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A3KFJ1

- A3KFJ1_HUMAN

UniProt

A3KFJ1 - A3KFJ1_HUMAN

Protein
Submitted name:

Aurora kinase A

Gene

AURKA

Organism
Homo sapiens (Human)
Status
Unreviewed - Annotation score: 1 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 61 (01 Oct 2014)
      Sequence version 2 (14 May 2014)
      Previous versions | rss
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    Functioni

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. protein kinase activity Source: InterPro

    GO - Biological processi

    1. mitotic cell cycle Source: Ensembl

    Keywords - Ligandi

    ATP-bindingUniRule annotation, Nucleotide-binding

    Enzyme and pathway databases

    SignaLinkiA3KFJ1.

    Names & Taxonomyi

    Protein namesi
    Submitted name:
    Aurora kinase AImported
    Gene namesi
    Name:AURKAImported
    OrganismiHomo sapiens (Human)Imported
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:11393. AURKA.

    PTM / Processingi

    Proteomic databases

    PRIDEiA3KFJ1.

    Expressioni

    Gene expression databases

    ArrayExpressiA3KFJ1.

    Structurei

    3D structure databases

    ProteinModelPortaliA3KFJ1.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Phylogenomic databases

    HOGENOMiHOG000233016.
    HOVERGENiHBG108519.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Fragment.

    A3KFJ1-1 [UniParc]FASTAAdd to Basket

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    MDRSKENCIS GPVKATAPVG GPKRVLVTQQ FPCQNPLPVN SGQAQRVLCP    50
    SNSSQRIPLQ AQKLVSSHKP VQNQKQKQLQ ATSVPHPVSR PLNNTQKSKQ 100
    PLPSAPENNP EEELASKQKN EESKKRQWAL EDFEIGRPLG KGKFGNVYLA 150
    REKQSKFILA LKVLFKAQLE KAGVEHQLRR EVEIQSHL 188
    Length:188
    Mass (Da):21,007
    Last modified:May 14, 2014 - v2
    Checksum:i6A10E69CD54F061A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei188 – 1881Imported

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL121914 Genomic DNA. No translation available.

    Genome annotation databases

    EnsembliENST00000420474; ENSP00000388073; ENSG00000087586.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL121914 Genomic DNA. No translation available.

    3D structure databases

    ProteinModelPortali A3KFJ1.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi A3KFJ1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000420474 ; ENSP00000388073 ; ENSG00000087586 .

    Organism-specific databases

    HGNCi HGNC:11393. AURKA.
    GenAtlasi Search...

    Phylogenomic databases

    HOGENOMi HOG000233016.
    HOVERGENi HBG108519.

    Enzyme and pathway databases

    SignaLinki A3KFJ1.

    Miscellaneous databases

    NextBioi 35461476.

    Gene expression databases

    ArrayExpressi A3KFJ1.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    2. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    4. Ensembl
      Submitted (JUL-2011) to UniProtKB
      Cited for: IDENTIFICATION.

    Entry informationi

    Entry nameiA3KFJ1_HUMAN
    AccessioniPrimary (citable) accession number: A3KFJ1
    Entry historyi
    Integrated into UniProtKB/TrEMBL: April 3, 2007
    Last sequence update: May 14, 2014
    Last modified: October 1, 2014
    This is version 61 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Caution

    The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data.Imported

    Keywords - Technical termi

    Complete proteome, Reference proteomeImported

    External Data

    Dasty 3