseudosubstrate-based peptide inhibitors like CIYKYYF act as inhibitors. Phosphorylation at Tyr-424 increases kinase activity.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei303 – 3031ATP By similarity
Active sitei394 – 3941Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi281 – 2899ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ephrin receptor binding Source: UniProtKB
  3. heme binding Source: UniProtKB
  4. kinase activity Source: MGI
  5. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC
  6. protein binding Source: UniProtKB
  7. protein domain specific binding Source: MGI
  8. protein kinase activity Source: MGI
  9. protein tyrosine kinase activity Source: MGI
Complete GO annotation...

GO - Biological processi

  1. bone resorption Source: UniProtKB
  2. branching involved in mammary gland duct morphogenesis Source: MGI
  3. cell adhesion Source: UniProtKB-KW
  4. cell cycle Source: UniProtKB-KW
  5. cell migration Source: MGI
  6. forebrain development Source: MGI
  7. immune system process Source: UniProtKB-KW
  8. intracellular signal transduction Source: Ensembl
  9. negative regulation of anoikis Source: Ensembl
  10. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
  11. negative regulation of extrinsic apoptotic signaling pathway Source: Ensembl
  12. negative regulation of intrinsic apoptotic signaling pathway Source: Ensembl
  13. negative regulation of mitochondrial depolarization Source: Ensembl
  14. negative regulation of protein homooligomerization Source: Ensembl
  15. oogenesis Source: MGI
  16. peptidyl-tyrosine phosphorylation Source: MGI
  17. positive regulation of ERK1 and ERK2 cascade Source: BHF-UCL
  18. positive regulation of canonical Wnt signaling pathway Source: MGI
  19. positive regulation of podosome assembly Source: MGI
  20. positive regulation of protein kinase B signaling Source: Ensembl
  21. protein autophosphorylation Source: Ensembl
  22. protein phosphorylation Source: MGI
  23. regulation of intracellular estrogen receptor signaling pathway Source: MGI
  24. regulation of protein binding Source: MGI
  25. response to interleukin-1 Source: Ensembl
  26. uterus development Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Cell adhesion, Cell cycle, Immunity

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.2. 3474.
ReactomeiREACT_188191. Signaling by ERBB2.
REACT_188578. Signaling by SCF-KIT.
REACT_196487. FCGR activation.
REACT_198526. Spry regulation of FGF signaling.
REACT_204081. CD28 co-stimulation.
REACT_206286. GAB1 signalosome.
REACT_207601. p38MAPK events.
REACT_220322. Thrombin signalling through proteinase activated receptors (PARs).
REACT_224600. c-src mediated regulation of Cx43 function and closure of gap junctions.
REACT_227425. Regulation of KIT signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Neuronal proto-oncogene tyrosine-protein kinase Src (EC:2.7.10.2)
Alternative name(s):
Proto-oncogene c-Src
pp60c-src
Short name:
p60-Src
Gene namesi
Name:Src
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:98397. Src.

Subcellular locationi

Cell membrane. Mitochondrion inner membrane. Nucleus. Cytoplasmcytoskeleton
Note: Localizes to focal adhesion sites after integrin engagement. Localization to focal adhesion sites requires myristoylation and the SH3 domain.1 Publication

GO - Cellular componenti

  1. caveola Source: Ensembl
  2. cytoskeleton Source: UniProtKB-SubCell
  3. cytosol Source: Reactome
  4. late endosome Source: Ensembl
  5. lysosome Source: Ensembl
  6. mitochondrial inner membrane Source: UniProtKB-SubCell
  7. nucleus Source: UniProtKB-SubCell
  8. plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 541540Neuronal proto-oncogene tyrosine-protein kinase Src
PRO_0000088142Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine By similarity
Modified residuei17 – 171Phosphoserine By similarity
Modified residuei34 – 341Phosphoserine By similarity
Modified residuei68 – 681Phosphoserine By similarity
Modified residuei73 – 731Phosphothreonine By similarity
Modified residuei74 – 741Phosphoserine; by CDK5 By similarity
Modified residuei192 – 1921Phosphotyrosine1 Publication
Modified residuei424 – 4241Phosphotyrosine; by autocatalysis; alternate By similarity
Modified residuei424 – 4241Phosphotyrosine; by FAK2; alternate By similarity
Modified residuei444 – 4441Phosphotyrosine By similarity
Modified residuei516 – 5161Phosphothreonine By similarity
Modified residuei527 – 5271Phosphotyrosine By similarity
Modified residuei535 – 5351Phosphotyrosine; by CSK By similarity

