Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P97477

- AURKA_MOUSE

UniProt

P97477 - AURKA_MOUSE

Protein

Aurora kinase A

Gene

Aurka

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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. Required for initial activation of CDK1 at centrosomes. Phosphorylates numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B, DLGP5, HDAC6, KIF2A, LATS2, NDEL1, PARD3, PPP1R2, PLK1, RASSF1, TACC3, p53/TP53 and TPX2. Regulates KIF2A tubulin depolymerase activity. Required for normal axon formation. Plays a role in microtubule remodeling during neurite extension. Important for microtubule formation and/or stabilization. Also acts as a key regulatory component of the p53/TP53 pathway, and particularly the checkpoint-response pathways critical for oncogenic transformation of cells, by phosphorylating and stabilizing p53/TP53. Phosphorylates its own inhibitors, the protein phosphatase type 1 (PP1) isoforms, to inhibit their activity. Necessary for proper cilia disassembly prior to mitosis.4 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Enzyme regulationi

    Activation of CDK1, appears to be an upstream event of AURKA activation. Phosphatase inhibitor-2 (PPP1R2) and TPX2 act also as activators. Inactivated by the G2 checkpoint. Inhibited by GADD45A and p53/TP53, and through dephosphorylation by protein phosphatase type 1 (PP1). MLN8054 is also a potent and selective inhibitor By similarity. Activated during the early phase of cilia disassembly in the presence of PIFO.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei134 – 1341ATP; via amide nitrogenPROSITE-ProRule annotation
    Binding sitei153 – 1531ATPPROSITE-ProRule annotation
    Active sitei247 – 2471Proton acceptorPROSITE-ProRule annotation
    Binding sitei265 – 2651ATPPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi201 – 2044ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. histone serine kinase activity Source: MGI
    3. protein binding Source: UniProtKB
    4. protein kinase activity Source: UniProtKB
    5. ubiquitin protein ligase binding Source: MGI

    GO - Biological processi

    1. anterior/posterior axis specification Source: MGI
    2. centrosome localization Source: MGI
    3. centrosome organization Source: MGI
    4. histone-serine phosphorylation Source: GOC
    5. meiotic nuclear division Source: MGI
    6. meiotic spindle organization Source: MGI
    7. microtubule cytoskeleton organization Source: MGI
    8. mitotic cell cycle Source: MGI
    9. mitotic centrosome separation Source: MGI
    10. mitotic nuclear division Source: MGI
    11. mitotic spindle organization Source: MGI
    12. negative regulation of apoptotic process Source: MGI
    13. negative regulation of protein binding Source: Ensembl
    14. negative regulation of spindle checkpoint Source: MGI
    15. neuron projection extension Source: MGI
    16. positive regulation of oocyte maturation Source: MGI
    17. positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: MGI
    18. protein localization to centrosome Source: MGI
    19. protein phosphorylation Source: MGI
    20. regulation of protein stability Source: Ensembl
    21. spindle assembly involved in female meiosis I Source: MGI
    22. spindle stabilization Source: Ensembl

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Cell cycle, Cell division, Cilium biogenesis/degradation, Mitosis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_196635. Regulation of PLK1 Activity at G2/M Transition.
    REACT_226135. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aurora kinase A (EC:2.7.11.1)
    Alternative name(s):
    Aurora 2
    Aurora family kinase 1
    Aurora/IPL1-related kinase 1
    Short name:
    ARK-1
    Short name:
    Aurora-related kinase 1
    Ipl1- and aurora-related kinase 1
    Serine/threonine-protein kinase 6
    Serine/threonine-protein kinase Ayk1
    Serine/threonine-protein kinase aurora-A
    Gene namesi
    Name:Aurka
    Synonyms:Aik, Airk, Ark1, Aura, Ayk1, Btak, Iak1, Stk15, Stk6
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:894678. Aurka.

    Subcellular locationi

    Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasmcytoskeletonspindle pole
    Note: Localizes on centrosomes in interphase cells and at each spindle pole in mitosis. Associates with both the pericentriolar material (PCM) and centrioles. Colocalized with SIRT2 at centrosome By similarity. Detected at the neurite hillock in developing neurons.By similarity

    GO - Cellular componenti

    1. axon hillock Source: MGI
    2. centrosome Source: MGI
    3. germinal vesicle Source: MGI
    4. meiotic spindle Source: MGI
    5. microtubule organizing center Source: MGI
    6. mitotic spindle Source: MGI
    7. perinuclear region of cytoplasm Source: Ensembl
    8. pronucleus Source: MGI
    9. spindle microtubule Source: Ensembl
    10. spindle pole centrosome Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Microtubule

    Pathology & Biotechi

    Disruption phenotypei

    Death at the blastocyst stage due to mitotic defects and failure of cell proliferation.1 Publication

