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Aurora kinase B (EC 2.7.11.1) (Aurora 1) (Aurora- and IPL1-like midbody-associated protein 1) (AIM-1) (Aurora/IPL1-related kinase 2) (ARK-2) (Aurora-related kinase 2) (STK-1) (Serine/threonine-protein kinase 12) (Serine/threonine-protein kinase 5) (Serine/threonine-protein kinase aurora-B)

 AURKB_HUMAN             Reviewed;         344 AA.
Q96GD4; B4DNM4; C7G533; C7G534; C7G535; D3DTR4; J9JID1; O14630;
O60446; O95083; Q96DV5; Q9UQ46;
17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 3.
20-JUN-2018, entry version 198.
RecName: Full=Aurora kinase B;
EC=2.7.11.1;
AltName: Full=Aurora 1;
AltName: Full=Aurora- and IPL1-like midbody-associated protein 1;
Short=AIM-1;
AltName: Full=Aurora/IPL1-related kinase 2;
Short=ARK-2;
Short=Aurora-related kinase 2;
AltName: Full=STK-1;
AltName: Full=Serine/threonine-protein kinase 12;
AltName: Full=Serine/threonine-protein kinase 5;
AltName: Full=Serine/threonine-protein kinase aurora-B;
Name=AURKB; Synonyms=AIK2, AIM1, AIRK2, ARK2, STK1, STK12, STK5;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT THR-298.
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).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
VARIANT THR-298.
PubMed=9809983;
Tatsuka M., Katayama H., Ota T., Tanaka T., Odashima S., Suzuki F.,
Terada Y.;
"Multinuclearity and increased ploidy caused by overexpression of the
aurora- and Ipl1-like midbody-associated protein mitotic kinase in
human cancer cells.";
Cancer Res. 58:4811-4816(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
VARIANT THR-298.
TISSUE=Liver, and Spleen;
PubMed=9858806;
Kimura M., Matsuda Y., Yoshioka T., Sumi N., Okano Y.;
"Identification and characterization of STK12/Aik2: a human gene
related to aurora of Drosophila and yeast IPL1.";
Cytogenet. Cell Genet. 82:147-152(1998).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT THR-298.
PubMed=11471245;
Prigent C., Gill R., Trower M., Sanseau P.;
"In silico cloning of a new protein kinase, Aik2, related to
Drosophila aurora using the new tool: EST Blast.";
In Silico Biol. 1:123-128(1999).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT THR-298.
Zhang Q., Yu L., Bi A.;
"Cloning of a novel human gene homologous to mouse STK-1.";
Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), AND ALTERNATIVE
SPLICING.
PubMed=19134008; DOI=10.1111/j.1349-7006.2008.01068.x;
Yasen M., Mizushima H., Mogushi K., Obulhasim G., Miyaguchi K.,
Inoue K., Nakahara I., Ohta T., Aihara A., Tanaka S., Arii S.,
Tanaka H.;
"Expression of Aurora B and alternative variant forms in
hepatocellular carcinoma and adjacent tissue.";
Cancer Sci. 100:472-480(2009).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
THR-298.
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[10]
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.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), AND VARIANT
THR-298.
TISSUE=Lung, Lymph, 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).
[12]
IDENTIFICATION IN THE CPC COMPLEX, SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=11516652; DOI=10.1016/S0960-9822(01)00238-X;
Wheatley S.P., Carvalho A., Vagnarelli P., Earnshaw W.C.;
"INCENP is required for proper targeting of Survivin to the
centromeres and the anaphase spindle during mitosis.";
Curr. Biol. 11:886-890(2001).
[13]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=11756469; DOI=10.1083/jcb.200108125;
Zeitlin S.G., Shelby R.D., Sullivan K.F.;
"CENP-A is phosphorylated by Aurora B kinase and plays an unexpected
role in completion of cytokinesis.";
J. Cell Biol. 155:1147-1157(2001).
[14]
REVIEW.
PubMed=11413462; DOI=10.1038/35048096;
Nigg E.A.;
"Mitotic kinases as regulators of cell division and its checkpoints.";
Nat. Rev. Mol. Cell Biol. 2:21-32(2001).
[15]
FUNCTION IN PHOSPHORYLATION OF HISTONE H3.
PubMed=11856369; DOI=10.1046/j.1356-9597.2001.00498.x;
Goto H., Yasui Y., Nigg E.A., Inagaki M.;
"Aurora-B phosphorylates Histone H3 at serine28 with regard to the
mitotic chromosome condensation.";
Genes Cells 7:11-17(2002).
[16]
FUNCTION IN PHOSPHORYLATION OF HISTONE H3.
PubMed=11784863; DOI=10.1128/MCB.22.3.874-885.2002;
Crosio C., Fimia G.M., Loury R., Kimura M., Okano Y., Zhou H., Sen S.,
Allis C.D., Sassone-Corsi P.;
"Mitotic phosphorylation of histone H3: spatio-temporal regulation by
mammalian Aurora kinases.";
Mol. Cell. Biol. 22:874-885(2002).
[17]
FUNCTION, AND INTERACTION WITH RACGAP1.