Post-translational modificationi

Myristoylated at Gly-2, and this is essential for targeting to membranes By similarity.
Dephosphorylated at Tyr-535 by PTPRJ By similarity. Phosphorylated on Tyr-535 by c-Src kinase (CSK). The phosphorylated form is termed pp60c-src. Dephosphorylated by PTPRJ at Tyr-424. Normally maintained in an inactive conformation with the SH2 domain engaged with Tyr-535, the SH3 domain engaged with the SH2-kinase linker, and Tyr-424 dephosphorylated. Dephosphorylation of Tyr-535 as a result of protein tyrosine phosphatase (PTP) action disrupts the intramolecular interaction between the SH2 domain and Tyr-535, Tyr-424 can then become autophosphorylated, resulting in SRC activation. Phosphorylation of Tyr-535 by CSK allows this interaction to reform, resulting in SRC inactivation. CDK5-mediated phosphorylation at Ser-74 targets SRC to ubiquitin-dependent degradation and thus leads to cytoskeletal reorganization. Phosphorylated by PTK2/FAK1; this enhances kinase activity. Phosphorylated by PTK2B/PYK2; this enhances kinase activity By similarity.
S-nitrosylation is important for activation of its kinase activity By similarity.
Ubiquitinated in response to CDK5-mediated phosphorylation. Ubiquitination mediated by CBLC requires SRC autophosphorylation at Tyr-424 and may lead to lysosomal degradation By similarity.

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP05480.
PaxDbiP05480.
PRIDEiP05480.

PTM databases

PhosphoSiteiP05480.

Expressioni

Gene expression databases

ArrayExpressiP05480.
BgeeiP05480.
CleanExiMM_SRC.
GenevestigatoriP05480.

Interactioni

Subunit structurei

Interacts with CDCP1, PELP1, TGFB1I1 and TOM1L2. Interacts with DDEF1/ASAP1 via its SH3 domain. Interacts with CCPG1. Interacts with the cytoplasmic domain of MUC1, phosphorylates it and increases binding of MUC1 with beta-catenin. Interacts with RALGPS1 via its SH3 domain. Interacts with CAV2 (tyrosine phosphorylated form). Interacts (via the SH3 domain and the protein kinase domain) with ARRB1; the interaction is independent of the phosphorylation state of SRC C-terminus. Interacts with FCAMR and PXN. Interacts with ARRB2. Interacts with ARRB1. Interacts with SRCIN1. Interacts with SRCIN1. Interacts with NDFIP2 and more weakly with NDFIP1. Interacts with PIK3CA and/or PIK3C2B, PTK2/FAK1, ESR1 (dimethylated on arginine) and FAK. Interacts (via SH2 and SH3 domain) with TNK2. Interacts (via protein kinase domain) with the tyrosine phosphorylated form of RUNX3 (via runt domain). Interacts with TRAF3 (via RING-type zinc finger domain). Interacts with DDX58, MAVS and TBK1. Interacts (via SH2 domain) with GNB2L1/RACK1; the interaction is enhanced by tyrosine phosphorylation of GNB2L1 and inhibits SRC activity. Interacts (via SH2 domain) with the 'Tyr-402' phosphorylated form of PTK2B/PYK2. Interacts (via SH2 domain) with FLT3 (tyrosine phosphorylated). Identified in a complex containing FGFR4, NCAM1, CDH2, PLCG1, FRS2, SRC, SHC1, GAP43 and CTTN. Interacts with EPHB1; activates the MAPK/ERK cascade to regulate cell migration. Interacts with ERBB2 and STAT1. Interacts with PDGFRA (tyrosine phosphorylated). Interacts with CSF1R. Interacts (via SH2 domain) with the 'Tyr-9' phosphorylated form of PDPK1. Interacts with DDR2. Interacts with AMOTL2; this interaction regulates the translocation of phosphorylated SRC to peripheral cell-matrix adhesion sites. Interacts with DDR1 and DAB2. Interacts with TRAP1. Interacts with CBLC; the interaction is enhanced when SRC is phosphorylated at 'Tyr-424'.12 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Bcar1Q637672EBI-298680,EBI-1176801From a different organism.
Csf1P071412EBI-298680,EBI-777188
Dlg4P310169EBI-298680,EBI-375655From a different organism.
enaQ8T4F72EBI-298680,EBI-466810From a different organism.
Ephb2P547633EBI-298680,EBI-537711
Grin2aQ009595EBI-298680,EBI-630970From a different organism.
ITGB3P051065EBI-298680,EBI-702847From a different organism.
PTK2Q053975EBI-298680,EBI-702142From a different organism.
PtpraP180522EBI-298680,EBI-6597520
PXNP490232EBI-298680,EBI-702209From a different organism.
ROR1Q019733EBI-298680,EBI-6082337From a different organism.
WasP703152EBI-298680,EBI-644195