    Keywords - Diseasei

    Proto-oncogene

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 395395Aurora kinase APRO_0000086693Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei40 – 401PhosphoserineBy similarity
    Modified residuei50 – 501PhosphoserineBy similarity
    Modified residuei278 – 2781PhosphothreonineBy similarity
    Modified residuei279 – 2791PhosphothreonineBy similarity
    Modified residuei333 – 3331Phosphoserine; by PKA and PAKBy similarity

    Post-translational modificationi

    Activated by phosphorylation at Thr-279; this brings about a change in the conformation of the activation segment. Phosphorylation at Thr-279 varies during the cell cycle and is highest during M phase. Autophosphorylated at Thr-279 upon TPX2 binding. Thr-279 can be phosphorylated by several kinases, including PAK and PKA. Protein phosphatase type 1 (PP1) binds AURKA and inhibits its activity by dephosphorylating Thr-279 during mitosis. Phosphorylation at Ser-333 decreases the kinase activity. PPP2CA controls degradation by dephosphorylating Ser-52 at the end of mitosis By similarity.By similarity
    Ubiquitinated by the anaphase-promoting complex (APC), leading to its degradation by the proteasome By similarity. Ubiquitinated by CHFR, leading to its degradation by the proteasome. Ubiquitinated by the E3 ubiquitin-protein ligase complex SCF(FBXL7) during mitosis, leading to its degradation by the proteasome.By similarity2 Publications

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiP97477.
    PRIDEiP97477.

    PTM databases

    PhosphoSiteiP97477.

    Expressioni

    Tissue specificityi

    Detected in embryonic neurons in dorsal root ganglia and brain cortex (at protein level). Highly expressed in testis, in about one third of the seminiferous tubules. Expression is restricted to specific spermatocytes nearing completion of prophase, with levels falling off on transition to elongated spermatids. Highly expressed in the ovary, expression in the oocyte starts around the transition to large growing follicle. Abundant expression is seen in the proliferating granulosa and thecal cells of the growing follicle, and in the young corpus luteum. Very weakly expressed in spleen and intestine.2 Publications

    Developmental stagei

    At 7.5-9.5 dpc expressed evenly all over the embryo. At later stages, expression is mainly restricted to proliferating zones. The highest levels of expression at mid-embryonic development (13.5 dpc) were observed in the liver, lung, kidney and back (trapezius) muscle and all regions in active proliferation.

    Inductioni

    expression is cell cycle regulated and peaks at phase G2/M.1 Publication

    Gene expression databases

    ArrayExpressiP97477.
    BgeeiP97477.
    CleanExiMM_AURKA.
    GenevestigatoriP97477.

    Interactioni

    Subunit structurei

    Interacts with CPEB1, JTB, TACC1, TPX2, PPP2CA, as well as with the protein phosphatase type 1 (PP1) isoforms PPP1CA, PPP1CB and PPP1CC By similarity. Interacts also with its substrates ARHGEF2, BORA, BRCA1, KIF2A, PARD3, and p53/TP53. Interaction with BORA promotes phosphorylation of PLK1. Interacts with GADD45A, competing with its oligomerization By similarity. Interacts with FBXL7 and PIFO. Interacts (via C-terminus) with AUNIP (via C-terminus) By similarity. Identified in a complex with AUNIP and NIN By similarity. Interacts with SIRT2 By similarity. Interacts with FRY; this interaction facilitates AURKA-mediated PLK1 phosphorylation.By similarity5 Publications

    Protein-protein interaction databases

    BioGridi203548. 6 interactions.
    IntActiP97477. 1 interaction.

    Structurei

    Secondary structure

    1
    395
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi121 – 1233
    Beta strandi124 – 1296
    Helixi131 – 1333
    Beta strandi136 – 1438
    Turni144 – 1463
    Beta strandi149 – 1568
    Helixi157 – 1637
    Helixi166 – 17611
    Beta strandi187 – 1926
    Beta strandi194 – 2018
    Helixi209 – 2168
    Helixi221 – 24020
    Helixi250 – 2523
    Beta strandi253 – 2553
    Beta strandi261 – 2633
    Beta strandi270 – 2723
    Helixi284 – 2863
    Helixi289 – 2924
    Helixi299 – 31517
    Helixi325 – 3339
    Helixi345 – 35410
    Helixi359 – 3613
    Helixi365 – 3706
    Helixi372 – 3776

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3D14X-ray1.90A116-381[»]
    3D15X-ray2.30A116-381[»]
    3D2IX-ray2.90A116-381[»]
    3D2KX-ray2.50A116-381[»]
    3DAJX-ray2.00A116-381[»]
    3DJ5X-ray1.80A116-381[»]
    3DJ6X-ray1.70A116-381[»]
    3DJ7X-ray2.80A116-381[»]
    ProteinModelPortaliP97477.
    SMRiP97477. Positions 5-379.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP97477.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini124 – 374251Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni271 – 28414Activation 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

    eggNOGiCOG0515.
    GeneTreeiENSGT00550000074590.
    HOVERGENiHBG108519.
    InParanoidiQ8C3H8.
    KOiK11481.
    OMAiMERSKEN.
    OrthoDBiEOG74FF1F.
    PhylomeDBiP97477.
    TreeFamiTF105331.