PubMed=12689593; DOI=10.1016/S1534-5807(03)00089-3;
Minoshima Y., Kawashima T., Hirose K., Tonozuka Y., Kawajiri A.,
Bao Y.C., Deng X., Tatsuka M., Narumiya S., May W.S. Jr., Nosaka T.,
Semba K., Inoue T., Satoh T., Inagaki M., Kitamura T.;
"Phosphorylation by aurora B converts MgcRacGAP to a RhoGAP during
cytokinesis.";
Dev. Cell 4:549-560(2003).
[18]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=12458200; DOI=10.1074/jbc.M210892200;
Goto H., Yasui Y., Kawajiri A., Nigg E.A., Terada Y., Tatsuka M.,
Nagata K., Inagaki M.;
"Aurora-B regulates the cleavage furrow-specific vimentin
phosphorylation in the cytokinetic process.";
J. Biol. Chem. 278:8526-8530(2003).
[19]
FUNCTION, AND MUTAGENESIS OF LYS-106.
PubMed=12686604; DOI=10.1091/mbc.E02-09-0612;
Kawajiri A., Yasui Y., Goto H., Tatsuka M., Takahashi M., Nagata K.,
Inagaki M.;
"Functional significance of the specific sites phosphorylated in
desmin at cleavage furrow: Aurora-B may phosphorylate and regulate
type III intermediate filaments during cytokinesis coordinatedly with
Rho-kinase.";
Mol. Biol. Cell 14:1489-1500(2003).
[20]
IDENTIFICATION IN THE CPC COMPLEX, FUNCTION OF THE CPC COMPLEX,
INDUCTION, SUBCELLULAR LOCATION, ENZYME REGULATION, AND MUTAGENESIS OF
LYS-106.
PubMed=12925766; DOI=10.1091/mbc.E02-11-0769;
Honda R., Korner R., Nigg E.A.;
"Exploring the functional interactions between Aurora B, INCENP, and
survivin in mitosis.";
Mol. Biol. Cell 14:3325-3341(2003).
[21]
INTERACTION WITH PSMA3.
PubMed=14674694; DOI=10.1023/A:1027317014159;
Shu F., Guo S., Dang Y., Qi M., Zhou G., Guo Z., Zhang Y., Wu C.,
Zhao S., Yu L.;
"Human Aurora-B binds to a proteasome alpha-subunit HC8 and undergoes
degradation in a proteasome-dependent manner.";
Mol. Cell. Biochem. 254:157-162(2003).
[22]
FUNCTION.
PubMed=14610074; DOI=10.1074/jbc.M311299200;
Wheatley S.P., Henzing A.J., Dodson H., Khaled W., Earnshaw W.C.;
"Aurora-B phosphorylation in vitro identifies a residue of survivin
that is essential for its localization and binding to inner centromere
protein (INCENP) in vivo.";
J. Biol. Chem. 279:5655-5660(2004).
[23]
PHOSPHORYLATION AT THR-232, FUNCTION, INTERACTION WITH INCENP, ENZYME
REGULATION, AND MUTAGENESIS OF LYS-106.
PubMed=14722118; DOI=10.1074/jbc.M311128200;
Yasui Y., Urano T., Kawajiri A., Nagata K., Tatsuka M., Saya H.,
Furukawa K., Takahashi T., Izawa I., Inagaki M.;
"Autophosphorylation of a newly identified site of Aurora-B is
indispensable for cytokinesis.";
J. Biol. Chem. 279:12997-13003(2004).
[24]
FUNCTION.
PubMed=15020684; DOI=10.1242/jcs.01006;
Johnson V.L., Scott M.I., Holt S.V., Hussein D., Taylor S.S.;
"Bub1 is required for kinetochore localization of BubR1, Cenp-E, Cenp-
F and Mad2, and chromosome congression.";
J. Cell Sci. 117:1577-1589(2004).
[25]
INTERACTION WITH CDCA8, ENZYME REGULATION, AND FUNCTION.
PubMed=15249581; DOI=10.1083/jcb.200404001;
Gassmann R., Carvalho A., Henzing A.J., Ruchaud S., Hudson D.F.,
Honda R., Nigg E.A., Gerloff D.L., Earnshaw W.C.;
"Borealin: a novel chromosomal passenger required for stability of the
bipolar mitotic spindle.";
J. Cell Biol. 166:179-191(2004).
[26]
FUNCTION, AND INTERACTION WITH CDCA1 AND NDC80.
PubMed=14602875; DOI=10.1074/mcp.M300072-MCP200;
Tien A.-C., Lin M.-H., Su L.-J., Hong Y.-R., Cheng T.-S., Lee Y.-C.G.,
Lin W.-J., Still I.H., Huang C.-Y.F.;
"Identification of the substrates and interaction proteins of aurora
kinases from a protein-protein interaction model.";
Mol. Cell. Proteomics 3:93-104(2004).
[27]
INTERACTION WITH TACC1.
PubMed=15064709; DOI=10.1038/sj.onc.1207593;
Delaval B., Ferrand A., Conte N., Larroque C., Hernandez-Verdun D.,
Prigent C., Birnbaum D.;
"Aurora B -TACC1 protein complex in cytokinesis.";
Oncogene 23:4516-4522(2004).
