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P00524

- SRC_RSVSA

UniProt

P00524 - SRC_RSVSA

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Protein

Tyrosine-protein kinase transforming protein Src

Gene
V-SRC
Organism
Avian leukosis virus RSA (RSV-SRA) (Rous sarcoma virus (strain Schmidt-Ruppin A))
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei295 – 2951ATP By similarity
Active sitei386 – 3861Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi273 – 2819ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase, Tyrosine-protein kinase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.2. 5464.

Names & Taxonomyi

Protein namesi
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 namesi
Name:V-SRC
OrganismiAvian leukosis virus RSA (RSV-SRA) (Rous sarcoma virus (strain Schmidt-Ruppin A))
Taxonomic identifieri269446 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeAlpharetrovirus
Virus hostiGallus gallus (Chicken) [TaxID: 9031]

Pathology & Biotechi

Keywords - Diseasei

Oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed; by host By similarity
Chaini2 – 526525Tyrosine-protein kinase transforming protein SrcPRO_0000088153Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine; by host By similarity
Modified residuei416 – 4161Phosphotyrosine; by autocatalysis1 Publication

Post-translational modificationi

The phosphorylated form is termed pp60v-src.1 Publication

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

IntActiP00524. 1 interaction.
MINTiMINT-215689.

Structurei

Secondary structure

1
526
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi149 – 1524
Helixi155 – 1628
Beta strandi172 – 1765
Beta strandi178 – 1803
Beta strandi184 – 1929
Turni193 – 1953
Beta strandi196 – 20611
Beta strandi208 – 2103
Beta strandi212 – 2154
Beta strandi219 – 2224
Helixi223 – 2308
Beta strandi237 – 2393

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BKLX-ray2.10A145-249[»]
1BKMX-ray2.00A145-249[»]
1IS0X-ray1.90A/B144-249[»]
1KC2X-ray2.10A145-247[»]
1NZLX-ray1.90A/B145-247[»]
1NZVX-ray2.10A/B145-247[»]
1SHAX-ray1.50A144-247[»]
1SHBX-ray2.00A144-247[»]
1SKJX-ray2.00A145-249[»]
1SPRX-ray2.50A/B/C/D144-247[»]
1SPSX-ray2.70A/B/C144-247[»]
ProteinModelPortaliP00524.
SMRiP00524. Positions 83-516.

Miscellaneous databases

EvolutionaryTraceiP00524.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini81 – 14262SH3Add
BLAST
Domaini148 – 24598SH2Add
BLAST
Domaini267 – 517251Protein kinaseAdd
BLAST

Sequence similaritiesi

Contains 1 SH2 domain.
Contains 1 SH3 domain.

Keywords - Domaini

SH2 domain, SH3 domain

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR011009. 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]
PfamiPF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00109. TYRKINASE.
SMARTiSM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00107. 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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00524-1 [UniParc]FASTAAdd to Basket

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MGSSKSKPKD PSQRRCSLEP PDSTHHGGFP ASQTPNKTAA PDTHRTPSRS    50
FGTVATEPKL FGGFNTSDTV TSPQRAGALA GGVTTFVALY DYESRTETDL 100
SFKKGERLQI VNNTEGDWWL AHSLTTGQTG YIPSNYVAPS DSIQAEEWYF 150
GKITRRESER LLLNPENPRG TFLVRESETT KGAYCLSVSD FDNAKGLNVK 200
HYKIRKLDSG GFYITSRTQF SSLQQLVAYY SKHADGLCHR LTNVCPTSKP 250
QTQGLAKDAW EIPRESLRLE VKLGQGCFGE VWMGTWNGTT RVAIKTLKPG 300
TMSPEAFLQE AQVMKKLRHE KLVQLYAVVS EEPIYIVTEY MSKGSLLDFL 350
KGEMGKYLRL PQLVDMAAQI ASGMAYVERM NYVHRDLRAA NILVGENLVC 400
KVADFGLARL IEDNEYTARQ GAKFPIKWTA PEAALYGRFT IKSDVWSFGI 450
LLTELTTKGR VPYPGMGNGE VLDRVERGYR MPCPPECPES LHDLMCQCWR 500
RDPEERPTFE YLQAQLLPAC VLEVAE 526
Length:526
Mass (Da):58,878
Last modified:January 23, 2007 - v5
Checksum:i7DB3903F80233E49
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti16 – 161C → R1 Publication
Sequence conflicti16 – 161C → R1 Publication
Sequence conflicti95 – 962RT → WI1 Publication
Sequence conflicti95 – 962RT → WI1 Publication
Sequence conflicti117 – 1171D → N1 Publication
Sequence conflicti117 – 1171D → N1 Publication
Sequence conflicti338 – 3381T → I1 Publication
Sequence conflicti338 – 3381T → I1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L29199 Genomic DNA. Translation: AAA42563.1.
V01169 Genomic RNA. Translation: CAA24495.1.
K00928 Genomic RNA. Translation: AAA42565.1.
PIRiA38017. TVFV60.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L29199 Genomic DNA. Translation: AAA42563.1 .
V01169 Genomic RNA. Translation: CAA24495.1 .
K00928 Genomic RNA. Translation: AAA42565.1 .
PIRi A38017. TVFV60.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BKL X-ray 2.10 A 145-249 [» ]
1BKM X-ray 2.00 A 145-249 [» ]
1IS0 X-ray 1.90 A/B 144-249 [» ]
1KC2 X-ray 2.10 A 145-247 [» ]
1NZL X-ray 1.90 A/B 145-247 [» ]
1NZV X-ray 2.10 A/B 145-247 [» ]
1SHA X-ray 1.50 A 144-247 [» ]
1SHB X-ray 2.00 A 144-247 [» ]
1SKJ X-ray 2.00 A 145-249 [» ]
1SPR X-ray 2.50 A/B/C/D 144-247 [» ]
1SPS X-ray 2.70 A/B/C 144-247 [» ]
ProteinModelPortali P00524.
SMRi P00524. Positions 83-516.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P00524. 1 interaction.
MINTi MINT-215689.

