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O14965

- AURKA_HUMAN

UniProt

O14965 - AURKA_HUMAN

Protein

Aurora kinase A

Gene

AURKA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 168 (01 Oct 2014)
      Sequence version 2 (27 Jan 2003)
      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. 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.21 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.4 Publications

    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. Activated during the early phase of cilia disassembly in the presence of PIFO.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei143 – 1431ATP; via amide nitrogen
    Binding sitei162 – 1621ATP
    Active sitei256 – 2561Proton acceptor1 PublicationPROSITE-ProRule annotation
    Binding sitei274 – 2741ATP

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi210 – 2134ATP

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. protein binding Source: UniProtKB
    3. protein kinase activity Source: UniProtKB
    4. protein kinase binding Source: UniProtKB
    5. protein serine/threonine/tyrosine kinase activity Source: UniProtKB
    6. protein serine/threonine kinase activity Source: Reactome

    GO - Biological processi

    1. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
    2. cell cycle Source: UniProtKB
    3. cell projection organization Source: UniProtKB-KW
    4. G2/M transition of mitotic cell cycle Source: Reactome
    5. mitotic cell cycle Source: Reactome
    6. mitotic nuclear division Source: ProtInc
    7. negative regulation of protein binding Source: UniProtKB
    8. phosphatidylinositol-mediated signaling Source: UniProtKB
    9. positive regulation of mitosis Source: UniProtKB
    10. protein autophosphorylation Source: UniProtKB
    11. protein phosphorylation Source: UniProtKB
    12. regulation of centrosome cycle Source: UniProtKB
    13. regulation of protein stability Source: UniProtKB
    14. spindle organization Source: UniProtKB
    15. spindle stabilization Source: UniProtKB

    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_160315. Regulation of PLK1 Activity at G2/M Transition.
    REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
    SignaLinkiO14965.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aurora kinase A (EC:2.7.11.1)
    Alternative name(s):
    Aurora 2
    Aurora/IPL1-related kinase 1
    Short name:
    ARK-1
    Short name:
    Aurora-related kinase 1
    Short name:
    hARK1
    Breast tumor-amplified kinase
    Serine/threonine-protein kinase 15
    Serine/threonine-protein kinase 6
    Serine/threonine-protein kinase aurora-A
    Gene namesi
    Name:AURKA
    Synonyms:AIK, AIRK1, ARK1, AURA, AYK1, BTAK, IAK1, STK15, STK6
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:11393. AURKA.

    Subcellular locationi

    Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasmcytoskeletonspindle pole
    Note: Detected at the neurite hillock in developing neurons By similarity. Localizes at the centrosome in mitotic cells from early prophase until telophase, but also localizes to the spindle pole MTs from prophase to anaphase. Colocalized with SIRT2 at centrosome. Moves to the midbody during both telophase and cytokinesis. Associates with both the pericentriolar material (PCM) and centrioles.By similarity

    GO - Cellular componenti

    1. centrosome Source: UniProtKB
    2. cytosol Source: Reactome
    3. microtubule Source: UniProtKB-KW
    4. microtubule cytoskeleton Source: BHF-UCL
    5. midbody Source: UniProtKB
    6. nucleus Source: BHF-UCL
    7. perinuclear region of cytoplasm Source: BHF-UCL
    8. spindle Source: UniProtKB
    9. spindle pole centrosome Source: BHF-UCL

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Microtubule

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi162 – 1621K → R: Loss of kinase activity. 2 Publications
    Mutagenesisi165 – 1651F → A: Decreases the interaction with phosphatase type 1 isoforms. 1 Publication
    Mutagenesisi198 – 1981G → N: Reduces interaction with TPX2. Reduces kinase activity tenfold. Promotes interaction with the AURKB binding partners INCENP and BIRC5 that are normally not bound by AURKA. 1 Publication
    Mutagenesisi205 – 2051R → A: Reduces ubiquitination and proteasomal degradation. 1 Publication
    Mutagenesisi274 – 2741D → N: Abolishes autophosphorylation. 1 Publication
    Mutagenesisi287 – 2871T → A: No direct effect on catalytic activity. 1 Publication
    Mutagenesisi287 – 2871T → E: Enhances interaction with TPX2. 1 Publication
    Mutagenesisi288 – 2881T → D: Mimics phosphorylation state and increases kinase activity. 1 Publication
    Mutagenesisi346 – 3461F → A: Decreases the interaction with phosphatase type 1 isoforms. 1 Publication

    Keywords - Diseasei

    Proto-oncogene

    Organism-specific databases

    PharmGKBiPA36201.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 403403Aurora kinase APRO_0000086692Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei41 – 411Phosphoserine1 Publication
    Modified residuei51 – 511Phosphoserine1 Publication
    Modified residuei287 – 2871Phosphothreonine2 Publications
    Modified residuei288 – 2881Phosphothreonine7 Publications
    Modified residuei342 – 3421Phosphoserine; by PKA and PAK1 Publication

    Post-translational modificationi

    Activated by phosphorylation at Thr-288; this brings about a change in the conformation of the activation segment. Phosphorylation at Thr-288 varies during the cell cycle and is highest during M phase. Autophosphorylated at Thr-288 upon TPX2 binding. Thr-288 can be phosphorylated by several kinases, including PAK and PKA. Protein phosphatase type 1 (PP1) binds AURKA and inhibits its activity by dephosphorylating Thr-288 during mitosis. Phosphorylation at Ser-342 decreases the kinase activity. PPP2CA controls degradation by dephosphorylating Ser-51 at the end of mitosis.11 Publications
    Ubiquitinated by the E3 ubiquitin-protein ligase complex SCF(FBXL7) during mitosis, leading to its degradation by the proteasome. Ubiquitinated by CHFR, leading to its degradation by the proteasome By similarity. Ubiquitinated by the anaphase-promoting complex (APC), leading to its degradation by the proteasome.By similarity2 Publications

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiO14965.
    PaxDbiO14965.
    PRIDEiO14965.

