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P10869

- AK_YEAST

UniProt

P10869 - AK_YEAST

Protein

Aspartokinase

Gene

HOM3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 2 (01 Aug 1990)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    ATP + L-aspartate = ADP + 4-phospho-L-aspartate.

    Pathwayi

    GO - Molecular functioni

    1. amino acid binding Source: InterPro
    2. aspartate kinase activity Source: SGD
    3. ATP binding Source: UniProtKB-KW

    GO - Biological processi

    1. homoserine biosynthetic process Source: SGD
    2. lysine biosynthetic process via diaminopimelate Source: UniProtKB-UniPathway
    3. methionine biosynthetic process Source: SGD
    4. threonine biosynthetic process Source: SGD

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Amino-acid biosynthesis, Threonine biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:YER052C-MONOMER.
    BRENDAi2.7.2.4. 984.
    SABIO-RKP10869.
    UniPathwayiUPA00034; UER00015.
    UPA00050; UER00461.
    UPA00051; UER00462.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aspartokinase (EC:2.7.2.4)
    Alternative name(s):
    Aspartate kinase
    Gene namesi
    Name:HOM3
    Ordered Locus Names:YER052C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome V

    Organism-specific databases

    CYGDiYER052c.
    SGDiS000000854. HOM3.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 527527AspartokinasePRO_0000066690Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei333 – 3331Phosphothreonine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP10869.
    PaxDbiP10869.
    PeptideAtlasiP10869.

    Expressioni

    Gene expression databases

    GenevestigatoriP10869.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FPR1P200815EBI-2430,EBI-6961

    Protein-protein interaction databases

    BioGridi36791. 157 interactions.
    DIPiDIP-1319N.
    IntActiP10869. 8 interactions.
    MINTiMINT-392511.
    STRINGi4932.YER052C.

    Structurei

    3D structure databases

    ProteinModelPortaliP10869.
    SMRiP10869. Positions 16-501.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini367 – 44074ACT 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini442 – 52786ACT 2PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the aspartokinase family.Curated
    Contains 2 ACT domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0527.
    HOGENOMiHOG000293094.
    KOiK00928.
    OMAiQSCLQIK.
    OrthoDBiEOG7NPG3J.

    Family and domain databases

    Gene3Di3.40.1160.10. 2 hits.
    InterProiIPR002912. ACT_dom.
    IPR001048. Asp/Glu/Uridylate_kinase.
    IPR001341. Asp_kinase_dom.
    IPR018042. Aspartate_kinase_CS.
    IPR027795. GATS-like_ACT_dom.
    [Graphical view]
    PfamiPF00696. AA_kinase. 1 hit.
    PF13840. ACT_7. 1 hit.
    [Graphical view]
    SUPFAMiSSF53633. SSF53633. 1 hit.
    TIGRFAMsiTIGR00657. asp_kinases. 1 hit.
    PROSITEiPS51671. ACT. 1 hit.
    PS00324. ASPARTOKINASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P10869-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPMDFQPTSS HSNWVVQKFG GTSVGKFPVQ IVDDIVKHYS KPDGPNNNVA    50
    VVCSARSSYT KAEGTTSRLL KCCDLASQES EFQDIIEVIR QDHIDNADRF 100
    ILNPALQAKL VDDTNKELEL VKKYLNASKV LGEVSSRTVD LVMSCGEKLS 150
    CLFMTALCND RGCKAKYVDL SHIVPSDFSA SALDNSFYTF LVQALKEKLA 200
    PFVSAKERIV PVFTGFFGLV PTGLLNGVGR GYTDLCAALI AVAVNADELQ 250
    VWKEVDGIFT ADPRKVPEAR LLDSVTPEEA SELTYYGSEV IHPFTMEQVI 300
    RAKIPIRIKN VQNPLGNGTI IYPDNVAKKG ESTPPHPPEN LSSSFYEKRK 350
    RGATAITTKN DIFVINIHSN KKTLSHGFLA QIFTILDKYK LVVDLISTSE 400
    VHVSMALPIP DADSLKSLRQ AEEKLRILGS VDITKKLSIV SLVGKHMKQY 450
    IGIAGTMFTT LAEEGINIEM ISQGANEINI SCVINESDSI KALQCIHAKL 500
    LSERTNTSNQ FEHAIDERLE QLKRLGI 527
    Length:527
    Mass (Da):58,110
    Last modified:August 1, 1990 - v2
    Checksum:iD4D28FB8D4374898
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03526 Genomic DNA. Translation: AAA34681.1.
    U18796 Genomic DNA. Translation: AAB64587.1.
    BK006939 Genomic DNA. Translation: DAA07708.1.
    PIRiA35888. KIBYD.
    RefSeqiNP_010972.1. NM_001178943.1.