[28]
SUBCELLULAR LOCATION, INTERACTION WITH SEPT1, AND MUTAGENESIS OF
LYS-106.
PubMed=16179162; DOI=10.1016/j.bbrc.2005.06.212;
Qi M., Yu W., Liu S., Jia H., Tang L., Shen M., Yan X., Saiyin H.,
Lang Q., Wan B., Zhao S., Yu L.;
"Septin1, a new interaction partner for human serine/threonine kinase
aurora-B.";
Biochem. Biophys. Res. Commun. 336:994-1000(2005).
[29]
FUNCTION.
PubMed=16103226; DOI=10.1083/jcb.200501097;
Yuce O., Piekny A., Glotzer M.;
"An ECT2-centralspindlin complex regulates the localization and
function of RhoA.";
J. Cell Biol. 170:571-582(2005).
[30]
INTERACTION WITH EVI5.
PubMed=16764853; DOI=10.1016/j.yexcr.2006.03.032;
Faitar S.L., Sossey-Alaoui K., Ranalli T.A., Cowell J.K.;
"EVI5 protein associates with the INCENP-aurora B kinase-survivin
chromosomal passenger complex and is involved in the completion of
cytokinesis.";
Exp. Cell Res. 312:2325-2335(2006).
[31]
FUNCTION.
PubMed=17617734; DOI=10.4161/cc.6.13.4442;
Pouwels J., Kukkonen A.M., Lan W., Daum J.R., Gorbsky G.J.,
Stukenberg T., Kallio M.J.;
"Shugoshin 1 plays a central role in kinetochore assembly and is
required for kinetochore targeting of Plk1.";
Cell Cycle 6:1579-1585(2007).
[32]
UBIQUITINATION.
PubMed=17543862; DOI=10.1016/j.devcel.2007.03.019;
Sumara I., Quadroni M., Frei C., Olma M.H., Sumara G., Ricci R.,
Peter M.;
"A Cul3-based E3 ligase removes Aurora B from mitotic chromosomes,
regulating mitotic progression and completion of cytokinesis in human
cells.";
Dev. Cell 12:887-900(2007).
[33]
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).
[34]
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).
[35]
INTERACTION WITH BIRC5.
PubMed=18591255; DOI=10.1128/MCB.02039-07;
Xia F., Canovas P.M., Guadagno T.M., Altieri D.C.;
"A survivin-ran complex regulates spindle formation in tumor cells.";
Mol. Cell. Biol. 28:5299-5311(2008).
[36]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-35, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[37]
UBIQUITINATION.
PubMed=19995937; DOI=10.1083/jcb.200906117;
Maerki S., Olma M.H., Staubli T., Steigemann P., Gerlich D.W.,
Quadroni M., Sumara I., Peter M.;
"The Cul3-KLHL21 E3 ubiquitin ligase targets aurora B to midzone
microtubules in anaphase and is required for cytokinesis.";
J. Cell Biol. 187:791-800(2009).
[38]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[39]
INTERACTION WITH SPDYC, AND SUBCELLULAR LOCATION.
PubMed=20605920; DOI=10.1242/jcs.059964;
Mouron S., de Carcer G., Seco E., Fernandez-Miranda G., Malumbres M.,
Nebreda A.R.;
"RINGO C is required to sustain the spindle-assembly checkpoint.";
J. Cell Sci. 123:2586-2595(2010).
[40]
INTERACTION WITH INCENP.
PubMed=20562864; DOI=10.1038/ncb2075;
Nozawa R.S., Nagao K., Masuda H.T., Iwasaki O., Hirota T., Nozaki N.,
Kimura H., Obuse C.;
"Human POGZ modulates dissociation of HP1alpha from mitotic chromosome
arms through Aurora B activation.";
Nat. Cell Biol. 12:719-727(2010).
[41]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62 AND THR-64, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[42]
SUBCELLULAR LOCATION.
PubMed=20929775; DOI=10.1126/science.1194498;
Yamagishi Y., Honda T., Tanno Y., Watanabe Y.;
"Two histone marks establish the inner centromere and chromosome bi-
orientation.";
Science 330:239-243(2010).
[43]
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).
[44]
FUNCTION IN PHOSPHORYLATION OF HASPIN.
PubMed=21658950; DOI=10.1016/j.cub.2011.05.016;
Wang F., Ulyanova N.P., van der Waal M.S., Patnaik D., Lens S.M.,
Higgins J.M.;
"A positive feedback loop involving Haspin and Aurora B promotes CPC
accumulation at centromeres in mitosis.";
Curr. Biol. 21:1061-1069(2011).
[45]
FUNCTION IN PHOSPHORYLATION OF TP53, INTERACTION WITH NOC2L AND TP53,
AND SUBCELLULAR LOCATION.
PubMed=20959462; DOI=10.1074/jbc.M110.174755;
Wu L., Ma C.A., Zhao Y., Jain A.;
"Aurora B interacts with NIR-p53, leading to p53 phosphorylation in
its DNA-binding domain and subsequent functional suppression.";
J. Biol. Chem. 286:2236-2244(2011).
[46]
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).
[47]
INTERACTION WITH TTC28, AND SUBCELLULAR LOCATION.
PubMed=23036704; DOI=10.1016/j.gene.2012.09.061;
Izumiyama T., Minoshima S., Yoshida T., Shimizu N.;
"A novel big protein TPRBK possessing 25 units of TPR motif is
essential for the progress of mitosis and cytokinesis.";
Gene 511:202-217(2012).
[48]
FUNCTION, AND INTERACTION WITH CHMP4C.
PubMed=22422861; DOI=10.1126/science.1217180;
Carlton J.G., Caballe A., Agromayor M., Kloc M., Martin-Serrano J.;
"ESCRT-III governs the Aurora B-mediated abscission checkpoint through
CHMP4C.";
Science 336:220-225(2012).
[49]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[50]
FUNCTION.
PubMed=24814515; DOI=10.1038/ncb2959;
Thoresen S.B., Campsteijn C., Vietri M., Schink K.O., Liestoel K.,
Andersen J.S., Raiborg C., Stenmark H.;
"ANCHR mediates Aurora-B-dependent abscission checkpoint control
through retention of VPS4.";
Nat. Cell Biol. 16:550-560(2014).
[51]
SUBUNIT.
PubMed=27332895; DOI=10.1371/journal.pone.0157305;
Sasai K., Katayama H., Hawke D.H., Sen S.;
"Aurora-C interactions with survivin and INCENP reveal shared and
distinct features compared with Aurora-B chromosome passenger protein
complex.";
PLoS ONE 11:E0157305-E0157305(2016).
[52]
X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 55-344 IN COMPLEX WITH
INCENP.
PubMed=22920039; DOI=10.1021/jm3008954;
Elkins J.M., Santaguida S., Musacchio A., Knapp S.;
"Crystal structure of human aurora B in complex with INCENP and VX-
680.";
J. Med. Chem. 55:7841-7848(2012).
[53]
VARIANT THR-298.
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).
[54]
VARIANTS [LARGE SCALE ANALYSIS] VAL-52 AND MET-179.
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: Serine/threonine-protein kinase component of the
chromosomal passenger complex (CPC), a complex that acts as a key
regulator of mitosis. The CPC complex has essential functions at
the centromere in ensuring correct chromosome alignment and
segregation and is required for chromatin-induced microtubule
stabilization and spindle assembly. Involved in the bipolar
attachment of spindle microtubules to kinetochores and is a key
regulator for the onset of cytokinesis during mitosis. Required
for central/midzone spindle assembly and cleavage furrow
formation. Key component of the cytokinesis checkpoint, a process
required to delay abscission to prevent both premature resolution
of intercellular chromosome bridges and accumulation of DNA
damage: phosphorylates CHMP4C, leading to retain abscission-
competent VPS4 (VPS4A and/or VPS4B) at the midbody ring until
abscission checkpoint signaling is terminated at late cytokinesis
(PubMed:22422861, PubMed:24814515). AURKB phosphorylates the CPC
complex subunits BIRC5/survivin, CDCA8/borealin and INCENP.
Phosphorylation of INCENP leads to increased AURKB activity. Other
known AURKB substrates involved in centromeric functions and
mitosis are CENPA, DES/desmin, GPAF, KIF2C, NSUN2, RACGAP1, SEPT1,
VIM/vimentin, HASPIN, and histone H3. A positive feedback loop
involving HASPIN and AURKB contributes to localization of CPC to
centromeres. Phosphorylation of VIM controls vimentin filament
segregation in cytokinetic process, whereas histone H3 is
phosphorylated at 'Ser-10' and 'Ser-28' during mitosis (H3S10ph
and H3S28ph, respectively). A positive feedback between HASPIN and
AURKB contributes to CPC localization. AURKB is also required for
kinetochore localization of BUB1 and SGO1. Phosphorylation of
p53/TP53 negatively regulates its transcriptional activity. Key
regulator of active promoters in resting B- and T-lymphocytes:
acts by mediating phosphorylation of H3S28ph at active promoters
in resting B-cells, inhibiting RNF2/RING1B-mediated ubiquitination
of histone H2A and enhancing binding and activity of the USP16
deubiquitinase at transcribed genes. {ECO:0000269|PubMed:11516652,
ECO:0000269|PubMed:11756469, ECO:0000269|PubMed:11784863,
ECO:0000269|PubMed:11856369, ECO:0000269|PubMed:12458200,
ECO:0000269|PubMed:12686604, ECO:0000269|PubMed:12689593,
ECO:0000269|PubMed:12925766, ECO:0000269|PubMed:14602875,
ECO:0000269|PubMed:14610074, ECO:0000269|PubMed:14722118,
ECO:0000269|PubMed:15020684, ECO:0000269|PubMed:15249581,
ECO:0000269|PubMed:16103226, ECO:0000269|PubMed:17617734,
ECO:0000269|PubMed:20959462, ECO:0000269|PubMed:21658950,
ECO:0000269|PubMed:22422861, ECO:0000269|PubMed:24814515}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- ENZYME REGULATION: Activity is greatly increased when AURKB is
within the CPC complex. In particular, AURKB-phosphorylated INCENP
acts as an activator of AURKB. Positive feedback between HASPIN
and AURKB contributes to CPC localization.
