P63185 (SRC_RSVSE) 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 Schmidt-Ruppin E) (RSV-SR-E)

Taxonomic identifier

270623 [NCBI]

Taxonomic lineage

Viruses › Retro-transcribing viruses › Retroviridae › Orthoretrovirinae › Alpharetrovirus › Rous sarcoma virus › Rous sarcoma virus (strain Schmidt-Ruppin)

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 By similarity.
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.
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	3D-structure
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_0000088154

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 By similarity

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

526

Helix Strand Turn

Details...

Beta strand

149 – 152

4

Helix

155 – 162

8

Beta strand

171 – 176

6

Beta strand

178 – 180

3

Beta strand

184 – 192

9

Turn

193 – 195

3

Beta strand

196 – 206

11

Beta strand

212 – 217

6

Beta strand

220 – 222

3

Helix

223 – 230

8

Beta strand

237 – 239

3

Sequences

	Sequence		Length	Mass (Da)
	P63185 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 85D356B6B8ECB14D	FASTA	526	58,953
	10 20 30 40 50 60 MGSSKSKPKG PSQRRRSLEP PDSTHHGGFP ASQTPNKTAA PDTHRTPSRS FGTVATEPKL 70 80 90 100 110 120 FGDFNTSDTV TSPQRAGALA GGVTTFVALY DYESWIETDL SFKKGERLQI VNNTEGNWWL 130 140 150 160 170 180 AHSVTTGQTG 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 AQVMKKLRHK 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 VPYPGMGNGE VLDRVERGYR 490 500 510 520 MPCPPECPES LHDLMSQCWR RDPEERPTFE YLQAQLLPAC VLEVAE

References

[1]	"Nucleotide sequence of the src gene of the Schmidt-Ruppin strain of Rous sarcoma virus type E." Barnier J.V., Dezelee P., Marx M., Calothy G. Nucleic Acids Res. 17:1252-1252(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X13745 Genomic DNA. Translation: CAA32012.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2JYQ	NMR	-	A	144-249	[»]

ProteinModelPortal

P63185.

SMR

P63185. Positions 83-516.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

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...

Other

EvolutionaryTrace

P63185.

Entry information

Entry name

SRC_RSVSE

Accession

Primary (citable) accession number: P63185

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 27, 2004
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 66 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program