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P00524

- SRC_RSVSA

UniProt

P00524 - SRC_RSVSA

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
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 5 (23 Jan 2007)
      Previous versions | rss
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    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.PROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei295 – 2951ATPPROSITE-ProRule annotation
    Active sitei386 – 3861Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi273 – 2819ATPPROSITE-ProRule annotation

    GO - Molecular functioni

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

    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 hostBy similarity
    Chaini2 – 526525Tyrosine-protein kinase transforming protein SrcPRO_0000088153Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycine; by hostBy 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. 4 interactions.
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00524.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini81 – 14262SH3PROSITE-ProRule annotationAdd
    BLAST
    Domaini148 – 24598SH2PROSITE-ProRule annotationAdd
    BLAST
    Domaini267 – 517251Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation
    Contains 1 SH2 domain.PROSITE-ProRule annotation
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    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

    « Hide

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti16 – 161C → R(PubMed:6253794)Curated
    Sequence conflicti16 – 161C → R(PubMed:6298633)Curated
    Sequence conflicti95 – 962RT → WI(PubMed:6253794)Curated
    Sequence conflicti95 – 962RT → WI(PubMed:6298633)Curated
    Sequence conflicti117 – 1171D → N(PubMed:6253794)Curated
    Sequence conflicti117 – 1171D → N(PubMed:6298633)Curated
    Sequence conflicti338 – 3381T → I(PubMed:6253794)Curated
    Sequence conflicti338 – 3381T → I(PubMed:6298633)Curated

    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. 4 interactions.
    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: October 1, 2014
    This is version 136 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