Protein-protein interaction databases

BioGridi203491. 37 interactions.
DIPiDIP-31071N.
IntActiP05480. 27 interactions.
MINTiMINT-85032.
STRINGi10090.ENSMUSP00000105155.

Structurei

3D structure databases

ProteinModelPortaliP05480.
SMRiP05480. Positions 56-541.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini83 – 15068SH3
Add
BLAST
Domaini156 – 25398SH2
Add
BLAST
Domaini275 – 528254Protein kinase
Add
BLAST

Sequence similaritiesi

Contains 1 SH2 domain.
Contains 1 SH3 domain.

Keywords - Domaini

SH2 domain, SH3 domain

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00620000087702.
HOGENOMiHOG000233858.
HOVERGENiHBG008761.
InParanoidiQ2M4I4.
KOiK05704.
OMAiCQCWRKD.
OrthoDBiEOG7GTT2V.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PfamiPF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00109. TYRKINASE.
SMARTiSM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P05480-1 [UniParc]FASTAAdd to Basket

« Hide

MGSNKSKPKD ASQRRRSLEP SENVHGAGGA FPASQTPSKP ASADGHRGPS    50
AAFVPPAAEP KLFGGFNSSD TVTSPQRAGP LAGGVTTFVA LYDYESRTET 100
DLSFKKGERL QIVNNTRKVD VREGDWWLAH SLSTGQTGYI PSNYVAPSDS 150
IQAEEWYFGK ITRRESERLL LNAENPRGTF LVRESETTKG AYCLSVSDFD 200
NAKGLNVKHY KIRKLDSGGF YITSRTQFNS LQQLVAYYSK HADGLCHRLT 250
TVCPTSKPQT QGLAKDAWEI PRESLRLEVK LGQGCFGEVW MGTWNGTTRV 300
AIKTLKPGTM SPEAFLQEAQ VMKKLRHEKL VQLYAVVSEE PIYIVTEYMN 350
KGSLLDFLKG ETGKYLRLPQ LVDMSAQIAS GMAYVERMNY VHRDLRAANI 400
LVGENLVCKV ADFGLARLIE DNEYTARQGA KFPIKWTAPE AALYGRFTIK 450
SDVWSFGILL TELTTKGRVP YPGMVNREVL DQVERGYRMP CPPECPESLH 500
DLMCQCWRKE PEERPTFEYL QAFLEDYFTS TEPQYQPGEN L 541
Length:541
Mass (Da):60,645
Last modified:July 27, 2011 - v4
Checksum:i0534AF027783BCCF
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti80 – 801P → A in AAA40135. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M17031 mRNA. Translation: AAA40135.1.
AY902331 Genomic DNA. Translation: AAX90616.1.
AL672259 Genomic DNA. Translation: CAM16141.1.
CH466551 Genomic DNA. Translation: EDL06234.1.
CCDSiCCDS38305.1.
PIRiA43610.
RefSeqiNP_001020566.1. NM_001025395.2.
NP_033297.2. NM_009271.3.
UniGeneiMm.22845.

