AURKA_HUMAN
ID AURKA_HUMAN Reviewed; 403 AA.
AC O14965; E1P5F9; O60445; O75873; Q9BQD6; Q9UPG5;
DT 27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 3.
DT 03-AUG-2022, entry version 237.
DE RecName: Full=Aurora kinase A;
DE EC=2.7.11.1 {ECO:0000269|PubMed:12237287, ECO:0000269|PubMed:16337122, ECO:0000269|PubMed:19140666, ECO:0000269|PubMed:19402633, ECO:0000269|PubMed:27837025, ECO:0000269|PubMed:28218735};
DE AltName: Full=Aurora 2;
DE AltName: Full=Aurora/IPL1-related kinase 1;
DE Short=ARK-1;
DE Short=Aurora-related kinase 1;
DE Short=hARK1;
DE AltName: Full=Breast tumor-amplified kinase;
DE AltName: Full=Serine/threonine-protein kinase 15;
DE AltName: Full=Serine/threonine-protein kinase 6;
DE AltName: Full=Serine/threonine-protein kinase aurora-A;
GN Name=AURKA {ECO:0000312|HGNC:HGNC:11393};
GN Synonyms=AIK, AIRK1, ARK1, AURA, AYK1, BTAK, IAK1,
GN STK15 {ECO:0000303|PubMed:15867347, ECO:0000303|PubMed:16011022}, STK6;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, SUBCELLULAR LOCATION, AND VARIANT
RP VAL-57.
RC TISSUE=Blood;
RX PubMed=9153231; DOI=10.1074/jbc.272.21.13766;
RA Kimura M., Kotani S., Hattori T., Sumi N., Yoshioka T., Todokoro K.,
RA Okano Y.;
RT "Cell cycle-dependent expression and spindle pole localization of a novel
RT human protein kinase, Aik, related to Aurora of Drosophila and yeast
RT Ipl1.";
RL J. Biol. Chem. 272:13766-13771(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-57.
RX PubMed=9514916; DOI=10.1006/bbrc.1998.8250;
RA Shindo M., Nakano H., Kuroyanagi H., Shirasawa T., Mihara M., Gilbert D.J.,
RA Jenkins N.A., Copeland N.G., Yagita H., Okumura K.;
RT "cDNA cloning, expression, subcellular localization, and chromosomal
RT assignment of mammalian aurora homologues, aurora-related kinase (ARK) 1
RT and 2.";
RL Biochem. Biophys. Res. Commun. 244:285-292(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ILE-31 AND VAL-57.
RC TISSUE=Mammary gland;
RX PubMed=9771714; DOI=10.1038/2496;
RA Zhou H., Kuang J., Zhong L., Kuo W.-L., Gray J.W., Sahin A., Brinkley B.R.,
RA Sen S.;
RT "Tumour amplified kinase STK15/BTAK induces centrosome amplification,
RT aneuploidy and transformation.";
RL Nat. Genet. 20:189-193(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Wang L., Thibodeau S.N.;
RT "Mutational analysis of the STK15 gene in human tumors.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-57.
RC TISSUE=Cervix, Colon, Kidney, and Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9606188; DOI=10.1093/emboj/17.11.3052;
RA Bischoff J.R., Anderson L., Zhu Y., Mossie K., Ng L., Souza B.,
RA Schryver B., Flanagan P., Clairvoyant F., Ginther C., Chan C.S.,
RA Novotny M., Slamon D.J., Plowman G.D.;
RT "A homologue of Drosophila aurora kinase is oncogenic and amplified in
RT human colorectal cancers.";
RL EMBO J. 17:3052-3065(1998).
RN [9]
RP UBIQUITINATION, PROTEASOMAL DEGRADATION, AND MUTAGENESIS OF ARG-205.
RX PubMed=10851084; DOI=10.1038/sj.onc.1203609;
RA Honda K., Mihara H., Kato Y., Yamaguchi A., Tanaka H., Yasuda H.,
RA Furukawa K., Urano T.;
RT "Degradation of human Aurora2 protein kinase by the anaphase-promoting
RT complex-ubiquitin-proteasome pathway.";
RL Oncogene 19:2812-2819(2000).
RN [10]
RP FUNCTION, PHOSPHORYLATION AT THR-288, MUTAGENESIS OF THR-288,
RP UBIQUITINATION, AND ACTIVITY REGULATION.
RX PubMed=11039908; DOI=10.1038/sj.onc.1203847;
RA Walter A.O., Seghezzi W., Korver W., Sheung J., Lees E.;
RT "The mitotic serine/threonine kinase Aurora2/AIK is regulated by
RT phosphorylation and degradation.";
RL Oncogene 19:4906-4916(2000).
RN [11]
RP FUNCTION, INTERACTION WITH PPP1CA; PPP1CB AND PPP1CC, MUTAGENESIS OF
RP PHE-165 AND PHE-346, AND PHOSPHORYLATION.
RX PubMed=11551964; DOI=10.1074/jbc.m107540200;
RA Katayama H., Zhou H., Li Q., Tatsuka M., Sen S.;
RT "Interaction and feedback regulation between STK15/BTAK/Aurora-A kinase and
RT protein phosphatase 1 through mitotic cell division cycle.";
RL J. Biol. Chem. 276:46219-46224(2001).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=12576638; DOI=10.1247/csf.27.457;
RA Sugimoto K., Urano T., Zushi H., Inoue K., Tasaka H., Tachibana M.,
RA Dotsu M.;
RT "Molecular dynamics of Aurora-A kinase in living mitotic cells
RT simultaneously visualized with histone H3 and nuclear membrane protein
RT importinalpha.";
RL Cell Struct. Funct. 27:457-467(2002).
RN [13]
RP FUNCTION, INDUCTION, PHOSPHORYLATION, AND ACTIVITY REGULATION.
RX PubMed=12390251; DOI=10.1046/j.1365-2443.2002.00592.x;
RA Marumoto T., Hirota T., Morisaki T., Kunitoku N., Zhang D., Ichikawa Y.,
RA Sasayama T., Kuninaka S., Mimori T., Tamaki N., Kimura M., Okano Y.,
RA Saya H.;
RT "Roles of aurora-A kinase in mitotic entry and G2 checkpoint in mammalian
RT cells.";
RL Genes Cells 7:1173-1182(2002).
RN [14]
RP INDUCTION.
RX PubMed=11790771; DOI=10.1074/jbc.m108252200;
RA Tanaka M., Ueda A., Kanamori H., Ideguchi H., Yang J., Kitajima S.,
RA Ishigatsubo Y.;
RT "Cell-cycle-dependent regulation of human aurora A transcription is
RT mediated by periodic repression of E4TF1.";
RL J. Biol. Chem. 277:10719-10726(2002).
RN [15]
RP FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT THR-288.
RX PubMed=13678582; DOI=10.1016/s0092-8674(03)00642-1;
RA Hirota T., Kunitoku N., Sasayama T., Marumoto T., Zhang D., Nitta M.,
RA Hatakeyama K., Saya H.;
RT "Aurora-A and an interacting activator, the LIM protein Ajuba, are required
RT for mitotic commitment in human cells.";
RL Cell 114:585-598(2003).
RN [16]
RP FUNCTION.
RX PubMed=14523000; DOI=10.1074/jbc.m306275200;
RA Marumoto T., Honda S., Hara T., Nitta M., Hirota T., Kohmura E., Saya H.;
RT "Aurora-A kinase maintains the fidelity of early and late mitotic events in
RT HeLa cells.";
RL J. Biol. Chem. 278:51786-51795(2003).
RN [17]
RP INTERACTION WITH TACC1.
RX PubMed=14603251; DOI=10.1038/sj.onc.1206972;
RA Conte N., Delaval B., Ginestier C., Ferrand A., Isnardon D., Larroque C.,
RA Prigent C., Seraphin B., Jacquemier J., Birnbaum D.;
RT "TACC1-chTOG-Aurora A protein complex in breast cancer.";
RL Oncogene 22:8102-8116(2003).
RN [18]
RP FUNCTION.
RX PubMed=15147269; DOI=10.1111/j.1356-9597.2004.00732.x;
RA Toji S., Yabuta N., Hosomi T., Nishihara S., Kobayashi T., Suzuki S.,
RA Tamai K., Nojima H.;
RT "The centrosomal protein Lats2 is a phosphorylation target of Aurora-A
RT kinase.";
RL Genes Cells 9:383-397(2004).
RN [19]
RP RETRACTED PAPER.
RX PubMed=14990569; DOI=10.1074/jbc.m311780200;
RA Ouchi M., Fujiuchi N., Sasai K., Katayama H., Minamishima Y.A.,
RA Ongusaha P.P., Deng C., Sen S., Lee S.W., Ouchi T.;
RT "BRCA1 phosphorylation by Aurora-A in the regulation of G2 to M
RT transition.";
RL J. Biol. Chem. 279:19643-19648(2004).
RN [20]
RP RETRACTION NOTICE OF PUBMED:14990569.
RX PubMed=26341884; DOI=10.1074/jbc.a115.311780;
RA Ouchi M., Fujiuchi N., Sasai K., Katayama H., Minamishima Y.A.,
RA Ongusaha P.P., Deng C., Sen S., Lee S.W., Ouchi T.;
RL J. Biol. Chem. 290:22311-22311(2015).
RN [21]
RP FUNCTION.
RX PubMed=15128871; DOI=10.1242/jcs.01108;
RA Dutertre S., Cazales M., Quaranta M., Froment C., Trabut V., Dozier C.,
RA Mirey G., Bouche J.P., Theis-Febvre N., Schmitt E., Monsarrat B.,
RA Prigent C., Ducommun B.;
RT "Phosphorylation of CDC25B by Aurora-A at the centrosome contributes to the
RT G2-M transition.";
RL J. Cell Sci. 117:2523-2531(2004).
RN [22]
RP FUNCTION, MUTAGENESIS OF LYS-162, AND INTERACTION WITH TP53.
RX PubMed=14702041; DOI=10.1038/ng1279;
RA Katayama H., Sasai K., Kawai H., Yuan Z.M., Bondaruk J., Suzuki F.,
RA Fujii S., Arlinghaus R.B., Czerniak B.A., Sen S.;
RT "Phosphorylation by aurora kinase A induces Mdm2-mediated destabilization
RT and inhibition of p53.";
RL Nat. Genet. 36:55-62(2004).
RN [23]
RP INTERACTION WITH CPEB1.
RX PubMed=15966895; DOI=10.1111/j.1365-2443.2005.00870.x;
RA Sasayama T., Marumoto T., Kunitoku N., Zhang D., Tamaki N., Kohmura E.,
RA Saya H., Hirota T.;
RT "Over-expression of Aurora-A targets cytoplasmic polyadenylation element
RT binding protein and promotes mRNA polyadenylation of Cdk1 and cyclin B1.";
RL Genes Cells 10:627-638(2005).