    PTM databases

    PhosphoSiteiO14965.

    Expressioni

    Tissue specificityi

    Highly expressed in testis and weakly in skeletal muscle, thymus and spleen. Also highly expressed in colon, ovarian, prostate, neuroblastoma, breast and cervical cancer cell lines.

    Inductioni

    Expression is cell-cycle regulated, low in G1/S, accumulates during G2/M, and decreases rapidly after.5 Publications

    Gene expression databases

    ArrayExpressiO14965.
    BgeeiO14965.
    CleanExiHS_AURKA.
    GenevestigatoriO14965.

    Organism-specific databases

    HPAiCAB001454.
    HPA002636.

    Interactioni

    Subunit structurei

    Interacts with FBXL7 By similarity. Interacts with CPEB1, JTB, TACC1, TPX2, PPP2CA, as well as with the protein phosphatase type 1 (PP1) isoforms PPP1CA, PPP1CB and PPP1CC. Interacts also with its substrates ARHGEF2, BORA, BRCA1, KIF2A, PARD3, and p53/TP53. Interaction with BORA promotes phosphorylation of PLK1. Interacts with PIFO. Interacts with GADD45A, competing with its oligomerization. Interacts (via C-terminus) with AUNIP (via C-terminus). Identified in a complex with AUNIP and NIN. Interacts with FRY; this interaction facilitates AURKA-mediated PLK1 phosphorylation. Interacts with SIRT2.By similarity26 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AURKAIP1Q9NWT82EBI-448680,EBI-448665
    HNRNPKP619782EBI-448680,EBI-304185
    IKQ131233EBI-448680,EBI-713456
    MYCNP041987EBI-448680,EBI-878369
    NPM1P067483EBI-448680,EBI-78579
    Sirt2Q8VDQ85EBI-448680,EBI-911012From a different organism.
    TP73O1535011EBI-448680,EBI-389606

    Protein-protein interaction databases

    BioGridi112666. 86 interactions.
    DIPiDIP-33068N.
    IntActiO14965. 28 interactions.
    MINTiMINT-254096.
    STRINGi9606.ENSP00000216911.

    Structurei

    Secondary structure

    1
    403
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi130 – 1323
    Beta strandi133 – 1419
    Beta strandi143 – 15210
    Turni153 – 1553
    Beta strandi158 – 1658
    Helixi166 – 1727
    Helixi175 – 18713
    Beta strandi191 – 1933
    Beta strandi196 – 2016
    Beta strandi203 – 2108
    Beta strandi214 – 2174
    Helixi218 – 2258
    Helixi230 – 24920
    Helixi259 – 2613
    Beta strandi262 – 2643
    Beta strandi266 – 2683
    Beta strandi270 – 2723
    Helixi275 – 2773
    Beta strandi279 – 2835
    Beta strandi288 – 2925
    Helixi293 – 2953
    Helixi298 – 3014
    Turni302 – 3043
    Helixi309 – 32416
    Helixi334 – 34310
    Beta strandi350 – 3523
    Helixi354 – 36310
    Helixi368 – 3703
    Helixi374 – 3785
    Helixi381 – 3866

