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 29-MAY-2024, entry version 247. DE RecName: Full=Aurora kinase A {ECO:0000312|HGNC:HGNC:11393}; 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 {ECO:0000303|PubMed:10851084}; DE AltName: Full=Aurora/IPL1-related kinase 1 {ECO:0000303|PubMed:9153231}; DE Short=ARK-1 {ECO:0000303|PubMed:9153231}; DE Short=Aurora-related kinase 1 {ECO:0000303|PubMed:9514916}; DE AltName: Full=Breast tumor-amplified kinase {ECO:0000303|PubMed:11790771}; DE AltName: Full=Ipl1- and aurora-related kinase 1 {ECO:0000250|UniProtKB:P97477}; DE AltName: Full=Serine/threonine-protein kinase 15 {ECO:0000303|PubMed:15867347, ECO:0000303|PubMed:16011022}; DE AltName: Full=Serine/threonine-protein kinase 6 {ECO:0000303|PubMed:9771714}; DE AltName: Full=Serine/threonine-protein kinase Ayk1 {ECO:0000250|UniProtKB:P97477}; DE AltName: Full=Serine/threonine-protein kinase aurora-A {ECO:0000250|UniProtKB:P59241}; GN Name=AURKA {ECO:0000312|HGNC:HGNC:11393}; GN Synonyms=AIK {ECO:0000303|PubMed:9153231}, GN AIRK1 {ECO:0000312|HGNC:HGNC:11393}, ARK1 {ECO:0000312|HGNC:HGNC:11393}, GN AURA {ECO:0000312|HGNC:HGNC:11393}, AYK1 {ECO:0000250|UniProtKB:P97477}, GN BTAK {ECO:0000303|PubMed:9771714}, IAK1 {ECO:0000250|UniProtKB:P97477}, GN STK15 {ECO:0000303|PubMed:15867347, ECO:0000303|PubMed:16011022}, GN STK6 {ECO:0000303|PubMed:9771714}; 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, INTERACTION WITH HDAC6, SUBCELLULAR LOCATION, AND MUTAGENESIS OF RP ASP-274 AND THR-288. 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 CIMAP3, AND ACTIVATION BY CIMAP3. 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 IDENTIFICATION IN A COMPLEX WITH AUNIP AND NIN. 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 IDENTIFICATION IN A COMPLEX WITH NEDD9 AND CTTN. RX PubMed=24574519; DOI=10.1158/1541-7786.mcr-13-0654; RA Kozyreva V.K., McLaughlin S.L., Livengood R.H., Calkins R.A., Kelley L.C., RA Rajulapati A., Ice R.J., Smolkin M.B., Weed S.A., Pugacheva E.N.; RT "NEDD9 regulates actin dynamics through cortactin deacetylation in an RT AURKA/HDAC6-dependent manner."; RL Mol. Cancer Res. 12:681-693(2014). RN [71] 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:11039908, PubMed:12390251, CC PubMed:17125279, PubMed:17360485, PubMed:18615013, PubMed:26246606). 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:14523000, CC PubMed:26246606). 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:11551964, PubMed:14702041, PubMed:15128871, CC PubMed:15147269, PubMed:15987997, PubMed:17604723, PubMed:18056443, 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). Inhibits cilia CC outgrowth (By similarity). Required for cilia disassembly via CC phosphorylation of HDAC6 and subsequent deacetylation of alpha-tubulin CC (PubMed:17604723, PubMed:20643351). Regulates protein levels of the CC anti-apoptosis protein BIRC5 by suppressing the expression of the CC SCF(FBXL7) E3 ubiquitin-protein ligase substrate adapter FBXL7 through CC the phosphorylation of the transcription factor FOXP1 CC (PubMed:28218735). {ECO:0000250|UniProtKB:A0A8I3S724, 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 CIMAP3. 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: Part of a complex composed of NEDD9, AURKA and CTTN; within CC the complex NEDD9 acts as a scaffold protein and is required for CC complex formation (PubMed:24574519). Identified in a complex with AUNIP CC and NIN (PubMed:20596670). Interacts with FBXL7 (By similarity). CC Interacts with CPEB1, JTB, TACC1, TPX2, PPP2CA, as well as with the CC protein phosphatase type 1 (PP1) isoforms PPP1CA, PPP1CB and PPP1CC CC (PubMed:11551964, PubMed:14580337, PubMed:14603251, PubMed:15966895, CC PubMed:17229885, PubMed:18662907, PubMed:19357306, PubMed:19668197, CC PubMed:19801554, PubMed:21225229, PubMed:27837025). Interacts also with CC its substrates ARHGEF2, BORA, KIF2A, PARD3, and p53/TP53 CC (PubMed:14702041, PubMed:16890155, PubMed:17488622, PubMed:19351716, CC PubMed:19812038). Interaction with BORA promotes phosphorylation of CC PLK1 (By similarity). Interacts with CIMAP3 (PubMed:20643351). CC Interacts with GADD45A, competing with its oligomerization CC (PubMed:20460379). Interacts (via C-terminus) with AUNIP (via C- CC terminus) (PubMed:20596670). Interacts with FRY; this interaction CC facilitates AURKA-mediated PLK1 phosphorylation (PubMed:22753416). CC Interacts with SIRT2 (PubMed:17726514, PubMed:22014574). Interacts with CC MYCN; interaction is phospho-independent and triggers AURKA activation; CC AURKA competes with FBXW7 for binding to unphosphorylated MYCN but not CC for binding to phosphorylated MYCN (PubMed:27837025). Interacts with CC HNRNPU (PubMed:21242313, PubMed:25986610). Interacts with AAAS CC (PubMed:26246606). Interacts with KLHL18 and CUL3 (PubMed:23213400). CC Interacts with FOXP1 (PubMed:28218735). Interacts with HDAC6; AURKA- CC mediated phosphorylation of HDAC6 promotes deacetylation of alpha- CC tubulin (PubMed:17604723). {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:17604723, 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:24574519, 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; Q6PGQ7: BORA; NbExp=3; IntAct=EBI-448680, EBI-719836; 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, microtubule CC organizing center, centrosome, centriole CC {ECO:0000250|UniProtKB:P97477}. Cell projection, neuron projection CC {ECO:0000250|UniProtKB:P97477}. Cell projection, cilium CC {ECO:0000269|PubMed:17604723}. Cytoplasm, cytoskeleton, cilium basal CC body {ECO:0000269|PubMed:17604723}. Basolateral cell membrane CC {ECO:0000250|UniProtKB:F1PNY0}. 