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P25020 (SRC_RSVH1) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tyrosine-protein kinase transforming protein Src

EC=2.7.10.2
Alternative name(s):
pp60v-src
Short name=p60-Src
Short name=v-Src
Gene names
Name:V-SRC
OrganismRous sarcoma virus (strain H-19)
Taxonomic identifier11887 [NCBI]
Taxonomic lineageVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeAlpharetrovirus
Virus hostGallus gallus (Chicken) [TaxID: 9031]

Protein attributes

Sequence length526 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This phosphoprotein, required for both the initiation and the maintenance of neoplastic transformation, is a protein kinase that catalyzes the phosphorylation of tyrosine residues in vitro.

Catalytic activity

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

Cofactor

Manganese By similarity.

Post-translational modification

The phosphorylated form is termed pp60v-src.

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

PDGFRBP096194EBI-8636140,EBI-641237From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed; by host By similarity
Chain2 – 526525Tyrosine-protein kinase transforming protein Src
PRO_0000088155

Regions

Domain81 – 14262SH3
Domain148 – 24598SH2
Domain267 – 517251Protein kinase
Nucleotide binding273 – 2819ATP By similarity

Sites

Active site3861Proton acceptor By similarity
Binding site2951ATP By similarity

Amino acid modifications

Modified residue4161Phosphotyrosine; by autocatalysis By similarity
Lipidation21N-myristoyl glycine; by host Ref.2

Sequences

Sequence LengthMass (Da)Tools
P25020 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 33B212BCC943C6AF

FASTA52659,075
        10         20         30         40         50         60 
MGSSKSKPKD PSQRRRSLEP PDSTHHGGFP ASQTPDETAA PDAHRNPSRS FGTVATEPKL 

        70         80         90        100        110        120 
FWGFNTSDTV TSPQRAGALA GGVTTFVALY DYESWTETDL SFKKGERLQI VNNTEGDWWL 

       130        140        150        160        170        180 
AHSLTTGQTG YIPSNYVAPS DSIQAEEWYF GKITRRESER LLLNPENPRG TFLVRKSETA 

       190        200        210        220        230        240 
KGAYCLSVSD FDNAKGPNVK HYKICKLYSG GFYITSRTQF GSLQQLVAYY SKHADGLCHR 

       250        260        270        280        290        300 
LTNVCPTSKP QTQGLAKDAW EIPRESLRLE AKLGQGCFGE VWMGTWNGTT RVAIKTLKPG 

       310        320        330        340        350        360 
TMSPEAFLQE AQVMKKLRHE KLVQLYAVVS EEPIYIVIEY MSKGSLLDFL KGEMGKYLRL 

       370        380        390        400        410        420 
PQLVDMAAQI ASGMAYVERM NYVHRDLRAA NILVGENLVC KVADFGLARL IEDNEYTARQ 

       430        440        450        460        470        480 
GAKFPIKWTA PEAALYGRFT IKSDVWSFGI LLTELTTKGR VPYPGMVNRE VLDQVERAYR 

       490        500        510        520 
MPCPPECPES LHDLMCQCWR KDPEERPTFK YLQAQLLPAC VLEVAE 

« Hide

References

[1]"Complete nucleotide sequence of LTR, v-src, LTR provirus H-19."
Bodor J., Poliak E., Pichrtova J., Geryk J., Svoboda J.
Nucleic Acids Res. 17:8869-8869(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Antibodies to an NH2-terminal myristoyl glycine moiety can detect NH2-terminal myristoylated proteins in the retrovirus-infected cells."
Shoji S., Tashiro A., Furuishi K., Takenaka O., Kida Y., Horiuchi S., Funakoshi T., Kubota Y.
Biochem. Biophys. Res. Commun. 162:724-732(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-9, MYRISTOYLATION AT GLY-2.
Strain: Isolate tsNY68.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X15345 mRNA. Translation: CAA33404.1.
PIROKFVYR. S09609.

3D structure databases

ProteinModelPortalP25020.
SMRP25020. Positions 83-516.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP25020. 1 interaction.
MINTMINT-8013578.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA2.7.10.2. 5464.

Family and domain databases

Gene3D3.30.505.10. 1 hit.
InterProIPR011009. 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]
PfamPF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00109. TYRKINASE.
SMARTSM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
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]
ProtoNetSearch...

Entry information

Entry nameSRC_RSVH1
AccessionPrimary (citable) accession number: P25020
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 102 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families