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1MQ4X-ray1.90A125-391[»]
    1MUOX-ray2.90A107-403[»]
    1OL5X-ray2.50A122-403[»]
    1OL6X-ray3.00A122-403[»]
    1OL7X-ray2.75A122-403[»]
    2BMCX-ray2.60A/B/C/D/E/F100-403[»]
    2C6DX-ray2.20A124-398[»]
    2C6EX-ray2.10A/B123-401[»]
    2DWBX-ray2.50A122-403[»]
    2J4ZX-ray2.00A/B100-403[»]
    2J50X-ray3.00A/B126-403[»]
    2NP8X-ray2.25A125-391[»]
    2W1CX-ray3.24A122-389[»]
    2W1DX-ray2.97A122-389[»]
    2W1EX-ray2.93A122-389[»]
    2W1FX-ray2.85A122-389[»]
    2W1GX-ray2.71A122-389[»]
    2WQEX-ray2.50A127-388[»]
    2WTVX-ray2.40A/B/C/D122-403[»]
    2WTWX-ray3.30A122-403[»]
    2X6DX-ray2.80A122-403[»]
    2X6EX-ray3.35A122-403[»]
    2X81X-ray2.91A126-391[»]
    2XNEX-ray2.80A122-392[»]
    2XNGX-ray2.60A122-403[»]
    2XRUX-ray2.90A126-403[»]
    3COHX-ray2.70A/B124-391[»]
    3E5AX-ray2.30A125-391[»]
    3EFWX-ray2.29A/B125-391[»]
    3FDNX-ray1.90A123-401[»]
    3H0YX-ray2.50A124-391[»]
    3H0ZX-ray2.92A/B/C124-391[»]
    3H10X-ray2.20A/B/D124-391[»]
    3HA6X-ray2.36A125-391[»]
    3K5UX-ray2.35A123-401[»]
    3LAUX-ray2.10A125-399[»]
    3M11X-ray2.75A123-401[»]
    3MYGX-ray2.40A125-391[»]
    3NRMX-ray3.05A126-403[»]
    3O50X-ray2.00A/B125-391[»]
    3O51X-ray3.20A125-391[»]
    3P9JX-ray2.80A125-391[»]
    3QBNX-ray3.50A124-403[»]
    3R21X-ray2.90A126-391[»]
    3R22X-ray2.90A126-391[»]
    3UNZX-ray2.80A/B123-401[»]
    3UO4X-ray2.45A123-401[»]
    3UO5X-ray2.70A123-401[»]
    3UO6X-ray2.80A/B123-401[»]
    3UODX-ray2.50A123-401[»]
    3UOHX-ray2.80A/B123-401[»]
    3UOJX-ray2.90A/B123-401[»]
    3UOKX-ray2.95A/B123-401[»]
    3UOLX-ray2.40A/B123-401[»]
    3UP2X-ray2.30A123-401[»]
    3UP7X-ray3.05A123-401[»]
    3VAPX-ray2.66A125-391[»]
    3W10X-ray2.70A126-403[»]
    3W16X-ray2.80A126-403[»]
    3W18X-ray2.50A/B126-403[»]
    3W2CX-ray2.45A/C/E/G128-388[»]
    4B0GX-ray2.50A122-403[»]
    4BN1X-ray2.50A122-403[»]
    4BYIX-ray2.60A122-403[»]
    4BYJX-ray2.75A122-403[»]
    4C3PX-ray2.69A/D122-403[»]
    4C3RX-ray2.79A122-403[»]
    4DEAX-ray2.45A123-401[»]
    4DEBX-ray3.05A123-401[»]
    4DEDX-ray3.05A123-401[»]
    4DEEX-ray2.30A123-401[»]
    4DHFX-ray2.80A/B126-391[»]
    4JAIX-ray3.20A122-396[»]
    4JAJX-ray2.70A122-396[»]
    4JBOX-ray2.49A123-401[»]
    4JBPX-ray2.45A123-401[»]
    4JBQX-ray2.30A123-401[»]
    ProteinModelPortaliO14965.
    SMRiO14965. Positions 76-394.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO14965.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini133 – 383251Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni280 – 29314Activation segmentAdd
    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.
    HOVERGENiHBG108519.
    InParanoidiO14965.
    KOiK11481.
    OrthoDBiEOG74FF1F.
    PhylomeDBiO14965.
    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]

    Sequencei

    Sequence statusi: Complete.

    O14965-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDRSKENCIS GPVKATAPVG GPKRVLVTQQ FPCQNPLPVN SGQAQRVLCP    50
    SNSSQRVPLQ AQKLVSSHKP VQNQKQKQLQ ATSVPHPVSR PLNNTQKSKQ 100
    PLPSAPENNP EEELASKQKN EESKKRQWAL EDFEIGRPLG KGKFGNVYLA 150
    REKQSKFILA LKVLFKAQLE KAGVEHQLRR EVEIQSHLRH PNILRLYGYF 200
    HDATRVYLIL EYAPLGTVYR ELQKLSKFDE QRTATYITEL ANALSYCHSK 250
    RVIHRDIKPE NLLLGSAGEL KIADFGWSVH APSSRRTTLC GTLDYLPPEM 300
    IEGRMHDEKV DLWSLGVLCY EFLVGKPPFE ANTYQETYKR ISRVEFTFPD 350
    FVTEGARDLI SRLLKHNPSQ RPMLREVLEH PWITANSSKP SNCQNKESAS 400
    KQS 403
    Length:403
    Mass (Da):45,809
    Last modified:January 27, 2003 - v2
    Checksum:i125F3594834CD157
    GO

    Sequence cautioni

    The sequence BAA23592.1 differs from that shown. Reason: Frameshift at positions 105, 125, 129, 235 and 241.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti11 – 111G → R.
    Corresponds to variant rs6069717 [ dbSNP | Ensembl ].
    VAR_030840
    Natural varianti31 – 311F → I.5 Publications
    Corresponds to variant rs2273535 [ dbSNP | Ensembl ].
    VAR_030841
    Natural varianti50 – 501P → L.1 Publication
    Corresponds to variant rs34572020 [ dbSNP | Ensembl ].
    VAR_041127
    Natural varianti57 – 571V → I.4 Publications
    Corresponds to variant rs1047972 [ dbSNP | Ensembl ].
    VAR_030842
    Natural varianti104 – 1041S → L.
    Corresponds to variant rs2230743 [ dbSNP | Ensembl ].
    VAR_061745
    Natural varianti155 – 1551S → R in a colorectal adenocarcinoma sample; somatic mutation; reduces interaction with TPX2. 1 Publication
    VAR_041128
    Natural varianti174 – 1741V → M in a metastatic melanoma sample; somatic mutation; constitutively enhanced kinase activity. 1 Publication
    VAR_041129
    Natural varianti373 – 3731M → V.1 Publication
    Corresponds to variant rs33923703 [ dbSNP | Ensembl ].
    VAR_041130