RN [24]
RP PHOSPHORYLATION AT THR-288 AND SER-342.
RX PubMed=16246726; DOI=10.1016/j.molcel.2005.08.035;
RA Zhao Z.S., Lim J.P., Ng Y.W., Lim L., Manser E.;
RT "The GIT-associated kinase PAK targets to the centrosome and regulates
RT Aurora-A.";
RL Mol. Cell 20:237-249(2005).
RN [25]
RP INDUCTION, AND FUNCTION.
RX PubMed=15987997; DOI=10.1128/mcb.25.14.5789-5800.2005;
RA Yu C.T., Hsu J.M., Lee Y.C., Tsou A.P., Chou C.K., Huang C.Y.;
RT "Phosphorylation and stabilization of HURP by Aurora-A: implication of HURP
RT as a transforming target of Aurora-A.";
RL Mol. Cell. Biol. 25:5789-5800(2005).
RN [26]
RP INTERACTION WITH BORA.
RX PubMed=16890155; DOI=10.1016/j.devcel.2006.06.002;
RA Hutterer A., Berdnik D., Wirtz-Peitz F., Zigman M., Schleiffer A.,
RA Knoblich J.A.;
RT "Mitotic activation of the kinase Aurora-A requires its binding partner
RT Bora.";
RL Dev. Cell 11:147-157(2006).
RN [27]
RP FUNCTION.
RX PubMed=18056443; DOI=10.1158/0008-5472.can-07-2578;
RA Sankaran S., Crone D.E., Palazzo R.E., Parvin J.D.;
RT "Aurora-A kinase regulates breast cancer associated gene 1 inhibition of
RT centrosome-dependent microtubule nucleation.";
RL Cancer Res. 67:11186-11194(2007).
RN [28]
RP FUNCTION.
RX PubMed=17604723; DOI=10.1016/j.cell.2007.04.035;
RA Pugacheva E.N., Jablonski S.A., Hartman T.R., Henske E.P., Golemis E.A.;
RT "HEF1-dependent Aurora A activation induces disassembly of the primary
RT cilium.";
RL Cell 129:1351-1363(2007).
RN [29]
RP INTERACTION WITH ARHGEF2.
RX PubMed=17488622; DOI=10.1016/j.devcel.2007.03.014;
RA Birkenfeld J., Nalbant P., Bohl B.P., Pertz O., Hahn K.M., Bokoch G.M.;
RT "GEF-H1 modulates localized RhoA activation during cytokinesis under the
RT control of mitotic kinases.";
RL Dev. Cell 12:699-712(2007).
RN [30]
RP SUBCELLULAR LOCATION, INTERACTION WITH PPP2CA, AND PHOSPHORYLATION AT
RP SER-51.
RX PubMed=17229885; DOI=10.1091/mbc.e06-12-1152;
RA Horn V., Thelu J., Garcia A., Albiges-Rizo C., Block M.R., Viallet J.;
RT "Functional interaction of Aurora-A and PP2A during mitosis.";
RL Mol. Biol. Cell 18:1233-1241(2007).
RN [31]
RP INTERACTION WITH SIRT2, AND SUBCELLULAR LOCATION.
RX PubMed=17726514; DOI=10.1371/journal.pone.0000784;
RA North B.J., Verdin E.;
RT "Interphase nucleo-cytoplasmic shuttling and localization of SIRT2 during
RT mitosis.";
RL PLoS ONE 2:E784-E784(2007).
RN [32]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=17360485; DOI=10.1073/pnas.0608798104;
RA Manfredi M.G., Ecsedy J.A., Meetze K.A., Balani S.K., Burenkova O.,
RA Chen W., Galvin K.M., Hoar K.M., Huck J.J., LeRoy P.J., Ray E.T.,
RA Sells T.B., Stringer B., Stroud S.G., Vos T.J., Weatherhead G.S.,
RA Wysong D.R., Zhang M., Bolen J.B., Claiborne C.F.;
RT "Antitumor activity of MLN8054, an orally active small-molecule inhibitor
RT of Aurora A kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:4106-4111(2007).
RN [33]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [34]
RP FUNCTION.
RX PubMed=18615013; DOI=10.1038/nature07185;
RA Macurek L., Lindqvist A., Lim D., Lampson M.A., Klompmaker R., Freire R.,
RA Clouin C., Taylor S.S., Yaffe M.B., Medema R.H.;
RT "Polo-like kinase-1 is activated by aurora A to promote checkpoint
RT recovery.";
RL Nature 455:119-123(2008).
RN [35]
RP FUNCTION, AUTOPHOSPHORYLATION, AND INTERACTION WITH PARD3.
RX PubMed=19812038; DOI=10.1074/jbc.m109.055897;
RA Khazaei M.R., Puschel A.W.;
RT "Phosphorylation of the par polarity complex protein Par3 at serine 962 is
RT mediated by aurora A and regulates its function in neuronal polarity.";
RL J. Biol. Chem. 284:33571-33579(2009).
RN [36]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH KIF2A.
RX PubMed=19351716; DOI=10.1242/jcs.044321;
RA Jang C.Y., Coppinger J.A., Seki A., Yates J.R. III, Fang G.;
RT "Plk1 and Aurora A regulate the depolymerase activity and the cellular
RT localization of Kif2a.";
RL J. Cell Sci. 122:1334-1341(2009).
RN [37]
RP FUNCTION, INTERACTION WITH TPX2, PHOSPHORYLATION AT THR-287 AND THR-288,
RP AND MUTAGENESIS OF THR-287.
RX PubMed=19668197; DOI=10.1038/ncb1919;
RA Mori D., Yamada M., Mimori-Kiyosue Y., Shirai Y., Suzuki A., Ohno S.,
RA Saya H., Wynshaw-Boris A., Hirotsune S.;
RT "An essential role of the aPKC-Aurora A-NDEL1 pathway in neurite elongation
RT by modulation of microtubule dynamics.";
RL Nat. Cell Biol. 11:1057-1068(2009).
RN [38]
RP INTERACTION WITH TPX2, MUTAGENESIS OF GLY-198, AND SUBCELLULAR LOCATION.
RX PubMed=19357306; DOI=10.1073/pnas.0900833106;
RA Fu J., Bian M., Liu J., Jiang Q., Zhang C.;
RT "A single amino acid change converts Aurora-A into Aurora-B-like kinase in
RT terms of partner specificity and cellular function.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:6939-6944(2009).
RN [39]
RP FUNCTION, INTERACTION WITH PIFO, AND ACTIVATION BY PIFO.
RX PubMed=20643351; DOI=10.1016/j.devcel.2010.06.005;
RA Kinzel D., Boldt K., Davis E.E., Burtscher I., Trumbach D., Diplas B.,
RA Attie-Bitach T., Wurst W., Katsanis N., Ueffing M., Lickert H.;
RT "Pitchfork regulates primary cilia disassembly and left-right asymmetry.";
RL Dev. Cell 19:66-77(2010).
RN [40]
RP INTERACTION WITH AUNIP.
RX PubMed=20596670; DOI=10.3892/ijo_00000691;
RA Lieu A.S., Cheng T.S., Chou C.H., Wu C.H., Hsu C.Y., Huang C.Y.,
RA Chang L.K., Loh J.K., Chang C.S., Hsu C.M., Howng S.L., Hong Y.R.;
RT "Functional characterization of AIBp, a novel Aurora-A binding protein in
RT centrosome structure and spindle formation.";
RL Int. J. Oncol. 37:429-436(2010).
RN [41]
RP INTERACTION WITH GADD45A.
RX PubMed=20460379; DOI=10.1074/jbc.m109.069344;
RA Sanchez R., Pantoja-Uceda D., Prieto J., Diercks T., Marcaida M.J.,
RA Montoya G., Campos-Olivas R., Blanco F.J.;
RT "Solution structure of human growth arrest and DNA damage 45alpha
RT (Gadd45alpha) and its interactions with proliferating cell nuclear antigen
RT (PCNA) and Aurora A kinase.";
RL J. Biol. Chem. 285:22196-22201(2010).
RN [42]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [43]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH JTB.
RX PubMed=21225229; DOI=10.3892/ijo.2011.900;
RA Platica M., Ionescu A., Ivan E., Holland J.F., Mandeli J., Platica O.;
RT "PAR, a protein involved in the cell cycle, is functionally related to
RT chromosomal passenger proteins.";
RL Int. J. Oncol. 38:777-785(2011).
RN [44]
RP REVIEW ON FUNCTION.
RX PubMed=14625535; DOI=10.1038/nrm1245;
RA Carmena M., Earnshaw W.C.;
RT "The cellular geography of aurora kinases.";
RL Nat. Rev. Mol. Cell Biol. 4:842-854(2003).
RN [45]
RP REVIEW ON FUNCTION.
RX PubMed=19774610; DOI=10.1002/em.20533;
RA Lukasiewicz K.B., Lingle W.L.;
RT "Aurora A, centrosome structure, and the centrosome cycle.";
RL Environ. Mol. Mutagen. 50:602-619(2009).
RN [46]
RP INTERACTION WITH SIRT2, AND SUBCELLULAR LOCATION.
RX PubMed=22014574; DOI=10.1016/j.ccr.2011.09.004;
RA Kim H.S., Vassilopoulos A., Wang R.H., Lahusen T., Xiao Z., Xu X., Li C.,
RA Veenstra T.D., Li B., Yu H., Ji J., Wang X.W., Park S.H., Cha Y.I.,
RA Gius D., Deng C.X.;
RT "SIRT2 maintains genome integrity and suppresses tumorigenesis through
RT regulating APC/C activity.";
RL Cancer Cell 20:487-499(2011).
RN [47]
RP INTERACTION WITH HNRNPU.
RX PubMed=21242313; DOI=10.1242/jcs.063347;
RA Ma N., Matsunaga S., Morimoto A., Sakashita G., Urano T., Uchiyama S.,
RA Fukui K.;
RT "The nuclear scaffold protein SAF-A is required for kinetochore-microtubule
RT attachment and contributes to the targeting of Aurora-A to mitotic
RT spindles.";
RL J. Cell Sci. 124:394-404(2011).
RN [48]
RP INTERACTION WITH KLHL18 AND CUL3, UBIQUITINATION, AND SUBCELLULAR LOCATION.
RX PubMed=23213400; DOI=10.1242/bio.2011018;
RA Moghe S., Jiang F., Miura Y., Cerny R.L., Tsai M.Y., Furukawa M.;
RT "The CUL3-KLHL18 ligase regulates mitotic entry and ubiquitylates Aurora-
RT A.";
RL Biol. Open 1:82-91(2012).
RN [49]
RP INTERACTION WITH FRY.
