ID AURKA_HUMAN Reviewed; 403 AA. AC O14965; E1P5F9; O60445; O75873; Q9BQD6; Q9UPG5; DT 27-JAN-2003, integrated into UniProtKB/Swiss-Prot. DT 27-JAN-2003, sequence version 2. DT 16-OCT-2019, entry version 222. DE RecName: Full=Aurora kinase A; DE EC=2.7.11.1 {ECO:0000269|PubMed:27837025}; 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; GN Synonyms=AIK, AIRK1, ARK1, AURA, AYK1, BTAK, IAK1, STK15, STK6; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, AND SUBCELLULAR LOCATION. 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 RT novel human protein kinase, Aik, related to Aurora of Drosophila and RT yeast Ipl1."; RL J. Biol. Chem. 272:13766-13771(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ILE-57. RX PubMed=9514916; DOI=10.1006/bbrc.1998.8250; RA Shindo M., Nakano H., Kuroyanagi H., Shirasawa T., Mihara M., RA Gilbert D.J., 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) RT 1 and 2."; RL Biochem. Biophys. Res. Commun. 244:285-292(1998). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ILE-31. 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., RA Brinkley B.R., 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., RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., RA 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., RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., RA 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., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP INDUCTION, FUNCTION, 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 RT kinase and protein phosphatase 1 through mitotic cell division RT 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., RA Ichikawa Y., Sasayama T., Kuninaka S., Mimori T., Tamaki N., RA Kimura M., Okano Y., Saya H.; RT "Roles of aurora-A kinase in mitotic entry and G2 checkpoint in RT mammalian 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 RT required 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., RA Saya H.; RT "Aurora-A kinase maintains the fidelity of early and late mitotic RT events in 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., RA Larroque C., 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 FUNCTION, INTERACTION WITH BRCA1, PHOSPHORYLATION AT THR-288, AND RP MUTAGENESIS OF LYS-162. 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 FUNCTION. RX PubMed=15128871; DOI=10.1242/jcs.01108; RA Dutertre S., Cazales M., Quaranta M., Froment C., Trabut V., RA Dozier C., Mirey G., Bouche J.P., Theis-Febvre N., Schmitt E., RA Monsarrat B., Prigent C., Ducommun B.; RT "Phosphorylation of CDC25B by Aurora-A at the centrosome contributes RT to the G2-M transition."; RL J. Cell Sci. 117:2523-2531(2004). RN [21] 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 RT destabilization and inhibition of p53."; RL Nat. Genet. 36:55-62(2004). RN [22] 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., RA Kohmura E., Saya H., Hirota T.; RT "Over-expression of Aurora-A targets cytoplasmic polyadenylation RT element binding protein and promotes mRNA polyadenylation of Cdk1 and RT cyclin B1."; RL Genes Cells 10:627-638(2005). RN [23] 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 [24] 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 RT HURP as a transforming target of Aurora-A."; RL Mol. Cell. Biol. 25:5789-5800(2005). RN [25] 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 RT partner Bora."; RL Dev. Cell 11:147-157(2006). RN [26] 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 RT of centrosome-dependent microtubule nucleation."; RL Cancer Res. 67:11186-11194(2007). RN [27] 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., RA Golemis E.A.; RT "HEF1-dependent Aurora A activation induces disassembly of the primary RT cilium."; RL Cell 129:1351-1363(2007). RN [28] 