    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P97477-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MDRCKENCVS RPVKTTVPFG PKRVLVTEQI PSQNLGSASS GQAQRVLCPS    50
    NSQRVPSQAQ KLGAGQKPAP KQLPAASVPR PVSRLNNPQK NEQPAASGND 100
    SEKEQASLQK TEDTKKRQWT LEDFDIGRPL GKGKFGNVYL ARERQSKFIL 150
    ALKVLFKTQL EKANVEHQLR REVEIQSHLR HPNILRLYGY FHDATRVYLI 200
    LEYAPLGTVY RELQKLSKFD EQRTATYITE LANALSYCHS KRVIHRDIKP 250
    ENLLLGSNGE LKIADFGWSV HAPSSRRTTM CGTLDYLPPE MIEGRMHDEK 300
    VDLWSLGVLC YEFLVGMPPF EAHTYQETYR RISRVEFTFP DFVTEGARDL 350
    ISRLLKHNAS QRLTLAEVLE HPWIKANSSK PPTGHTSKEP TSKSS 395
    Length:395
    Mass (Da):44,772
    Last modified:May 1, 1997 - v1
    Checksum:i26B6B65105A1A812
    GO
    Isoform 2 (identifier: P97477-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MAVEGEPGCCKRIGKAVWRRGDM

    Note: May be less abundant or less stable.

    Show »
    Length:417
    Mass (Da):47,173
    Checksum:iC9FD861C803EF5C5
    GO

    Sequence cautioni

    The sequence BAC39557.1 differs from that shown. Reason: Frameshift at position 382.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti234 – 2341A → T in AAB63205. (PubMed:9245792)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MAVEGEPGCCKRIGKAVWRR GDM in isoform 2. 2 PublicationsVSP_004871

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U80932 mRNA. Translation: AAB62982.1.
    AF007817 mRNA. Translation: AAB63205.1.
    U69106 mRNA. Translation: AAC12682.1.
    AK085861 mRNA. Translation: BAC39557.1. Frameshift.
    BC005425 mRNA. Translation: AAH05425.1.
    BC014711 mRNA. Translation: AAH14711.1.
    CCDSiCCDS17129.1. [P97477-2]
    CCDS71204.1. [P97477-1]
    PIRiJC5975.
    RefSeqiNP_001278114.1. NM_001291185.1. [P97477-1]
    NP_035627.1. NM_011497.4. [P97477-2]
    XP_006499138.1. XM_006499075.1. [P97477-1]
    UniGeneiMm.249363.

    Genome annotation databases

    EnsembliENSMUST00000028997; ENSMUSP00000028997; ENSMUSG00000027496. [P97477-2]
    ENSMUST00000109139; ENSMUSP00000104767; ENSMUSG00000027496. [P97477-1]
    ENSMUST00000109140; ENSMUSP00000104768; ENSMUSG00000027496. [P97477-1]
    GeneIDi20878.
    KEGGimmu:20878.
    UCSCiuc008ocn.1. mouse. [P97477-2]
    uc008oco.1. mouse. [P97477-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U80932 mRNA. Translation: AAB62982.1 .
    AF007817 mRNA. Translation: AAB63205.1 .
    U69106 mRNA. Translation: AAC12682.1 .
    AK085861 mRNA. Translation: BAC39557.1 . Frameshift.
    BC005425 mRNA. Translation: AAH05425.1 .
    BC014711 mRNA. Translation: AAH14711.1 .
    CCDSi CCDS17129.1. [P97477-2 ]
    CCDS71204.1. [P97477-1 ]
    PIRi JC5975.
    RefSeqi NP_001278114.1. NM_001291185.1. [P97477-1 ]
    NP_035627.1. NM_011497.4. [P97477-2 ]
    XP_006499138.1. XM_006499075.1. [P97477-1 ]
    UniGenei Mm.249363.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3D14 X-ray 1.90 A 116-381 [» ]
    3D15 X-ray 2.30 A 116-381 [» ]
    3D2I X-ray 2.90 A 116-381 [» ]
    3D2K X-ray 2.50 A 116-381 [» ]
    3DAJ X-ray 2.00 A 116-381 [» ]
    3DJ5 X-ray 1.80 A 116-381 [» ]
    3DJ6 X-ray 1.70 A 116-381 [» ]
    3DJ7 X-ray 2.80 A 116-381 [» ]
    ProteinModelPortali P97477.
    SMRi P97477. Positions 5-379.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 203548. 6 interactions.
    IntActi P97477. 1 interaction.