RX PubMed=22753416; DOI=10.1074/jbc.m112.378968;
RA Ikeda M., Chiba S., Ohashi K., Mizuno K.;
RT "Furry protein promotes Aurora A-mediated polo-like kinase 1 activation.";
RL J. Biol. Chem. 287:27670-27681(2012).
RN [50]
RP SUBCELLULAR LOCATION.
RX PubMed=25657325; DOI=10.1091/mbc.e14-09-1366;
RA Ohta S., Wood L., Toramoto I., Yagyu K., Fukagawa T., Earnshaw W.C.;
RT "CENP-32 is required to maintain centrosomal dominance in bipolar spindle
RT assembly.";
RL Mol. Biol. Cell 26:1225-1237(2015).
RN [51]
RP INTERACTION WITH HNRNPU.
RX PubMed=25986610; DOI=10.1128/mcb.01312-14;
RA Douglas P., Ye R., Morrice N., Britton S., Trinkle-Mulcahy L.,
RA Lees-Miller S.P.;
RT "Phosphorylation of SAF-A/hnRNP-U serine 59 by polo-like kinase 1 is
RT required for mitosis.";
RL Mol. Cell. Biol. 35:2699-2713(2015).
RN [52]
RP FUNCTION.
RX PubMed=27335426; DOI=10.1242/jcs.184416;
RA Kotak S., Afshar K., Busso C., Goenczy P.;
RT "Aurora A kinase regulates proper spindle positioning in C. elegans and in
RT human cells.";
RL J. Cell Sci. 129:3015-3025(2016).
RN [53]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-258, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [54]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND INTERACTION WITH
RP FOXP1.
RX PubMed=28218735; DOI=10.1038/oncsis.2016.80;
RA Kamran M., Long Z.J., Xu D., Lv S.S., Liu B., Wang C.L., Xu J., Lam E.W.,
RA Liu Q.;
RT "Aurora kinase A regulates Survivin stability through targeting FBXL7 in
RT gastric cancer drug resistance and prognosis.";
RL Oncogenesis 6:E298-E298(2017).
RN [55]
RP SUBCELLULAR LOCATION.
RX PubMed=30538148; DOI=10.1261/rna.069773.118;
RA Jiao A.L., Perales R., Umbreit N.T., Haswell J.R., Piper M.E., Adams B.D.,
RA Pellman D., Kennedy S., Slack F.J.;
RT "Human nuclear RNAi-defective 2 (NRDE2) is an essential RNA splicing
RT factor.";
RL RNA 25:352-363(2019).
RN [56]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 107-403 IN COMPLEX WITH ADENOSINE,
RP AND CATALYTIC ACTIVITY.
RX PubMed=12237287; DOI=10.1074/jbc.c200426200;
RA Cheetham G.M., Knegtel R.M., Coll J.T., Renwick S.B., Swenson L., Weber P.,
RA Lippke J.A., Austen D.A.;
RT "Crystal structure of aurora-2, an oncogenic serine/threonine kinase.";
RL J. Biol. Chem. 277:42419-42422(2002).
RN [57]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 125-391 IN COMPLEX WITH ADP.
RX PubMed=12467573; DOI=10.1016/s0969-2126(02)00907-3;
RA Nowakowski J., Cronin C.N., McRee D.E., Knuth M.W., Nelson C.G.,
RA Pavletich N.P., Rogers J., Sang B.C., Scheibe D.N., Swanson R.V.,
RA Thompson D.A.;
RT "Structures of the cancer-related Aurora-A, FAK, and EphA2 protein kinases
RT from nanovolume crystallography.";
RL Structure 10:1659-1667(2002).
RN [58]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 122-403 IN COMPLEX WITH TPX2,
RP MUTAGENESIS OF ASP-274, ACTIVE SITE, PHOSPHORYLATION AT THR-287 AND
RP THR-288, AND REGION ACTIVATION SEGMENT.
RX PubMed=14580337; DOI=10.1016/s1097-2765(03)00392-7;
RA Bayliss R., Sardon T., Vernos I., Conti E.;
RT "Structural basis of Aurora-A activation by TPX2 at the mitotic spindle.";
RL Mol. Cell 12:851-862(2003).
RN [59]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 123-401 IN COMPLEXES WITH ADPNP
RP AND 5-AMINOPYRIMIDINYL QUINAZOLINE INHIBITOR, AND CATALYTIC ACTIVITY.
RX PubMed=16337122; DOI=10.1016/j.bmcl.2005.11.053;
RA Heron N.M., Anderson M., Blowers D.P., Breed J., Eden J.M., Green S.,
RA Hill G.B., Johnson T., Jung F.H., McMiken H.H., Mortlock A.A.,
RA Pannifer A.D., Pauptit R.A., Pink J., Roberts N.J., Rowsell S.;
RT "SAR and inhibitor complex structure determination of a novel class of
RT potent and specific Aurora kinase inhibitors.";
RL Bioorg. Med. Chem. Lett. 16:1320-1323(2006).
RN [60]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 100-403 IN COMPLEXES WITH
RP SYNTHETIC INHIBITORS, AND FUNCTION.
RX PubMed=17125279; DOI=10.1021/jm060897w;
RA Fancelli D., Moll J., Varasi M., Bravo R., Artico R., Berta D., Bindi S.,
RA Cameron A., Candiani I., Cappella P., Carpinelli P., Croci W., Forte B.,
RA Giorgini M.L., Klapwijk J., Marsiglio A., Pesenti E., Rocchetti M.,
RA Roletto F., Severino D., Soncini C., Storici P., Tonani R., Zugnoni P.,
RA Vianello P.;
RT "1,4,5,6-tetrahydropyrrolo[3,4-c]pyrazoles: identification of a potent
RT aurora kinase inhibitor with a favorable antitumor kinase inhibition
RT profile.";
RL J. Med. Chem. 49:7247-7251(2006).
RN [61]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 125-391 IN COMPLEX WITH VX-680 AND
RP TPX2, PHOSPHORYLATION AT THR-288, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP SUBUNIT.
RX PubMed=18662907; DOI=10.1110/ps.036590.108;
RA Zhao B., Smallwood A., Yang J., Koretke K., Nurse K., Calamari A.,
RA Kirkpatrick R.B., Lai Z.;
RT "Modulation of kinase-inhibitor interactions by auxiliary protein binding:
RT crystallography studies on Aurora A interactions with VX-680 and with
RT TPX2.";
RL Protein Sci. 17:1791-1797(2008).
RN [62]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 127-388 IN COMPLEX WITH ADP,
RP CHARACTERIZATION OF VARIANTS ARG-155 AND MET-174, AND INTERACTION WITH
RP TPX2.
RX PubMed=19801554; DOI=10.1074/jbc.m109.032722;
RA Bibby R.A., Tang C., Faisal A., Drosopoulos K., Lubbe S., Houlston R.,
RA Bayliss R., Linardopoulos S.;
RT "A cancer-associated aurora A mutant is mislocalized and misregulated due
RT to loss of interaction with TPX2.";
RL J. Biol. Chem. 284:33177-33184(2009).
RN [63]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 123-401 IN COMPLEX WITH SYNTHETIC
RP INHIBITOR, AND CATALYTIC ACTIVITY.
RX PubMed=19140666; DOI=10.1021/jm801270e;
RA Coumar M.S., Leou J.S., Shukla P., Wu J.S., Dixit A.K., Lin W.H.,
RA Chang C.Y., Lien T.W., Tan U.K., Chen C.H., Hsu J.T., Chao Y.S., Wu S.Y.,
RA Hsieh H.P.;
RT "Structure-based drug design of novel Aurora kinase A inhibitors:
RT structural basis for potency and specificity.";
RL J. Med. Chem. 52:1050-1062(2009).
RN [64]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 125-391 IN COMPLEX WITH SYNTHETIC
RP INHIBITOR, AND CATALYTIC ACTIVITY.
RX PubMed=19402633; DOI=10.1021/jm9000314;
RA Aliagas-Martin I., Burdick D., Corson L., Dotson J., Drummond J.,
RA Fields C., Huang O.W., Hunsaker T., Kleinheinz T., Krueger E., Liang J.,
RA Moffat J., Phillips G., Pulk R., Rawson T.E., Ultsch M., Walker L.,
RA Wiesmann C., Zhang B., Zhu B.Y., Cochran A.G.;
RT "A class of 2,4-bisanilinopyrimidine Aurora A inhibitors with unusually
RT high selectivity against Aurora B.";
RL J. Med. Chem. 52:3300-3307(2009).
RN [65]
RP X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) OF 122-403 OF MUTANTS ALA-290 AND
RP ALA-393 IN COMPLEX WITH ADP, INTERACTION WITH MYCN AND TPX2, MUTAGENESIS OF
RP CYS-290; TYR-334; GLN-335 AND CYS-393, AND CATALYTIC ACTIVITY.
RX PubMed=27837025; DOI=10.1073/pnas.1610626113;
RA Richards M.W., Burgess S.G., Poon E., Carstensen A., Eilers M., Chesler L.,
RA Bayliss R.;
RT "Structural basis of N-Myc binding by Aurora-A and its destabilization by
RT kinase inhibitors.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:13726-13731(2016).
RN [66]
RP VARIANTS ILE-31 AND VAL-57, AND CHARACTERIZATION OF VARIANT VAL-57.
RX PubMed=15867347; DOI=10.1158/0008-5472.can-04-2149;
RA Kimura M.T., Mori T., Conroy J., Nowak N.J., Satomi S., Tamai K.,
RA Nagase H.;
RT "Two functional coding single nucleotide polymorphisms in STK15 (Aurora-A)
RT coordinately increase esophageal cancer risk.";
RL Cancer Res. 65:3548-3554(2005).
RN [67]
RP VARIANTS ILE-31 AND VAL-57.
RX PubMed=16011022;
RA Chen L., Ao X., Ren Q., Wang Z.N., Lu C., Xu Y., Jiang L., Luo Y., Xu H.M.,
RA Zhang X.;
RT "Linkage disequilibrium and haplotype analysis of two single nucleotide
RT polymorphisms in STK15 in Chinese.";
RL Yi Chuan Xue Bao 32:331-336(2005).
RN [68]
RP VARIANT ILE-31.
RX PubMed=16762494; DOI=10.1016/j.canlet.2006.05.002;
RA Tchatchou S., Wirtenberger M., Hemminki K., Sutter C., Meindl A.,
RA Wappenschmidt B., Kiechle M., Bugert P., Schmutzler R.K., Bartram C.R.,
RA Burwinkel B.;
RT "Aurora kinases A and B and familial breast cancer risk.";
RL Cancer Lett. 247:266-272(2007).
RN [69]
RP VARIANTS [LARGE SCALE ANALYSIS] ILE-31; LEU-50; VAL-57; ARG-155; MET-174
RP AND VAL-373.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
RN [70]
RP FUNCTION, INTERACTION WITH AAAS, SUBCELLULAR LOCATION, AND PHOSPHORYLATION
RP AT THR-288.