{ECO:0000269|PubMed:12925766, ECO:0000269|PubMed:14722118,
ECO:0000269|PubMed:15249581}.
-!- SUBUNIT: Component of the chromosomal passenger complex (CPC)
composed of at least BIRC5/survivin, CDCA8/borealin, INCENP, AURKB
or AURKC; predominantly independent AURKB- and AURKC-containing
complexes exist. Associates with RACGAP1 during M phase. Interacts
with CDCA1, EVI5, JTB, NDC80, PSMA3, SEPT1, SIRT2 and TACC1.
Interacts with SPDYC; this interaction may be required for proper
localization of active, Thr-232-phosphorylated AURKB form during
prometaphase and metaphase. Interacts with p53/TP53. Interacts
(via the middle kinase domain) with NOC2L (via the N- and C-
terminus domains). Interacts with TTC28. Interacts with
RNF2/RING1B. {ECO:0000269|PubMed:11516652,
ECO:0000269|PubMed:12689593, ECO:0000269|PubMed:12925766,
ECO:0000269|PubMed:14602875, ECO:0000269|PubMed:14674694,
ECO:0000269|PubMed:14722118, ECO:0000269|PubMed:15064709,
ECO:0000269|PubMed:15249581, ECO:0000269|PubMed:16179162,
ECO:0000269|PubMed:16764853, ECO:0000269|PubMed:17726514,
ECO:0000269|PubMed:18591255, ECO:0000269|PubMed:20562864,
ECO:0000269|PubMed:20605920, ECO:0000269|PubMed:20959462,
ECO:0000269|PubMed:21225229, ECO:0000269|PubMed:22422861,
ECO:0000269|PubMed:23036704, ECO:0000269|PubMed:27332895}.
-!- INTERACTION:
O15392:BIRC5; NbExp=13; IntAct=EBI-624291, EBI-518823;
O15392-1:BIRC5; NbExp=2; IntAct=EBI-624291, EBI-518838;
O15392-2:BIRC5; NbExp=2; IntAct=EBI-624291, EBI-518842;
Q16543:CDC37; NbExp=4; IntAct=EBI-624291, EBI-295634;
Q53HL2:CDCA8; NbExp=9; IntAct=EBI-624291, EBI-979174;
Q86XJ1:GAS2L3; NbExp=4; IntAct=EBI-624291, EBI-9248152;
Q16695:HIST3H3; NbExp=8; IntAct=EBI-624291, EBI-358900;
P08238:HSP90AB1; NbExp=3; IntAct=EBI-624291, EBI-352572;
Q9NQS7:INCENP; NbExp=18; IntAct=EBI-624291, EBI-307907;
Q9NQS7-1:INCENP; NbExp=2; IntAct=EBI-624291, EBI-15767972;
Q92993:KAT5; NbExp=4; IntAct=EBI-624291, EBI-399080;
Q15691:MAPRE1; NbExp=5; IntAct=EBI-624291, EBI-1004115;
P06748:NPM1; NbExp=5; IntAct=EBI-624291, EBI-78579;
P30153:PPP2R1A; NbExp=2; IntAct=EBI-624291, EBI-302388;
Q8WYJ6:SEPT1; NbExp=6; IntAct=EBI-624291, EBI-693002;
O75410-6:TACC1; NbExp=2; IntAct=EBI-624291, EBI-624278;
Q99986:VRK1; NbExp=14; IntAct=EBI-624291, EBI-1769146;
-!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Chromosome, centromere.
Cytoplasm, cytoskeleton, spindle. Midbody. Note=Localizes on
chromosome arms and inner centromeres from prophase through
metaphase and then transferring to the spindle midzone and midbody
from anaphase through cytokinesis. Colocalized with gamma tubulin
in the midbody. Proper localization of the active, Thr-232-
phosphorylated form during metaphase may be dependent upon
interaction with SPDYC. Colocalized with SIRT2 during cytokinesis
with the midbody. Localization (and probably targeting of the CPC)
to the inner centromere occurs predominantly in regions with
overlapping mitosis-specific histone phosphorylations H3pT3 and
H2ApT12. {ECO:0000269|PubMed:20929775}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=Q96GD4-1; Sequence=Displayed;
Name=2; Synonyms=aurkb-sv1;
IsoId=Q96GD4-2; Sequence=VSP_044385;
Name=3; Synonyms=aurkb-sv2;
IsoId=Q96GD4-3; Sequence=VSP_044384, VSP_044386, VSP_044387;
Note=Not expressed in normal liver, high expression in
metastatic liver.;
Name=4;
IsoId=Q96GD4-4; Sequence=VSP_047103;
Name=5;
IsoId=Q96GD4-5; Sequence=VSP_044384;
-!- TISSUE SPECIFICITY: High level expression seen in the thymus. It
is also expressed in the spleen, lung, testis, colon, placenta and
fetal liver. Expressed during S and G2/M phase and expression is
up-regulated in cancer cells during M phase.
{ECO:0000269|PubMed:9809983, ECO:0000269|PubMed:9858806}.
-!- INDUCTION: Expression is cell cycle-regulated, with a low in G1/S,
an increase during G2 and M. Expression decreases again after M
phase. {ECO:0000269|PubMed:12925766}.
