Reviewed, UniProtKB/Swiss-Prot P00525 (SRC_AVISR)

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

Avian sarcoma virus (strain rASV1441)

Taxonomic identifier

11894 [NCBI]

Taxonomic lineage

Viruses › Retro-transcribing viruses › Retroviridae › Orthoretrovirinae › Alpharetrovirus › unclassified Alpharetrovirus

Virus host

Galliformes [TaxID: 8976]

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.
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 Nucleotide-binding
Molecular function	Kinase Oncogene Transferase Tyrosine-protein kinase
PTM	Lipoprotein Myristate Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
None. [Check GOA]

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Initiator methionine

1

1

Removed; by host By similarity

Chain

2 – 526

525

Tyrosine-protein kinase transforming protein Src

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

Lipidation

2

1

N-myristoyl glycine; by host By similarity

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

526

Helix Strand Turn

Details...

Beta strand

86 – 90

5

Beta strand

106 – 110

5

Beta strand

114 – 123

10

Turn

124 – 127

4

Beta strand

128 – 133

6

Helix

134 – 136

3

Beta strand

137 – 139

3

Sequences

	Sequence		Length	Mass (Da)
	P00525-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 7DB3903F80233E49	FASTA	526	58,878
	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

References

[1]	"DNA sequence of the viral and cellular src gene of chickens. 1. Complete nucleotide sequence of an EcoRI fragment of recovered avian sarcoma virus which codes for gp37 and pp60src." Takeya T., Feldman R.A., Hanafusa H. J. Virol. 44:1-11(1982) [PubMed: 6292477] [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: 6264320] [Abstract] Cited for: PHOSPHORYLATION AT TYR-416.
[3]	"Two binding orientations for peptides to the Src SH3 domain: development of a general model for SH3-ligand interactions." Feng S., Chen J.K., Yu H., Simon J.A., Schreiber S.L. Science 266:1241-1247(1994) [PubMed: 7526465] [Abstract] Cited for: STRUCTURE BY NMR OF 85-140.

Cross-references

Sequence databases

EMBLGenBankDDBJ

K00928 Genomic RNA. Translation: AAA42565.1.

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1QWE	NMR	-	A	81-140	[»]
1QWF	NMR	-	A	81-140	[»]

SMR

P00525. Positions 83-515, 84-516.

ModBase

Search...

Family and domain databases

InterPro

IPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_bd_CS.
IPR000980. SH2.
IPR001452. SH3.
IPR001245. Tyr_pkinase.
IPR008266. Tyr_pkinase_AS.
[Graphical view]

Gene3D

G3DSA:3.30.505.10. SH2. 1 hit.

Pfam

PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]

PRINTS

PR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00109. TYRKINASE.

ProDom

PD000001. Prot_kinase. 1 hit.
PD000093. SH2. 1 hit.
PD000066. SH3. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]

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]

BLOCKS

Search...

Other Resources

BindingDB

P00525.

LinkHub

P00525.

ProtoNet

Search...

Entry information

Entry name

SRC_AVISR

Accession

Primary (citable) accession number: P00525

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	September 2, 2008
This is version 94 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Virus (Virus annotation project)