RX PubMed=26246606; DOI=10.1091/mbc.e15-02-0113;
RA Carvalhal S., Ribeiro S.A., Arocena M., Kasciukovic T., Temme A.,
RA Koehler K., Huebner A., Griffis E.R.;
RT "The nucleoporin ALADIN regulates Aurora A localization to ensure robust
RT mitotic spindle formation.";
RL Mol. Biol. Cell 26:3424-3438(2015).
CC -!- FUNCTION: Mitotic serine/threonine kinase that contributes to the
CC regulation of cell cycle progression (PubMed:26246606, PubMed:12390251,
CC PubMed:18615013, PubMed:11039908, PubMed:17125279, PubMed:17360485).
CC Associates with the centrosome and the spindle microtubules during
CC mitosis and plays a critical role in various mitotic events including
CC the establishment of mitotic spindle, centrosome duplication,
CC centrosome separation as well as maturation, chromosomal alignment,
CC spindle assembly checkpoint, and cytokinesis (PubMed:26246606,
CC PubMed:14523000). Required for normal spindle positioning during
CC mitosis and for the localization of NUMA1 and DCTN1 to the cell cortex
CC during metaphase (PubMed:27335426). Required for initial activation of
CC CDK1 at centrosomes (PubMed:13678582, PubMed:15128871). Phosphorylates
CC numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B,
CC DLGP5, HDAC6, KIF2A, LATS2, NDEL1, PARD3, PPP1R2, PLK1, RASSF1, TACC3,
CC p53/TP53 and TPX2 (PubMed:18056443, PubMed:15128871, PubMed:14702041,
CC PubMed:11551964, PubMed:15147269, PubMed:15987997, PubMed:17604723,
CC PubMed:18615013). Regulates KIF2A tubulin depolymerase activity
CC (PubMed:19351716). Important for microtubule formation and/or
CC stabilization (PubMed:18056443). Required for normal axon formation
CC (PubMed:19812038). Plays a role in microtubule remodeling during
CC neurite extension (PubMed:19668197). Also acts as a key regulatory
CC component of the p53/TP53 pathway, and particularly the checkpoint-
CC response pathways critical for oncogenic transformation of cells, by
CC phosphorylating and destabilizing p53/TP53 (PubMed:14702041).
CC Phosphorylates its own inhibitors, the protein phosphatase type 1 (PP1)
CC isoforms, to inhibit their activity (PubMed:11551964). Necessary for
CC proper cilia disassembly prior to mitosis (PubMed:17604723,
CC PubMed:20643351). Regulates protein levels of the anti-apoptosis
CC protein BIRC5 by suppressing the expression of the SCF(FBXL7) E3
CC ubiquitin-protein ligase substrate adapter FBXL7 through the
CC phosphorylation of the transcription factor FOXP1 (PubMed:28218735).
CC {ECO:0000269|PubMed:11039908, ECO:0000269|PubMed:11551964,
CC ECO:0000269|PubMed:12390251, ECO:0000269|PubMed:13678582,
CC ECO:0000269|PubMed:14523000, ECO:0000269|PubMed:14702041,
CC ECO:0000269|PubMed:15128871, ECO:0000269|PubMed:15147269,
CC ECO:0000269|PubMed:15987997, ECO:0000269|PubMed:17125279,
CC ECO:0000269|PubMed:17360485, ECO:0000269|PubMed:17604723,
CC ECO:0000269|PubMed:18056443, ECO:0000269|PubMed:18615013,
CC ECO:0000269|PubMed:19351716, ECO:0000269|PubMed:19668197,
CC ECO:0000269|PubMed:19812038, ECO:0000269|PubMed:20643351,
CC ECO:0000269|PubMed:26246606, ECO:0000269|PubMed:27335426,
CC ECO:0000269|PubMed:28218735}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000269|PubMed:12237287, ECO:0000269|PubMed:16337122,
CC ECO:0000269|PubMed:19140666, ECO:0000269|PubMed:19402633,
CC ECO:0000269|PubMed:27837025, ECO:0000269|PubMed:28218735};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000269|PubMed:12237287,
CC ECO:0000269|PubMed:16337122, ECO:0000269|PubMed:19140666,
CC ECO:0000269|PubMed:19402633, ECO:0000269|PubMed:27837025,
CC ECO:0000269|PubMed:28218735};
CC -!- ACTIVITY REGULATION: Activation of CDK1, appears to be an upstream
CC event of AURKA activation. Phosphatase inhibitor-2 (PPP1R2) and TPX2
CC act also as activators. Inactivated by the G2 checkpoint. Inhibited by
CC GADD45A and p53/TP53, and through dephosphorylation by protein
CC phosphatase type 1 (PP1). MLN8054 is also a potent and selective
CC inhibitor. Activated during the early phase of cilia disassembly in the
CC presence of PIFO. Inhibited by the small molecule inhibitor VX-680
CC (PubMed:28218735). {ECO:0000269|PubMed:11039908,
CC ECO:0000269|PubMed:12390251, ECO:0000269|PubMed:17360485,
CC ECO:0000269|PubMed:28218735}.
CC -!- SUBUNIT: Interacts with FBXL7 (By similarity). Interacts with CPEB1,
CC JTB, TACC1, TPX2, PPP2CA, as well as with the protein phosphatase type
CC 1 (PP1) isoforms PPP1CA, PPP1CB and PPP1CC. Interacts also with its
CC substrates ARHGEF2, BORA, KIF2A, PARD3, and p53/TP53. Interaction with
CC BORA promotes phosphorylation of PLK1. Interacts with PIFO. Interacts
CC with GADD45A, competing with its oligomerization. Interacts (via C-
CC terminus) with AUNIP (via C-terminus). Identified in a complex with
CC AUNIP and NIN. Interacts with FRY; this interaction facilitates AURKA-
CC mediated PLK1 phosphorylation. Interacts with SIRT2 (PubMed:17726514,
CC PubMed:22014574). Interacts with MYCN; interaction is phospho-
CC independent and triggers AURKA activation; AURKA competes with FBXW7
CC for binding to unphosphorylated MYCN but not for binding to
CC phosphorylated MYCN (PubMed:27837025). Interacts with HNRNPU
CC (PubMed:21242313, PubMed:25986610). Interacts with AAAS
CC (PubMed:26246606). Interacts with KLHL18 and CUL3 (PubMed:23213400).
CC Interacts with FOXP1 (PubMed:28218735). {ECO:0000250|UniProtKB:P97477,
CC ECO:0000269|PubMed:11551964, ECO:0000269|PubMed:12237287,
CC ECO:0000269|PubMed:12467573, ECO:0000269|PubMed:14580337,
CC ECO:0000269|PubMed:14603251, ECO:0000269|PubMed:14702041,
CC ECO:0000269|PubMed:15966895, ECO:0000269|PubMed:16890155,
CC ECO:0000269|PubMed:17229885, ECO:0000269|PubMed:17488622,
CC ECO:0000269|PubMed:17726514, ECO:0000269|PubMed:18662907,
CC ECO:0000269|PubMed:19140666, ECO:0000269|PubMed:19351716,
CC ECO:0000269|PubMed:19357306, ECO:0000269|PubMed:19402633,
CC ECO:0000269|PubMed:19668197, ECO:0000269|PubMed:19801554,
CC ECO:0000269|PubMed:19812038, ECO:0000269|PubMed:20460379,
CC ECO:0000269|PubMed:20596670, ECO:0000269|PubMed:20643351,
CC ECO:0000269|PubMed:21225229, ECO:0000269|PubMed:21242313,
CC ECO:0000269|PubMed:22014574, ECO:0000269|PubMed:22753416,
CC ECO:0000269|PubMed:23213400, ECO:0000269|PubMed:25986610,
CC ECO:0000269|PubMed:26246606, ECO:0000269|PubMed:27837025,
CC ECO:0000269|PubMed:28218735}.
CC -!- INTERACTION:
CC O14965; Q9NWT8: AURKAIP1; NbExp=2; IntAct=EBI-448680, EBI-448665;
CC O14965; O15392: BIRC5; NbExp=2; IntAct=EBI-448680, EBI-518823;
CC O14965; P00533: EGFR; NbExp=4; IntAct=EBI-448680, EBI-297353;
CC O14965; P61978: HNRNPK; NbExp=2; IntAct=EBI-448680, EBI-304185;
CC O14965; Q13123: IK; NbExp=3; IntAct=EBI-448680, EBI-713456;
CC O14965; O14920: IKBKB; NbExp=2; IntAct=EBI-448680, EBI-81266;
CC O14965; Q9NQS7: INCENP; NbExp=2; IntAct=EBI-448680, EBI-307907;
CC O14965; Q9NQS7-1: INCENP; NbExp=2; IntAct=EBI-448680, EBI-15767972;
CC O14965; P04198: MYCN; NbExp=12; IntAct=EBI-448680, EBI-878369;
CC O14965; P06748: NPM1; NbExp=3; IntAct=EBI-448680, EBI-78579;
CC O14965; P53350: PLK1; NbExp=4; IntAct=EBI-448680, EBI-476768;
CC O14965; P23468: PTPRD; NbExp=2; IntAct=EBI-448680, EBI-2682990;
CC O14965; Q96R06: SPAG5; NbExp=3; IntAct=EBI-448680, EBI-413317;
CC O14965; O15350: TP73; NbExp=11; IntAct=EBI-448680, EBI-389606;
CC O14965; Q9ULW0: TPX2; NbExp=8; IntAct=EBI-448680, EBI-1037322;
CC O14965; Q8VDQ8: Sirt2; Xeno; NbExp=5; IntAct=EBI-448680, EBI-911012;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:12576638,
CC ECO:0000269|PubMed:13678582, ECO:0000269|PubMed:17229885,
CC ECO:0000269|PubMed:17726514, ECO:0000269|PubMed:19357306,
CC ECO:0000269|PubMed:21225229, ECO:0000269|PubMed:22014574,
CC ECO:0000269|PubMed:23213400, ECO:0000269|PubMed:25657325,
CC ECO:0000269|PubMed:30538148, ECO:0000269|PubMed:9153231}. Cytoplasm,
CC cytoskeleton, spindle pole {ECO:0000269|PubMed:12576638,
CC ECO:0000269|PubMed:13678582, ECO:0000269|PubMed:17726514,
CC ECO:0000269|PubMed:19351716, ECO:0000269|PubMed:25657325,
CC ECO:0000269|PubMed:26246606, ECO:0000269|PubMed:9153231,
CC ECO:0000269|PubMed:9606188}. Cytoplasm, cytoskeleton, cilium basal body
CC {ECO:0000250|UniProtKB:P97477}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriole
CC {ECO:0000250|UniProtKB:P97477}. Cell projection, neuron projection
CC {ECO:0000250|UniProtKB:P97477}. Note=Detected at the neurite hillock in
CC developing neurons (By similarity). Localizes at the centrosome in
CC mitotic cells from early prophase until telophase, but also localizes
CC to the spindle pole MTs from prophase to anaphase (PubMed:9606188,
CC PubMed:17229885, PubMed:21225229). Colocalized with SIRT2 at centrosome
CC (PubMed:22014574). Moves to the midbody during both telophase and
CC cytokinesis (PubMed:17726514). Associates with both the pericentriolar
CC material (PCM) and centrioles (PubMed:22014574). The localization to
CC the spindle poles is regulated by AAAS (PubMed:26246606).