Genome annotation databases

EnsembliENSMUST00000092576; ENSMUSP00000090237; ENSMUSG00000027646.
ENSMUST00000109529; ENSMUSP00000105155; ENSMUSG00000027646.
GeneIDi20779.
KEGGimmu:20779.
UCSCiuc008npa.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M17031 mRNA. Translation: AAA40135.1 .
AY902331 Genomic DNA. Translation: AAX90616.1 .
AL672259 Genomic DNA. Translation: CAM16141.1 .
CH466551 Genomic DNA. Translation: EDL06234.1 .
CCDSi CCDS38305.1.
PIRi A43610.
RefSeqi NP_001020566.1. NM_001025395.2.
NP_033297.2. NM_009271.3.
UniGenei Mm.22845.

3D structure databases

ProteinModelPortali P05480.
SMRi P05480. Positions 56-541.
ModBasei Search...

Protein-protein interaction databases

BioGridi 203491. 37 interactions.
DIPi DIP-31071N.
IntActi P05480. 27 interactions.
MINTi MINT-85032.
STRINGi 10090.ENSMUSP00000105155.

Chemistry

BindingDBi P05480.
ChEMBLi CHEMBL3074.

PTM databases

PhosphoSitei P05480.

Proteomic databases

MaxQBi P05480.
PaxDbi P05480.
PRIDEi P05480.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000092576 ; ENSMUSP00000090237 ; ENSMUSG00000027646 .
ENSMUST00000109529 ; ENSMUSP00000105155 ; ENSMUSG00000027646 .
GeneIDi 20779.
KEGGi mmu:20779.
UCSCi uc008npa.1. mouse.

Organism-specific databases

CTDi 6714.
MGIi MGI:98397. Src.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00620000087702.
HOGENOMi HOG000233858.
HOVERGENi HBG008761.
InParanoidi Q2M4I4.
KOi K05704.
OMAi CQCWRKD.
OrthoDBi EOG7GTT2V.

Enzyme and pathway databases

BRENDAi 2.7.10.2. 3474.
Reactomei REACT_188191. Signaling by ERBB2.
REACT_188578. Signaling by SCF-KIT.
REACT_196487. FCGR activation.
REACT_198526. Spry regulation of FGF signaling.
REACT_204081. CD28 co-stimulation.
REACT_206286. GAB1 signalosome.
REACT_207601. p38MAPK events.
REACT_220322. Thrombin signalling through proteinase activated receptors (PARs).
REACT_224600. c-src mediated regulation of Cx43 function and closure of gap junctions.
REACT_227425. Regulation of KIT signaling.

Miscellaneous databases

NextBioi 299503.
PROi P05480.
SOURCEi Search...

Gene expression databases

ArrayExpressi P05480.
Bgeei P05480.
CleanExi MM_SRC.
Genevestigatori P05480.

