P00526 (SRC_RSVP) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Rous sarcoma virus (strain Prague C) (RSV-PrC) [Complete proteome]

Taxonomic identifier

11888 [NCBI]

Taxonomic lineage

Viruses › Retro-transcribing viruses › Retroviridae › Orthoretrovirinae › Alpharetrovirus › Rous sarcoma virus

Virus host

Gallus gallus (Chicken) [TaxID: 9031]

Protein attributes

Sequence length	526 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Disease	Oncogene
Domain	SH2 domain SH3 domain
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase Tyrosine-protein kinase
PTM	Lipoprotein Myristate Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW non-membrane spanning protein tyrosine kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed; by host By similarity
	Chain	2 – 526	525	Tyrosine-protein kinase transforming protein Src		PRO_0000088152
Regions
	Domain	81 – 142	62	SH3
	Domain	148 – 245	98	SH2
	Domain	267 – 517	251	Protein kinase
	Nucleotide binding	273 – 281	9	ATP By similarity
Sites
	Active site	386	1	Proton acceptor By similarity
	Binding site	295	1	ATP By similarity
Amino acid modifications
	Modified residue	416	1	Phosphotyrosine; by autocatalysis Ref.2
	Lipidation	2	1	N-myristoyl glycine; by host By similarity
Natural variations
	Natural variant	242	1	A → T.
	Natural variant	288	1	D → G.

Sequences

	Sequence		Length	Mass (Da)
	P00526 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 12C12DE33FFFAB11	FASTA	526	59,130
	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

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.
PIR	TVFVR. A00632.
3D structure databases
ProteinModelPortal	P00526.
SMR	P00526. Positions 83-516.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
BRENDA	2.7.10.2. 5464.
Family and domain databases
Gene3D	3.30.505.10. 1 hit.
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_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]
Pfam	PF07714. Pkinase_Tyr. 1 hit. PF00017. SH2. 1 hit. PF00018. SH3_1. 1 hit. [Graphical view]
PRINTS	PR00401. SH2DOMAIN. PR00452. SH3DOMAIN. PR00109. TYRKINASE.
SMART	SM00252. SH2. 1 hit. SM00326. SH3. 1 hit. SM00219. TyrKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit. SSF50044. SH3. 1 hit.
PROSITE	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]
ProtoNet	Search...

Entry information

Entry name

SRC_RSVP

Accession

Primary (citable) accession number: P00526

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 111 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program