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., RA Bokoch G.M.; RT "GEF-H1 modulates localized RhoA activation during cytokinesis under RT the control of mitotic kinases."; RL Dev. Cell 12:699-712(2007). RN [29] 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 [30] 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 RT during mitosis."; RL PLoS ONE 2:E784-E784(2007). RN [31] 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 RT inhibitor of Aurora A kinase."; RL Proc. Natl. Acad. Sci. U.S.A. 104:4106-4111(2007). RN [32] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41, AND IDENTIFICATION RP BY 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 RT the kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [33] RP FUNCTION. RX PubMed=18615013; DOI=10.1038/nature07185; RA Macurek L., Lindqvist A., Lim D., Lampson M.A., Klompmaker R., RA Freire R., 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 [34] 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 RT 962 is mediated by aurora A and regulates its function in neuronal RT polarity."; RL J. Biol. Chem. 284:33571-33579(2009). RN [35] 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 [36] RP FUNCTION, INTERACTION WITH TPX2, PHOSPHORYLATION AT THR-287 AND RP THR-288, 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 RT elongation by modulation of microtubule dynamics."; RL Nat. Cell Biol. 11:1057-1068(2009). RN [37] RP INTERACTION WITH TPX2, MUTAGENESIS OF GLY-198, SUBCELLULAR LOCATION, RP AND FUNCTION. 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 RT kinase in terms of partner specificity and cellular function."; RL Proc. Natl. Acad. Sci. U.S.A. 106:6939-6944(2009). RN [38] 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 RT asymmetry."; RL Dev. Cell 19:66-77(2010). RN [39] 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 RT in centrosome structure and spindle formation."; RL Int. J. Oncol. 37:429-436(2010). RN [40] 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 RT antigen (PCNA) and Aurora A kinase."; RL J. Biol. Chem. 285:22196-22201(2010). RN [41] 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., RA Buerckstuemmer T., 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 [42] 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 [43] 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 [44] 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 [45] 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., RA Li C., Veenstra T.D., Li B., Yu H., Ji J., Wang X.W., Park S.H., RA Cha Y.I., 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 [46] 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- RT microtubule attachment and contributes to the targeting of Aurora-A to RT mitotic spindles."; RL J. Cell Sci. 124:394-404(2011). RN [47] RP INTERACTION WITH KLHL18 AND CUL3, UBIQUITINATION, AND SUBCELLULAR RP 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 RT Aurora-A."; RL Biol. Open 1:82-91(2012). RN [48] 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 RT activation."; RL J. Biol. Chem. 287:27670-27681(2012). RN [49] 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 RT spindle assembly."; RL Mol. Biol. Cell 26:1225-1237(2015). RN [50] 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 [51] 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 RT and in human cells."; RL J. Cell Sci. 129:3015-3025(2016). RN [52] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-258, AND IDENTIFICATION BY RP MASS 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- RT modification with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [53] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 107-403 IN COMPLEX WITH RP ADENOSINE, 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., RA Weber P., Lippke