Chemistry

BindingDBi P00524.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BRENDAi 2.7.10.2. 5464.

Miscellaneous databases

EvolutionaryTracei P00524.

Family and domain databases

Gene3Di 3.30.505.10. 1 hit.
InterProi IPR011009. 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 ]
Pfami PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view ]
PRINTSi PR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00109. TYRKINASE.
SMARTi SM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi 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 ]
ProtoNeti Search...

Publicationsi

  1. "Nucleotide sequence of an avian sarcoma virus oncogene (src) and proposed amino acid sequence for gene product."
    Czernilofsky A.P., Levinson A.D., Varmus H.E., Bishop J.M., Tischer E., Goodman H.M.
    Nature 287:198-203(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  2. "Corrections to the nucleotide sequence of the src gene of Rous sarcoma virus."
    Czernilofsky A.P., Levinson A.D., Varmus H.E., Bishop J.M., Tischer E., Goodman H.
    Nature 301:736-738(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  3. "Structure and sequence of the cellular gene homologous to the RSV src gene and the mechanism for generating the transforming virus."
    Takeya T., Hanafusa H.
    Cell 32:881-890(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: Isolate td mutant 1441.
  4. "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.
  5. "Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides."
    Waksman G., Kominos D., Robertson S.C., Pant N., Baltimore D., Birge R.B., Cowburn D., Hanafusa H., Mayer B.J., Overduin M., Resh M.D., Rios C.B., Silverman L., Kuriyan J.
    Nature 358:646-653(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 148-245 (SH2 DOMAIN).
  6. "Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: crystal structures of the complexed and peptide-free forms."
    Waksman G., Shoelson S.E., Pant N., Cowburn D., Kuriyan J.
    Cell 72:779-790(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 146-247 (SH2 DOMAIN).
  7. "Design, synthesis, and cocrystal structure of a nonpeptide Src SH2 domain ligand."
    Plummer M.S., Holland D.R., Shahripour A., Lunney E.A., Fergus J.H., Marks J.S., McConnell P., Mueller W.T., Sawyer T.K.
    J. Med. Chem. 40:3719-3725(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 146-247 (SH2 DOMAIN).
  8. "Dissection of the energetic coupling across the Src SH2 domain-tyrosyl phosphopeptide interface."
    Lubman O.Y., Waksman G.
    J. Mol. Biol. 316:291-304(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 145-247 (SH2 DOMAIN).
  9. "Calorimetric and structural studies of 1,2,3-trisubstituted cyclopropanes as conformationally constrained peptide inhibitors of Src SH2 domain binding."
    Davidson J.P., Lubman O.Y., Rose T., Waksman G., Martin S.F.
    J. Am. Chem. Soc. 124:205-215(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 146-248 (SH2 DOMAIN).
  10. "Structural and thermodynamic basis for the interaction of the Src SH2 domain with the activated form of the PDGF beta-receptor."
    Lubman O.Y., Waksman G.
    J. Mol. Biol. 328:655-668(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 145-247 (SH2 DOMAIN).

Entry informationi

Entry nameiSRC_RSVSA
AccessioniPrimary (citable) accession number: P00524
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 135 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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