    Genome annotation databases

    EnsemblFungiiYER052C; YER052C; YER052C.
    GeneIDi856778.
    KEGGisce:YER052C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03526 Genomic DNA. Translation: AAA34681.1 .
    U18796 Genomic DNA. Translation: AAB64587.1 .
    BK006939 Genomic DNA. Translation: DAA07708.1 .
    PIRi A35888. KIBYD.
    RefSeqi NP_010972.1. NM_001178943.1.

    3D structure databases

    ProteinModelPortali P10869.
    SMRi P10869. Positions 16-501.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 36791. 157 interactions.
    DIPi DIP-1319N.
    IntActi P10869. 8 interactions.
    MINTi MINT-392511.
    STRINGi 4932.YER052C.

    Proteomic databases

    MaxQBi P10869.
    PaxDbi P10869.
    PeptideAtlasi P10869.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YER052C ; YER052C ; YER052C .
    GeneIDi 856778.
    KEGGi sce:YER052C.

    Organism-specific databases

    CYGDi YER052c.
    SGDi S000000854. HOM3.

    Phylogenomic databases

    eggNOGi COG0527.
    HOGENOMi HOG000293094.
    KOi K00928.
    OMAi QSCLQIK.
    OrthoDBi EOG7NPG3J.

    Enzyme and pathway databases

    UniPathwayi UPA00034 ; UER00015 .
    UPA00050 ; UER00461 .
    UPA00051 ; UER00462 .
    BioCyci YEAST:YER052C-MONOMER.
    BRENDAi 2.7.2.4. 984.
    SABIO-RK P10869.

    Miscellaneous databases

    NextBioi 982982.
    PROi P10869.

    Gene expression databases

    Genevestigatori P10869.

    Family and domain databases

    Gene3Di 3.40.1160.10. 2 hits.
    InterProi IPR002912. ACT_dom.
    IPR001048. Asp/Glu/Uridylate_kinase.
    IPR001341. Asp_kinase_dom.
    IPR018042. Aspartate_kinase_CS.
    IPR027795. GATS-like_ACT_dom.
    [Graphical view ]
    Pfami PF00696. AA_kinase. 1 hit.
    PF13840. ACT_7. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53633. SSF53633. 1 hit.
    TIGRFAMsi TIGR00657. asp_kinases. 1 hit.
    PROSITEi PS51671. ACT. 1 hit.
    PS00324. ASPARTOKINASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structure of the yeast HOM3 gene which encodes aspartokinase."
      Rafalski J.A., Falco S.C.
      J. Biol. Chem. 263:2146-2151(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Structure of the yeast HOM3 gene which encodes aspartokinase."
      Rafalski J.A., Falco S.C.
      J. Biol. Chem. 265:15346-15346(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    6. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-333, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    7. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
      Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
      Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiAK_YEAST
    AccessioniPrimary (citable) accession number: P10869
    Secondary accession number(s): D3DLV4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: August 1, 1990
    Last modified: October 1, 2014
    This is version 135 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 48100 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome V
      Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

    External Data

    Dasty 3