CC {ECO:0000250|UniProtKB:P97477, ECO:0000269|PubMed:17229885,
CC ECO:0000269|PubMed:17726514, ECO:0000269|PubMed:21225229,
CC ECO:0000269|PubMed:22014574, ECO:0000269|PubMed:26246606,
CC ECO:0000269|PubMed:9606188}.
CC -!- TISSUE SPECIFICITY: Highly expressed in testis and weakly in skeletal
CC muscle, thymus and spleen. Also highly expressed in colon, ovarian,
CC prostate, neuroblastoma, breast and cervical cancer cell lines.
CC -!- INDUCTION: Expression is cell-cycle regulated, low in G1/S, accumulates
CC during G2/M, and decreases rapidly after. {ECO:0000269|PubMed:11790771,
CC ECO:0000269|PubMed:12390251, ECO:0000269|PubMed:15987997,
CC ECO:0000269|PubMed:9153231, ECO:0000269|PubMed:9606188}.
CC -!- PTM: Activated by phosphorylation at Thr-288; this brings about a
CC change in the conformation of the activation segment. Phosphorylation
CC at Thr-288 varies during the cell cycle and is highest during M phase.
CC Autophosphorylated at Thr-288 upon TPX2 binding. Thr-288 can be
CC phosphorylated by several kinases, including PAK and PKA. Protein
CC phosphatase type 1 (PP1) binds AURKA and inhibits its activity by
CC dephosphorylating Thr-288 during mitosis. Phosphorylation at Ser-342
CC decreases the kinase activity. PPP2CA controls degradation by
CC dephosphorylating Ser-51 at the end of mitosis.
CC {ECO:0000269|PubMed:11039908, ECO:0000269|PubMed:11551964,
CC ECO:0000269|PubMed:12390251, ECO:0000269|PubMed:13678582,
CC ECO:0000269|PubMed:14580337, ECO:0000269|PubMed:16246726,
CC ECO:0000269|PubMed:17229885, ECO:0000269|PubMed:18662907,
CC ECO:0000269|PubMed:19668197}.
CC -!- PTM: Ubiquitinated by the E3 ubiquitin-protein ligase complex
CC SCF(FBXL7) during mitosis, leading to its degradation by the proteasome
CC (By similarity). Ubiquitinated by CHFR, leading to its degradation by
CC the proteasome (By similarity). Ubiquitinated by the anaphase-promoting
CC complex (APC), leading to its degradation by the proteasome
CC (PubMed:10851084, PubMed:11039908). Ubiquitinated by the CUL3-KLHL18
CC ligase leading to its activation at the centrosome which is required
CC for initiating mitotic entry (PubMed:23213400). Ubiquitination mediated
CC by CUL3-KLHL18 ligase does not lead to its degradation by the
CC proteasome (PubMed:23213400). {ECO:0000250|UniProtKB:P97477,
CC ECO:0000269|PubMed:10851084, ECO:0000269|PubMed:11039908,
CC ECO:0000269|PubMed:23213400}.
CC -!- MISCELLANEOUS: Centrosome amplification can occur when the cycles are
CC uncoupled, and this amplification is associated with cancer and with an
CC increase in the levels of chromosomal instability.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. Aurora subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
CC -!- CAUTION: Authors initially considered AURKA/STK6 and STK15 as 2
CC different proteins (PubMed:9771714). It is clear that they are the same
CC protein. {ECO:0000305|PubMed:9771714}.
CC -!- CAUTION: An article that concluded that AURKA-mediated phosphorylation
CC of BRCA1 'Ser-308' plays a role in the normal cell cycle G2/M
CC transition was withdrawn due to data manipulation of flow cytometry
CC data. {ECO:0000305|PubMed:14990569, ECO:0000305|PubMed:26341884}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA23592.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/AURKAID730ch20q13.html";
CC ---------------------------------------------------------------------------
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DR EMBL; D84212; BAA23592.1; ALT_FRAME; mRNA.
DR EMBL; AF008551; AAC12708.1; -; mRNA.
DR EMBL; AF011467; AAC23448.1; -; Genomic_DNA.
DR EMBL; AF011468; AAC63902.1; -; mRNA.
DR EMBL; AF195947; AAF29508.1; -; Genomic_DNA.
DR EMBL; AF195942; AAF29508.1; JOINED; Genomic_DNA.
DR EMBL; AF195943; AAF29508.1; JOINED; Genomic_DNA.
DR EMBL; AF195944; AAF29508.1; JOINED; Genomic_DNA.
DR EMBL; AF195945; AAF29508.1; JOINED; Genomic_DNA.
DR EMBL; AF195946; AAF29508.1; JOINED; Genomic_DNA.
DR EMBL; AL121914; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW75550.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75551.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75552.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75553.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75554.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75555.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75556.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75557.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75558.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75559.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75561.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75562.1; -; Genomic_DNA.
DR EMBL; BC001280; AAH01280.1; -; mRNA.
DR EMBL; BC002499; AAH02499.1; -; mRNA.
DR EMBL; BC006423; AAH06423.1; -; mRNA.
DR EMBL; BC027464; AAH27464.1; -; mRNA.
DR CCDS; CCDS13451.1; -.
DR PIR; JC5974; JC5974.
DR RefSeq; NP_001310232.1; NM_001323303.1.
DR RefSeq; NP_001310233.1; NM_001323304.1.
DR RefSeq; NP_001310234.1; NM_001323305.1.
DR RefSeq; NP_003591.2; NM_003600.3.
DR RefSeq; NP_940835.1; NM_198433.2.
DR RefSeq; NP_940836.1; NM_198434.2.
DR RefSeq; NP_940837.1; NM_198435.2.
DR RefSeq; NP_940838.1; NM_198436.2.
DR RefSeq; NP_940839.1; NM_198437.2.
DR RefSeq; XP_016883524.1; XM_017028035.1.
DR PDB; 1MQ4; X-ray; 1.90 A; A=125-391.
DR PDB; 1MUO; X-ray; 2.90 A; A=107-403.
DR PDB; 1OL5; X-ray; 2.50 A; A=122-403.
DR PDB; 1OL6; X-ray; 3.00 A; A=122-403.
DR PDB; 1OL7; X-ray; 2.75 A; A=122-403.
DR PDB; 2BMC; X-ray; 2.60 A; A/B/C/D/E/F=100-403.
DR PDB; 2C6D; X-ray; 2.20 A; A=124-398.
DR PDB; 2C6E; X-ray; 2.10 A; A/B=123-401.
DR PDB; 2DWB; X-ray; 2.50 A; A=122-403.
DR PDB; 2J4Z; X-ray; 2.00 A; A/B=100-403.
DR PDB; 2J50; X-ray; 3.00 A; A/B=126-403.
DR PDB; 2NP8; X-ray; 2.25 A; A=125-391.
DR PDB; 2W1C; X-ray; 3.24 A; A=122-389.
DR PDB; 2W1D; X-ray; 2.97 A; A=122-389.
DR PDB; 2W1E; X-ray; 2.93 A; A=122-389.
DR PDB; 2W1F; X-ray; 2.85 A; A=122-389.
DR PDB; 2W1G; X-ray; 2.71 A; A=122-389.
DR PDB; 2WQE; X-ray; 2.50 A; A=127-388.
DR PDB; 2WTV; X-ray; 2.40 A; A/B/C/D=122-403.
DR PDB; 2WTW; X-ray; 3.30 A; A=122-403.
DR PDB; 2X6D; X-ray; 2.80 A; A=122-403.
DR PDB; 2X6E; X-ray; 3.35 A; A=122-403.
DR PDB; 2X81; X-ray; 2.91 A; A=126-391.
DR PDB; 2XNE; X-ray; 2.80 A; A=122-392.
DR PDB; 2XNG; X-ray; 2.60 A; A=122-403.
DR PDB; 2XRU; X-ray; 2.90 A; A=126-403.
DR PDB; 3COH; X-ray; 2.70 A; A/B=124-391.
DR PDB; 3E5A; X-ray; 2.30 A; A=125-391.
DR PDB; 3EFW; X-ray; 2.29 A; A/B=125-391.
DR PDB; 3FDN; X-ray; 1.90 A; A=123-401.
DR PDB; 3H0Y; X-ray; 2.50 A; A=124-391.
DR PDB; 3H0Z; X-ray; 2.92 A; A/B/C=124-391.
DR PDB; 3H10; X-ray; 2.20 A; A/B/D=124-391.
DR PDB; 3HA6; X-ray; 2.36 A; A=125-391.
DR PDB; 3K5U; X-ray; 2.35 A; A=123-401.
DR PDB; 3LAU; X-ray; 2.10 A; A=125-399.
DR PDB; 3M11; X-ray; 2.75 A; A=123-401.
DR PDB; 3MYG; X-ray; 2.40 A; A=125-391.
DR PDB; 3NRM; X-ray; 3.05 A; A=126-403.
DR PDB; 3O50; X-ray; 2.00 A; A/B=125-391.
DR PDB; 3O51; X-ray; 3.20 A; A=125-391.
DR PDB; 3P9J; X-ray; 2.80 A; A=125-391.
DR PDB; 3QBN; X-ray; 3.50 A; A=124-403.
DR PDB; 3R21; X-ray; 2.90 A; A=126-391.
DR PDB; 3R22; X-ray; 2.90 A; A=126-391.
DR PDB; 3UNZ; X-ray; 2.80 A; A/B=123-401.
DR PDB; 3UO4; X-ray; 2.45 A; A=123-401.
DR PDB; 3UO5; X-ray; 2.70 A; A=123-401.
DR PDB; 3UO6; X-ray; 2.80 A; A/B=123-401.
DR PDB; 3UOD; X-ray; 2.50 A; A=123-401.
DR PDB; 3UOH; X-ray; 2.80 A; A/B=123-401.
DR PDB; 3UOJ; X-ray; 2.90 A; A/B=123-401.
DR PDB; 3UOK; X-ray; 2.95 A; A/B=123-401.
DR PDB; 3UOL; X-ray; 2.40 A; A/B=123-401.
DR PDB; 3UP2; X-ray; 2.30 A; A=123-401.
DR PDB; 3UP7; X-ray; 3.05 A; A=123-401.
