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P14085 (SRC_AVIST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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 sarcoma virus (strain S2)
Taxonomic identifier11882 [NCBI]
Taxonomic lineageVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeAlpharetrovirusunclassified Alpharetrovirus
Virus hostGalliformes [TaxID: 8976]

Protein attributes

Sequence length557 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed; by host By similarity
Chain2 – 557556Tyrosine-protein kinase transforming protein Src
PRO_0000088149

Regions

Domain81 – 14262SH3
Domain148 – 24598SH2
Domain267 – 520254Protein kinase
Nucleotide binding273 – 2819ATP By similarity

Sites

Active site3861Proton acceptor By similarity
Binding site2951ATP By similarity

Amino acid modifications

Modified residue4161Phosphotyrosine; by autocatalysis By similarity
Lipidation21N-myristoyl glycine; by host By similarity

Sequences

Sequence LengthMass (Da)Tools
P14085 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: BBC2A04CB99CEAFE

FASTA55762,583
        10         20         30         40         50         60 
MGSSKSKPKD PSQRRRSLEP 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 VPYPGMVNRE VLDQVERGYR 

       490        500        510        520        530        540 
MPCPPECPES LHDLMCQCWR KDPEERPTFE YLQAFLEDYL GILAWTPWED KQEGPRGETA 

       550 
SNKQERPGED TLAADES 

« Hide

References

[1]"Activation of the cellular src gene by transducing retrovirus."
Ikawa S., Hagino-Yamagishi K., Kawai S., Yamamoto T., Toyoshima K.
Mol. Cell. Biol. 6:2420-2428(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.

Cross-references

Sequence databases

PIRTVFVS2. B25375.

3D structure databases

ProteinModelPortalP14085.
SMRP14085. Positions 83-550.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA2.7.10.2. 600.

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...

Entry information

Entry nameSRC_AVIST
AccessionPrimary (citable) accession number: P14085
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 106 of the entry and version 3 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