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D84212 mRNA. Translation: BAA23592.1. Frameshift.
    AF008551 mRNA. Translation: AAC12708.1.
    AF011467 Genomic DNA. Translation: AAC23448.1.
    AF011468 mRNA. Translation: AAC63902.1.
    AF195947
    , AF195942, AF195943, AF195944, AF195945, AF195946 Genomic DNA. Translation: AAF29508.1.
    AL121914 Genomic DNA. Translation: CAC12717.1.
    CH471077 Genomic DNA. Translation: EAW75550.1.
    CH471077 Genomic DNA. Translation: EAW75551.1.
    CH471077 Genomic DNA. Translation: EAW75552.1.
    CH471077 Genomic DNA. Translation: EAW75553.1.
    CH471077 Genomic DNA. Translation: EAW75554.1.
    CH471077 Genomic DNA. Translation: EAW75555.1.
    CH471077 Genomic DNA. Translation: EAW75556.1.
    CH471077 Genomic DNA. Translation: EAW75557.1.
    CH471077 Genomic DNA. Translation: EAW75558.1.
    CH471077 Genomic DNA. Translation: EAW75559.1.
    CH471077 Genomic DNA. Translation: EAW75561.1.
    CH471077 Genomic DNA. Translation: EAW75562.1.
    BC001280 mRNA. Translation: AAH01280.1.
    BC002499 mRNA. Translation: AAH02499.1.
    BC006423 mRNA. Translation: AAH06423.1.
    BC027464 mRNA. Translation: AAH27464.1.
    CCDSiCCDS13451.1.
    PIRiJC5974.
    RefSeqiNP_003591.2. NM_003600.2.
    NP_940835.1. NM_198433.1.
    NP_940836.1. NM_198434.1.
    NP_940837.1. NM_198435.1.
    NP_940838.1. NM_198436.1.
    NP_940839.1. NM_198437.1.
    XP_005260591.1. XM_005260534.1.
    XP_006723935.1. XM_006723872.1.
    UniGeneiHs.250822.

