P25020 (SRC_RSVH1) 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 H-19)

Taxonomic identifier

11887 [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.
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.

Ontologies

Keywords
Domain	SH2 domain SH3 domain
Ligand	ATP-binding Manganese Metal-binding Nucleotide-binding
Molecular function	Kinase Transferase Tyrosine-protein kinase
PTM	Lipoprotein Myristate Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion 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_0000088155
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 By similarity
	Lipidation	2	1	N-myristoyl glycine; by host Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P25020 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 33B212BCC943C6AF	FASTA	526	59,075
	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

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.
PIR	OKFVYR. S09609.
3D structure databases
ProteinModelPortal	P25020.
SMR	P25020. Positions 83-516.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-8013578.
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_RSVH1

Accession

Primary (citable) accession number: P25020

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 98 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program