-!- PTM: The phosphorylation of Thr-232 requires the binding to INCENP
and occurs by means of an autophosphorylation mechanism. Thr-232
phosphorylation is indispensable for the AURKB kinase activity.
{ECO:0000269|PubMed:14722118}.
-!- PTM: Ubiquitinated by different BCR (BTB-CUL3-RBX1) E3 ubiquitin
ligase complexes. Ubiquitinated by the BCR(KLHL9-KLHL13) E3
ubiquitin ligase complex, ubiquitination leads to removal from
mitotic chromosomes and is required for cytokinesis. During
anaphase, the BCR(KLHL21) E3 ubiquitin ligase complex recruits the
CPC complex from chromosomes to the spindle midzone and mediates
the ubiquitination of AURKB. Ubiquitination of AURKB by
BCR(KLHL21) E3 ubiquitin ligase complex may not lead to its
degradation by the proteasome. {ECO:0000269|PubMed:17543862,
ECO:0000269|PubMed:19995937}.
-!- DISEASE: Note=Disruptive regulation of expression is a possible
mechanism of the perturbation of chromosomal integrity in cancer
cells through its dominant-negative effect on cytokinesis.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. Aurora subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-!- SEQUENCE CAUTION:
Sequence=AAH13300.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF008552; AAC12709.1; -; mRNA.
EMBL; AB011450; BAA32136.1; -; mRNA.
EMBL; AB011446; BAA82709.1; -; mRNA.
EMBL; AF004022; AAB65786.1; -; mRNA.
EMBL; AF015254; AAC98891.1; -; mRNA.
EMBL; AB519677; BAI23190.1; -; mRNA.
EMBL; AB519678; BAI23191.1; -; mRNA.
EMBL; AB519679; BAI23192.1; -; mRNA.
EMBL; BT019534; AAV38341.1; -; mRNA.
EMBL; AK297976; BAG60286.1; -; mRNA.
EMBL; AC135178; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471108; EAW90075.1; -; Genomic_DNA.
EMBL; CH471108; EAW90077.1; -; Genomic_DNA.
EMBL; CH471108; EAW90078.1; -; Genomic_DNA.
EMBL; BC000442; AAH00442.3; -; mRNA.
EMBL; BC009751; AAH09751.1; -; mRNA.
EMBL; BC013300; AAH13300.2; ALT_INIT; mRNA.
EMBL; BC080581; AAH80581.1; -; mRNA.
CCDS; CCDS11134.1; -. [Q96GD4-1]
CCDS; CCDS58514.1; -. [Q96GD4-4]
CCDS; CCDS67162.1; -. [Q96GD4-5]
CCDS; CCDS82065.1; -. [Q96GD4-2]
RefSeq; NP_001243763.1; NM_001256834.2. [Q96GD4-4]
RefSeq; NP_001271455.1; NM_001284526.1. [Q96GD4-5]
RefSeq; NP_001300879.1; NM_001313950.1. [Q96GD4-1]
RefSeq; NP_001300880.1; NM_001313951.1. [Q96GD4-4]
RefSeq; NP_001300881.1; NM_001313952.1.
RefSeq; NP_001300882.1; NM_001313953.1. [Q96GD4-2]
RefSeq; NP_001300883.1; NM_001313954.1.
RefSeq; NP_001300884.1; NM_001313955.1.
RefSeq; NP_004208.2; NM_004217.3. [Q96GD4-1]
RefSeq; XP_011522372.1; XM_011524070.2.
RefSeq; XP_011522374.1; XM_011524072.2. [Q96GD4-4]
RefSeq; XP_016880796.1; XM_017025307.1. [Q96GD4-4]
UniGene; Hs.442658; -.
PDB; 4AF3; X-ray; 2.75 A; A=55-344.
PDBsum; 4AF3; -.
ProteinModelPortal; Q96GD4; -.
SMR; Q96GD4; -.
BioGrid; 114646; 164.
ComplexPortal; CPX-116; Chromosomal passenger complex.
CORUM; Q96GD4; -.
DIP; DIP-34530N; -.
ELM; Q96GD4; -.
IntAct; Q96GD4; 88.
MINT; Q96GD4; -.
STRING; 9606.ENSP00000463999; -.
BindingDB; Q96GD4; -.
ChEMBL; CHEMBL2185; -.
DrugBank; DB05169; AT9283.
DrugBank; DB04703; HESPERIDIN.
GuidetoPHARMACOLOGY; 1937; -.
iPTMnet; Q96GD4; -.
PhosphoSitePlus; Q96GD4; -.
SwissPalm; Q96GD4; -.
BioMuta; AURKB; -.
DMDM; 317373473; -.
EPD; Q96GD4; -.
MaxQB; Q96GD4; -.
PaxDb; Q96GD4; -.
PeptideAtlas; Q96GD4; -.
PRIDE; Q96GD4; -.
ProteomicsDB; 76623; -.
DNASU; 9212; -.
