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Q91820

- AURAA_XENLA

UniProt

Q91820 - AURAA_XENLA

Protein

Aurora kinase A-A

Gene

aurka-a

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Mitotic serine/threonine kinases that contributes to the regulation of cell cycle progression. Associates with the centrosome and the spindle microtubules during mitosis and plays a critical role in various mitotic events including the establishment of mitotic spindle, centrosome duplication, centrosome separation as well as maturation, chromosomal alignment, spindle assembly checkpoint, and cytokinesis. Phosphorylates numerous target proteins. Important for microtubule formation and/or stabilization.3 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei150 – 1501ATP; via amide nitrogenPROSITE-ProRule annotation
    Binding sitei169 – 1691ATPCurated
    Active sitei263 – 2631Proton acceptorPROSITE-ProRule annotation
    Binding sitei281 – 2811ATPPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi217 – 2204ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. kinesin binding Source: UniProtKB
    3. microtubule binding Source: UniProtKB
    4. protein serine/threonine kinase activity Source: UniProtKB

    GO - Biological processi

    1. peptidyl-serine phosphorylation Source: UniProtKB
    2. protein autophosphorylation Source: UniProtKB
    3. spindle assembly involved in mitosis Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aurora kinase A-A (EC:2.7.11.1)
    Alternative name(s):
    Aurora/IPL1-related kinase 1
    Short name:
    ARK-1
    Short name:
    Aurora-related kinase 1
    Serine/threonine-protein kinase 6-A
    Serine/threonine-protein kinase Eg2-A
    Short name:
    pEg2
    Serine/threonine-protein kinase aurora-A
    p46Eg265
    Gene namesi
    Name:aurka-a
    Synonyms:aurka, eg2, stk6
    OrganismiXenopus laevis (African clawed frog)
    Taxonomic identifieri8355 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

    Organism-specific databases

    XenbaseiXB-GENE-866460. aurka.

    Subcellular locationi

    Cytoplasmcytoskeletonspindle. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome
    Note: Localizes to the spindle pole during mitosis especially from prophase through anaphase. Partially colocalized with gamma tubulin in the centrosome, from S to M phase.

    GO - Cellular componenti

    1. centrosome Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. spindle microtubule Source: UniProtKB
    4. spindle pole Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Microtubule

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi169 – 1691K → R: Lacks kinase activity. Disrupts mitotic spindle assembly. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 407407Aurora kinase A-APRO_0000086695Add
    BLAST

    Post-translational modificationi

    Phosphorylated. Autophosphorylated on a serine residue.

    Keywords - PTMi

    Phosphoprotein

    Expressioni

    Tissue specificityi

    Highly expressed in ovary and testis.1 Publication

    Developmental stagei

    Expressed maternally in oocytes, unfertilized eggs and embryos up to the mid-blastula transition (MBT).1 Publication

    Interactioni

    Subunit structurei

    Interacts with kif2c and kif11.2 Publications

    Protein-protein interaction databases

    BioGridi99261. 1 interaction.
    IntActiQ91820. 2 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ91820.
    SMRiQ91820. Positions 131-394.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini140 – 390251Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni287 – 30014Activation segmentBy similarityAdd
    BLAST

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Aurora subfamily.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    HOVERGENiHBG108519.
    KOiK11481.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q91820-1 [UniParc]FASTAAdd to Basket

    « Hide

    MERAVKENHK PSNVKIFHPM TEGAKRIPVN QPQSTQFRPP GTAVSAQRIL    50
    GPSNVPQRVL AQAQKPILSS QKPTTQIPLR PATQGHQSSK PQGPNENRNP 100
    QQTSHSSTPN VEKKGSTDQG KTSAVPKEEG KKKQWCLEDF EIGRPLGKGK 150
    FGNVYLARER ESKFILALKV LFKSQLEKAG VEHQLRREVE IQSHLRHPNI 200
    LRLYGYFHDA SRVYLILDYA PGGELFRELQ KCTRFDDQRS AMYIKQLAEA 250
    LLYCHSKKVI HRDIKPENLL LGSNGELKIA DFGWSVHAPS SRRTTLCGTL 300
    DYLPPEMIEG RMHDETVDLW SLGVLCYEFL VGKPPFETDT HQETYRRISK 350
    VEFQYPPYVS EEARDLVSKL LKHNPNHRLP LKGVLEHPWI IKNSQLKKKD 400
    EPLPGAQ 407
    Length:407
    Mass (Da):46,372
    Last modified:November 1, 1996 - v1
    Checksum:iDE1628A2C6D11277
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z17207 mRNA. Translation: CAA78915.1.
    BC072133 mRNA. Translation: AAH72133.1.
    PIRiS52243.
    RefSeqiNP_001081565.1. NM_001088096.1.
    UniGeneiXl.124.

    Genome annotation databases

    GeneIDi397925.
    KEGGixla:397925.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z17207 mRNA. Translation: CAA78915.1 .
    BC072133 mRNA. Translation: AAH72133.1 .
    PIRi S52243.
    RefSeqi NP_001081565.1. NM_001088096.1.
    UniGenei Xl.124.

    3D structure databases

    ProteinModelPortali Q91820.
    SMRi Q91820. Positions 131-394.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 99261. 1 interaction.
    IntActi Q91820. 2 interactions.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 397925.
    KEGGi xla:397925.

    Organism-specific databases

    CTDi 6790.
    Xenbasei XB-GENE-866460. aurka.

    Phylogenomic databases

    HOVERGENi HBG108519.
    KOi K11481.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The Xenopus protein kinase pEg2 associates with the centrosome in a cell cycle-dependent manner, binds to the spindle microtubules and is involved in bipolar mitotic spindle assembly."
      Roghi C., Giet R., Uzbekov R., Morin N., Chartrain I., Le Guellec R., Couturier A., Doree M., Phillippe M., Prigent C.
      J. Cell Sci. 111:557-572(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, MUTAGENESIS OF LYS-169.
      Tissue: Egg.
    2. NIH - Xenopus Gene Collection (XGC) project
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Ovary.
    3. "The Xenopus laevis aurora-related protein kinase pEg2 associates with and phosphorylates the kinesin-related protein XlEg5."
      Giet R., Uzbekov R., Cubizolles F., Le Guellec K., Prigent C.
      J. Biol. Chem. 274:15005-15013(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH KIF11, SUBCELLULAR LOCATION.
    4. "Aurora A phosphorylates MCAK to control ran-dependent spindle bipolarity."
      Zhang X., Ems-McClung S.C., Walczak C.E.
      Mol. Biol. Cell 19:2752-2765(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH KIF2C.

    Entry informationi

    Entry nameiAURAA_XENLA
    AccessioniPrimary (citable) accession number: Q91820
    Secondary accession number(s): Q6INY9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 27, 2003
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 100 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3