    Chemistry

    BindingDBi P97477.
    ChEMBLi CHEMBL2211.

    PTM databases

    PhosphoSitei P97477.

    Proteomic databases

    PaxDbi P97477.
    PRIDEi P97477.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000028997 ; ENSMUSP00000028997 ; ENSMUSG00000027496 . [P97477-2 ]
    ENSMUST00000109139 ; ENSMUSP00000104767 ; ENSMUSG00000027496 . [P97477-1 ]
    ENSMUST00000109140 ; ENSMUSP00000104768 ; ENSMUSG00000027496 . [P97477-1 ]
    GeneIDi 20878.
    KEGGi mmu:20878.
    UCSCi uc008ocn.1. mouse. [P97477-2 ]
    uc008oco.1. mouse. [P97477-1 ]

    Organism-specific databases

    CTDi 6790.
    MGIi MGI:894678. Aurka.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00550000074590.
    HOVERGENi HBG108519.
    InParanoidi Q8C3H8.
    KOi K11481.
    OMAi MERSKEN.
    OrthoDBi EOG74FF1F.
    PhylomeDBi P97477.
    TreeFami TF105331.

    Enzyme and pathway databases

    Reactomei REACT_196635. Regulation of PLK1 Activity at G2/M Transition.
    REACT_226135. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.

    Miscellaneous databases

    EvolutionaryTracei P97477.
    NextBioi 299731.
    PROi P97477.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P97477.
    Bgeei P97477.
    CleanExi MM_AURKA.
    Genevestigatori P97477.

    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. "A novel mammalian, mitotic spindle-associated kinase is related to yeast and fly chromosome segregation regulators."
      Gopalan G., Chan C.S.M., Donovan P.J.
      J. Cell Biol. 138:643-656(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INDUCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, FUNCTION.
      Strain: BALB/c.
      Tissue: Testis.
    2. "ayk1, a novel mammalian gene related to Drosophila aurora centrosome separation kinase, is specifically expressed during meiosis."
      Yanai A., Arama E., Kilfin G., Motro B.
      Oncogene 14:2943-2950(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Testis.
    3. "cDNA cloning, expression, subcellular localization, and chromosomal assignment of mammalian aurora homologues, aurora-related kinase (ARK) 1 and 2."
      Shindo M., Nakano H., Kuroyanagi H., Shirasawa T., Mihara M., Gilbert D.J., Jenkins N.A., Copeland N.G., Yagita H., Okumura K.
      Biochem. Biophys. Res. Commun. 244:285-292(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Strain: BALB/c.
    4. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Heart.
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Mammary gland.
    6. Cited for: UBIQUITINATION BY CHFR.
    7. Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
    8. "An essential role of the aPKC-Aurora A-NDEL1 pathway in neurite elongation by modulation of microtubule dynamics."
      Mori D., Yamada M., Mimori-Kiyosue Y., Shirai Y., Suzuki A., Ohno S., Saya H., Wynshaw-Boris A., Hirotsune S.
      Nat. Cell Biol. 11:1057-1068(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    9. Cited for: FUNCTION, INTERACTION WITH PIFO, ACTIVATION BY PIFO.
    10. "Novel E3 ligase component FBXL7 ubiquitinates and degrades Aurora A, causing mitotic arrest."
      Coon T.A., Glasser J.R., Mallampalli R.K., Chen B.B.
      Cell Cycle 11:721-729(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION, INTERACTION WITH FBXL7.
    11. "Furry protein promotes Aurora A-mediated polo-like kinase 1 activation."
      Ikeda M., Chiba S., Ohashi K., Mizuno K.
      J. Biol. Chem. 287:27670-27681(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FRY.
    12. "Discovery of an Aurora kinase inhibitor through site-specific dynamic combinatorial chemistry."
      Cancilla M.T., He M.M., Viswanathan N., Simmons R.L., Taylor M., Fung A.D., Cao K., Erlanson D.A.
      Bioorg. Med. Chem. Lett. 18:3978-3981(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 116-381 IN COMPLEX WITH SYNTHETIC INHIBITOR.
    13. Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 116-381 IN COMPLEX WITH SYNTHETIC INHIBITOR.

    Entry informationi

    Entry nameiAURKA_MOUSE
    AccessioniPrimary (citable) accession number: P97477
    Secondary accession number(s): O35624, Q8C3H8, Q91YU4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 27, 2003
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 144 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Centrosome amplification can occur when the cycles are uncoupled, and this amplification is associated with cancer and with an increase in the levels of chromosomal instability.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3