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Reviewed, UniProtKB/Swiss-Prot P05480 (SRC_MOUSE)

Last modified June 10, 2008. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesNeuronal proto-oncogene tyrosine-protein kinase Src
Also known as:
     EC 2.7.10.2
     pp60c-src
     p60-Src
     c-Src
Gene names
Name: Src
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

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

Subunit structure

Interacts with CDCP1, PELP1, TGFB1I1 and TOM1L2 By similarity. 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 By similarity. Interacts with RALGPS1 via its SH3 domain By similarity.

Post-translational modification

Phosphorylated on Tyr-535 by c-Src kinase (CSK). The phosphorylated form is termed pp60c-src. The phosphorylated tail interacts with the SH2 domain thereby repressing kinase activity By similarity.

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily.

Contains 1 protein kinase domain.

Contains 1 SH2 domain.

Contains 1 SH3 domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Csf1P071412EBI-298680,EBI-777188
enaQ8T4F72EBI-298680,EBI-466810From a different organism.
Ephb2P547631EBI-298680,EBI-537711

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 541540Neuronal proto-oncogene tyrosine-protein kinase Src

Regions

Domain83 – 15068SH3
Domain156 – 25398SH2
Domain275 – 528254Protein kinase
Nucleotide binding281 – 2899ATP By similarity

Sites

Active site3941Proton acceptor By similarity
Binding site3031ATP By similarity

Amino acid modifications

Modified residue171Phosphoserine By similarity
Modified residue681Phosphoserine By similarity
Modified residue731Phosphothreonine By similarity
Modified residue741Phosphoserine
Modified residue1921Phosphotyrosine
Modified residue4241Phosphotyrosine; by autocatalysis By similarity
Modified residue5351Phosphotyrosine; by CSK By similarity
Lipidation21N-myristoyl glycine By similarity

Sequences

Sequence LengthMass (Da)Tools
P05480-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 09BBA0EEF88A70B5

FASTA54160,619
        10         20         30         40         50         60 
MGSNKSKPKD ASQRRRSLEP SENVHGAGGA FPASQTPSKP ASADGHRGPS AAFVPPAAEP 

        70         80         90        100        110        120 
KLFGGFNSSD TVTSPQRAGA LAGGVTTFVA LYDYESRTET DLSFKKGERL QIVNNTRKVD 

       130        140        150        160        170        180 
VREGDWWLAH SLSTGQTGYI PSNYVAPSDS IQAEEWYFGK ITRRESERLL LNAENPRGTF 

       190        200        210        220        230        240 
LVRESETTKG AYCLSVSDFD NAKGLNVKHY KIRKLDSGGF YITSRTQFNS LQQLVAYYSK 

       250        260        270        280        290        300 
HADGLCHRLT TVCPTSKPQT QGLAKDAWEI PRESLRLEVK LGQGCFGEVW MGTWNGTTRV 

       310        320        330        340        350        360 
AIKTLKPGTM SPEAFLQEAQ VMKKLRHEKL VQLYAVVSEE PIYIVTEYMN KGSLLDFLKG 

       370        380        390        400        410        420 
ETGKYLRLPQ LVDMSAQIAS GMAYVERMNY VHRDLRAANI LVGENLVCKV ADFGLARLIE 

       430        440        450        460        470        480 
DNEYTARQGA KFPIKWTAPE AALYGRFTIK SDVWSFGILL TELTTKGRVP YPGMVNREVL 

       490        500        510        520        530        540 
DQVERGYRMP CPPECPESLH DLMCQCWRKE PEERPTFEYL QAFLEDYFTS TEPQYQPGEN 


L 

« Hide

References

« Hide 'large scale' references
[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: 2440106] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
[2]"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: 9819391] [Abstract]
Cited for: INTERACTION WITH DDEF1/ASAP1.
[3]"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: 17000758] [Abstract]
Cited for: INTERACTION WITH CCPG1.
[4]"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: 18034455] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-192, MASS SPECTROMETRY.
Tissue: Brain.
[5]"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
Mol. Cell. Proteomics 6:283-293(2007) [PubMed: 17114649] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, MASS SPECTROMETRY.
Tissue: Brain cortex.

Cross-references

Sequence databases

M17031 mRNA. Translation: AAA40135.1.
PIRA43610.
RefSeqNP_001020566.1.
NP_033297.2.
UniGeneMm.22845

3D structure databases

HSSPHSSP built from PDB template 1A09 based on UniProtKB P12931.
SMRP05480. Positions 86-541.
ModBaseSearch...

Protein-protein interaction databases

IntActP05480.

PTM databases

PhosphoSiteP05480.

Genome annotation databases

EnsemblENSMUSG00000027646. Mus musculus. [Contig view]
GeneID20779.
KEGGmmu:20779.

Organism-specific databases

MGIMGI:98397. Src.

Phylogenomic databases

HOGENOMP05480.
HOVERGENP05480.

Gene expression databases

ArrayExpressP05480.
CleanExMM_SRC.
GermOnlineENSMUSG00000027646. Mus musculus.

Family and domain databases

InterProIPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_bd_CS.
IPR000980. SH2.
IPR001452. SH3.
IPR001245. Tyr_pkinase.
IPR008266. Tyr_pkinase_AS.
[Graphical view]
Gene3DG3DSA:3.30.505.10. SH2. 1 hit.
PfamPF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00109. TYRKINASE.
ProDomPD000001. Prot_kinase. 1 hit.
PD000093. SH2. 1 hit.
PD000066. SH3. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
PROSITEPS00107. 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]
BLOCKSSearch...

Other Resources

SOURCESearch...
ProtoNetSearch...

Entry information

Entry nameSRC_MOUSE
AccessionPrimary (citable) accession number: P05480
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: January 23, 2007
Last modified: June 10, 2008
This is version 95 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

Names and origin · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents