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Aurora kinase A (EC 2.7.11.1) (Aurora 2) (Aurora/IPL1-related kinase 1) (ARK-1) (Aurora-related kinase 1) (hARK1) (Breast tumor-amplified kinase) (Serine/threonine-protein kinase 15) (Serine/threonine-protein kinase 6) (Serine/threonine-protein kinase aurora-A)

 AURKA_HUMAN             Reviewed;         403 AA.
O14965; E1P5F9; O60445; O75873; Q9BQD6; Q9UPG5;
27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
27-JAN-2003, sequence version 2.
30-AUG-2017, entry version 199.
RecName: Full=Aurora kinase A;
EC=2.7.11.1 {ECO:0000269|PubMed:27837025};
AltName: Full=Aurora 2;
AltName: Full=Aurora/IPL1-related kinase 1;
Short=ARK-1;
Short=Aurora-related kinase 1;
Short=hARK1;
AltName: Full=Breast tumor-amplified kinase;
AltName: Full=Serine/threonine-protein kinase 15;
AltName: Full=Serine/threonine-protein kinase 6;
AltName: Full=Serine/threonine-protein kinase aurora-A;
Name=AURKA;
Synonyms=AIK, AIRK1, ARK1, AURA, AYK1, BTAK, IAK1, STK15, STK6;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, AND SUBCELLULAR LOCATION.
TISSUE=Blood;
PubMed=9153231; DOI=10.1074/jbc.272.21.13766;
Kimura M., Kotani S., Hattori T., Sumi N., Yoshioka T., Todokoro K.,
Okano Y.;
"Cell cycle-dependent expression and spindle pole localization of a
novel human protein kinase, Aik, related to Aurora of Drosophila and
yeast Ipl1.";
J. Biol. Chem. 272:13766-13771(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ILE-57.
PubMed=9514916; DOI=10.1006/bbrc.1998.8250;
Shindo M., Nakano H., Kuroyanagi H., Shirasawa T., Mihara M.,
Gilbert D.J., Jenkins N.A., Copeland N.G., Yagita H., Okumura K.;
"cDNA cloning, expression, subcellular localization, and chromosomal
assignment of mammalian aurora homologues, aurora-related kinase (ARK)
1 and 2.";
Biochem. Biophys. Res. Commun. 244:285-292(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ILE-31.
TISSUE=Mammary gland;
PubMed=9771714; DOI=10.1038/2496;
Zhou H., Kuang J., Zhong L., Kuo W.-L., Gray J.W., Sahin A.,
Brinkley B.R., Sen S.;
"Tumour amplified kinase STK15/BTAK induces centrosome amplification,
aneuploidy and transformation.";
Nat. Genet. 20:189-193(1998).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Wang L., Thibodeau S.N.;
"Mutational analysis of the STK15 gene in human tumors.";
Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Cervix, Colon, Kidney, and Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
INDUCTION, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=9606188; DOI=10.1093/emboj/17.11.3052;
Bischoff J.R., Anderson L., Zhu Y., Mossie K., Ng L., Souza B.,
Schryver B., Flanagan P., Clairvoyant F., Ginther C., Chan C.S.,
Novotny M., Slamon D.J., Plowman G.D.;
"A homologue of Drosophila aurora kinase is oncogenic and amplified in
human colorectal cancers.";
EMBO J. 17:3052-3065(1998).
[9]
UBIQUITINATION, PROTEASOMAL DEGRADATION, AND MUTAGENESIS OF ARG-205.
PubMed=10851084; DOI=10.1038/sj.onc.1203609;
Honda K., Mihara H., Kato Y., Yamaguchi A., Tanaka H., Yasuda H.,
Furukawa K., Urano T.;
"Degradation of human Aurora2 protein kinase by the anaphase-promoting
complex-ubiquitin-proteasome pathway.";
Oncogene 19:2812-2819(2000).
[10]
FUNCTION, PHOSPHORYLATION AT THR-288, MUTAGENESIS OF THR-288,
UBIQUITINATION, AND ENZYME REGULATION.
PubMed=11039908; DOI=10.1038/sj.onc.1203847;
Walter A.O., Seghezzi W., Korver W., Sheung J., Lees E.;
"The mitotic serine/threonine kinase Aurora2/AIK is regulated by
phosphorylation and degradation.";
Oncogene 19:4906-4916(2000).
[11]
FUNCTION, INTERACTION WITH PPP1CA; PPP1CB AND PPP1CC, MUTAGENESIS OF
PHE-165 AND PHE-346, AND PHOSPHORYLATION.
PubMed=11551964; DOI=10.1074/jbc.M107540200;
Katayama H., Zhou H., Li Q., Tatsuka M., Sen S.;
"Interaction and feedback regulation between STK15/BTAK/Aurora-A
kinase and protein phosphatase 1 through mitotic cell division
cycle.";
J. Biol. Chem. 276:46219-46224(2001).
[12]
SUBCELLULAR LOCATION.
PubMed=12576638; DOI=10.1247/csf.27.457;
Sugimoto K., Urano T., Zushi H., Inoue K., Tasaka H., Tachibana M.,
Dotsu M.;
"Molecular dynamics of Aurora-A kinase in living mitotic cells
simultaneously visualized with histone H3 and nuclear membrane protein
importinalpha.";
Cell Struct. Funct. 27:457-467(2002).
[13]
FUNCTION, INDUCTION, PHOSPHORYLATION, AND ENZYME REGULATION.
PubMed=12390251; DOI=10.1046/j.1365-2443.2002.00592.x;
Marumoto T., Hirota T., Morisaki T., Kunitoku N., Zhang D.,
Ichikawa Y., Sasayama T., Kuninaka S., Mimori T., Tamaki N.,
Kimura M., Okano Y., Saya H.;
"Roles of aurora-A kinase in mitotic entry and G2 checkpoint in
mammalian cells.";
Genes Cells 7:1173-1182(2002).
[14]
INDUCTION.
PubMed=11790771; DOI=10.1074/jbc.M108252200;
Tanaka M., Ueda A., Kanamori H., Ideguchi H., Yang J., Kitajima S.,
Ishigatsubo Y.;
"Cell-cycle-dependent regulation of human aurora A transcription is
mediated by periodic repression of E4TF1.";
J. Biol. Chem. 277:10719-10726(2002).
[15]
FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT THR-288.
PubMed=13678582; DOI=10.1016/S0092-8674(03)00642-1;
Hirota T., Kunitoku N., Sasayama T., Marumoto T., Zhang D., Nitta M.,
Hatakeyama K., Saya H.;
"Aurora-A and an interacting activator, the LIM protein Ajuba, are
required for mitotic commitment in human cells.";
Cell 114:585-598(2003).
[16]
FUNCTION.
PubMed=14523000; DOI=10.1074/jbc.M306275200;
Marumoto T., Honda S., Hara T., Nitta M., Hirota T., Kohmura E.,
Saya H.;
"Aurora-A kinase maintains the fidelity of early and late mitotic
events in HeLa cells.";
J. Biol. Chem. 278:51786-51795(2003).
[17]
INTERACTION WITH TACC1.
PubMed=14603251; DOI=10.1038/sj.onc.1206972;
Conte N., Delaval B., Ginestier C., Ferrand A., Isnardon D.,
Larroque C., Prigent C., Seraphin B., Jacquemier J., Birnbaum D.;
"TACC1-chTOG-Aurora A protein complex in breast cancer.";
Oncogene 22:8102-8116(2003).
[18]
FUNCTION.
PubMed=15147269; DOI=10.1111/j.1356-9597.2004.00732.x;
Toji S., Yabuta N., Hosomi T., Nishihara S., Kobayashi T., Suzuki S.,
Tamai K., Nojima H.;
"The centrosomal protein Lats2 is a phosphorylation target of Aurora-A
kinase.";
Genes Cells 9:383-397(2004).
[19]
FUNCTION, INTERACTION WITH BRCA1, PHOSPHORYLATION AT THR-288, AND
MUTAGENESIS OF LYS-162.
PubMed=14990569; DOI=10.1074/jbc.M311780200;
Ouchi M., Fujiuchi N., Sasai K., Katayama H., Minamishima Y.A.,
Ongusaha P.P., Deng C., Sen S., Lee S.W., Ouchi T.;
"BRCA1 phosphorylation by Aurora-A in the regulation of G2 to M
transition.";
J. Biol. Chem. 279:19643-19648(2004).
[20]
FUNCTION.
PubMed=15128871; DOI=10.1242/jcs.01108;
Dutertre S., Cazales M., Quaranta M., Froment C., Trabut V.,
Dozier C., Mirey G., Bouche J.P., Theis-Febvre N., Schmitt E.,
Monsarrat B., Prigent C., Ducommun B.;
"Phosphorylation of CDC25B by Aurora-A at the centrosome contributes
to the G2-M transition.";
J. Cell Sci. 117:2523-2531(2004).
[21]
FUNCTION, MUTAGENESIS OF LYS-162, AND INTERACTION WITH TP53.
PubMed=14702041; DOI=10.1038/ng1279;
Katayama H., Sasai K., Kawai H., Yuan Z.M., Bondaruk J., Suzuki F.,
Fujii S., Arlinghaus R.B., Czerniak B.A., Sen S.;
"Phosphorylation by aurora kinase A induces Mdm2-mediated
destabilization and inhibition of p53.";
Nat. Genet. 36:55-62(2004).
[22]
INTERACTION WITH CPEB1.
PubMed=15966895; DOI=10.1111/j.1365-2443.2005.00870.x;
Sasayama T., Marumoto T., Kunitoku N., Zhang D., Tamaki N.,
Kohmura E., Saya H., Hirota T.;
"Over-expression of Aurora-A targets cytoplasmic polyadenylation
element binding protein and promotes mRNA polyadenylation of Cdk1 and
cyclin B1.";
Genes Cells 10:627-638(2005).
[23]
PHOSPHORYLATION AT THR-288 AND SER-342.
PubMed=16246726; DOI=10.1016/j.molcel.2005.08.035;
Zhao Z.S., Lim J.P., Ng Y.W., Lim L., Manser E.;
"The GIT-associated kinase PAK targets to the centrosome and regulates
Aurora-A.";
Mol. Cell 20:237-249(2005).
[24]
INDUCTION, AND FUNCTION.
PubMed=15987997; DOI=10.1128/MCB.25.14.5789-5800.2005;
Yu C.T., Hsu J.M., Lee Y.C., Tsou A.P., Chou C.K., Huang C.Y.;
"Phosphorylation and stabilization of HURP by Aurora-A: implication of
HURP as a transforming target of Aurora-A.";
Mol. Cell. Biol. 25:5789-5800(2005).
[25]
INTERACTION WITH BORA.
PubMed=16890155; DOI=10.1016/j.devcel.2006.06.002;
Hutterer A., Berdnik D., Wirtz-Peitz F., Zigman M., Schleiffer A.,
Knoblich J.A.;
"Mitotic activation of the kinase Aurora-A requires its binding
partner Bora.";
Dev. Cell 11:147-157(2006).
[26]
FUNCTION.
PubMed=18056443; DOI=10.1158/0008-5472.CAN-07-2578;
Sankaran S., Crone D.E., Palazzo R.E., Parvin J.D.;
"Aurora-A kinase regulates breast cancer associated gene 1 inhibition
of centrosome-dependent microtubule nucleation.";
Cancer Res. 67:11186-11194(2007).
[27]
FUNCTION.
PubMed=17604723; DOI=10.1016/j.cell.2007.04.035;
Pugacheva E.N., Jablonski S.A., Hartman T.R., Henske E.P.,
Golemis E.A.;
"HEF1-dependent Aurora A activation induces disassembly of the primary
cilium.";
Cell 129:1351-1363(2007).
[28]
INTERACTION WITH ARHGEF2.
PubMed=17488622; DOI=10.1016/j.devcel.2007.03.014;
Birkenfeld J., Nalbant P., Bohl B.P., Pertz O., Hahn K.M.,
Bokoch G.M.;
"GEF-H1 modulates localized RhoA activation during cytokinesis under
the control of mitotic kinases.";
Dev. Cell 12:699-712(2007).
[29]
SUBCELLULAR LOCATION, INTERACTION WITH PPP2CA, AND PHOSPHORYLATION AT
SER-51.
PubMed=17229885; DOI=10.1091/mbc.E06-12-1152;
Horn V., Thelu J., Garcia A., Albiges-Rizo C., Block M.R., Viallet J.;
"Functional interaction of Aurora-A and PP2A during mitosis.";
Mol. Biol. Cell 18:1233-1241(2007).
[30]
INTERACTION WITH SIRT2, AND SUBCELLULAR LOCATION.
PubMed=17726514; DOI=10.1371/journal.pone.0000784;
North B.J., Verdin E.;
"Interphase nucleo-cytoplasmic shuttling and localization of SIRT2
during mitosis.";
PLoS ONE 2:E784-E784(2007).
[31]
FUNCTION, AND ENZYME REGULATION.
PubMed=17360485; DOI=10.1073/pnas.0608798104;
Manfredi M.G., Ecsedy J.A., Meetze K.A., Balani S.K., Burenkova O.,
Chen W., Galvin K.M., Hoar K.M., Huck J.J., LeRoy P.J., Ray E.T.,
Sells T.B., Stringer B., Stroud S.G., Vos T.J., Weatherhead G.S.,
Wysong D.R., Zhang M., Bolen J.B., Claiborne C.F.;
"Antitumor activity of MLN8054, an orally active small-molecule
inhibitor of Aurora A kinase.";
Proc. Natl. Acad. Sci. U.S.A. 104:4106-4111(2007).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[33]
FUNCTION.
PubMed=18615013; DOI=10.1038/nature07185;
Macurek L., Lindqvist A., Lim D., Lampson M.A., Klompmaker R.,
Freire R., Clouin C., Taylor S.S., Yaffe M.B., Medema R.H.;
"Polo-like kinase-1 is activated by aurora A to promote checkpoint
recovery.";
Nature 455:119-123(2008).
[34]
FUNCTION, AUTOPHOSPHORYLATION, AND INTERACTION WITH PARD3.
PubMed=19812038; DOI=10.1074/jbc.M109.055897;
Khazaei M.R., Puschel A.W.;
"Phosphorylation of the par polarity complex protein Par3 at serine
962 is mediated by aurora A and regulates its function in neuronal
polarity.";
J. Biol. Chem. 284:33571-33579(2009).
[35]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH KIF2A.
PubMed=19351716; DOI=10.1242/jcs.044321;
Jang C.Y., Coppinger J.A., Seki A., Yates J.R. III, Fang G.;
"Plk1 and Aurora A regulate the depolymerase activity and the cellular
localization of Kif2a.";
J. Cell Sci. 122:1334-1341(2009).
[36]
FUNCTION, INTERACTION WITH TPX2, PHOSPHORYLATION AT THR-287 AND
THR-288, AND MUTAGENESIS OF THR-287.
PubMed=19668197; DOI=10.1038/ncb1919;
Mori D., Yamada M., Mimori-Kiyosue Y., Shirai Y., Suzuki A., Ohno S.,
Saya H., Wynshaw-Boris A., Hirotsune S.;
"An essential role of the aPKC-Aurora A-NDEL1 pathway in neurite
elongation by modulation of microtubule dynamics.";
Nat. Cell Biol. 11:1057-1068(2009).
[37]
INTERACTION WITH TPX2, MUTAGENESIS OF GLY-198, SUBCELLULAR LOCATION,
AND FUNCTION.
PubMed=19357306; DOI=10.1073/pnas.0900833106;
Fu J., Bian M., Liu J., Jiang Q., Zhang C.;
"A single amino acid change converts Aurora-A into Aurora-B-like
kinase in terms of partner specificity and cellular function.";
Proc. Natl. Acad. Sci. U.S.A. 106:6939-6944(2009).
[38]
FUNCTION, INTERACTION WITH PIFO, AND ACTIVATION BY PIFO.
PubMed=20643351; DOI=10.1016/j.devcel.2010.06.005;
Kinzel D., Boldt K., Davis E.E., Burtscher I., Trumbach D., Diplas B.,
Attie-Bitach T., Wurst W., Katsanis N., Ueffing M., Lickert H.;
"Pitchfork regulates primary cilia disassembly and left-right
asymmetry.";
Dev. Cell 19:66-77(2010).
[39]
INTERACTION WITH AUNIP.
PubMed=20596670;
Lieu A.S., Cheng T.S., Chou C.H., Wu C.H., Hsu C.Y., Huang C.Y.,
Chang L.K., Loh J.K., Chang C.S., Hsu C.M., Howng S.L., Hong Y.R.;
"Functional characterization of AIBp, a novel Aurora-A binding protein
in centrosome structure and spindle formation.";
Int. J. Oncol. 37:429-436(2010).
[40]
INTERACTION WITH GADD45A.
PubMed=20460379; DOI=10.1074/jbc.M109.069344;
Sanchez R., Pantoja-Uceda D., Prieto J., Diercks T., Marcaida M.J.,
Montoya G., Campos-Olivas R., Blanco F.J.;
"Solution structure of human growth arrest and DNA damage 45alpha
(Gadd45alpha) and its interactions with proliferating cell nuclear
antigen (PCNA) and Aurora A kinase.";
J. Biol. Chem. 285:22196-22201(2010).
[41]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[42]
SUBCELLULAR LOCATION, AND INTERACTION WITH JTB.
PubMed=21225229; DOI=10.3892/ijo.2011.900;
Platica M., Ionescu A., Ivan E., Holland J.F., Mandeli J., Platica O.;
"PAR, a protein involved in the cell cycle, is functionally related to
chromosomal passenger proteins.";
Int. J. Oncol. 38:777-785(2011).
[43]
REVIEW ON FUNCTION.
PubMed=14625535; DOI=10.1038/nrm1245;
Carmena M., Earnshaw W.C.;
"The cellular geography of aurora kinases.";
Nat. Rev. Mol. Cell Biol. 4:842-854(2003).
[44]
REVIEW ON FUNCTION.
PubMed=19774610; DOI=10.1002/em.20533;
Lukasiewicz K.B., Lingle W.L.;
"Aurora A, centrosome structure, and the centrosome cycle.";
Environ. Mol. Mutagen. 50:602-619(2009).
[45]
INTERACTION WITH SIRT2, AND SUBCELLULAR LOCATION.
PubMed=22014574; DOI=10.1016/j.ccr.2011.09.004;
Kim H.S., Vassilopoulos A., Wang R.H., Lahusen T., Xiao Z., Xu X.,
Li C., Veenstra T.D., Li B., Yu H., Ji J., Wang X.W., Park S.H.,
Cha Y.I., Gius D., Deng C.X.;
"SIRT2 maintains genome integrity and suppresses tumorigenesis through
regulating APC/C activity.";
Cancer Cell 20:487-499(2011).
[46]
INTERACTION WITH FRY.
PubMed=22753416; DOI=10.1074/jbc.M112.378968;
Ikeda M., Chiba S., Ohashi K., Mizuno K.;
"Furry protein promotes Aurora A-mediated polo-like kinase 1
activation.";
J. Biol. Chem. 287:27670-27681(2012).
[47]
SUBCELLULAR LOCATION.
PubMed=25657325; DOI=10.1091/mbc.E14-09-1366;
Ohta S., Wood L., Toramoto I., Yagyu K., Fukagawa T., Earnshaw W.C.;
"CENP-32 is required to maintain centrosomal dominance in bipolar
spindle assembly.";
Mol. Biol. Cell 26:1225-1237(2015).
[48]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-258, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[49]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 107-403 IN COMPLEX WITH
ADENOSINE, AND CATALYTIC ACTIVITY.
PubMed=12237287; DOI=10.1074/jbc.C200426200;
Cheetham G.M., Knegtel R.M., Coll J.T., Renwick S.B., Swenson L.,
Weber P., Lippke J.A., Austen D.A.;
"Crystal structure of aurora-2, an oncogenic serine/threonine
kinase.";
J. Biol. Chem. 277:42419-42422(2002).
[50]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 125-391 IN COMPLEX WITH ADP.
PubMed=12467573; DOI=10.1016/S0969-2126(02)00907-3;
Nowakowski J., Cronin C.N., McRee D.E., Knuth M.W., Nelson C.G.,
Pavletich N.P., Rogers J., Sang B.C., Scheibe D.N., Swanson R.V.,
Thompson D.A.;
"Structures of the cancer-related Aurora-A, FAK, and EphA2 protein
kinases from nanovolume crystallography.";
Structure 10:1659-1667(2002).
[51]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 122-403 IN COMPLEX WITH TPX2,
MUTAGENESIS OF ASP-274, ACTIVE SITE, AND PHOSPHORYLATION AT THR-287
AND THR-288.
PubMed=14580337; DOI=10.1016/S1097-2765(03)00392-7;
Bayliss R., Sardon T., Vernos I., Conti E.;
"Structural basis of Aurora-A activation by TPX2 at the mitotic
spindle.";
Mol. Cell 12:851-862(2003).
[52]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 123-401 IN COMPLEXES WITH
ADPNP AND 5-AMINOPYRIMIDINYL QUINAZOLINE INHIBITOR, AND CATALYTIC
ACTIVITY.
PubMed=16337122; DOI=10.1016/j.bmcl.2005.11.053;
Heron N.M., Anderson M., Blowers D.P., Breed J., Eden J.M., Green S.,
Hill G.B., Johnson T., Jung F.H., McMiken H.H., Mortlock A.A.,
Pannifer A.D., Pauptit R.A., Pink J., Roberts N.J., Rowsell S.;
"SAR and inhibitor complex structure determination of a novel class of
potent and specific Aurora kinase inhibitors.";
Bioorg. Med. Chem. Lett. 16:1320-1323(2006).
[53]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 100-403 IN COMPLEXES WITH
SYNTHETIC INHIBITORS, AND FUNCTION.
PubMed=17125279; DOI=10.1021/jm060897w;
Fancelli D., Moll J., Varasi M., Bravo R., Artico R., Berta D.,
Bindi S., Cameron A., Candiani I., Cappella P., Carpinelli P.,
Croci W., Forte B., Giorgini M.L., Klapwijk J., Marsiglio A.,
Pesenti E., Rocchetti M., Roletto F., Severino D., Soncini C.,
Storici P., Tonani R., Zugnoni P., Vianello P.;
"1,4,5,6-tetrahydropyrrolo[3,4-c]pyrazoles: identification of a potent
aurora kinase inhibitor with a favorable antitumor kinase inhibition
profile.";
J. Med. Chem. 49:7247-7251(2006).
[54]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 125-391 IN COMPLEX WITH
VX-680 AND TPX2, PHOSPHORYLATION AT THR-288, IDENTIFICATION BY MASS
SPECTROMETRY, AND SUBUNIT.
PubMed=18662907; DOI=10.1110/ps.036590.108;
Zhao B., Smallwood A., Yang J., Koretke K., Nurse K., Calamari A.,
Kirkpatrick R.B., Lai Z.;
"Modulation of kinase-inhibitor interactions by auxiliary protein
binding: crystallography studies on Aurora A interactions with VX-680
and with TPX2.";
Protein Sci. 17:1791-1797(2008).
[55]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 127-388 IN COMPLEX WITH ADP,
CHARACTERIZATION OF VARIANTS ARG-155 AND MET-174, AND INTERACTION WITH
TPX2.
PubMed=19801554; DOI=10.1074/jbc.M109.032722;
Bibby R.A., Tang C., Faisal A., Drosopoulos K., Lubbe S., Houlston R.,
Bayliss R., Linardopoulos S.;
"A cancer-associated aurora A mutant is mislocalized and misregulated
due to loss of interaction with TPX2.";
J. Biol. Chem. 284:33177-33184(2009).
[56]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 123-401 IN COMPLEX WITH
SYNTHETIC INHIBITOR, AND CATALYTIC ACTIVITY.
PubMed=19140666; DOI=10.1021/jm801270e;
Coumar M.S., Leou J.S., Shukla P., Wu J.S., Dixit A.K., Lin W.H.,
Chang C.Y., Lien T.W., Tan U.K., Chen C.H., Hsu J.T., Chao Y.S.,
Wu S.Y., Hsieh H.P.;
"Structure-based drug design of novel Aurora kinase A inhibitors:
structural basis for potency and specificity.";
J. Med. Chem. 52:1050-1062(2009).
[57]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 125-391 IN COMPLEX WITH
SYNTHETIC INHIBITOR, AND CATALYTIC ACTIVITY.
PubMed=19402633; DOI=10.1021/jm9000314;
Aliagas-Martin I., Burdick D., Corson L., Dotson J., Drummond J.,
Fields C., Huang O.W., Hunsaker T., Kleinheinz T., Krueger E.,
Liang J., Moffat J., Phillips G., Pulk R., Rawson T.E., Ultsch M.,
Walker L., Wiesmann C., Zhang B., Zhu B.Y., Cochran A.G.;
"A class of 2,4-bisanilinopyrimidine Aurora A inhibitors with
unusually high selectivity against Aurora B.";
J. Med. Chem. 52:3300-3307(2009).
[58]
X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) OF 122-403 OF MUTANTS ALA-290
AND ALA-393 IN COMPLEX WITH ADP, INTERACTION WITH MYCN AND TPX2,
MUTAGENESIS OF CYS-290; TYR-334; GLN-335 AND CYS-393, AND CATALYTIC
ACTIVITY.
PubMed=27837025; DOI=10.1073/PNAS.1610626113;
Richards M.W., Burgess S.G., Poon E., Carstensen A., Eilers M.,
Chesler L., Bayliss R.;
"Structural basis of N-Myc binding by Aurora-A and its destabilization
by kinase inhibitors.";
Proc. Natl. Acad. Sci. U.S.A. 113:13726-13731(2016).
[59]
VARIANTS ILE-31 AND ILE-57.
PubMed=15867347; DOI=10.1158/0008-5472.CAN-04-2149;
Kimura M.T., Mori T., Conroy J., Nowak N.J., Satomi S., Tamai K.,
Nagase H.;
"Two functional coding single nucleotide polymorphisms in STK15
(Aurora-A) coordinately increase esophageal cancer risk.";
Cancer Res. 65:3548-3554(2005).
[60]
VARIANTS ILE-31 AND ILE-57.
PubMed=16011022;
Chen L., Ao X., Ren Q., Wang Z.N., Lu C., Xu Y., Jiang L., Luo Y.,
Xu H.M., Zhang X.;
"Linkage disequilibrium and haplotype analysis of two single
nucleotide polymorphisms in STK15 in Chinese.";
Yi Chuan Xue Bao 32:331-336(2005).
[61]
VARIANT ILE-31.
PubMed=16762494; DOI=10.1016/j.canlet.2006.05.002;
Tchatchou S., Wirtenberger M., Hemminki K., Sutter C., Meindl A.,
Wappenschmidt B., Kiechle M., Bugert P., Schmutzler R.K.,
Bartram C.R., Burwinkel B.;
"Aurora kinases A and B and familial breast cancer risk.";
Cancer Lett. 247:266-272(2007).
[62]
VARIANTS [LARGE SCALE ANALYSIS] ILE-31; LEU-50; ILE-57; ARG-155;
MET-174 AND VAL-373.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: Mitotic serine/threonine kinase that contributes to the
regulation of cell cycle progression. Associates with the
centrosome and the spindle microtubules during mitosis and plays a
critical role in various mitotic events including the
establishment of mitotic spindle, centrosome duplication,
centrosome separation as well as maturation, chromosomal
alignment, spindle assembly checkpoint, and cytokinesis. Required
for initial activation of CDK1 at centrosomes. Phosphorylates
numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B,
DLGP5, HDAC6, KIF2A, LATS2, NDEL1, PARD3, PPP1R2, PLK1, RASSF1,
TACC3, p53/TP53 and TPX2. Regulates KIF2A tubulin depolymerase
activity. Required for normal axon formation. Plays a role in
microtubule remodeling during neurite extension. Important for
microtubule formation and/or stabilization. Also acts as a key
regulatory component of the p53/TP53 pathway, and particularly the
checkpoint-response pathways critical for oncogenic transformation
of cells, by phosphorylating and stabilizing p53/TP53.
Phosphorylates its own inhibitors, the protein phosphatase type 1
(PP1) isoforms, to inhibit their activity. Necessary for proper
cilia disassembly prior to mitosis. {ECO:0000269|PubMed:11039908,
ECO:0000269|PubMed:11551964, ECO:0000269|PubMed:12390251,
ECO:0000269|PubMed:13678582, ECO:0000269|PubMed:14523000,
ECO:0000269|PubMed:14702041, ECO:0000269|PubMed:14990569,
ECO:0000269|PubMed:15128871, ECO:0000269|PubMed:15147269,
ECO:0000269|PubMed:15987997, ECO:0000269|PubMed:17125279,
ECO:0000269|PubMed:17360485, ECO:0000269|PubMed:17604723,
ECO:0000269|PubMed:18056443, ECO:0000269|PubMed:18615013,
ECO:0000269|PubMed:19351716, ECO:0000269|PubMed:19357306,
ECO:0000269|PubMed:19668197, ECO:0000269|PubMed:19812038,
ECO:0000269|PubMed:20643351, ECO:0000269|PubMed:9606188}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:12237287, ECO:0000269|PubMed:16337122,
ECO:0000269|PubMed:19140666, ECO:0000269|PubMed:19402633,
ECO:0000269|PubMed:27837025}.
-!- ENZYME REGULATION: Activation of CDK1, appears to be an upstream
event of AURKA activation. Phosphatase inhibitor-2 (PPP1R2) and
TPX2 act also as activators. Inactivated by the G2 checkpoint.
Inhibited by GADD45A and p53/TP53, and through dephosphorylation
by protein phosphatase type 1 (PP1). MLN8054 is also a potent and
selective inhibitor. Activated during the early phase of cilia
disassembly in the presence of PIFO. {ECO:0000269|PubMed:11039908,
ECO:0000269|PubMed:12390251, ECO:0000269|PubMed:17360485}.
-!- SUBUNIT: Interacts with FBXL7 (By similarity). Interacts with
CPEB1, JTB, TACC1, TPX2, PPP2CA, as well as with the protein
phosphatase type 1 (PP1) isoforms PPP1CA, PPP1CB and PPP1CC.
Interacts also with its substrates ARHGEF2, BORA, BRCA1, KIF2A,
PARD3, and p53/TP53. Interaction with BORA promotes
phosphorylation of PLK1. Interacts with PIFO. Interacts with
GADD45A, competing with its oligomerization. Interacts (via C-
terminus) with AUNIP (via C-terminus). Identified in a complex
with AUNIP and NIN. Interacts with FRY; this interaction
facilitates AURKA-mediated PLK1 phosphorylation. Interacts with
SIRT2. Interacts with MYCN; interaction is phospho-independent and
triggers AURKA activation; AURKA competes with FBXW7 for binding
to unphosphorylated MYCN but not for binding to phosphorylated
MYCN (PubMed:27837025). {ECO:0000250, ECO:0000269|PubMed:11551964,
ECO:0000269|PubMed:12237287, ECO:0000269|PubMed:12467573,
ECO:0000269|PubMed:14580337, ECO:0000269|PubMed:14603251,
ECO:0000269|PubMed:14702041, ECO:0000269|PubMed:14990569,
ECO:0000269|PubMed:15966895, ECO:0000269|PubMed:16890155,
ECO:0000269|PubMed:17229885, ECO:0000269|PubMed:17488622,
ECO:0000269|PubMed:17726514, ECO:0000269|PubMed:18662907,
ECO:0000269|PubMed:19140666, ECO:0000269|PubMed:19351716,
ECO:0000269|PubMed:19357306, ECO:0000269|PubMed:19402633,
ECO:0000269|PubMed:19668197, ECO:0000269|PubMed:19801554,
ECO:0000269|PubMed:19812038, ECO:0000269|PubMed:20460379,
ECO:0000269|PubMed:20596670, ECO:0000269|PubMed:20643351,
ECO:0000269|PubMed:21225229, ECO:0000269|PubMed:22014574,
ECO:0000269|PubMed:22753416, ECO:0000269|PubMed:27837025}.
-!- INTERACTION:
Q9NWT8:AURKAIP1; NbExp=2; IntAct=EBI-448680, EBI-448665;
P00533:EGFR; NbExp=4; IntAct=EBI-448680, EBI-297353;
P61978:HNRNPK; NbExp=2; IntAct=EBI-448680, EBI-304185;
Q13123:IK; NbExp=3; IntAct=EBI-448680, EBI-713456;
P04198:MYCN; NbExp=12; IntAct=EBI-448680, EBI-878369;
P06748:NPM1; NbExp=3; IntAct=EBI-448680, EBI-78579;
Q8VDQ8:Sirt2 (xeno); NbExp=5; IntAct=EBI-448680, EBI-911012;
O15350:TP73; NbExp=11; IntAct=EBI-448680, EBI-389606;
Q9ULW0:TPX2; NbExp=2; IntAct=EBI-448680, EBI-1037322;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome {ECO:0000269|PubMed:12576638,
ECO:0000269|PubMed:13678582, ECO:0000269|PubMed:17229885,
ECO:0000269|PubMed:17726514, ECO:0000269|PubMed:19357306,
ECO:0000269|PubMed:21225229, ECO:0000269|PubMed:22014574,
ECO:0000269|PubMed:25657325, ECO:0000269|PubMed:9153231}.