Ensembl; ENST00000316199; ENSP00000313950; ENSG00000178999. [Q96GD4-5]
Ensembl; ENST00000534871; ENSP00000443869; ENSG00000178999. [Q96GD4-4]
Ensembl; ENST00000578549; ENSP00000462207; ENSG00000178999. [Q96GD4-2]
Ensembl; ENST00000585124; ENSP00000463999; ENSG00000178999. [Q96GD4-1]
GeneID; 9212; -.
KEGG; hsa:9212; -.
UCSC; uc002gkm.5; human. [Q96GD4-1]
CTD; 9212; -.
DisGeNET; 9212; -.
EuPathDB; HostDB:ENSG00000178999.12; -.
GeneCards; AURKB; -.
H-InvDB; HIX0019005; -.
HGNC; HGNC:11390; AURKB.
HPA; CAB005862; -.
HPA; HPA037708; -.
MIM; 604970; gene.
neXtProt; NX_Q96GD4; -.
OpenTargets; ENSG00000178999; -.
PharmGKB; PA36199; -.
eggNOG; KOG0580; Eukaryota.
eggNOG; ENOG410XNRB; LUCA.
GeneTree; ENSGT00910000144066; -.
HOVERGEN; HBG108519; -.
InParanoid; Q96GD4; -.
KO; K11479; -.
OMA; PYGRQTT; -.
OrthoDB; EOG091G0EU2; -.
PhylomeDB; Q96GD4; -.
TreeFam; TF351439; -.
Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
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-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
Reactome; R-HSA-4615885; SUMOylation of DNA replication proteins.
Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
Reactome; R-HSA-68877; Mitotic Prometaphase.
SignaLink; Q96GD4; -.
SIGNOR; Q96GD4; -.
GeneWiki; Aurora_B_kinase; -.
GenomeRNAi; 9212; -.
PRO; PR:Q96GD4; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000178999; -.
CleanEx; HS_AIM1; -.
CleanEx; HS_AURKB; -.
ExpressionAtlas; Q96GD4; baseline and differential.
Genevisible; Q96GD4; HS.
GO; GO:0010369; C:chromocenter; IEA:Ensembl.
GO; GO:0032133; C:chromosome passenger complex; IPI:UniProtKB.
GO; GO:0000779; C:condensed chromosome, centromeric region; IDA:UniProtKB.
GO; GO:0000780; C:condensed nuclear chromosome, centromeric region; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0030496; C:midbody; IDA:UniProtKB.
GO; GO:1990023; C:mitotic spindle midzone; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005819; C:spindle; TAS:UniProtKB.
GO; GO:0005876; C:spindle microtubule; IBA:GO_Central.
GO; GO:0051233; C:spindle midzone; IBA:GO_Central.
GO; GO:0031616; C:spindle pole centrosome; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0035174; F:histone serine kinase activity; ISS:UniProtKB.
GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:FlyBase.
GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; TAS:UniProtKB.
GO; GO:0009838; P:abscission; ISS:UniProtKB.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; TAS:Reactome.
GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; TAS:UniProtKB.
GO; GO:0008283; P:cell proliferation; IEA:Ensembl.
GO; GO:0034644; P:cellular response to UV; IDA:UniProtKB.
GO; GO:0036089; P:cleavage furrow formation; IDA:UniProtKB.
GO; GO:0043988; P:histone H3-S28 phosphorylation; ISS:UniProtKB.
GO; GO:0016570; P:histone modification; TAS:UniProtKB.
GO; GO:0044878; P:mitotic cytokinesis checkpoint; ISS:UniProtKB.
GO; GO:0051256; P:mitotic spindle midzone assembly; IMP:UniProtKB.
GO; GO:0002903; P:negative regulation of B cell apoptotic process; IDA:UniProtKB.
GO; GO:0032466; P:negative regulation of cytokinesis; ISS:UniProtKB.
GO; GO:0032091; P:negative regulation of protein binding; IDA:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:0032467; P:positive regulation of cytokinesis; IMP:UniProtKB.
GO; GO:0051973; P:positive regulation of telomerase activity; IMP:BHF-UCL.
GO; GO:1904355; P:positive regulation of telomere capping; IMP:BHF-UCL.
GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; IMP:BHF-UCL.
GO; GO:0046777; P:protein autophosphorylation; TAS:UniProtKB.
GO; GO:0034501; P:protein localization to kinetochore; IMP:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0051983; P:regulation of chromosome segregation; TAS:UniProtKB.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
GO; GO:0031577; P:spindle checkpoint; IEA:InterPro.
GO; GO:0007051; P:spindle organization; IMP:UniProtKB.
InterPro; IPR030616; Aur.
InterPro; IPR028772; AURKB.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
PANTHER; PTHR24350; PTHR24350; 1.
PANTHER; PTHR24350:SF4; PTHR24350:SF4; 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; Alternative splicing; ATP-binding; Cell cycle;
Cell division; Centromere; Chromosome; Complete proteome; Cytoplasm;
Cytoskeleton; Kinase; Magnesium; Metal-binding; Mitosis;
Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Serine/threonine-protein kinase; Transferase;
Ubl conjugation.
CHAIN 1 344 Aurora kinase B.
/FTId=PRO_0000085656.
DOMAIN 77 327 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 83 91 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 200 200 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 106 106 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 35 35 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 62 62 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 64 64 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 227 227 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 232 232 Phosphothreonine; by autocatalysis.