J.A., Austen D.A.; RT "Crystal structure of aurora-2, an oncogenic serine/threonine RT kinase."; RL J. Biol. Chem. 277:42419-42422(2002). RN [54] 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 RT kinases from nanovolume crystallography."; RL Structure 10:1659-1667(2002). RN [55] 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 RT spindle."; RL Mol. Cell 12:851-862(2003). RN [56] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 123-401 IN COMPLEXES WITH RP ADPNP AND 5-AMINOPYRIMIDINYL QUINAZOLINE INHIBITOR, AND CATALYTIC RP 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 [57] 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., RA Bindi S., Cameron A., Candiani I., Cappella P., Carpinelli P., RA Croci W., Forte B., Giorgini M.L., Klapwijk J., Marsiglio A., RA Pesenti E., Rocchetti M., Roletto F., Severino D., Soncini C., RA Storici P., Tonani R., Zugnoni P., 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 [58] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 125-391 IN COMPLEX WITH RP VX-680 AND TPX2, PHOSPHORYLATION AT THR-288, IDENTIFICATION BY MASS RP SPECTROMETRY, AND 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 RT binding: crystallography studies on Aurora A interactions with VX-680 RT and with TPX2."; RL Protein Sci. 17:1791-1797(2008). RN [59] 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 RT due to loss of interaction with TPX2."; RL J. Biol. Chem. 284:33177-33184(2009). RN [60] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 123-401 IN COMPLEX WITH RP SYNTHETIC 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., RA Wu S.Y., 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 [61] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 125-391 IN COMPLEX WITH RP SYNTHETIC 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., RA Liang J., Moffat J., Phillips G., Pulk R., Rawson T.E., Ultsch M., RA Walker L., Wiesmann C., Zhang B., Zhu B.Y., Cochran A.G.; RT "A class of 2,4-bisanilinopyrimidine Aurora A inhibitors with RT unusually high selectivity against Aurora B."; RL J. Med. Chem. 52:3300-3307(2009). RN [62] RP X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) OF 122-403 OF MUTANTS ALA-290 RP AND ALA-393 IN COMPLEX WITH ADP, INTERACTION WITH MYCN AND TPX2, RP MUTAGENESIS OF CYS-290; TYR-334; GLN-335 AND CYS-393, AND CATALYTIC RP ACTIVITY. RX PubMed=27837025; DOI=10.1073/pnas.1610626113; RA Richards M.W., Burgess S.G., Poon E., Carstensen A., Eilers M., RA Chesler L., Bayliss R.; RT "Structural basis of N-Myc binding by Aurora-A and its destabilization RT by kinase inhibitors."; RL Proc. Natl. Acad. Sci. U.S.A. 113:13726-13731(2016). RN [63] RP VARIANTS ILE-31 AND ILE-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 RT (Aurora-A) coordinately increase esophageal cancer risk."; RL Cancer Res. 65:3548-3554(2005). RN [64] RP VARIANTS ILE-31 AND ILE-57. RX PubMed=16011022; RA Chen L., Ao X., Ren Q., Wang Z.N., Lu C., Xu Y., Jiang L., Luo Y., RA Xu H.M., Zhang X.; RT "Linkage disequilibrium and haplotype analysis of two single RT nucleotide polymorphisms in STK15 in Chinese."; RL Yi Chuan Xue Bao 32:331-336(2005). RN [65] 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., RA Bartram C.R., Burwinkel B.; RT "Aurora kinases A and B and familial breast cancer risk."; RL Cancer Lett. 247:266-272(2007). RN [66] RP VARIANTS [LARGE SCALE ANALYSIS] ILE-31; LEU-50; ILE-57; ARG-155; RP MET-174 AND VAL-373. RX PubMed=17344846; DOI=10.1038/nature05610; RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., RA Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., RA O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., RA Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E., RA Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., RA Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., RA Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., RA