    Genome annotation databases

    EnsembliENST00000312783; ENSP00000321591; ENSG00000087586.
    ENST00000347343; ENSP00000216911; ENSG00000087586.
    ENST00000371356; ENSP00000360407; ENSG00000087586.
    ENST00000395911; ENSP00000379247; ENSG00000087586.
    ENST00000395913; ENSP00000379249; ENSG00000087586.
    ENST00000395914; ENSP00000379250; ENSG00000087586.
    ENST00000395915; ENSP00000379251; ENSG00000087586.
    GeneIDi6790.
    KEGGihsa:6790.
    UCSCiuc002xxd.1. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D84212 mRNA. Translation: BAA23592.1 . Frameshift.
    AF008551 mRNA. Translation: AAC12708.1 .
    AF011467 Genomic DNA. Translation: AAC23448.1 .
    AF011468 mRNA. Translation: AAC63902.1 .
    AF195947
    , AF195942 , AF195943 , AF195944 , AF195945 , AF195946 Genomic DNA. Translation: AAF29508.1 .
    AL121914 Genomic DNA. Translation: CAC12717.1 .
    CH471077 Genomic DNA. Translation: EAW75550.1 .
    CH471077 Genomic DNA. Translation: EAW75551.1 .
    CH471077 Genomic DNA. Translation: EAW75552.1 .
    CH471077 Genomic DNA. Translation: EAW75553.1 .
    CH471077 Genomic DNA. Translation: EAW75554.1 .
    CH471077 Genomic DNA. Translation: EAW75555.1 .
    CH471077 Genomic DNA. Translation: EAW75556.1 .
    CH471077 Genomic DNA. Translation: EAW75557.1 .
    CH471077 Genomic DNA. Translation: EAW75558.1 .
    CH471077 Genomic DNA. Translation: EAW75559.1 .
    CH471077 Genomic DNA. Translation: EAW75561.1 .
    CH471077 Genomic DNA. Translation: EAW75562.1 .
    BC001280 mRNA. Translation: AAH01280.1 .
    BC002499 mRNA. Translation: AAH02499.1 .
    BC006423 mRNA. Translation: AAH06423.1 .
    BC027464 mRNA. Translation: AAH27464.1 .
    CCDSi CCDS13451.1.
    PIRi JC5974.
    RefSeqi NP_003591.2. NM_003600.2.
    NP_940835.1. NM_198433.1.
    NP_940836.1. NM_198434.1.
    NP_940837.1. NM_198435.1.
    NP_940838.1. NM_198436.1.
    NP_940839.1. NM_198437.1.
    XP_005260591.1. XM_005260534.1.
    XP_006723935.1. XM_006723872.1.
    UniGenei Hs.250822.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1MQ4 X-ray 1.90 A 125-391 [» ]
    1MUO X-ray 2.90 A 107-403 [» ]
    1OL5 X-ray 2.50 A 122-403 [» ]
    1OL6 X-ray 3.00 A 122-403 [» ]
    1OL7 X-ray 2.75 A 122-403 [» ]
    2BMC X-ray 2.60 A/B/C/D/E/F 100-403 [» ]
    2C6D X-ray 2.20 A 124-398 [» ]
    2C6E X-ray 2.10 A/B 123-401 [» ]
    2DWB X-ray 2.50 A 122-403 [» ]
    2J4Z X-ray 2.00 A/B 100-403 [» ]
    2J50 X-ray 3.00 A/B 126-403 [» ]
    2NP8 X-ray 2.25 A 125-391 [» ]
    2W1C X-ray 3.24 A 122-389 [» ]
    2W1D X-ray 2.97 A 122-389 [» ]
    2W1E X-ray 2.93 A 122-389 [» ]
    2W1F X-ray 2.85 A 122-389 [» ]
    2W1G X-ray 2.71 A 122-389 [» ]
    2WQE X-ray 2.50 A 127-388 [» ]
    2WTV X-ray 2.40 A/B/C/D 122-403 [» ]
    2WTW X-ray 3.30 A 122-403 [» ]
    2X6D X-ray 2.80 A 122-403 [» ]
    2X6E X-ray 3.35 A 122-403 [» ]
    2X81 X-ray 2.91 A 126-391 [» ]
    2XNE X-ray 2.80 A 122-392 [» ]
    2XNG X-ray 2.60 A 122-403 [» ]
    2XRU X-ray 2.90 A 126-403 [» ]
    3COH X-ray 2.70 A/B 124-391 [» ]
    3E5A X-ray 2.30 A 125-391 [» ]
    3EFW X-ray 2.29 A/B 125-391 [» ]
    3FDN X-ray 1.90 A 123-401 [» ]
    3H0Y X-ray 2.50 A 124-391 [» ]
    3H0Z X-ray 2.92 A/B/C 124-391 [» ]
    3H10 X-ray 2.20 A/B/D 124-391 [» ]
    3HA6 X-ray 2.36 A 125-391 [» ]
    3K5U X-ray 2.35 A 123-401 [» ]
    3LAU X-ray 2.10 A 125-399 [» ]
    3M11 X-ray 2.75 A 123-401 [» ]
    3MYG X-ray 2.40 A 125-391 [» ]
    3NRM X-ray 3.05 A 126-403 [» ]
    3O50 X-ray 2.00 A/B 125-391 [» ]
    3O51 X-ray 3.20 A 125-391 [» ]
    3P9J X-ray 2.80 A 125-391 [» ]
    3QBN X-ray 3.50 A 124-403 [» ]
    3R21 X-ray 2.90 A 126-391 [» ]
    3R22 X-ray 2.90 A 126-391 [» ]
    3UNZ X-ray 2.80 A/B 123-401 [» ]
    3UO4 X-ray 2.45 A 123-401 [» ]
    3UO5 X-ray 2.70 A 123-401 [» ]
    3UO6 X-ray 2.80 A/B 123-401 [» ]
    3UOD X-ray 2.50 A 123-401 [» ]
    3UOH X-ray 2.80 A/B 123-401 [» ]
    3UOJ X-ray 2.90 A/B 123-401 [» ]
    3UOK X-ray 2.95 A/B 123-401 [» ]
    3UOL X-ray 2.40 A/B 123-401 [» ]
    3UP2 X-ray 2.30 A 123-401 [» ]
    3UP7 X-ray 3.05 A 123-401 [» ]
    3VAP X-ray 2.66 A 125-391 [» ]
    3W10 X-ray 2.70 A 126-403 [» ]
    3W16 X-ray 2.80 A 126-403 [» ]
    3W18 X-ray 2.50 A/B 126-403 [» ]
    3W2C X-ray 2.45 A/C/E/G 128-388 [» ]
    4B0G X-ray 2.50 A 122-403 [» ]
    4BN1 X-ray 2.50 A 122-403 [» ]
    4BYI X-ray 2.60 A 122-403 [» ]
    4BYJ X-ray 2.75 A 122-403 [» ]
    4C3P X-ray 2.69 A/D 122-403 [» ]
    4C3R X-ray 2.79 A 122-403 [» ]
    4DEA X-ray 2.45 A 123-401 [» ]
    4DEB X-ray 3.05 A 123-401 [» ]
    4DED X-ray 3.05 A 123-401 [» ]
    4DEE X-ray 2.30 A 123-401 [» ]
    4DHF X-ray 2.80 A/B 126-391 [» ]
    4JAI X-ray 3.20 A 122-396 [» ]
    4JAJ X-ray 2.70 A 122-396 [» ]
    4JBO X-ray 2.49 A 123-401 [» ]
    4JBP X-ray 2.45 A 123-401 [» ]
    4JBQ X-ray 2.30 A 123-401 [» ]
    ProteinModelPortali O14965.
    SMRi O14965. Positions 76-394.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112666. 86 interactions.
    DIPi DIP-33068N.
    IntActi O14965. 28 interactions.
    MINTi MINT-254096.
    STRINGi 9606.ENSP00000216911.

    Chemistry

    BindingDBi O14965.
    ChEMBLi CHEMBL4722.
    GuidetoPHARMACOLOGYi 1936.

    PTM databases

    PhosphoSitei O14965.

    Proteomic databases

    MaxQBi O14965.
    PaxDbi O14965.
    PRIDEi O14965.

    Protocols and materials databases

    DNASUi 6790.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000312783 ; ENSP00000321591 ; ENSG00000087586 .
    ENST00000347343 ; ENSP00000216911 ; ENSG00000087586 .
    ENST00000371356 ; ENSP00000360407 ; ENSG00000087586 .
    ENST00000395911 ; ENSP00000379247 ; ENSG00000087586 .
    ENST00000395913 ; ENSP00000379249 ; ENSG00000087586 .
    ENST00000395914 ; ENSP00000379250 ; ENSG00000087586 .
    ENST00000395915 ; ENSP00000379251 ; ENSG00000087586 .
    GeneIDi 6790.
    KEGGi hsa:6790.
    UCSCi uc002xxd.1. human.

    Organism-specific databases

    CTDi 6790.
    GeneCardsi GC20M054944.
    H-InvDB HIX0015930.
    HGNCi HGNC:11393. AURKA.
    HPAi CAB001454.
    HPA002636.
    MIMi 603072. gene.
    neXtProti NX_O14965.
    PharmGKBi PA36201.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOVERGENi HBG108519.
    InParanoidi O14965.
    KOi K11481.
    OrthoDBi EOG74FF1F.
    PhylomeDBi O14965.
    TreeFami TF105331.