DR PDB; 3VAP; X-ray; 2.66 A; A=125-391.
DR PDB; 3W10; X-ray; 2.70 A; A=126-403.
DR PDB; 3W16; X-ray; 2.80 A; A=126-403.
DR PDB; 3W18; X-ray; 2.50 A; A/B=126-403.
DR PDB; 3W2C; X-ray; 2.45 A; A/C/E/G=128-388.
DR PDB; 4B0G; X-ray; 2.50 A; A=122-403.
DR PDB; 4BN1; X-ray; 2.50 A; A=122-403.
DR PDB; 4BYI; X-ray; 2.60 A; A=122-403.
DR PDB; 4BYJ; X-ray; 2.75 A; A=122-403.
DR PDB; 4C3P; X-ray; 2.69 A; A/D=122-403.
DR PDB; 4C3R; X-ray; 2.79 A; A=122-403.
DR PDB; 4CEG; X-ray; 2.10 A; A=122-403.
DR PDB; 4DEA; X-ray; 2.45 A; A=123-401.
DR PDB; 4DEB; X-ray; 3.05 A; A=123-401.
DR PDB; 4DED; X-ray; 3.05 A; A=123-401.
DR PDB; 4DEE; X-ray; 2.30 A; A=123-401.
DR PDB; 4DHF; X-ray; 2.80 A; A/B=126-391.
DR PDB; 4J8M; X-ray; 1.85 A; A=123-401.
DR PDB; 4J8N; X-ray; 3.14 A; A/B/C/D=123-401.
DR PDB; 4JAI; X-ray; 3.20 A; A=122-396.
DR PDB; 4JAJ; X-ray; 2.70 A; A=122-396.
DR PDB; 4JBO; X-ray; 2.49 A; A=123-401.
DR PDB; 4JBP; X-ray; 2.45 A; A=123-401.
DR PDB; 4JBQ; X-ray; 2.30 A; A=123-401.
DR PDB; 4O0S; X-ray; 2.50 A; A=122-403.
DR PDB; 4O0U; X-ray; 2.60 A; A=122-403.
DR PDB; 4O0W; X-ray; 2.60 A; A=122-403.
DR PDB; 4PRJ; X-ray; 2.80 A; A=124-391.
DR PDB; 4UYN; X-ray; 1.90 A; A=125-399.
DR PDB; 4UZD; X-ray; 3.20 A; A/B=125-399.
DR PDB; 4UZH; X-ray; 2.00 A; A=125-399.
DR PDB; 4ZS0; X-ray; 3.00 A; A=122-403.
DR PDB; 4ZTQ; X-ray; 2.80 A; A=122-403.
DR PDB; 4ZTR; X-ray; 2.85 A; A=122-403.
DR PDB; 4ZTS; X-ray; 2.90 A; A=122-403.
DR PDB; 5AAD; X-ray; 3.10 A; A=122-403.
DR PDB; 5AAE; X-ray; 3.11 A; A=122-403.
DR PDB; 5AAF; X-ray; 2.78 A; A=122-403.
DR PDB; 5AAG; X-ray; 2.85 A; A=122-403.
DR PDB; 5DN3; X-ray; 2.05 A; A=125-391.
DR PDB; 5DNR; X-ray; 1.95 A; A=125-391.
DR PDB; 5DOS; X-ray; 2.98 A; A=126-390.
DR PDB; 5DPV; X-ray; 2.29 A; A=126-390.
DR PDB; 5DR2; X-ray; 2.46 A; A=128-390.
DR PDB; 5DR6; X-ray; 2.53 A; A=126-390.
DR PDB; 5DR9; X-ray; 2.47 A; A=126-390.
DR PDB; 5DRD; X-ray; 2.13 A; A=126-390.
DR PDB; 5DT0; X-ray; 2.15 A; A=126-390.
DR PDB; 5DT3; X-ray; 2.33 A; A=126-390.
DR PDB; 5DT4; X-ray; 2.86 A; A=126-390.
DR PDB; 5EW9; X-ray; 2.18 A; A=123-390.
DR PDB; 5G15; X-ray; 2.06 A; A=122-403.
DR PDB; 5G1X; X-ray; 1.72 A; A=122-403.
DR PDB; 5L8J; X-ray; 1.68 A; A=122-403.
DR PDB; 5L8K; X-ray; 1.79 A; A=122-403.
DR PDB; 5L8L; X-ray; 1.67 A; A=122-403.
DR PDB; 5LXM; X-ray; 2.08 A; A=122-403.
DR PDB; 5OBJ; X-ray; 2.90 A; A=125-391.
DR PDB; 5OBR; X-ray; 2.62 A; A=125-391.
DR PDB; 5ODT; X-ray; 2.02 A; A=122-403.
DR PDB; 5ONE; X-ray; 2.60 A; A=122-403.
DR PDB; 5ORL; X-ray; 1.69 A; A=127-391.
DR PDB; 5ORN; X-ray; 2.19 A; A=127-391.
DR PDB; 5ORO; X-ray; 2.12 A; A=127-391.
DR PDB; 5ORP; X-ray; 2.19 A; A=127-391.
DR PDB; 5ORR; X-ray; 2.09 A; A=127-391.
DR PDB; 5ORS; X-ray; 1.98 A; A=127-391.
DR PDB; 5ORT; X-ray; 2.56 A; A=127-391.
DR PDB; 5ORV; X-ray; 1.88 A; A=127-391.
DR PDB; 5ORW; X-ray; 2.00 A; A=127-391.
DR PDB; 5ORX; X-ray; 1.88 A; A=127-391.
DR PDB; 5ORY; X-ray; 1.99 A; A=127-391.
DR PDB; 5ORZ; X-ray; 1.92 A; A=127-391.
DR PDB; 5OS0; X-ray; 1.74 A; A=127-391.
DR PDB; 5OS1; X-ray; 1.90 A; A=127-391.
DR PDB; 5OS2; X-ray; 1.92 A; A=127-391.
DR PDB; 5OS3; X-ray; 1.81 A; A=127-391.
DR PDB; 5OS4; X-ray; 1.88 A; A=127-391.
DR PDB; 5OS5; X-ray; 1.74 A; A=125-392.
DR PDB; 5OS6; X-ray; 2.20 A; A=127-391.
DR PDB; 5OSD; X-ray; 1.99 A; A=125-391.
DR PDB; 5OSE; X-ray; 1.90 A; A=127-391.
DR PDB; 5OSF; X-ray; 1.89 A; A=127-391.
DR PDB; 5ZAN; X-ray; 2.85 A; A=123-403.
DR PDB; 6C2R; X-ray; 1.96 A; A=125-391.
DR PDB; 6C2T; X-ray; 1.73 A; A=125-391.
DR PDB; 6C83; X-ray; 2.55 A; A/B=122-403.
DR PDB; 6CPE; X-ray; 2.45 A; A=122-403.
DR PDB; 6CPF; X-ray; 2.30 A; A=122-403.
DR PDB; 6CPG; X-ray; 2.80 A; A/D=122-403.
DR PDB; 6GRA; X-ray; 2.60 A; A=122-403.
DR PDB; 6HJJ; X-ray; 2.13 A; A=122-403.
DR PDB; 6HJK; X-ray; 2.40 A; A=122-403.
DR PDB; 6I2U; X-ray; 2.50 A; A=122-403.
DR PDB; 6R49; X-ray; 2.21 A; A=122-403.
DR PDB; 6R4A; X-ray; 1.94 A; A=122-403.
DR PDB; 6R4B; X-ray; 2.15 A; A=122-403.
DR PDB; 6R4C; X-ray; 2.04 A; A=122-403.
DR PDB; 6R4D; X-ray; 2.01 A; A=122-403.
DR PDB; 6VPG; X-ray; 2.64 A; A=117-389.
DR PDB; 6VPH; X-ray; 2.14 A; A=117-389.
DR PDB; 6VPI; X-ray; 2.00 A; A=117-389.
DR PDB; 6VPJ; X-ray; 2.10 A; A=117-389.
DR PDB; 6VPL; X-ray; 1.86 A; A/B=117-389.
DR PDB; 6VPM; X-ray; 1.58 A; A/B=117-389.
DR PDB; 6XKA; X-ray; 2.65 A; A=117-389.
DR PDB; 6Z4Y; X-ray; 2.25 A; A=122-403.
DR PDB; 7AYH; X-ray; 2.80 A; A=122-403.
DR PDB; 7AYI; X-ray; 2.86 A; A=122-403.
DR PDB; 7O2V; X-ray; 3.10 A; A=116-403.
DR PDBsum; 1MQ4; -.
DR PDBsum; 1MUO; -.
DR PDBsum; 1OL5; -.
DR PDBsum; 1OL6; -.
DR PDBsum; 1OL7; -.
DR PDBsum; 2BMC; -.
DR PDBsum; 2C6D; -.
DR PDBsum; 2C6E; -.
DR PDBsum; 2DWB; -.
DR PDBsum; 2J4Z; -.
DR PDBsum; 2J50; -.
DR PDBsum; 2NP8; -.
DR PDBsum; 2W1C; -.
DR PDBsum; 2W1D; -.
DR PDBsum; 2W1E; -.
DR PDBsum; 2W1F; -.
DR PDBsum; 2W1G; -.
DR PDBsum; 2WQE; -.
DR PDBsum; 2WTV; -.
DR PDBsum; 2WTW; -.
DR PDBsum; 2X6D; -.
DR PDBsum; 2X6E; -.
DR PDBsum; 2X81; -.
DR PDBsum; 2XNE; -.
DR PDBsum; 2XNG; -.
DR PDBsum; 2XRU; -.
DR PDBsum; 3COH; -.
DR PDBsum; 3E5A; -.
DR PDBsum; 3EFW; -.
DR PDBsum; 3FDN; -.
DR PDBsum; 3H0Y; -.
DR PDBsum; 3H0Z; -.
DR PDBsum; 3H10; -.
DR PDBsum; 3HA6; -.
DR PDBsum; 3K5U; -.
DR PDBsum; 3LAU; -.
DR PDBsum; 3M11; -.
DR PDBsum; 3MYG; -.
DR PDBsum; 3NRM; -.
DR PDBsum; 3O50; -.
DR PDBsum; 3O51; -.
DR PDBsum; 3P9J; -.
DR PDBsum; 3QBN; -.
DR PDBsum; 3R21; -.
DR PDBsum; 3R22; -.
DR PDBsum; 3UNZ; -.
DR PDBsum; 3UO4; -.
DR PDBsum; 3UO5; -.
DR PDBsum; 3UO6; -.
DR PDBsum; 3UOD; -.
DR PDBsum; 3UOH; -.
DR PDBsum; 3UOJ; -.
DR PDBsum; 3UOK; -.
DR PDBsum; 3UOL; -.
DR PDBsum; 3UP2; -.