West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., RA Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., RA DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., RA Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., RA Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.; RT "Patterns of somatic mutation in human cancer genomes."; RL Nature 446:153-158(2007). RN [67] RP FUNCTION, INTERACTION WITH AAAS, SUBCELLULAR LOCATION, AND RP PHOSPHORYLATION 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 RT robust 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). Associates CC with the centrosome and the spindle microtubules during mitosis CC and plays a critical role in various mitotic events including the CC establishment of mitotic spindle, centrosome duplication, CC centrosome separation as well as maturation, chromosomal CC alignment, spindle assembly checkpoint, and cytokinesis CC (PubMed:26246606). Required for normal spindle positioning during CC mitosis and for the localization of NUMA1 and DCTN1 to the cell CC cortex during metaphase (PubMed:27335426). Required for initial CC activation of CDK1 at centrosomes. Phosphorylates numerous target CC proteins, including ARHGEF2, BORA, BRCA1, CDC25B, DLGP5, HDAC6, CC KIF2A, LATS2, NDEL1, PARD3, PPP1R2, PLK1, RASSF1, TACC3, p53/TP53 CC and TPX2. Regulates KIF2A tubulin depolymerase activity. Required CC for normal axon formation. Plays a role in microtubule remodeling CC during neurite extension. Important for microtubule formation CC and/or stabilization. Also acts as a key regulatory component of CC the p53/TP53 pathway, and particularly the checkpoint-response CC pathways critical for oncogenic transformation of cells, by CC phosphorylating and stabilizing p53/TP53. Phosphorylates its own CC inhibitors, the protein phosphatase type 1 (PP1) isoforms, to CC inhibit their activity. Necessary for proper cilia disassembly CC prior to mitosis. {ECO:0000269|PubMed:11039908, CC ECO:0000269|PubMed:11551964, ECO:0000269|PubMed:12390251, CC ECO:0000269|PubMed:13678582, ECO:0000269|PubMed:14523000, CC ECO:0000269|PubMed:14702041, ECO:0000269|PubMed:14990569, 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:19357306, CC ECO:0000269|PubMed:19668197, ECO:0000269|PubMed:19812038, CC ECO:0000269|PubMed:20643351, ECO:0000269|PubMed:26246606, CC ECO:0000269|PubMed:27335426, ECO:0000269|PubMed:9606188}. 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, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, 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 -!- 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 -!- ACTIVITY REGULATION: Activation of CDK1, appears to be an upstream CC event of AURKA activation. Phosphatase inhibitor-2 (PPP1R2) and CC TPX2 act also as activators. Inactivated by the G2 checkpoint. CC Inhibited by GADD45A and p53/TP53, and through dephosphorylation CC by protein phosphatase type 1 (PP1). MLN8054 is also a potent and CC selective inhibitor. Activated during the early phase of cilia CC disassembly in the presence of PIFO. {ECO:0000269|PubMed:11039908, CC ECO:0000269|PubMed:12390251, ECO:0000269|PubMed:17360485}. CC -!- SUBUNIT: Interacts with FBXL7 (By similarity). Interacts with CC CPEB1, JTB, TACC1, TPX2, PPP2CA, as well as with the protein CC phosphatase type 1 (PP1) isoforms PPP1CA, PPP1CB and PPP1CC. CC Interacts also with its substrates ARHGEF2, BORA, BRCA1, KIF2A, CC PARD3, and p53/TP53. Interaction with BORA promotes CC phosphorylation of PLK1. Interacts with PIFO. Interacts with CC GADD45A, competing with its oligomerization. Interacts (via C- CC terminus) with AUNIP (via C-terminus). Identified in a complex CC with AUNIP and NIN. Interacts with FRY; this interaction CC facilitates AURKA-mediated PLK1 phosphorylation. Interacts with CC SIRT2 (PubMed:17726514, PubMed:22014574). Interacts with MYCN; CC interaction is phospho-independent and triggers AURKA activation; CC AURKA competes with FBXW7 for binding to unphosphorylated MYCN but CC not for binding to phosphorylated MYCN (PubMed:27837025). CC Interacts with HNRNPU (PubMed:21242313, PubMed:25986610). CC Interacts with AAAS (PubMed:26246606). Interacts with KLHL18 and CC CUL3 (PubMed:23213400). {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:14990569, ECO:0000269|PubMed:15966895, CC ECO:0000269|PubMed:16890155, ECO:0000269|PubMed:17229885, CC ECO:0000269|PubMed:17488622, ECO:0000269|PubMed:17726514, CC ECO:0000269|PubMed:18662907, ECO:0000269|PubMed:19140666, CC ECO:0000269|PubMed:19351716, ECO:0000269|PubMed:19357306, CC ECO:0000269|PubMed:19402633, ECO:0000269|PubMed:19668197, CC ECO:0000269|PubMed:19801554, ECO:0000269|PubMed:19812038, CC ECO:0000269|PubMed:20460379, ECO:0000269|PubMed:20596670, CC ECO:0000269|PubMed:20643351, ECO:0000269|PubMed:21225229, CC ECO:0000269|PubMed:21242313, ECO:0000269|PubMed:22014574, CC ECO:0000269|PubMed:22753416, ECO:0000269|PubMed:23213400, CC ECO:0000269|PubMed:25986610, ECO:0000269|PubMed:26246606, CC ECO:0000269|PubMed:27837025}. CC -!- INTERACTION: CC Q9NWT8:AURKAIP1; NbExp=2; IntAct=EBI-448680, EBI-448665; CC O15392:BIRC5; NbExp=2; IntAct=EBI-448680, EBI-518823; CC P00533:EGFR; NbExp=4; IntAct=EBI-448680, EBI-297353; CC P61978:HNRNPK; NbExp=2; IntAct=EBI-448680, EBI-304185; CC Q13123:IK; NbExp=3; IntAct=EBI-448680, EBI-713456; CC O14920:IKBKB; NbExp=2; IntAct=EBI-448680, EBI-81266; CC Q9NQS7:INCENP; NbExp=2; IntAct=EBI-448680, EBI-307907; CC Q9NQS7-1:INCENP; NbExp=2; IntAct=EBI-448680, EBI-15767972; CC P04198:MYCN; NbExp=12; IntAct=EBI-448680, EBI-878369; CC P06748:NPM1; NbExp=3; IntAct=EBI-448680, EBI-78579; CC P53350:PLK1; NbExp=4; IntAct=EBI-448680, EBI-476768; CC P23468:PTPRD; NbExp=2; IntAct=EBI-448680, EBI-2682990; CC Q8VDQ8:Sirt2 (xeno); NbExp=5; IntAct=EBI-448680, EBI-911012; CC Q96R06:SPAG5; NbExp=3; IntAct=EBI-448680, EBI-413317; CC O15350:TP73; NbExp=11; IntAct=EBI-448680, EBI-389606; CC Q9ULW0:TPX2; NbExp=8; IntAct=EBI-448680, EBI-1037322; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule CC organizing 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:9153231}. Cytoplasm, cytoskeleton, spindle pole CC {ECO:0000269|PubMed:12576638, ECO:0000269|PubMed:13678582, CC ECO:0000269|PubMed:17726514, ECO:0000269|PubMed:19351716, CC ECO:0000269|PubMed:25657325, ECO:0000269|PubMed:26246606, CC ECO:0000269|PubMed:9153231, ECO:0000269|PubMed:9606188}. CC Cytoplasm, cytoskeleton, cilium basal body CC {ECO:0000250|UniProtKB:P97477}. Cytoplasm, cytoskeleton, CC microtubule organizing center, centrosome, centriole CC {ECO:0000250|UniProtKB:P97477}. Cell projection, Neuron projection CC {ECO:0000250|UniProtKB:P97477}. Note=Detected at the neurite CC hillock in developing neurons (By similarity). Localizes at the CC centrosome in mitotic cells from early prophase until telophase, CC but also localizes to the spindle pole MTs from prophase to CC anaphase (PubMed:9606188, PubMed:17229885, PubMed:21225229). CC Colocalized with SIRT2 at centrosome (PubMed:22014574). Moves to CC the midbody during both telophase and cytokinesis CC (PubMed:17726514). Associates with both the pericentriolar CC material (PCM) and centrioles (PubMed:22014574). The localization CC to 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 CC skeletal muscle, thymus and spleen. Also highly expressed in CC colon, ovarian, prostate, neuroblastoma, breast and cervical CC cancer cell lines. CC -!