Cytoplasm, cytoskeleton, spindle pole
{ECO:0000269|PubMed:12576638, ECO:0000269|PubMed:13678582,
ECO:0000269|PubMed:17726514, ECO:0000269|PubMed:19351716,
ECO:0000269|PubMed:25657325, ECO:0000269|PubMed:9153231,
ECO:0000269|PubMed:9606188}. Cytoplasm, cytoskeleton, cilium basal
body {ECO:0000250|UniProtKB:P97477}. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome, centriole
{ECO:0000250|UniProtKB:P97477}. Note=Detected at the neurite
hillock in developing neurons (By similarity). Localizes at the
centrosome in mitotic cells from early prophase until telophase,
but also localizes to the spindle pole MTs from prophase to
anaphase (PubMed:9606188, PubMed:17229885, PubMed:21225229).
Colocalized with SIRT2 at centrosome (PubMed:22014574). Moves to
the midbody during both telophase and cytokinesis
(PubMed:17726514). Associates with both the pericentriolar
material (PCM) and centrioles (PubMed:22014574).
{ECO:0000250|UniProtKB:P97477, ECO:0000269|PubMed:17229885,
ECO:0000269|PubMed:17726514, ECO:0000269|PubMed:21225229,
ECO:0000269|PubMed:22014574, ECO:0000269|PubMed:9606188}.
-!- TISSUE SPECIFICITY: Highly expressed in testis and weakly in
skeletal muscle, thymus and spleen. Also highly expressed in
colon, ovarian, prostate, neuroblastoma, breast and cervical
cancer cell lines.
-!- INDUCTION: Expression is cell-cycle regulated, low in G1/S,
accumulates during G2/M, and decreases rapidly after.
{ECO:0000269|PubMed:11790771, ECO:0000269|PubMed:12390251,
ECO:0000269|PubMed:15987997, ECO:0000269|PubMed:9153231,
ECO:0000269|PubMed:9606188}.
-!- PTM: Activated by phosphorylation at Thr-288; this brings about a
change in the conformation of the activation segment.
Phosphorylation at Thr-288 varies during the cell cycle and is
highest during M phase. Autophosphorylated at Thr-288 upon TPX2
binding. Thr-288 can be phosphorylated by several kinases,
including PAK and PKA. Protein phosphatase type 1 (PP1) binds
AURKA and inhibits its activity by dephosphorylating Thr-288
during mitosis. Phosphorylation at Ser-342 decreases the kinase
activity. PPP2CA controls degradation by dephosphorylating Ser-51
at the end of mitosis. {ECO:0000269|PubMed:11039908,
ECO:0000269|PubMed:11551964, ECO:0000269|PubMed:12390251,
ECO:0000269|PubMed:13678582, ECO:0000269|PubMed:14580337,
ECO:0000269|PubMed:14990569, ECO:0000269|PubMed:16246726,
ECO:0000269|PubMed:17229885, ECO:0000269|PubMed:18662907,
ECO:0000269|PubMed:19668197}.
-!- PTM: Ubiquitinated by the E3 ubiquitin-protein ligase complex
SCF(FBXL7) during mitosis, leading to its degradation by the
proteasome. Ubiquitinated by CHFR, leading to its degradation by
the proteasome (By similarity). Ubiquitinated by the anaphase-
promoting complex (APC), leading to its degradation by the
proteasome. {ECO:0000250, ECO:0000269|PubMed:10851084,
ECO:0000269|PubMed:11039908}.
-!- MISCELLANEOUS: Centrosome amplification can occur when the cycles
are uncoupled, and this amplification is associated with cancer
and with an increase in the levels of chromosomal instability.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. Aurora subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-!- CAUTION: Authors initially considered AURKA/STK6 and STK15 as 2
different proteins (PubMed:9771714). It is clear that they are the
same protein. {ECO:0000305|PubMed:9771714}.
-!- SEQUENCE CAUTION:
Sequence=BAA23592.1; Type=Frameshift; Positions=105, 125, 129, 235, 241; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/AURKAID730ch20q13.html";
-----------------------------------------------------------------------
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EMBL; D84212; BAA23592.1; ALT_FRAME; mRNA.
EMBL; AF008551; AAC12708.1; -; mRNA.
EMBL; AF011467; AAC23448.1; -; Genomic_DNA.
EMBL; AF011468; AAC63902.1; -; mRNA.
EMBL; AF195947; AAF29508.1; -; Genomic_DNA.
EMBL; AF195942; AAF29508.1; JOINED; Genomic_DNA.
EMBL; AF195943; AAF29508.1; JOINED; Genomic_DNA.
EMBL; AF195944; AAF29508.1; JOINED; Genomic_DNA.
EMBL; AF195945; AAF29508.1; JOINED; Genomic_DNA.
EMBL; AF195946; AAF29508.1; JOINED; Genomic_DNA.
EMBL; AL121914; CAC12717.1; -; Genomic_DNA.
EMBL; CH471077; EAW75550.1; -; Genomic_DNA.
EMBL; CH471077; EAW75551.1; -; Genomic_DNA.
EMBL; CH471077; EAW75552.1; -; Genomic_DNA.
EMBL; CH471077; EAW75553.1; -; Genomic_DNA.
EMBL; CH471077; EAW75554.1; -; Genomic_DNA.
EMBL; CH471077; EAW75555.1; -; Genomic_DNA.
EMBL; CH471077; EAW75556.1; -; Genomic_DNA.
EMBL; CH471077; EAW75557.1; -; Genomic_DNA.
EMBL; CH471077; EAW75558.1; -; Genomic_DNA.
EMBL; CH471077; EAW75559.1; -; Genomic_DNA.
EMBL; CH471077; EAW75561.1; -; Genomic_DNA.
EMBL; CH471077; EAW75562.1; -; Genomic_DNA.
EMBL; BC001280; AAH01280.1; -; mRNA.
EMBL; BC002499; AAH02499.1; -; mRNA.
EMBL; BC006423; AAH06423.1; -; mRNA.
EMBL; BC027464; AAH27464.1; -; mRNA.
CCDS; CCDS13451.1; -.
PIR; JC5974; JC5974.
RefSeq; NP_001310232.1; NM_001323303.1.
RefSeq; NP_001310233.1; NM_001323304.1.
RefSeq; NP_001310234.1; NM_001323305.1.
RefSeq; NP_003591.2; NM_003600.3.
RefSeq; NP_940835.1; NM_198433.2.
RefSeq; NP_940836.1; NM_198434.2.
RefSeq; NP_940837.1; NM_198435.2.
RefSeq; NP_940838.1; NM_198436.2.
RefSeq; NP_940839.1; NM_198437.2.
RefSeq; XP_016883524.1; XM_017028035.1.
UniGene; Hs.250822; -.
PDB; 1MQ4; X-ray; 1.90 A; A=125-391.
PDB; 1MUO; X-ray; 2.90 A; A=107-403.
PDB; 1OL5; X-ray; 2.50 A; A=122-403.
PDB; 1OL6; X-ray; 3.00 A; A=122-403.
PDB; 1OL7; X-ray; 2.75 A; A=122-403.
PDB; 2BMC; X-ray; 2.60 A; A/B/C/D/E/F=100-403.
PDB; 2C6D; X-ray; 2.20 A; A=124-398.
PDB; 2C6E; X-ray; 2.10 A; A/B=123-401.
PDB; 2DWB; X-ray; 2.50 A; A=122-403.
PDB; 2J4Z; X-ray; 2.00 A; A/B=100-403.
PDB; 2J50; X-ray; 3.00 A; A/B=126-403.
PDB; 2NP8; X-ray; 2.25 A; A=125-391.
PDB; 2W1C; X-ray; 3.24 A; A=122-389.
PDB; 2W1D; X-ray; 2.97 A; A=122-389.
PDB; 2W1E; X-ray; 2.93 A; A=122-389.
PDB; 2W1F; X-ray; 2.85 A; A=122-389.
PDB; 2W1G; X-ray; 2.71 A; A=122-389.
PDB; 2WQE; X-ray; 2.50 A; A=127-388.
PDB; 2WTV; X-ray; 2.40 A; A/B/C/D=122-403.
PDB; 2WTW; X-ray; 3.30 A; A=122-403.
PDB; 2X6D; X-ray; 2.80 A; A=122-403.
PDB; 2X6E; X-ray; 3.35 A; A=122-403.
PDB; 2X81; X-ray; 2.91 A; A=126-391.
PDB; 2XNE; X-ray; 2.80 A; A=122-392.
PDB; 2XNG; X-ray; 2.60 A; A=122-403.
PDB; 2XRU; X-ray; 2.90 A; A=126-403.
PDB; 3COH; X-ray; 2.70 A; A/B=124-391.
PDB; 3E5A; X-ray; 2.30 A; A=125-391.
PDB; 3EFW; X-ray; 2.29 A; A/B=125-391.
PDB; 3FDN; X-ray; 1.90 A; A=123-401.
PDB; 3H0Y; X-ray; 2.50 A; A=124-391.
PDB; 3H0Z; X-ray; 2.92 A; A/B/C=124-391.
PDB; 3H10; X-ray; 2.20 A; A/B/D=124-391.
PDB; 3HA6; X-ray; 2.36 A; A=125-391.
PDB; 3K5U; X-ray; 2.35 A; A=123-401.
PDB; 3LAU; X-ray; 2.10 A; A=125-399.
PDB; 3M11; X-ray; 2.75 A; A=123-401.
PDB; 3MYG; X-ray; 2.40 A; A=125-391.
PDB; 3NRM; X-ray; 3.05 A; A=126-403.
PDB; 3O50; X-ray; 2.00 A; A/B=125-391.
PDB; 3O51; X-ray; 3.20 A; A=125-391.
PDB; 3P9J; X-ray; 2.80 A; A=125-391.
PDB; 3QBN; X-ray; 3.50 A; A=124-403.
PDB; 3R21; X-ray; 2.90 A; A=126-391.
PDB; 3R22; X-ray; 2.90 A; A=126-391.
PDB; 3UNZ; X-ray; 2.80 A; A/B=123-401.
PDB; 3UO4; X-ray; 2.45 A; A=123-401.
PDB; 3UO5; X-ray; 2.70 A; A=123-401.
PDB; 3UO6; X-ray; 2.80 A; A/B=123-401.
PDB; 3UOD; X-ray; 2.50 A; A=123-401.
PDB; 3UOH; X-ray; 2.80 A; A/B=123-401.
PDB; 3UOJ; X-ray; 2.90 A; A/B=123-401.
PDB; 3UOK; X-ray; 2.95 A; A/B=123-401.
PDB; 3UOL; X-ray; 2.40 A; A/B=123-401.
PDB; 3UP2; X-ray; 2.30 A; A=123-401.
PDB; 3UP7; X-ray; 3.05 A; A=123-401.
PDB; 3VAP; X-ray; 2.66 A; A=125-391.
PDB; 3W10; X-ray; 2.70 A; A=126-403.
PDB; 3W16; X-ray; 2.80 A; A=126-403.
PDB; 3W18; X-ray; 2.50 A; A/B=126-403.
PDB; 3W2C; X-ray; 2.45 A; A/C/E/G=128-388.
PDB; 4B0G; X-ray; 2.50 A; A=122-403.
PDB; 4BN1; X-ray; 2.50 A; A=122-403.
PDB; 4BYI; X-ray; 2.60 A; A=122-403.
PDB; 4BYJ; X-ray; 2.75 A; A=122-403.
PDB; 4C3P; X-ray; 2.69 A; A/D=122-403.
PDB; 4C3R; X-ray; 2.79 A; A=122-403.
PDB; 4CEG; X-ray; 2.10 A; A=122-403.
PDB; 4DEA; X-ray; 2.45 A; A=123-401.
PDB; 4DEB; X-ray; 3.05 A; A=123-401.
PDB; 4DED; X-ray; 3.05 A; A=123-401.
PDB; 4DEE; X-ray; 2.30 A; A=123-401.
PDB; 4DHF; X-ray; 2.80 A; A/B=126-391.
PDB; 4J8M; X-ray; 1.85 A; A=123-401.
PDB; 4J8N; X-ray; 3.14 A; A/B/C/D=123-401.
PDB; 4JAI; X-ray; 3.20 A; A=122-396.
PDB; 4JAJ; X-ray; 2.70 A; A=122-396.
PDB; 4JBO; X-ray; 2.49 A; A=123-401.
PDB; 4JBP; X-ray; 2.45 A; A=123-401.
PDB; 4JBQ; X-ray; 2.30 A; A=123-401.
PDB; 4O0S; X-ray; 2.50 A; A=122-403.
PDB; 4O0U; X-ray; 2.60 A; A=122-403.
PDB; 4O0W; X-ray; 2.60 A; A=122-403.
PDB; 4PRJ; X-ray; 2.80 A; A=124-391.
PDB; 4UTD; X-ray; 2.36 A; A=122-403.
PDB; 4UYN; X-ray; 1.90 A; A=125-399.
PDB; 4UZD; X-ray; 3.20 A; A/B=125-399.
PDB; 4UZH; X-ray; 2.00 A; A=125-399.
PDB; 4ZS0; X-ray; 3.00 A; A=122-403.
PDB; 4ZTQ; X-ray; 2.80 A; A=122-403.
PDB; 4ZTR; X-ray; 2.85 A; A=122-403.
PDB; 4ZTS; X-ray; 2.90 A; A=122-403.
PDB; 5AAD; X-ray; 3.10 A; A=122-403.
PDB; 5AAE; X-ray; 3.11 A; A=122-403.
PDB; 5AAF; X-ray; 2.78 A; A=122-403.
PDB; 5AAG; X-ray; 2.85 A; A=122-403.
PDB; 5DN3; X-ray; 2.05 A; A=125-391.
PDB; 5DNR; X-ray; 1.95 A; A=125-391.
PDB; 5DOS; X-ray; 2.98 A; A=126-390.
PDB; 5DPV; X-ray; 2.29 A; A=126-390.
PDB; 5DR2; X-ray; 2.46 A; A=128-390.
PDB; 5DR6; X-ray; 2.53 A; A=126-390.
PDB; 5DR9; X-ray; 2.47 A; A=126-390.
PDB; 5DRD; X-ray; 2.13 A; A=126-390.
PDB; 5DT0; X-ray; 2.15 A; A=126-390.
PDB; 5DT3; X-ray; 2.33 A; A=126-390.
PDB; 5DT4; X-ray; 2.86 A; A=126-390.
PDB; 5EW9; X-ray; 2.18 A; A=123-390.
PDB; 5G1X; X-ray; 1.72 A; A=122-403.
PDB; 5L8J; X-ray; 1.68 A; A=122-403.
PDB; 5L8K; X-ray; 1.79 A; A=122-403.
PDB; 5L8L; X-ray; 1.67 A; A=122-403.
PDB; 5LXM; X-ray; 2.08 A; A=122-403.
PDBsum; 1MQ4; -.
PDBsum; 1MUO; -.
PDBsum; 1OL5; -.
PDBsum; 1OL6; -.
PDBsum; 1OL7; -.
PDBsum; 2BMC; -.
PDBsum; 2C6D; -.
PDBsum; 2C6E; -.
PDBsum; 2DWB; -.
PDBsum; 2J4Z; -.
PDBsum; 2J50; -.
PDBsum; 2NP8; -.
PDBsum; 2W1C; -.
PDBsum; 2W1D; -.
PDBsum; 2W1E; -.
PDBsum; 2W1F; -.
PDBsum; 2W1G; -.
PDBsum; 2WQE; -.
PDBsum; 2WTV; -.
PDBsum; 2WTW; -.
PDBsum; 2X6D; -.
PDBsum; 2X6E; -.
PDBsum; 2X81; -.
PDBsum; 2XNE; -.
PDBsum; 2XNG; -.
PDBsum; 2XRU; -.
PDBsum; 3COH; -.
PDBsum; 3E5A; -.
PDBsum; 3EFW; -.
PDBsum; 3FDN; -.
PDBsum; 3H0Y; -.
PDBsum; 3H0Z; -.
PDBsum; 3H10; -.
PDBsum; 3HA6; -.
PDBsum; 3K5U; -.
PDBsum; 3LAU; -.
PDBsum; 3M11; -.
PDBsum; 3MYG; -.
PDBsum; 3NRM; -.
PDBsum; 3O50; -.
PDBsum; 3O51; -.
PDBsum; 3P9J; -.
PDBsum; 3QBN; -.
PDBsum; 3R21; -.
PDBsum; 3R22; -.
PDBsum; 3UNZ; -.
PDBsum; 3UO4; -.
PDBsum; 3UO5; -.
PDBsum; 3UO6; -.
PDBsum; 3UOD; -.
PDBsum; 3UOH; -.
PDBsum; 3UOJ; -.
PDBsum; 3UOK; -.
PDBsum; 3UOL; -.
PDBsum; 3UP2; -.
PDBsum; 3UP7; -.
PDBsum; 3VAP; -.
PDBsum; 3W10; -.
PDBsum; 3W16; -.
PDBsum; 3W18; -.
PDBsum; 3W2C; -.
PDBsum; 4B0G; -.
PDBsum; 4BN1; -.
PDBsum; 4BYI; -.
PDBsum; 4BYJ; -.
PDBsum; 4C3P; -.
PDBsum; 4C3R; -.
PDBsum; 4CEG; -.
PDBsum; 4DEA; -.
PDBsum; 4DEB; -.
PDBsum; 4DED; -.
PDBsum; 4DEE; -.
PDBsum; 4DHF; -.
PDBsum; 4J8M; -.
PDBsum; 4J8N; -.
PDBsum; 4JAI; -.
PDBsum; 4JAJ; -.
PDBsum; 4JBO; -.
PDBsum; 4JBP; -.
PDBsum; 4JBQ; -.
PDBsum; 4O0S; -.
PDBsum; 4O0U; -.
PDBsum; 4O0W; -.
PDBsum; 4PRJ; -.
PDBsum; 4UTD; -.
PDBsum; 4UYN; -.
PDBsum; 4UZD; -.
PDBsum; 4UZH; -.
PDBsum; 4ZS0; -.
PDBsum; 4ZTQ; -.
PDBsum; 4ZTR; -.
PDBsum; 4ZTS; -.
PDBsum; 5AAD; -.
PDBsum; 5AAE; -.
PDBsum; 5AAF; -.
PDBsum; 5AAG; -.
PDBsum; 5DN3; -.
PDBsum; 5DNR; -.
PDBsum; 5DOS; -.
PDBsum; 5DPV; -.
PDBsum; 5DR2; -.
PDBsum; 5DR6; -.
PDBsum; 5DR9; -.
PDBsum; 5DRD; -.
PDBsum; 5DT0; -.
PDBsum; 5DT3; -.
PDBsum; 5DT4; -.
PDBsum; 5EW9; -.
PDBsum; 5G1X; -.
PDBsum; 5L8J; -.
PDBsum; 5L8K; -.
PDBsum; 5L8L; -.
PDBsum; 5LXM; -.
ProteinModelPortal; O14965; -.
SMR; O14965; -.
BioGrid; 112666; 327.
DIP; DIP-33068N; -.
ELM; O14965; -.
IntAct; O14965; 99.
MINT; MINT-254096; -.
STRING; 9606.ENSP00000216911; -.
BindingDB; O14965; -.
ChEMBL; CHEMBL4722; -.
DrugBank; DB08065; 2-(1H-pyrazol-3-yl)-1H-benzimidazole.
DrugBank; DB05169; AT9283.
DrugBank; DB05198; CYC116.
DrugBank; DB05220; MLN8237.
DrugBank; DB08066; N-[3-(1H-BENZIMIDAZOL-2-YL)-1H-PYRAZOL-4-YL]BENZAMIDE.
DrugBank; DB07801; N-butyl-3-{[6-(9H-purin-6-ylamino)hexanoyl]amino}benzamide.
DrugBank; DB07545; N-{3-[(4-{[3-(TRIFLUOROMETHYL)PHENYL]AMINO}PYRIMIDIN-2-YL)AMINO]PHENYL}CYCLOPROPANECARBOXAMIDE.
DrugBank; DB02482; Phosphonothreonine.
GuidetoPHARMACOLOGY; 1936; -.
iPTMnet; O14965; -.
PhosphoSitePlus; O14965; -.
BioMuta; AURKA; -.
EPD; O14965; -.
MaxQB; O14965; -.
PaxDb; O14965; -.
PeptideAtlas; O14965; -.
PRIDE; O14965; -.
DNASU; 6790; -.
Ensembl; ENST00000312783; ENSP00000321591; ENSG00000087586.
Ensembl; ENST00000347343; ENSP00000216911; ENSG00000087586.
Ensembl; ENST00000371356; ENSP00000360407; ENSG00000087586.
Ensembl; ENST00000395911; ENSP00000379247; ENSG00000087586.
Ensembl; ENST00000395913; ENSP00000379249; ENSG00000087586.
Ensembl; ENST00000395914; ENSP00000379250; ENSG00000087586.
Ensembl; ENST00000395915; ENSP00000379251; ENSG00000087586.
GeneID; 6790; -.
KEGG; hsa:6790; -.
UCSC; uc002xxe.1; human.
CTD; 6790; -.
DisGeNET; 6790; -.
GeneCards; AURKA; -.
H-InvDB; HIX0015930; -.
HGNC; HGNC:11393; AURKA.
HPA; CAB001454; -.
HPA; HPA002636; -.
MalaCards; AURKA; -.
MIM; 603072; gene.
neXtProt; NX_O14965; -.
PharmGKB; PA36201; -.
eggNOG; KOG0580; Eukaryota.
eggNOG; ENOG410XNRB; LUCA.
HOVERGEN; HBG108519; -.
InParanoid; O14965; -.
KO; K11481; -.
OrthoDB; EOG091G0EU2; -.
PhylomeDB; O14965; -.
TreeFam; TF105331; -.
BRENDA; 2.7.11.1; 2681.
Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
Reactome; R-HSA-4615885; SUMOylation of DNA replication proteins.
Reactome; R-HSA-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
Reactome; R-HSA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
Reactome; R-HSA-8854518; AURKA Activation by TPX2.
Reactome; R-HSA-8854521; Interaction between PHLDA1 and AURKA.
SignaLink; O14965; -.
SIGNOR; O14965; -.
EvolutionaryTrace; O14965; -.
GeneWiki; Aurora_A_kinase; -.
GenomeRNAi; 6790; -.
PRO; PR:O14965; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000087586; -.
CleanEx; HS_AURKA; -.
ExpressionAtlas; O14965; baseline and differential.
Genevisible; O14965; HS.
GO; GO:0043203; C:axon hillock; IEA:Ensembl.
GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0032133; C:chromosome passenger complex; IBA:GO_Central.
GO; GO:0005929; C:cilium; IEA:UniProtKB-KW.
GO; GO:0000780; C:condensed nuclear chromosome, centromeric region; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0042585; C:germinal vesicle; IEA:Ensembl.
GO; GO:0072687; C:meiotic spindle; IEA:Ensembl.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0015630; C:microtubule cytoskeleton; IDA:BHF-UCL.
GO; GO:0030496; C:midbody; TAS:UniProtKB.
GO; GO:0097431; C:mitotic spindle pole; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
GO; GO:0045120; C:pronucleus; IEA:Ensembl.
GO; GO:0005819; C:spindle; TAS:UniProtKB.
GO; GO:0051233; C:spindle midzone; IBA:GO_Central.
GO; GO:0031616; C:spindle pole centrosome; IDA:BHF-UCL.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0035174; F:histone serine kinase activity; IBA:GO_Central.
GO; GO:0046982; F:protein heterodimerization activity; IPI:CAFA.
GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; EXP:Reactome.
GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; TAS:UniProtKB.
GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; TAS:Reactome.
GO; GO:0009948; P:anterior/posterior axis specification; IEA:Ensembl.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0051642; P:centrosome localization; IEA:Ensembl.
GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0097421; P:liver regeneration; IDA:MGI.
GO; GO:0000278; P:mitotic cell cycle; TAS:ProtInc.
GO; GO:0007100; P:mitotic centrosome separation; IEA:Ensembl.
GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0032091; P:negative regulation of protein binding; IDA:UniProtKB.
GO; GO:1990138; P:neuron projection extension; IEA:Ensembl.
GO; GO:0045840; P:positive regulation of mitotic nuclear division; TAS:UniProtKB.
GO; GO:1900195; P:positive regulation of oocyte maturation; IEA:Ensembl.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Ensembl.
GO; GO:0046777; P:protein autophosphorylation; TAS:UniProtKB.