DR PDBsum; 3UP7; -.
DR PDBsum; 3VAP; -.
DR PDBsum; 3W10; -.
DR PDBsum; 3W16; -.
DR PDBsum; 3W18; -.
DR PDBsum; 3W2C; -.
DR PDBsum; 4B0G; -.
DR PDBsum; 4BN1; -.
DR PDBsum; 4BYI; -.
DR PDBsum; 4BYJ; -.
DR PDBsum; 4C3P; -.
DR PDBsum; 4C3R; -.
DR PDBsum; 4CEG; -.
DR PDBsum; 4DEA; -.
DR PDBsum; 4DEB; -.
DR PDBsum; 4DED; -.
DR PDBsum; 4DEE; -.
DR PDBsum; 4DHF; -.
DR PDBsum; 4J8M; -.
DR PDBsum; 4J8N; -.
DR PDBsum; 4JAI; -.
DR PDBsum; 4JAJ; -.
DR PDBsum; 4JBO; -.
DR PDBsum; 4JBP; -.
DR PDBsum; 4JBQ; -.
DR PDBsum; 4O0S; -.
DR PDBsum; 4O0U; -.
DR PDBsum; 4O0W; -.
DR PDBsum; 4PRJ; -.
DR PDBsum; 4UYN; -.
DR PDBsum; 4UZD; -.
DR PDBsum; 4UZH; -.
DR PDBsum; 4ZS0; -.
DR PDBsum; 4ZTQ; -.
DR PDBsum; 4ZTR; -.
DR PDBsum; 4ZTS; -.
DR PDBsum; 5AAD; -.
DR PDBsum; 5AAE; -.
DR PDBsum; 5AAF; -.
DR PDBsum; 5AAG; -.
DR PDBsum; 5DN3; -.
DR PDBsum; 5DNR; -.
DR PDBsum; 5DOS; -.
DR PDBsum; 5DPV; -.
DR PDBsum; 5DR2; -.
DR PDBsum; 5DR6; -.
DR PDBsum; 5DR9; -.
DR PDBsum; 5DRD; -.
DR PDBsum; 5DT0; -.
DR PDBsum; 5DT3; -.
DR PDBsum; 5DT4; -.
DR PDBsum; 5EW9; -.
DR PDBsum; 5G15; -.
DR PDBsum; 5G1X; -.
DR PDBsum; 5L8J; -.
DR PDBsum; 5L8K; -.
DR PDBsum; 5L8L; -.
DR PDBsum; 5LXM; -.
DR PDBsum; 5OBJ; -.
DR PDBsum; 5OBR; -.
DR PDBsum; 5ODT; -.
DR PDBsum; 5ONE; -.
DR PDBsum; 5ORL; -.
DR PDBsum; 5ORN; -.
DR PDBsum; 5ORO; -.
DR PDBsum; 5ORP; -.
DR PDBsum; 5ORR; -.
DR PDBsum; 5ORS; -.
DR PDBsum; 5ORT; -.
DR PDBsum; 5ORV; -.
DR PDBsum; 5ORW; -.
DR PDBsum; 5ORX; -.
DR PDBsum; 5ORY; -.
DR PDBsum; 5ORZ; -.
DR PDBsum; 5OS0; -.
DR PDBsum; 5OS1; -.
DR PDBsum; 5OS2; -.
DR PDBsum; 5OS3; -.
DR PDBsum; 5OS4; -.
DR PDBsum; 5OS5; -.
DR PDBsum; 5OS6; -.
DR PDBsum; 5OSD; -.
DR PDBsum; 5OSE; -.
DR PDBsum; 5OSF; -.
DR PDBsum; 5ZAN; -.
DR PDBsum; 6C2R; -.
DR PDBsum; 6C2T; -.
DR PDBsum; 6C83; -.
DR PDBsum; 6CPE; -.
DR PDBsum; 6CPF; -.
DR PDBsum; 6CPG; -.
DR PDBsum; 6GRA; -.
DR PDBsum; 6HJJ; -.
DR PDBsum; 6HJK; -.
DR PDBsum; 6I2U; -.
DR PDBsum; 6R49; -.
DR PDBsum; 6R4A; -.
DR PDBsum; 6R4B; -.
DR PDBsum; 6R4C; -.
DR PDBsum; 6R4D; -.
DR PDBsum; 6VPG; -.
DR PDBsum; 6VPH; -.
DR PDBsum; 6VPI; -.
DR PDBsum; 6VPJ; -.
DR PDBsum; 6VPL; -.
DR PDBsum; 6VPM; -.
DR PDBsum; 6XKA; -.
DR PDBsum; 6Z4Y; -.
DR PDBsum; 7AYH; -.
DR PDBsum; 7AYI; -.
DR PDBsum; 7O2V; -.
DR AlphaFoldDB; O14965; -.
DR BioGRID; 112666; 457.
DR CORUM; O14965; -.
DR DIP; DIP-33068N; -.
DR ELM; O14965; -.
DR IntAct; O14965; 184.
DR MINT; O14965; -.
DR STRING; 9606.ENSP00000216911; -.
DR BindingDB; O14965; -.
DR ChEMBL; CHEMBL4722; -.
DR DrugBank; DB07362; 1-(5-{2-[(1-methyl-1H-pyrazolo[4,3-d]pyrimidin-7-yl)amino]ethyl}-1,3-thiazol-2-yl)-3-[3-(trifluoromethyl)phenyl]urea.
DR DrugBank; DB07360; 1-{5-[2-(thieno[3,2-d]pyrimidin-4-ylamino)ethyl]-1,3-thiazol-2-yl}-3-[3-(trifluoromethyl)phenyl]urea.
DR DrugBank; DB08065; 2-(1H-pyrazol-3-yl)-1H-benzimidazole.
DR DrugBank; DB07186; 4-(4-METHYLPIPERAZIN-1-YL)-N-[5-(2-THIENYLACETYL)-1,5-DIHYDROPYRROLO[3,4-C]PYRAZOL-3-YL]BENZAMIDE.
DR DrugBank; DB07266; AKI-001.
DR DrugBank; DB05220; Alisertib.
DR DrugBank; DB05169; AT9283.
DR DrugBank; DB06347; Cenisertib.
DR DrugBank; DB05198; CYC116.
DR DrugBank; DB06486; Enzastaurin.
DR DrugBank; DB12010; Fostamatinib.
DR DrugBank; DB13061; MLN8054.
DR DrugBank; DB08066; N-[3-(1H-BENZIMIDAZOL-2-YL)-1H-PYRAZOL-4-YL]BENZAMIDE.
DR DrugBank; DB07801; N-butyl-3-{[6-(9H-purin-6-ylamino)hexanoyl]amino}benzamide.
DR DrugBank; DB07545; N-{3-[(4-{[3-(TRIFLUOROMETHYL)PHENYL]AMINO}PYRIMIDIN-2-YL)AMINO]PHENYL}CYCLOPROPANECARBOXAMIDE.
DR DrugBank; DB02482; Phosphonothreonine.
DR DrugBank; DB06134; SNS-314.
DR DrugCentral; O14965; -.
DR GuidetoPHARMACOLOGY; 1936; -.
DR iPTMnet; O14965; -.
DR PhosphoSitePlus; O14965; -.
DR BioMuta; AURKA; -.
DR CPTAC; CPTAC-1341; -.
DR EPD; O14965; -.
DR jPOST; O14965; -.
DR MassIVE; O14965; -.
DR MaxQB; O14965; -.
DR PaxDb; O14965; -.
DR PeptideAtlas; O14965; -.
DR PRIDE; O14965; -.
DR ProteomicsDB; 48339; -.
DR ABCD; O14965; 1 sequenced antibody.
DR Antibodypedia; 1129; 1081 antibodies from 47 providers.
DR DNASU; 6790; -.
DR Ensembl; ENST00000312783.10; ENSP00000321591.6; ENSG00000087586.18.
DR Ensembl; ENST00000347343.6; ENSP00000216911.2; ENSG00000087586.18.
DR Ensembl; ENST00000371356.6; ENSP00000360407.2; ENSG00000087586.18.
DR Ensembl; ENST00000395911.5; ENSP00000379247.1; ENSG00000087586.18.
DR Ensembl; ENST00000395913.7; ENSP00000379249.3; ENSG00000087586.18.
DR Ensembl; ENST00000395914.5; ENSP00000379250.1; ENSG00000087586.18.
DR Ensembl; ENST00000395915.8; ENSP00000379251.3; ENSG00000087586.18.
DR GeneID; 6790; -.
DR KEGG; hsa:6790; -.
DR MANE-Select; ENST00000395915.8; ENSP00000379251.3; NM_198437.3; NP_940839.1.
DR UCSC; uc002xxe.1; human.
DR CTD; 6790; -.
DR DisGeNET; 6790; -.
DR GeneCards; AURKA; -.
DR HGNC; HGNC:11393; AURKA.
DR HPA; ENSG00000087586; Tissue enhanced (lymphoid tissue, testis).
DR MalaCards; AURKA; -.
DR MIM; 603072; gene.
DR neXtProt; NX_O14965; -.
DR OpenTargets; ENSG00000087586; -.
DR PharmGKB; PA36201; -.
DR VEuPathDB; HostDB:ENSG00000087586; -.
DR eggNOG; KOG0580; Eukaryota.
DR GeneTree; ENSGT00940000154900; -.
DR InParanoid; O14965; -.
DR OrthoDB; 954262at2759; -.
DR PhylomeDB; O14965; -.
DR TreeFam; TF105331; -.
DR BRENDA; 2.7.11.1; 2681.
DR PathwayCommons; O14965; -.
DR Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-HSA-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-HSA-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
DR Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-HSA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-HSA-8854518; AURKA Activation by TPX2.
DR Reactome; R-HSA-8854521; Interaction between PHLDA1 and AURKA.
DR SignaLink; O14965; -.
DR SIGNOR; O14965; -.
DR BioGRID-ORCS; 6790; 685 hits in 1128 CRISPR screens.
DR ChiTaRS; AURKA; human.
DR EvolutionaryTrace; O14965; -.
DR GeneWiki; Aurora_A_kinase; -.
DR GenomeRNAi; 6790; -.
DR Pharos; O14965; Tchem.
DR PRO; PR:O14965; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; O14965; protein.
DR Bgee; ENSG00000087586; Expressed in oocyte and 158 other tissues.
DR ExpressionAtlas; O14965; baseline and differential.
DR Genevisible; O14965; HS.
DR GO; GO:0043203; C:axon hillock; IEA:Ensembl.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0032133; C:chromosome passenger complex; IBA:GO_Central.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0042585; C:germinal vesicle; IEA:Ensembl.
DR GO; GO:0072687; C:meiotic spindle; IEA:Ensembl.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:BHF-UCL.
DR GO; GO:0030496; C:midbody; TAS:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; IDA:HPA.