    Enzyme and pathway databases

    Reactomei REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
    REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
    SignaLinki O14965.

    Miscellaneous databases

    EvolutionaryTracei O14965.
    GeneWikii Aurora_A_kinase.
    GenomeRNAii 6790.
    NextBioi 26512.
    PROi O14965.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O14965.
    Bgeei O14965.
    CleanExi HS_AURKA.
    Genevestigatori O14965.

    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. "Cell cycle-dependent expression and spindle pole localization of a novel human protein kinase, Aik, related to Aurora of Drosophila and yeast Ipl1."
      Kimura M., Kotani S., Hattori T., Sumi N., Yoshioka T., Todokoro K., Okano Y.
      J. Biol. Chem. 272:13766-13771(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, SUBCELLULAR LOCATION.
      Tissue: Blood.
    2. "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], VARIANT ILE-57.
    3. "Tumour amplified kinase STK15/BTAK induces centrosome amplification, aneuploidy and transformation."
      Zhou H., Kuang J., Zhong L., Kuo W.-L., Gray J.W., Sahin A., Brinkley B.R., Sen S.
      Nat. Genet. 20:189-193(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ILE-31.
      Tissue: Mammary gland.
    4. "Mutational analysis of the STK15 gene in human tumors."
      Wang L., Thibodeau S.N.
      Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "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].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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].
      Tissue: Cervix, Colon, Kidney and Muscle.
    8. "A homologue of Drosophila aurora kinase is oncogenic and amplified in human colorectal cancers."
      Bischoff J.R., Anderson L., Zhu Y., Mossie K., Ng L., Souza B., Schryver B., Flanagan P., Clairvoyant F., Ginther C., Chan C.S., Novotny M., Slamon D.J., Plowman G.D.
      EMBO J. 17:3052-3065(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION, FUNCTION, SUBCELLULAR LOCATION.
    9. "Degradation of human Aurora2 protein kinase by the anaphase-promoting complex-ubiquitin-proteasome pathway."
      Honda K., Mihara H., Kato Y., Yamaguchi A., Tanaka H., Yasuda H., Furukawa K., Urano T.
      Oncogene 19:2812-2819(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION, PROTEASOMAL DEGRADATION, MUTAGENESIS OF ARG-205.
    10. "The mitotic serine/threonine kinase Aurora2/AIK is regulated by phosphorylation and degradation."
      Walter A.O., Seghezzi W., Korver W., Sheung J., Lees E.
      Oncogene 19:4906-4916(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT THR-288, MUTAGENESIS OF THR-288, UBIQUITINATION, ENZYME REGULATION.
    11. "Interaction and feedback regulation between STK15/BTAK/Aurora-A kinase and protein phosphatase 1 through mitotic cell division cycle."
      Katayama H., Zhou H., Li Q., Tatsuka M., Sen S.
      J. Biol. Chem. 276:46219-46224(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PPP1CA; PPP1CB AND PPP1CC, MUTAGENESIS OF PHE-165 AND PHE-346, PHOSPHORYLATION.
    12. "Molecular dynamics of Aurora-A kinase in living mitotic cells simultaneously visualized with histone H3 and nuclear membrane protein importinalpha."
      Sugimoto K., Urano T., Zushi H., Inoue K., Tasaka H., Tachibana M., Dotsu M.
      Cell Struct. Funct. 27:457-467(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    13. Cited for: FUNCTION, INDUCTION, PHOSPHORYLATION, ENZYME REGULATION.
    14. "Cell-cycle-dependent regulation of human aurora A transcription is mediated by periodic repression of E4TF1."
      Tanaka M., Ueda A., Kanamori H., Ideguchi H., Yang J., Kitajima S., Ishigatsubo Y.
      J. Biol. Chem. 277:10719-10726(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    15. "Aurora-A and an interacting activator, the LIM protein Ajuba, are required for mitotic commitment in human cells."
      Hirota T., Kunitoku N., Sasayama T., Marumoto T., Zhang D., Nitta M., Hatakeyama K., Saya H.
      Cell 114:585-598(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-288.
    16. "Aurora-A kinase maintains the fidelity of early and late mitotic events in HeLa cells."
      Marumoto T., Honda S., Hara T., Nitta M., Hirota T., Kohmura E., Saya H.
      J. Biol. Chem. 278:51786-51795(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    17. Cited for: INTERACTION WITH TACC1.
    18. "The centrosomal protein Lats2 is a phosphorylation target of Aurora-A kinase."
      Toji S., Yabuta N., Hosomi T., Nishihara S., Kobayashi T., Suzuki S., Tamai K., Nojima H.
      Genes Cells 9:383-397(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    19. Cited for: FUNCTION, INTERACTION WITH BRCA1, PHOSPHORYLATION AT THR-288, MUTAGENESIS OF LYS-162.
    20. Cited for: FUNCTION.
    21. "Phosphorylation by aurora kinase A induces Mdm2-mediated destabilization and inhibition of p53."
      Katayama H., Sasai K., Kawai H., Yuan Z.M., Bondaruk J., Suzuki F., Fujii S., Arlinghaus R.B., Czerniak B.A., Sen S.
      Nat. Genet. 36:55-62(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF LYS-162, INTERACTION WITH TP53.
    22. "Over-expression of Aurora-A targets cytoplasmic polyadenylation element binding protein and promotes mRNA polyadenylation of Cdk1 and cyclin B1."