GO; GO:0071539; P:protein localization to centrosome; IEA:Ensembl.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; TAS:Reactome.
GO; GO:0046605; P:regulation of centrosome cycle; TAS:UniProtKB.
GO; GO:0032465; P:regulation of cytokinesis; IBA:GO_Central.
GO; GO:0031647; P:regulation of protein stability; IMP:UniProtKB.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
GO; GO:0009611; P:response to wounding; IDA:MGI.
GO; GO:0007057; P:spindle assembly involved in female meiosis I; IEA:Ensembl.
GO; GO:0007051; P:spindle organization; IMP:UniProtKB.
CDD; cd14116; STKc_Aurora-A; 1.
InterPro; IPR030616; Aur.
InterPro; IPR030611; AURKA.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
PANTHER; PTHR24350; PTHR24350; 1.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Cell cycle; Cell division; Cell projection;
Cilium; Cilium biogenesis/degradation; Complete proteome; Cytoplasm;
Cytoskeleton; Isopeptide bond; Kinase; Microtubule; Mitosis;
Nucleotide-binding; Phosphoprotein; Polymorphism; Proto-oncogene;
Reference proteome; Serine/threonine-protein kinase; Transferase;
Ubl conjugation.
CHAIN 1 403 Aurora kinase A.
/FTId=PRO_0000086692.
DOMAIN 133 383 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 211 213 ATP. {ECO:0000244|PDB:5G1X,
ECO:0000269|PubMed:27837025}.
NP_BIND 260 261 ATP. {ECO:0000244|PDB:5G1X,
ECO:0000269|PubMed:27837025}.
REGION 280 293 Activation segment.
ACT_SITE 256 256 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027,
ECO:0000269|PubMed:14580337}.
BINDING 143 143 ATP; via amide nitrogen.
{ECO:0000244|PDB:5G1X,
ECO:0000269|PubMed:27837025}.
BINDING 162 162 ATP. {ECO:0000244|PDB:5G1X,
ECO:0000269|PubMed:27837025}.
BINDING 274 274 ATP. {ECO:0000244|PDB:5G1X,
ECO:0000269|PubMed:27837025}.
MOD_RES 41 41 Phosphoserine.
{ECO:0000244|PubMed:18691976}.
MOD_RES 51 51 Phosphoserine.
{ECO:0000269|PubMed:17229885}.
MOD_RES 287 287 Phosphothreonine.
{ECO:0000269|PubMed:14580337,
ECO:0000269|PubMed:19668197}.
MOD_RES 288 288 Phosphothreonine.
{ECO:0000269|PubMed:11039908,
ECO:0000269|PubMed:13678582,
ECO:0000269|PubMed:14580337,
ECO:0000269|PubMed:14990569,
ECO:0000269|PubMed:16246726,
ECO:0000269|PubMed:18662907,
ECO:0000269|PubMed:19668197}.
MOD_RES 342 342 Phosphoserine; by PKA and PAK.
{ECO:0000269|PubMed:16246726}.
CROSSLNK 258 258 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VARIANT 11 11 G -> R (in dbSNP:rs6069717).
/FTId=VAR_030840.
VARIANT 31 31 F -> I (in dbSNP:rs2273535).
{ECO:0000269|PubMed:15867347,
ECO:0000269|PubMed:16011022,
ECO:0000269|PubMed:16762494,
ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:9771714}.
/FTId=VAR_030841.
VARIANT 50 50 P -> L (in dbSNP:rs34572020).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041127.
VARIANT 57 57 V -> I (in dbSNP:rs1047972).
{ECO:0000269|PubMed:15867347,
ECO:0000269|PubMed:16011022,
ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:9514916}.
/FTId=VAR_030842.
VARIANT 104 104 S -> L (in dbSNP:rs2230743).
/FTId=VAR_061745.
VARIANT 155 155 S -> R (in a colorectal adenocarcinoma
sample; somatic mutation; reduces
interaction with TPX2).
{ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:19801554}.
/FTId=VAR_041128.
VARIANT 174 174 V -> M (in a metastatic melanoma sample;
somatic mutation; constitutively enhanced
kinase activity).
{ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:19801554}.
/FTId=VAR_041129.
VARIANT 373 373 M -> V (in dbSNP:rs33923703).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041130.
MUTAGEN 162 162 K->R: Loss of kinase activity.
{ECO:0000269|PubMed:14702041,
ECO:0000269|PubMed:14990569}.
MUTAGEN 165 165 F->A: Decreases the interaction with
phosphatase type 1 isoforms.
{ECO:0000269|PubMed:11551964}.
MUTAGEN 198 198 G->N: Reduces interaction with TPX2.
Reduces kinase activity tenfold. Promotes
interaction with the AURKB binding
partners INCENP and BIRC5 that are
normally not bound by AURKA.
{ECO:0000269|PubMed:19357306}.
MUTAGEN 205 205 R->A: Reduces ubiquitination and
proteasomal degradation.
{ECO:0000269|PubMed:10851084}.
MUTAGEN 274 274 D->N: Abolishes autophosphorylation.
{ECO:0000269|PubMed:14580337}.
MUTAGEN 287 287 T->A: No direct effect on catalytic
activity. {ECO:0000269|PubMed:19668197}.
MUTAGEN 287 287 T->E: Enhances interaction with TPX2.
{ECO:0000269|PubMed:19668197}.
MUTAGEN 288 288 T->D: Mimics phosphorylation state and
increases kinase activity.
{ECO:0000269|PubMed:11039908}.
MUTAGEN 290 290 C->A: Enhances stability; when associated
with A-393.
{ECO:0000269|PubMed:27837025}.
MUTAGEN 334 334 Y->A: Reduces binding to MYCN.
{ECO:0000269|PubMed:27837025}.
MUTAGEN 335 335 Q->A: Reduces binding to MYCN.
{ECO:0000269|PubMed:27837025}.
MUTAGEN 346 346 F->A: Decreases the interaction with
phosphatase type 1 isoforms.
{ECO:0000269|PubMed:11551964}.
MUTAGEN 393 393 C->A: Enhances stability; when associated
with A-290.
{ECO:0000269|PubMed:27837025}.
HELIX 130 132 {ECO:0000244|PDB:5L8L}.
STRAND 133 141 {ECO:0000244|PDB:5L8L}.
STRAND 143 152 {ECO:0000244|PDB:5L8L}.
TURN 153 155 {ECO:0000244|PDB:5L8L}.
STRAND 158 165 {ECO:0000244|PDB:5L8L}.
HELIX 166 171 {ECO:0000244|PDB:5L8L}.
TURN 172 174 {ECO:0000244|PDB:4O0S}.
HELIX 175 185 {ECO:0000244|PDB:5L8L}.
STRAND 191 193 {ECO:0000244|PDB:3UO6}.
STRAND 196 201 {ECO:0000244|PDB:5L8L}.
STRAND 203 210 {ECO:0000244|PDB:5L8L}.
STRAND 214 217 {ECO:0000244|PDB:2J50}.
HELIX 218 225 {ECO:0000244|PDB:5L8L}.
HELIX 230 249 {ECO:0000244|PDB:5L8L}.
HELIX 259 261 {ECO:0000244|PDB:5L8L}.
STRAND 262 264 {ECO:0000244|PDB:5L8L}.
STRAND 266 268 {ECO:0000244|PDB:3UOL}.
STRAND 270 272 {ECO:0000244|PDB:5L8L}.
STRAND 277 279 {ECO:0000244|PDB:4J8M}.
STRAND 280 283 {ECO:0000244|PDB:5L8L}.
STRAND 287 289 {ECO:0000244|PDB:4J8M}.
HELIX 290 292 {ECO:0000244|PDB:1MUO}.
HELIX 293 295 {ECO:0000244|PDB:5L8J}.
HELIX 298 302 {ECO:0000244|PDB:5L8L}.
HELIX 307 309 {ECO:0000244|PDB:2BMC}.
HELIX 310 324 {ECO:0000244|PDB:5L8L}.
HELIX 334 342 {ECO:0000244|PDB:5L8L}.
STRAND 350 352 {ECO:0000244|PDB:1OL6}.
HELIX 354 363 {ECO:0000244|PDB:5L8L}.
HELIX 368 370 {ECO:0000244|PDB:5L8L}.
HELIX 374 378 {ECO:0000244|PDB:5L8L}.
HELIX 381 386 {ECO:0000244|PDB:5L8L}.
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


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