DR GO; GO:0097431; C:mitotic spindle pole; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
DR GO; GO:0045120; C:pronucleus; IEA:Ensembl.
DR GO; GO:0005819; C:spindle; TAS:UniProtKB.
DR GO; GO:0051233; C:spindle midzone; IBA:GO_Central.
DR GO; GO:0031616; C:spindle pole centrosome; IDA:BHF-UCL.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0035174; F:histone serine kinase activity; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:CAFA.
DR GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IMP:UniProtKB.
DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; TAS:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0009948; P:anterior/posterior axis specification; IEA:Ensembl.
DR GO; GO:0006915; P:apoptotic process; IEA:Ensembl.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051642; P:centrosome localization; IEA:Ensembl.
DR GO; GO:0061523; P:cilium disassembly; IMP:UniProtKB.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0097421; P:liver regeneration; IDA:MGI.
DR GO; GO:0000278; P:mitotic cell cycle; TAS:ProtInc.
DR GO; GO:0007100; P:mitotic centrosome separation; IEA:Ensembl.
DR GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0032091; P:negative regulation of protein binding; IDA:UniProtKB.
DR GO; GO:1990138; P:neuron projection extension; IEA:Ensembl.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IMP:UniProtKB.
DR GO; GO:0090141; P:positive regulation of mitochondrial fission; IMP:UniProtKB.
DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; TAS:UniProtKB.
DR GO; GO:1900195; P:positive regulation of oocyte maturation; IEA:Ensembl.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR GO; GO:0046777; P:protein autophosphorylation; TAS:UniProtKB.
DR GO; GO:0071539; P:protein localization to centrosome; IEA:Ensembl.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0046605; P:regulation of centrosome cycle; TAS:UniProtKB.
DR GO; GO:0032465; P:regulation of cytokinesis; IBA:GO_Central.
DR GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0031647; P:regulation of protein stability; IMP:UniProtKB.
DR GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
DR GO; GO:0009611; P:response to wounding; IDA:MGI.
DR GO; GO:0007057; P:spindle assembly involved in female meiosis I; IEA:Ensembl.
DR GO; GO:0007051; P:spindle organization; IMP:UniProtKB.
DR CDD; cd14116; STKc_Aurora-A; 1.
DR InterPro; IPR030616; Aur.
DR InterPro; IPR030611; AURKA.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24350; PTHR24350; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell cycle; Cell division; Cell projection;
KW Cilium; Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton;
KW Isopeptide bond; Kinase; Microtubule; Mitosis; Nucleotide-binding;
KW Phosphoprotein; Proto-oncogene; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Ubl conjugation.
FT CHAIN 1..403
FT /note="Aurora kinase A"
FT /id="PRO_0000086692"
FT DOMAIN 133..383
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..293
FT /note="Activation segment"
FT /evidence="ECO:0000269|PubMed:14580337"
FT COMPBIAS 28..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 256
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027,
FT ECO:0000269|PubMed:14580337"
FT BINDING 143
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:27837025,
FT ECO:0007744|PDB:5G1X"
FT BINDING 162
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:27837025,
FT ECO:0007744|PDB:5G1X"
FT BINDING 211..213
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:27837025,
FT ECO:0007744|PDB:5G1X"
FT BINDING 260..261
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:27837025,
FT ECO:0007744|PDB:5G1X"
FT BINDING 274
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:27837025,
FT ECO:0007744|PDB:5G1X"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17229885"
FT MOD_RES 287
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:14580337,
FT ECO:0000269|PubMed:19668197"
FT MOD_RES 288
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:11039908,
FT ECO:0000269|PubMed:13678582, ECO:0000269|PubMed:14580337,
FT ECO:0000269|PubMed:16246726, ECO:0000269|PubMed:18662907,
FT ECO:0000269|PubMed:19668197, ECO:0000269|PubMed:26246606"
FT MOD_RES 342
FT /note="Phosphoserine; by PKA and PAK"
FT /evidence="ECO:0000269|PubMed:16246726"
FT CROSSLNK 258
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 11
FT /note="G -> R (in dbSNP:rs6069717)"
FT /id="VAR_030840"
FT VARIANT 31
FT /note="F -> I (in dbSNP:rs2273535)"
FT /evidence="ECO:0000269|PubMed:15867347,
FT ECO:0000269|PubMed:16011022, ECO:0000269|PubMed:16762494,
FT ECO:0000269|PubMed:17344846, ECO:0000269|PubMed:9771714"
FT /id="VAR_030841"
FT VARIANT 50
FT /note="P -> L (in dbSNP:rs34572020)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041127"
FT VARIANT 57
FT /note="I -> V (increased kinase activity; dbSNP:rs1047972)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:15867347, ECO:0000269|PubMed:16011022,
FT ECO:0000269|PubMed:17344846, ECO:0000269|PubMed:9153231,
FT ECO:0000269|PubMed:9514916, ECO:0000269|PubMed:9771714"
FT /id="VAR_030842"
FT VARIANT 104
FT /note="S -> L (in dbSNP:rs2230743)"
FT /id="VAR_061745"
FT VARIANT 155
FT /note="S -> R (in a colorectal adenocarcinoma sample;
FT somatic mutation; reduces interaction with TPX2)"
FT /evidence="ECO:0000269|PubMed:17344846,
FT ECO:0000269|PubMed:19801554"
FT /id="VAR_041128"
FT VARIANT 174
FT /note="V -> M (in a metastatic melanoma sample; somatic
FT mutation; constitutively enhanced kinase activity)"
FT /evidence="ECO:0000269|PubMed:17344846,
FT ECO:0000269|PubMed:19801554"
FT /id="VAR_041129"
FT VARIANT 373
FT /note="M -> V (in dbSNP:rs33923703)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041130"
FT MUTAGEN 162
FT /note="K->R: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:14702041"
FT MUTAGEN 165
FT /note="F->A: Decreases the interaction with phosphatase
FT type 1 isoforms."
FT /evidence="ECO:0000269|PubMed:11551964"
FT MUTAGEN 198
FT /note="G->N: Reduces interaction with TPX2. Reduces kinase
FT activity tenfold. Promotes interaction with the AURKB
FT binding partners INCENP and BIRC5 that are normally not
FT bound by AURKA."
FT /evidence="ECO:0000269|PubMed:19357306"
FT MUTAGEN 205
FT /note="R->A: Reduces ubiquitination and proteasomal
FT degradation."
FT /evidence="ECO:0000269|PubMed:10851084"
FT MUTAGEN 274
FT /note="D->N: Abolishes autophosphorylation."
FT /evidence="ECO:0000269|PubMed:14580337"
FT MUTAGEN 287
FT /note="T->A: No direct effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:19668197"
FT MUTAGEN 287
FT /note="T->E: Enhances interaction with TPX2."
FT /evidence="ECO:0000269|PubMed:19668197"
FT MUTAGEN 288
FT /note="T->D: Mimics phosphorylation state and increases
FT kinase activity."
FT /evidence="ECO:0000269|PubMed:11039908"
FT MUTAGEN 290
FT /note="C->A: Enhances stability; when associated with A-
FT 393."
FT /evidence="ECO:0000269|PubMed:27837025"
FT MUTAGEN 334
FT /note="Y->A: Reduces binding to MYCN."
FT /evidence="ECO:0000269|PubMed:27837025"
FT MUTAGEN 335
FT /note="Q->A: Reduces binding to MYCN."
FT /evidence="ECO:0000269|PubMed:27837025"
FT MUTAGEN 346
FT /note="F->A: Decreases the interaction with phosphatase
FT type 1 isoforms."
FT /evidence="ECO:0000269|PubMed:11551964"
FT MUTAGEN 393
FT /note="C->A: Enhances stability; when associated with A-
FT 290."
FT /evidence="ECO:0000269|PubMed:27837025"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:6VPM"
FT STRAND 133..141
FT /evidence="ECO:0007829|PDB:6VPM"
FT STRAND 143..152
FT /evidence="ECO:0007829|PDB:6VPM"
FT TURN 153..156
FT /evidence="ECO:0007829|PDB:6VPM"
FT STRAND 157..165
FT /evidence="ECO:0007829|PDB:6VPM"
FT HELIX 166..172
FT /evidence="ECO:0007829|PDB:6VPM"
FT HELIX 175..185
FT /evidence="ECO:0007829|PDB:6VPM"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:3UO6"
FT STRAND 196..201
FT /evidence="ECO:0007829|PDB:6VPM"
FT STRAND 203..210
FT /evidence="ECO:0007829|PDB:6VPM"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:2J50"
FT HELIX 218..225
FT /evidence="ECO:0007829|PDB:6VPM"
FT HELIX 230..249
FT /evidence="ECO:0007829|PDB:6VPM"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:6XKA"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:6VPM"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:6VPM"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:3UOL"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:6VPM"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:5ORL"
FT STRAND 280..283
FT /evidence="ECO:0007829|PDB:5L8L"
FT HELIX 288..291
FT /evidence="ECO:0007829|PDB:6VPM"
FT HELIX 293..295
FT /evidence="ECO:0007829|PDB:5L8J"
FT HELIX 298..302
FT /evidence="ECO:0007829|PDB:6VPM"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:6VPM"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:6C2T"
FT HELIX 310..324
FT /evidence="ECO:0007829|PDB:6VPM"
FT HELIX 334..342
FT /evidence="ECO:0007829|PDB:6VPM"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:1OL6"
FT HELIX 354..363
FT /evidence="ECO:0007829|PDB:6VPM"
FT HELIX 368..370
FT /evidence="ECO:0007829|PDB:6VPM"
FT HELIX 374..378
FT /evidence="ECO:0007829|PDB:6VPM"
FT HELIX 381..386
FT /evidence="ECO:0007829|PDB:6VPM"
SQ SEQUENCE 403 AA; 45823 MW; 7C2E7B438D969187 CRC64;
MDRSKENCIS GPVKATAPVG GPKRVLVTQQ FPCQNPLPVN SGQAQRVLCP SNSSQRIPLQ
AQKLVSSHKP VQNQKQKQLQ ATSVPHPVSR PLNNTQKSKQ PLPSAPENNP EEELASKQKN
EESKKRQWAL EDFEIGRPLG KGKFGNVYLA REKQSKFILA LKVLFKAQLE KAGVEHQLRR
EVEIQSHLRH PNILRLYGYF HDATRVYLIL EYAPLGTVYR ELQKLSKFDE QRTATYITEL
ANALSYCHSK RVIHRDIKPE NLLLGSAGEL KIADFGWSVH APSSRRTTLC GTLDYLPPEM
IEGRMHDEKV DLWSLGVLCY EFLVGKPPFE ANTYQETYKR ISRVEFTFPD FVTEGARDLI
SRLLKHNPSQ RPMLREVLEH PWITANSSKP SNCQNKESAS KQS
