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P00526 (SRC_RSVP) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 115. 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·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 Prague C) (RSV-PrC) [Complete proteome]
Taxonomic identifier11888 [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.

Subunit structure

Homodimer By similarity.

Post-translational modification

The phosphorylated form is termed pp60v-src. Ref.2

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.

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_0000088152

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

Natural variations

Natural variant2421A → T.
Natural variant2881D → G.

Sequences

Sequence LengthMass (Da)Tools
P00526 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 12C12DE33FFFAB11

FASTA52659,130
        10         20         30         40         50         60 
MGSSKSKPKD PSQRRHSLEP 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 HYKIYKLYSG GFYITSRTQF GSLQQLVAYY SKHADGLCHR 

       250        260        270        280        290        300 
LANVCPTSKP QTQGLAKDAW EIPRESLRLE AKLGQGCFGE VWMGTWNDTT 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 VLDQVERGYR 

       490        500        510        520 
MPCPPECPES LHDLMCQCWR KDPEERPTFK YLQAQLLPAC VLEVAE 

« Hide

References

[1]"Nucleotide sequence of Rous sarcoma virus."
Schwartz D., Tizard R., Gilbert W.
Cell 32:853-869(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"Homologous tyrosine phosphorylation sites in transformation-specific gene products of distinct avian sarcoma viruses."
Neil J.C., Ghysdael J., Vogt P.K., Smart J.E.
Nature 291:675-677(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-416.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J02342 Genomic RNA. Translation: AAB59935.1.
PIRTVFVR. A00632.

3D structure databases

ProteinModelPortalP00526.
SMRP00526. Positions 83-516.
ModBaseSearch...
MobiDBSearch...

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_RSVP
AccessionPrimary (citable) accession number: P00526
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 115 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