- INDUCTION: Expression is cell-cycle regulated, low in G1/S, CC accumulates during G2/M, and decreases rapidly after. CC {ECO:0000269|PubMed:11790771, ECO:0000269|PubMed:12390251, CC ECO:0000269|PubMed:15987997, ECO:0000269|PubMed:9153231, CC 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. CC Phosphorylation at Thr-288 varies during the cell cycle and is CC highest during M phase. Autophosphorylated at Thr-288 upon TPX2 CC binding. Thr-288 can be phosphorylated by several kinases, CC including PAK and PKA. Protein phosphatase type 1 (PP1) binds CC AURKA and inhibits its activity by dephosphorylating Thr-288 CC during mitosis. Phosphorylation at Ser-342 decreases the kinase CC activity. PPP2CA controls degradation by dephosphorylating Ser-51 CC at the end of mitosis. {ECO:0000269|PubMed:11039908, CC ECO:0000269|PubMed:11551964, ECO:0000269|PubMed:12390251, CC ECO:0000269|PubMed:13678582, ECO:0000269|PubMed:14580337, CC ECO:0000269|PubMed:14990569, 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 CC proteasome (By similarity). Ubiquitinated by CHFR, leading to its CC degradation by the proteasome (By similarity). Ubiquitinated by CC the anaphase-promoting complex (APC), leading to its degradation CC by the proteasome (PubMed:10851084, PubMed:11039908). CC Ubiquitinated by the CUL3-KLHL18 ligase leading to its activation CC at the centrosome which is required for initiating mitotic entry CC (PubMed:23213400). Ubiquitination mediated by CUL3-KLHL18 ligase CC does not lead to its degradation by the proteasome CC (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 CC are uncoupled, and this amplification is associated with cancer CC and with an increase in the levels of chromosomal instability. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr CC protein 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 CC same protein. {ECO:0000305|PubMed:9771714}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA23592.1; Type=Frameshift; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology CC and Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/AURKAID730ch20q13.html"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 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 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; 6R49; -. DR PDBsum; 6R4A; -. DR PDBsum; 6R4B; -. DR PDBsum; 6R4C; -. DR PDBsum; 6R4D; -. DR SMR; O14965; -. DR BioGrid; 112666; 376. DR CORUM; O14965; -. DR DIP; DIP-33068N; -. DR ELM; O14965; -. DR IntAct; O14965; 174. 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; 8-ethyl-3,10,10-trimethyl-4,5,6,8,10,12-hexahydropyrazolo[4',3':6,7]cyclohepta[1,2-b]pyrrolo[2,3-f]indol-9(1H)-one. 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; -. DR DNASU; 6790; -. DR Ensembl; ENST00000312783; ENSP00000321591; ENSG00000087586. DR Ensembl; ENST00000347343; ENSP00000216911; ENSG00000087586. DR Ensembl; ENST00000371356; ENSP00000360407; ENSG00000087586. DR Ensembl; ENST00000395911; ENSP00000379247; ENSG00000087586. DR Ensembl; ENST00000395913; ENSP00000379249; ENSG00000087586. DR Ensembl; ENST00000395914; ENSP00000379250; ENSG00000087586. DR Ensembl; ENST00000395915; ENSP00000379251; ENSG00000087586. DR GeneID; 6790; -. DR KEGG; hsa:6790; -. DR UCSC; uc002xxe.1; human. DR CTD; 6790; -. DR DisGeNET; 6790; -. DR GeneCards; AURKA; -. DR HGNC; HGNC:11393; AURKA. DR HPA; CAB001454; -. DR HPA; HPA002636; -. DR MalaCards; AURKA; -. DR MIM; 603072; gene. DR neXtProt; NX_O14965; -. DR PharmGKB; PA36201; -. DR eggNOG; KOG0580; Eukaryota. DR eggNOG; ENOG410XNRB; LUCA. DR InParanoid; O14965; -. DR KO; K11481; -. DR OrthoDB; 1464823at2759; -. DR PhylomeDB; O14965; -. DR TreeFam; TF105331; -. DR BRENDA; 2.7.11.1; 2681. 