      Sasayama T., Marumoto T., Kunitoku N., Zhang D., Tamaki N., Kohmura E., Saya H., Hirota T.
      Genes Cells 10:627-638(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CPEB1.
    23. "The GIT-associated kinase PAK targets to the centrosome and regulates Aurora-A."
      Zhao Z.S., Lim J.P., Ng Y.W., Lim L., Manser E.
      Mol. Cell 20:237-249(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-288 AND SER-342.
    24. "Phosphorylation and stabilization of HURP by Aurora-A: implication of HURP as a transforming target of Aurora-A."
      Yu C.T., Hsu J.M., Lee Y.C., Tsou A.P., Chou C.K., Huang C.Y.
      Mol. Cell. Biol. 25:5789-5800(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION, FUNCTION.
    25. "Mitotic activation of the kinase Aurora-A requires its binding partner Bora."
      Hutterer A., Berdnik D., Wirtz-Peitz F., Zigman M., Schleiffer A., Knoblich J.A.
      Dev. Cell 11:147-157(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BORA.
    26. "Aurora-A kinase regulates breast cancer associated gene 1 inhibition of centrosome-dependent microtubule nucleation."
      Sankaran S., Crone D.E., Palazzo R.E., Parvin J.D.
      Cancer Res. 67:11186-11194(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    27. "HEF1-dependent Aurora A activation induces disassembly of the primary cilium."
      Pugacheva E.N., Jablonski S.A., Hartman T.R., Henske E.P., Golemis E.A.
      Cell 129:1351-1363(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    28. "GEF-H1 modulates localized RhoA activation during cytokinesis under the control of mitotic kinases."
      Birkenfeld J., Nalbant P., Bohl B.P., Pertz O., Hahn K.M., Bokoch G.M.
      Dev. Cell 12:699-712(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ARHGEF2.
    29. "Functional interaction of Aurora-A and PP2A during mitosis."
      Horn V., Thelu J., Garcia A., Albiges-Rizo C., Block M.R., Viallet J.
      Mol. Biol. Cell 18:1233-1241(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PPP2CA, PHOSPHORYLATION AT SER-51.
    30. "Interphase nucleo-cytoplasmic shuttling and localization of SIRT2 during mitosis."
      North B.J., Verdin E.
      PLoS ONE 2:E784-E784(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SIRT2, SUBCELLULAR LOCATION.
    31. Cited for: FUNCTION, ENZYME REGULATION.
    32. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    33. "Polo-like kinase-1 is activated by aurora A to promote checkpoint recovery."
      Macurek L., Lindqvist A., Lim D., Lampson M.A., Klompmaker R., Freire R., Clouin C., Taylor S.S., Yaffe M.B., Medema R.H.
      Nature 455:119-123(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    34. "Phosphorylation of the par polarity complex protein Par3 at serine 962 is mediated by aurora A and regulates its function in neuronal polarity."
      Khazaei M.R., Puschel A.W.
      J. Biol. Chem. 284:33571-33579(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, AUTOPHOSPHORYLATION, INTERACTION WITH PARD3.
    35. "Plk1 and Aurora A regulate the depolymerase activity and the cellular localization of Kif2a."
      Jang C.Y., Coppinger J.A., Seki A., Yates J.R. III, Fang G.
      J. Cell Sci. 122:1334-1341(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH KIF2A.
    36. "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, INTERACTION WITH TPX2, PHOSPHORYLATION AT THR-287 AND THR-288, MUTAGENESIS OF THR-287.
    37. "A single amino acid change converts Aurora-A into Aurora-B-like kinase in terms of partner specificity and cellular function."
      Fu J., Bian M., Liu J., Jiang Q., Zhang C.
      Proc. Natl. Acad. Sci. U.S.A. 106:6939-6944(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TPX2, MUTAGENESIS OF GLY-198, SUBCELLULAR LOCATION, FUNCTION.
    38. Cited for: FUNCTION, INTERACTION WITH PIFO, ACTIVATION BY PIFO.
    39. "Functional characterization of AIBp, a novel Aurora-A binding protein in centrosome structure and spindle formation."
      Lieu A.S., Cheng T.S., Chou C.H., Wu C.H., Hsu C.Y., Huang C.Y., Chang L.K., Loh J.K., Chang C.S., Hsu C.M., Howng S.L., Hong Y.R.
      Int. J. Oncol. 37:429-436(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AUNIP.
    40. "Solution structure of human growth arrest and DNA damage 45alpha (Gadd45alpha) and its interactions with proliferating cell nuclear antigen (PCNA) and Aurora A kinase."
      Sanchez R., Pantoja-Uceda D., Prieto J., Diercks T., Marcaida M.J., Montoya G., Campos-Olivas R., Blanco F.J.
      J. Biol. Chem. 285:22196-22201(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GADD45A.
    41. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    42. "PAR, a protein involved in the cell cycle, is functionally related to chromosomal passenger proteins."
      Platica M., Ionescu A., Ivan E., Holland J.F., Mandeli J., Platica O.
      Int. J. Oncol. 38:777-785(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH JTB.
    43. Cited for: REVIEW ON FUNCTION.
    44. "Aurora A, centrosome structure, and the centrosome cycle."
      Lukasiewicz K.B., Lingle W.L.
      Environ. Mol. Mutagen. 50:602-619(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    45. "SIRT2 maintains genome integrity and suppresses tumorigenesis through regulating APC/C activity."
