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P00524 (SRC_RSVSA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
OrganismAvian leukosis virus RSA (RSV-SRA) (Rous sarcoma virus (strain Schmidt-Ruppin A))
Taxonomic identifier269446 [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.

Post-translational modification

The phosphorylated form is termed pp60v-src. Ref.4

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_0000088153

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.4
Lipidation21N-myristoyl glycine; by host By similarity

Experimental info

Sequence conflict161C → R Ref.1
Sequence conflict161C → R Ref.2
Sequence conflict95 – 962RT → WI Ref.1
Sequence conflict95 – 962RT → WI Ref.2
Sequence conflict1171D → N Ref.1
Sequence conflict1171D → N Ref.2
Sequence conflict3381T → I Ref.1
Sequence conflict3381T → I Ref.2

Secondary structure

...................... 526
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00524 [UniParc].

Last modified January 23, 2007. Version 5.
Checksum: 7DB3903F80233E49

FASTA52658,878
        10         20         30         40         50         60 
MGSSKSKPKD PSQRRCSLEP PDSTHHGGFP ASQTPNKTAA PDTHRTPSRS FGTVATEPKL 

        70         80         90        100        110        120 
FGGFNTSDTV TSPQRAGALA GGVTTFVALY DYESRTETDL SFKKGERLQI VNNTEGDWWL 

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

       190        200        210        220        230        240 
KGAYCLSVSD FDNAKGLNVK HYKIRKLDSG GFYITSRTQF SSLQQLVAYY SKHADGLCHR 

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

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

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

       430        440        450        460        470        480 
GAKFPIKWTA PEAALYGRFT IKSDVWSFGI LLTELTTKGR VPYPGMGNGE VLDRVERGYR 

       490        500        510        520 
MPCPPECPES LHDLMCQCWR RDPEERPTFE YLQAQLLPAC VLEVAE 

« Hide

References

[1]"Nucleotide sequence of an avian sarcoma virus oncogene (src) and proposed amino acid sequence for gene product."
Czernilofsky A.P., Levinson A.D., Varmus H.E., Bishop J.M., Tischer E., Goodman H.M.
Nature 287:198-203(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
[2]"Corrections to the nucleotide sequence of the src gene of Rous sarcoma virus."
Czernilofsky A.P., Levinson A.D., Varmus H.E., Bishop J.M., Tischer E., Goodman H.
Nature 301:736-738(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[3]"Structure and sequence of the cellular gene homologous to the RSV src gene and the mechanism for generating the transforming virus."
Takeya T., Hanafusa H.
Cell 32:881-890(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: Isolate td mutant 1441.
[4]"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.
[5]"Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides."
Waksman G., Kominos D., Robertson S.C., Pant N., Baltimore D., Birge R.B., Cowburn D., Hanafusa H., Mayer B.J., Overduin M., Resh M.D., Rios C.B., Silverman L., Kuriyan J.
Nature 358:646-653(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 148-245 (SH2 DOMAIN).
[6]"Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: crystal structures of the complexed and peptide-free forms."
Waksman G., Shoelson S.E., Pant N., Cowburn D., Kuriyan J.
Cell 72:779-790(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 146-247 (SH2 DOMAIN).
[7]"Design, synthesis, and cocrystal structure of a nonpeptide Src SH2 domain ligand."
Plummer M.S., Holland D.R., Shahripour A., Lunney E.A., Fergus J.H., Marks J.S., McConnell P., Mueller W.T., Sawyer T.K.
J. Med. Chem. 40:3719-3725(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 146-247 (SH2 DOMAIN).
[8]"Dissection of the energetic coupling across the Src SH2 domain-tyrosyl phosphopeptide interface."
Lubman O.Y., Waksman G.
J. Mol. Biol. 316:291-304(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 145-247 (SH2 DOMAIN).
[9]"Calorimetric and structural studies of 1,2,3-trisubstituted cyclopropanes as conformationally constrained peptide inhibitors of Src SH2 domain binding."
Davidson J.P., Lubman O.Y., Rose T., Waksman G., Martin S.F.
J. Am. Chem. Soc. 124:205-215(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 146-248 (SH2 DOMAIN).
[10]"Structural and thermodynamic basis for the interaction of the Src SH2 domain with the activated form of the PDGF beta-receptor."
Lubman O.Y., Waksman G.
J. Mol. Biol. 328:655-668(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 145-247 (SH2 DOMAIN).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L29199 Genomic DNA. Translation: AAA42563.1.
V01169 Genomic RNA. Translation: CAA24495.1.
K00928 Genomic RNA. Translation: AAA42565.1.
PIRTVFV60. A38017.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BKLX-ray2.10A145-249[»]
1BKMX-ray2.00A145-249[»]
1IS0X-ray1.90A/B144-249[»]
1KC2X-ray2.10A145-247[»]
1NZLX-ray1.90A/B145-247[»]
1NZVX-ray2.10A/B145-247[»]
1SHAX-ray1.50A144-247[»]
1SHBX-ray2.00A144-247[»]
1SKJX-ray2.00A145-249[»]
1SPRX-ray2.50A/B/C/D144-247[»]
1SPSX-ray2.70A/B/C144-247[»]
ProteinModelPortalP00524.
SMRP00524. Positions 83-516.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP00524. 1 interaction.
MINTMINT-215689.

Chemistry

BindingDBP00524.

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...

Other

EvolutionaryTraceP00524.

Entry information

Entry nameSRC_RSVSA
AccessionPrimary (citable) accession number: P00524
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 135 of the entry and version 5 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references