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 ChiTaRS; AURKA; human. DR EvolutionaryTrace; O14965; -. DR GeneWiki; Aurora_A_kinase; -. DR GenomeRNAi; 6790; -. DR Pharos; O14965; -. DR PRO; PR:O14965; -. DR Proteomes; UP000005640; Chromosome 20. DR Bgee; ENSG00000087586; Expressed in 175 organ(s), highest expression level in oocyte. 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:0005929; C:cilium; IEA:UniProtKB-KW. DR GO; GO:0000780; C:condensed nuclear chromosome, centromeric region; IBA:GO_Central. 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:0015630; C:microtubule cytoskeleton; IDA:BHF-UCL. DR GO; GO:0030496; C:midbody; TAS:UniProtKB. DR GO; GO:0097431; C:mitotic spindle pole; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. 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:0005876; C:spindle microtubule; IBA:GO_Central. 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:0004674; F:protein serine/threonine kinase activity; EXP:Reactome. 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:0031145; P:anaphase-promoting complex-dependent catabolic process; TAS:Reactome. DR GO; GO:0009948; P:anterior/posterior axis specification; IEA:Ensembl. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0051642; P:centrosome localization; IEA:Ensembl. DR GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome. 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:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; TAS:Reactome. 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: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: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 GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; TAS:Reactome. 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; Complete proteome; Cytoplasm; KW Cytoskeleton; Isopeptide bond; Kinase; Microtubule; Mitosis; KW Nucleotide-binding; Phosphoprotein; Polymorphism; Proto-oncogene; KW Reference proteome; Serine/threonine-protein kinase; Transferase; KW Ubl conjugation. FT CHAIN 1 403 Aurora kinase A. FT /FTId=PRO_0000086692. FT DOMAIN 133 383 Protein kinase. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT NP_BIND 211 213 ATP. {ECO:0000244|PDB:5G1X, FT ECO:0000269|PubMed:27837025}. FT NP_BIND 260 261 ATP. {ECO:0000244|PDB:5G1X, FT ECO:0000269|PubMed:27837025}. FT REGION 280 293 Activation segment. FT {ECO:0000269|PubMed:14580337}. FT ACT_SITE 256 256 Proton acceptor. {ECO:0000255|PROSITE- FT ProRule:PRU00159, ECO:0000255|PROSITE- FT ProRule:PRU10027, FT ECO:0000269|PubMed:14580337}. FT BINDING 143 143 ATP; via amide nitrogen. FT {ECO:0000244|PDB:5G1X, FT ECO:0000269|PubMed:27837025}. FT BINDING 162 162 ATP. {ECO:0000244|PDB:5G1X, FT ECO:0000269|PubMed:27837025}. FT BINDING 274 274 ATP. {ECO:0000244|PDB:5G1X, FT ECO:0000269|PubMed:27837025}. FT MOD_RES 41 41 Phosphoserine. FT {ECO:0000244|PubMed:18691976}. FT MOD_RES 51 51 Phosphoserine. FT {ECO:0000269|PubMed:17229885}. FT MOD_RES 287 287 Phosphothreonine. FT {ECO:0000269|PubMed:14580337, FT ECO:0000269|PubMed:19668197}. FT MOD_RES 288 288 Phosphothreonine. FT {ECO:0000269|PubMed:11039908, FT ECO:0000269|PubMed:13678582, FT ECO:0000269|PubMed:14580337, FT ECO:0000269|PubMed:14990569, FT ECO:0000269|PubMed:16246726, FT ECO:0000269|PubMed:18662907, FT ECO:0000269|PubMed:19668197, FT ECO:0000269|PubMed:26246606}. FT MOD_RES 342 342 Phosphoserine; by PKA and PAK. FT {ECO:0000269|PubMed:16246726}. FT CROSSLNK 258 258 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:28112733}. FT VARIANT 11 11 G -> R (in dbSNP:rs6069717). FT /FTId=VAR_030840. FT VARIANT 31 31 F -> I (in dbSNP:rs2273535). FT {ECO:0000269|PubMed:15867347, FT ECO:0000269|PubMed:16011022, FT ECO:0000269|PubMed:16762494, FT ECO:0000269|PubMed:17344846, FT ECO:0000269|PubMed:9771714}. FT /FTId=VAR_030841. FT VARIANT 50 50 P -> L (in dbSNP:rs34572020). FT {ECO:0000269|PubMed:17344846}. FT /FTId=VAR_041127. FT VARIANT 57 57 V -> I (in dbSNP:rs1047972). FT {ECO:0000269|PubMed:15867347, FT ECO:0000269|PubMed:16011022, FT ECO:0000269|PubMed:17344846, FT ECO:0000269|PubMed:9514916}. FT /FTId=VAR_030842. FT VARIANT 104 104 S -> L (in dbSNP:rs2230743). FT /FTId=VAR_061745. FT VARIANT 155 155 S -> R (in a colorectal adenocarcinoma FT sample; somatic mutation; reduces FT interaction with TPX2). FT {ECO:0000269|PubMed:17344846, FT ECO:0000269|PubMed:19801554}. FT /FTId=VAR_041128. FT VARIANT 174 174 V -> M (in a metastatic melanoma sample; FT somatic mutation; constitutively enhanced FT kinase activity). FT {ECO:0000269|PubMed:17344846, FT ECO:0000269|PubMed:19801554}. FT /FTId=VAR_041129. FT VARIANT 373 373 M -> V (in dbSNP:rs33923703). FT {ECO:0000269|PubMed:17344846}. FT /FTId=VAR_041130. FT MUTAGEN 162 162 K->R: Loss of kinase activity. FT {ECO:0000269|PubMed:14702041, FT ECO:0000269|PubMed:14990569}. FT MUTAGEN 165 165 F->A: Decreases the interaction with FT phosphatase type 1 isoforms. FT {ECO:0000269|PubMed:11551964}. FT MUTAGEN 198 198 G->N: Reduces interaction with TPX2. FT Reduces kinase activity tenfold. Promotes FT interaction with the AURKB binding FT partners INCENP and BIRC5 that are FT normally not bound by AURKA. FT {ECO:0000269|PubMed:19357306}. FT MUTAGEN 205 205 R->A: Reduces ubiquitination and FT proteasomal degradation. FT {ECO:0000269|PubMed:10851084}. FT MUTAGEN 274 274 D->N: Abolishes autophosphorylation. FT {ECO:0000269|PubMed:14580337}. FT MUTAGEN 287 287 T->A: No direct effect on catalytic FT activity. {ECO:0000269|PubMed:19668197}. FT MUTAGEN 287 287 T->E: Enhances interaction with TPX2. FT {ECO:0000269|PubMed:19668197}. FT MUTAGEN 288 288 T->D: Mimics phosphorylation state and FT increases kinase activity. FT {ECO:0000269|PubMed:11039908}. FT MUTAGEN 290 290 C->A: Enhances stability; when associated FT with A-393. FT {ECO:0000269|PubMed:27837025}. FT MUTAGEN 334 334 Y->A: Reduces binding to MYCN. FT {ECO:0000269|PubMed:27837025}. FT MUTAGEN 335 335 Q->A: Reduces binding to MYCN. FT {ECO:0000269|PubMed:27837025}. FT MUTAGEN 346 346 F->A: Decreases the interaction with FT phosphatase type 1 isoforms. FT {ECO:0000269|PubMed:11551964}. FT MUTAGEN 393 393 C->A: Enhances stability; when associated FT with A-290. FT {ECO:0000269|PubMed:27837025}. FT HELIX 130 132 {ECO:0000244|PDB:5L8L}. FT STRAND 133 141 {ECO:0000244|PDB:5L8L}. FT STRAND 143 152 {ECO:0000244|PDB:5L8L}. FT TURN 153 155 {ECO:0000244|PDB:5L8L}. FT STRAND 158 165 {ECO:0000244|PDB:5L8L}. FT HELIX 166 171 {ECO:0000244|PDB:5L8L}. FT TURN 172 174 {ECO:0000244|PDB:6CPF}. FT HELIX 175 185 {ECO:0000244|PDB:5L8L}. FT STRAND 191 193 {ECO:0000244|PDB:3UO6}. FT STRAND 196 201 {ECO:0000244|PDB:5L8L}. FT STRAND 203 210 {ECO:0000244|PDB:5L8L}. FT STRAND 214 217 {ECO:0000244|PDB:2J50}. FT HELIX 218 225 {ECO:0000244|PDB:5L8L}. FT HELIX 230 249 {ECO:0000244|PDB:5L8L}. FT HELIX 259 261 {ECO:0000244|PDB:5L8L}. FT STRAND 262 264 {ECO:0000244|PDB:5L8L}. FT STRAND 266 268 {ECO:0000244|PDB:3UOL}. FT STRAND 270 272 {ECO:0000244|PDB:5L8L}. FT HELIX 275 277 {ECO:0000244|PDB:5ORL}. FT STRAND 280 283 {ECO:0000244|PDB:5L8L}. FT STRAND 287 289 {ECO:0000244|PDB:4J8M}. FT HELIX 290 292 {ECO:0000244|PDB:1MUO}. FT HELIX 293 295 {ECO:0000244|PDB:5L8J}. FT HELIX 298 302 {ECO:0000244|PDB:5L8L}. FT STRAND 304 306 {ECO:0000244|PDB:6C2T}. FT HELIX 307 309 {ECO:0000244|PDB:6C2T}. FT HELIX 310 324 {ECO:0000244|PDB:5L8L}. FT HELIX 334 342 {ECO:0000244|PDB:5L8L}. FT STRAND 350 352 {ECO:0000244|PDB:1OL6}. FT HELIX 354 363 {ECO:0000244|PDB:5L8L}. FT HELIX 368 370 {ECO:0000244|PDB:5L8L}. FT HELIX 374 378 {ECO:0000244|PDB:5L8L}. FT HELIX 381 386 {ECO:0000244|PDB:5L8L}. SQ SEQUENCE 403 AA; 45809 MW; 125F3594834CD157 CRC64; MDRSKENCIS GPVKATAPVG GPKRVLVTQQ FPCQNPLPVN SGQAQRVLCP SNSSQRVPLQ 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 //