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:17229885, CC PubMed:21225229, PubMed:9606188). 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="https://atlasgeneticsoncology.org/gene/730/AURKA"; 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; 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; 7FIC; X-ray; 2.32 A; A=127-391. DR PDB; 7O2V; X-ray; 3.10 A; A=116-403. DR PDB; 7ZTL; X-ray; 1.90 A; A=122-403. DR PDB; 8C14; X-ray; 1.93 A; A=125-391. DR PDB; 8C15; X-ray; 2.41 A; A=126-388. DR PDB; 8C1D; X-ray; 2.12 A; A=126-388. DR PDB; 8C1E; X-ray; 2.80 A; A=125-391. DR PDB; 8C1F; X-ray; 1.92 A; A=126-388. DR PDB; 8C1G; X-ray; 1.96 A; A=126-388. DR PDB; 8C1H; X-ray; 2.23 A; A=126-388. DR PDB; 8C1I; X-ray; 2.81 A; A=126-388. DR PDB; 8C1K; X-ray; 2.43 A; A=126-390. DR PDB; 8C1M; X-ray; 2.84 A; A=125-391. DR PDB; 8GUW; X-ray; 2.70 A; A/B/C=123-403. DR PDB; 8JF4; X-ray; 2.89 A; A=127-389. DR PDB; 8JMX; X-ray; 2.95 A; A=127-389. DR PDB; 8SSO; X-ray; 1.97 A; A/D=122-403. DR PDB; 8SSP; X-ray; 2.60 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; 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; 7FIC; -. DR PDBsum; 7O2V; -. DR PDBsum; 7ZTL; -. DR PDBsum; 8C14; -. DR PDBsum; 8C15; -. DR PDBsum; 8C1D; -. DR PDBsum; 8C1E; -. DR PDBsum; 8C1F; -. DR PDBsum; 8C1G; -. DR PDBsum; 8C1H; -. DR PDBsum; 8C1I; -. DR PDBsum; 8C1K; -. DR PDBsum; 8C1M; -. DR PDBsum; 8GUW; -. DR PDBsum; 8JF4; -. DR PDBsum; 8JMX; -. DR PDBsum; 8SSO; -. DR PDBsum; 8SSP; -. DR AlphaFoldDB; O14965; -. DR SMR; O14965; -. DR BioGRID; 112666; 688. DR CORUM; O14965; -. DR DIP; DIP-33068N; -. DR ELM; O14965; -. DR IntAct; O14965; 186. 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; DB12556; MK-5108. 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 GlyGen; O14965; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; O14965; -. DR PhosphoSitePlus; O14965; -. DR BioMuta; AURKA; -. DR CPTAC; CPTAC-1341; -. DR CPTAC; CPTAC-3083; -. DR CPTAC; CPTAC-3084; -. DR EPD; O14965; -. DR jPOST; O14965; -. DR MassIVE; O14965; -. DR MaxQB; O14965; -. DR PaxDb; 9606-ENSP00000216911; -. DR PeptideAtlas; O14965; -. DR ProteomicsDB; 48339; -. DR Pumba; O14965; -. DR ABCD; O14965; 7 sequenced antibodies. DR Antibodypedia; 1129; 1244 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 AGR; HGNC:11393; -. 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 OMA; HPWIAAH; -. DR OrthoDB; 117459at2759; -. 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; 713 hits in 1214 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 159 other cell types or tissues. DR ExpressionAtlas; O14965; baseline and differential. DR GO; GO:0043203; C:axon hillock; IEA:Ensembl. DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB. 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:0098978; C:glutamatergic synapse; IEA:Ensembl. DR GO; GO:0000776; C:kinetochore; IBA:GO_Central. 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: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:0014069; C:postsynaptic density; IEA:Ensembl. DR GO; GO:0045120; C:pronucleus; IEA:Ensembl. DR GO; GO:0005819; C:spindle; TAS:UniProtKB. DR GO; GO:0005876; C:spindle microtubule; IEA:TreeGrafter. 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:0035175; F:histone H3S10 kinase activity; IEA:Ensembl. DR GO; GO:0140677; F:molecular function activator activity; EXP:DisProt. 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:0045931; P:positive regulation of mitotic cell cycle; ISS: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 Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR030616; Aur-like. 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:SF5; AURORA KINASE A; 1. DR PANTHER; PTHR24350; SERINE/THREONINE-PROTEIN KINASE IAL-RELATED; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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 membrane; KW Cell projection; Cilium; Cilium biogenesis/degradation; Cytoplasm; KW Cytoskeleton; Isopeptide bond; Kinase; Membrane; Microtubule; Mitosis; KW Nucleotide-binding; 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 cilia disassembly and kinase FT activity." FT /evidence="ECO:0000269|PubMed:14580337, FT ECO:0000269|PubMed:17604723" 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->A: Reduces cilia disassembly and kinase FT activity." FT /evidence="ECO:0000269|PubMed:17604723" 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 //