Family and domain databases

Gene3Di 3.30.505.10. 1 hit.
InterProi IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view ]
Pfami PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view ]
PRINTSi PR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00109. TYRKINASE.
SMARTi SM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Neuronal pp60c-src contains a six-amino acid insertion relative to its non-neuronal counterpart."
    Martinez R., Mathey-Prevot B., Bernards A., Baltimore D.
    Science 237:411-415(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
  2. "Characterization of quantitative trait loci influencing growth and adiposity using congenic mouse strains."
    Farber C.R., Corva P.M., Medrano J.F.
    Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: CAST/EiJ.
    Tissue: Brain.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "Activation of Src family kinases by colony stimulating factor-1, and their association with its receptor."
    Courtneidge S.A., Dhand R., Pilat D., Twamley G.M., Waterfield M.D., Roussel M.F.
    EMBO J. 12:943-950(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CSF1R.
  6. "Direct and specific interaction of c-Src with Neu is involved in signaling by the epidermal growth factor receptor."
    Muthuswamy S.K., Muller W.J.
    Oncogene 11:271-279(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ERBB2.
  7. "Activation of Src-family protein tyrosine kinases and phosphatidylinositol 3-kinase in 3T3-L1 mouse preadipocytes by interleukin-11."
    Fuhrer D.K., Yang Y.C.
    Exp. Hematol. 24:195-203(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN IL11-SIGNALING.
  8. "Bombesin, bradykinin, vasopressin, and phorbol esters rapidly and transiently activate Src family tyrosine kinases in Swiss 3T3 cells. Dissociation from tyrosine phosphorylation of p125 focal adhesion kinase."
    Rodriguez-Fernandez J.L., Rozengurt E.
    J. Biol. Chem. 271:27895-27901(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  9. "c-Src activates both STAT1 and STAT3 in PDGF-stimulated NIH3T3 cells."
    Cirri P., Chiarugi P., Marra F., Raugei G., Camici G., Manao G., Ramponi G.
    Biochem. Biophys. Res. Commun. 239:493-497(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH STAT1.
  10. "ASAP1, a phospholipid-dependent arf GTPase-activating protein that associates with and is phosphorylated by Src."
    Brown M.T., Andrade J., Radhakrishna H., Donaldson J.G., Cooper J.A., Randazzo P.A.
    Mol. Cell. Biol. 18:7038-7051(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DDEF1/ASAP1.
  11. "N-CAM modulates tumour-cell adhesion to matrix by inducing FGF-receptor signalling."
    Cavallaro U., Niedermeyer J., Fuxa M., Christofori G.
    Nat. Cell Biol. 3:650-657(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH NCAM1; CDH2; PLCG1; FRS2; FGFR4; SHC1; GAP43 AND CTTN.
  12. "The role of c-Src in platelet-derived growth factor alpha receptor internalization."
    Avrov K., Kazlauskas A.
    Exp. Cell Res. 291:426-434(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PDGFRA.
  13. "Regulation of cytochrome c oxidase activity by c-Src in osteoclasts."
    Miyazaki T., Neff L., Tanaka S., Horne W.C., Baron R.
    J. Cell Biol. 160:709-718(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  14. "EphB1 recruits c-Src and p52Shc to activate MAPK/ERK and promote chemotaxis."
    Vindis C., Cerretti D.P., Daniel T.O., Huynh-Do U.
    J. Cell Biol. 162:661-671(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EPHB1.
  15. "Src kinase activity is essential for osteoclast function."
    Miyazaki T., Sanjay A., Neff L., Tanaka S., Horne W.C., Baron R.
    J. Biol. Chem. 279:17660-17666(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PTK2B/PYK2.
  16. "Identification of Y589 and Y599 in the juxtamembrane domain of Flt3 as ligand-induced autophosphorylation sites involved in binding of Src family kinases and the protein tyrosine phosphatase SHP2."
    Heiss E., Masson K., Sundberg C., Pedersen M., Sun J., Bengtsson S., Ronnstrand L.
    Blood 108:1542-1550(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FLT3.
  17. "Ccpg1, a novel scaffold protein that regulates the activity of the Rho guanine nucleotide exchange factor Dbs."
    Kostenko E.V., Olabisi O.O., Sahay S., Rodriguez P.L., Whitehead I.P.
    Mol. Cell. Biol. 26:8964-8975(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CCPG1.
  18. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
    Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
    J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-192, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  19. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "Deficiency of a beta-arrestin-2 signal complex contributes to insulin resistance."
    Luan B., Zhao J., Wu H., Duan B., Shu G., Wang X., Li D., Jia W., Kang J., Pei G.
    Nature 457:1146-1149(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARRB2.
  21. "Collagen stimulates discoidin domain receptor 1-mediated migration of smooth muscle cells through Src."
    Lu K.K., Trcka D., Bendeck M.P.
    Cardiovasc. Pathol. 20:71-76(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DDR1.
  22. Cited for: REVIEW ON FUNCTION.
  23. "Cellular functions regulated by Src family kinases."
    Thomas S.M., Brugge J.S.
    Annu. Rev. Cell Dev. Biol. 13:513-609(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  24. "Novel regulation and function of Src tyrosine kinase."
    Ma Y.C., Huang X.Y.
    Cell. Mol. Life Sci. 59:456-462(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.

Entry informationi

Entry nameiSRC_MOUSE
AccessioniPrimary (citable) accession number: P05480
Secondary accession number(s): Q2M4I4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: July 27, 2011
Last modified: September 3, 2014
This is version 162 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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