      Kim H.S., Vassilopoulos A., Wang R.H., Lahusen T., Xiao Z., Xu X., Li C., Veenstra T.D., Li B., Yu H., Ji J., Wang X.W., Park S.H., Cha Y.I., Gius D., Deng C.X.
      Cancer Cell 20:487-499(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SIRT2, SUBCELLULAR LOCATION.
    46. "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.
    47. Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 107-403 IN COMPLEX WITH ADENOSINE, CATALYTIC ACTIVITY.
    48. "Structures of the cancer-related Aurora-A, FAK, and EphA2 protein kinases from nanovolume crystallography."
      Nowakowski J., Cronin C.N., McRee D.E., Knuth M.W., Nelson C.G., Pavletich N.P., Rogers J., Sang B.C., Scheibe D.N., Swanson R.V., Thompson D.A.
      Structure 10:1659-1667(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 125-391 IN COMPLEX WITH ADP.
    49. "Structural basis of Aurora-A activation by TPX2 at the mitotic spindle."
      Bayliss R., Sardon T., Vernos I., Conti E.
      Mol. Cell 12:851-862(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 122-403 IN COMPLEX WITH TPX2, MUTAGENESIS OF ASP-274, ACTIVE SITE, PHOSPHORYLATION AT THR-287 AND THR-288.
    50. "SAR and inhibitor complex structure determination of a novel class of potent and specific Aurora kinase inhibitors."
      Heron N.M., Anderson M., Blowers D.P., Breed J., Eden J.M., Green S., Hill G.B., Johnson T., Jung F.H., McMiken H.H., Mortlock A.A., Pannifer A.D., Pauptit R.A., Pink J., Roberts N.J., Rowsell S.
      Bioorg. Med. Chem. Lett. 16:1320-1323(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 123-401 IN COMPLEXES WITH ADPNP AND 5-AMINOPYRIMIDINYL QUINAZOLINE INHIBITOR, CATALYTIC ACTIVITY.
    51. "1,4,5,6-tetrahydropyrrolo[3,4-c]pyrazoles: identification of a potent aurora kinase inhibitor with a favorable antitumor kinase inhibition profile."
      Fancelli D., Moll J., Varasi M., Bravo R., Artico R., Berta D., Bindi S., Cameron A., Candiani I., Cappella P., Carpinelli P., Croci W., Forte B., Giorgini M.L., Klapwijk J., Marsiglio A., Pesenti E., Rocchetti M.
      , Roletto F., Severino D., Soncini C., Storici P., Tonani R., Zugnoni P., Vianello P.
      J. Med. Chem. 49:7247-7251(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 100-403 IN COMPLEXES WITH SYNTHETIC INHIBITORS, FUNCTION.
    52. "Modulation of kinase-inhibitor interactions by auxiliary protein binding: crystallography studies on Aurora A interactions with VX-680 and with TPX2."
      Zhao B., Smallwood A., Yang J., Koretke K., Nurse K., Calamari A., Kirkpatrick R.B., Lai Z.
      Protein Sci. 17:1791-1797(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 125-391 IN COMPLEX WITH VX-680 AND TPX2, PHOSPHORYLATION AT THR-288, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT.
    53. "A cancer-associated aurora A mutant is mislocalized and misregulated due to loss of interaction with TPX2."
      Bibby R.A., Tang C., Faisal A., Drosopoulos K., Lubbe S., Houlston R., Bayliss R., Linardopoulos S.
      J. Biol. Chem. 284:33177-33184(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 127-388 IN COMPLEX WITH ADP, CHARACTERIZATION OF VARIANTS ARG-155 AND MET-174, INTERACTION WITH TPX2.
    54. "Structure-based drug design of novel Aurora kinase A inhibitors: structural basis for potency and specificity."
      Coumar M.S., Leou J.S., Shukla P., Wu J.S., Dixit A.K., Lin W.H., Chang C.Y., Lien T.W., Tan U.K., Chen C.H., Hsu J.T., Chao Y.S., Wu S.Y., Hsieh H.P.
      J. Med. Chem. 52:1050-1062(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 123-401 IN COMPLEX WITH SYNTHETIC INHIBITOR, CATALYTIC ACTIVITY.
    55. Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 125-391 IN COMPLEX WITH SYNTHETIC INHIBITOR, CATALYTIC ACTIVITY.
    56. "Two functional coding single nucleotide polymorphisms in STK15 (Aurora-A) coordinately increase esophageal cancer risk."
      Kimura M.T., Mori T., Conroy J., Nowak N.J., Satomi S., Tamai K., Nagase H.
      Cancer Res. 65:3548-3554(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ILE-31 AND ILE-57.
    57. "Linkage disequilibrium and haplotype analysis of two single nucleotide polymorphisms in STK15 in Chinese."
      Chen L., Ao X., Ren Q., Wang Z.N., Lu C., Xu Y., Jiang L., Luo Y., Xu H.M., Zhang X.
      Yi Chuan Xue Bao 32:331-336(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ILE-31 AND ILE-57.
    58. Cited for: VARIANT ILE-31.
    59. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] ILE-31; LEU-50; ILE-57; ARG-155; MET-174 AND VAL-373.

    Entry informationi

    Entry nameiAURKA_HUMAN
    AccessioniPrimary (citable) accession number: O14965
    Secondary accession number(s): E1P5F9
    , O60445, O75873, Q9BQD6, Q9UPG5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 27, 2003
    Last sequence update: January 27, 2003
    Last modified: October 1, 2014
    This is version 168 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    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

    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.

    Caution

    Authors initially considered AURKA/STK6 and STK15 as 2 different proteins (PubMed:9771714). It is clear that they are the same protein.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 20
      Human chromosome 20: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3