{ECO:0000269|PubMed:14722118}.
VAR_SEQ 1 41 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_047103.
VAR_SEQ 69 69 T -> TR (in isoform 3 and isoform 5).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:19134008}.
/FTId=VSP_044384.
VAR_SEQ 86 134 GKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREI
EIQAHLHH -> ALLCLWPEASSVSSPSH (in isoform
2). {ECO:0000303|PubMed:19134008}.
/FTId=VSP_044385.
VAR_SEQ 133 141 HHPNILRLY -> QSWRSWQML (in isoform 3).
{ECO:0000303|PubMed:19134008}.
/FTId=VSP_044386.
VAR_SEQ 142 344 Missing (in isoform 3).
{ECO:0000303|PubMed:19134008}.
/FTId=VSP_044387.
VARIANT 52 52 A -> V (in dbSNP:rs55878091).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040383.
VARIANT 100 100 H -> Q (in dbSNP:rs3027254).
/FTId=VAR_027970.
VARIANT 179 179 T -> M (in dbSNP:rs55871613).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040384.
VARIANT 298 298 M -> T (in dbSNP:rs1059476).
{ECO:0000269|PubMed:11471245,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:16762494,
ECO:0000269|PubMed:9514916,
ECO:0000269|PubMed:9809983,
ECO:0000269|PubMed:9858806,
ECO:0000269|Ref.5, ECO:0000269|Ref.7}.
/FTId=VAR_027971.
MUTAGEN 106 106 K->R: Leads to loss of kinase activity
and severely impairs mitotic progression.
{ECO:0000269|PubMed:12686604,
ECO:0000269|PubMed:12925766,
ECO:0000269|PubMed:14722118,
ECO:0000269|PubMed:16179162}.
CONFLICT 14 15 RQ -> DK (in Ref. 5; AAC98891).
{ECO:0000305}.
CONFLICT 161 161 E -> M (in Ref. 4; AAB65786 and 5;
AAC98891). {ECO:0000305}.
CONFLICT 167 169 QKS -> HKT (in Ref. 4; AAB65786).
{ECO:0000305}.
CONFLICT 179 179 T -> TVRR (in Ref. 4; AAB65786).
{ECO:0000305}.
CONFLICT 180 180 I -> VRAV (in Ref. 5; AAC98891).
{ECO:0000305}.
CONFLICT 226 226 P -> T (in Ref. 3; BAA82709).
{ECO:0000305}.
CONFLICT 249 250 MH -> ID (in Ref. 3; BAA82709).
{ECO:0000305}.
CONFLICT 271 271 Missing (in Ref. 3; BAA82709).
{ECO:0000305}.
HELIX 74 76 {ECO:0000244|PDB:4AF3}.
STRAND 77 82 {ECO:0000244|PDB:4AF3}.
STRAND 89 96 {ECO:0000244|PDB:4AF3}.
TURN 97 99 {ECO:0000244|PDB:4AF3}.
STRAND 102 109 {ECO:0000244|PDB:4AF3}.
HELIX 110 116 {ECO:0000244|PDB:4AF3}.
HELIX 119 130 {ECO:0000244|PDB:4AF3}.
STRAND 140 145 {ECO:0000244|PDB:4AF3}.
STRAND 147 155 {ECO:0000244|PDB:4AF3}.
HELIX 162 169 {ECO:0000244|PDB:4AF3}.
HELIX 174 193 {ECO:0000244|PDB:4AF3}.
HELIX 203 205 {ECO:0000244|PDB:4AF3}.
STRAND 206 208 {ECO:0000244|PDB:4AF3}.
STRAND 214 216 {ECO:0000244|PDB:4AF3}.
HELIX 242 245 {ECO:0000244|PDB:4AF3}.
HELIX 253 268 {ECO:0000244|PDB:4AF3}.
HELIX 278 286 {ECO:0000244|PDB:4AF3}.
HELIX 298 307 {ECO:0000244|PDB:4AF3}.
HELIX 312 314 {ECO:0000244|PDB:4AF3}.
HELIX 318 322 {ECO:0000244|PDB:4AF3}.
HELIX 325 330 {ECO:0000244|PDB:4AF3}.
SEQUENCE 344 AA; 39311 MW; A5ED13EF5A1FAFBF CRC64;
MAQKENSYPW PYGRQTAPSG LSTLPQRVLR KEPVTPSALV LMSRSNVQPT AAPGQKVMEN
SSGTPDILTR HFTIDDFEIG RPLGKGKFGN VYLAREKKSH FIVALKVLFK SQIEKEGVEH
QLRREIEIQA HLHHPNILRL YNYFYDRRRI YLILEYAPRG ELYKELQKSC TFDEQRTATI
MEELADALMY CHGKKVIHRD IKPENLLLGL KGELKIADFG WSVHAPSLRR KTMCGTLDYL
PPEMIEGRMH NEKVDLWCIG VLCYELLVGN PPFESASHNE TYRRIVKVDL KFPASVPMGA
QDLISKLLRH NPSERLPLAQ VSAHPWVRAN SRRVLPPSAL QSVA


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