AURKB_HUMAN
ID AURKB_HUMAN Reviewed; 344 AA.
AC Q96GD4; B4DNM4; C7G533; C7G534; C7G535; D3DTR4; J9JID1; O14630; O60446;
AC O95083; Q96DV5; Q9UQ46;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 3.
DT 03-AUG-2022, entry version 225.
DE RecName: Full=Aurora kinase B {ECO:0000303|PubMed:33542149};
DE EC=2.7.11.1 {ECO:0000269|PubMed:26829474, ECO:0000269|PubMed:33542149};
DE AltName: Full=Aurora 1;
DE AltName: Full=Aurora- and IPL1-like midbody-associated protein 1 {ECO:0000303|PubMed:9809983};
DE Short=AIM-1 {ECO:0000303|PubMed:9809983};
DE AltName: Full=Aurora/IPL1-related kinase 2 {ECO:0000303|PubMed:9514916};
DE Short=ARK-2 {ECO:0000303|PubMed:9514916};
DE Short=Aurora-related kinase 2;
DE AltName: Full=STK-1;
DE AltName: Full=Serine/threonine-protein kinase 12 {ECO:0000303|PubMed:9858806};
DE AltName: Full=Serine/threonine-protein kinase 5;
DE AltName: Full=Serine/threonine-protein kinase aurora-B {ECO:0000305};
GN Name=AURKB;
GN Synonyms=AIK2 {ECO:0000303|PubMed:9858806},
GN AIM1 {ECO:0000303|PubMed:9809983}, AIRK2,
GN ARK2 {ECO:0000303|PubMed:9514916}, STK1,
GN STK12 {ECO:0000303|PubMed:9858806}, STK5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT THR-298.
RX PubMed=9514916; DOI=10.1006/bbrc.1998.8250;
RA Shindo M., Nakano H., Kuroyanagi H., Shirasawa T., Mihara M., Gilbert D.J.,
RA Jenkins N.A., Copeland N.G., Yagita H., Okumura K.;
RT "cDNA cloning, expression, subcellular localization, and chromosomal
RT assignment of mammalian aurora homologues, aurora-related kinase (ARK) 1
RT and 2.";
RL Biochem. Biophys. Res. Commun. 244:285-292(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND VARIANT
RP THR-298.
RX PubMed=9809983;
RA Tatsuka M., Katayama H., Ota T., Tanaka T., Odashima S., Suzuki F.,
RA Terada Y.;
RT "Multinuclearity and increased ploidy caused by overexpression of the
RT aurora- and Ipl1-like midbody-associated protein mitotic kinase in human
RT cancer cells.";
RL Cancer Res. 58:4811-4816(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND VARIANT
RP THR-298.
RC TISSUE=Liver, and Spleen;
RX PubMed=9858806; DOI=10.1159/000015089;
RA Kimura M., Matsuda Y., Yoshioka T., Sumi N., Okano Y.;
RT "Identification and characterization of STK12/Aik2: a human gene related to
RT aurora of Drosophila and yeast IPL1.";
RL Cytogenet. Cell Genet. 82:147-152(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT THR-298.
RX PubMed=11471245;
RA Prigent C., Gill R., Trower M., Sanseau P.;
RT "In silico cloning of a new protein kinase, Aik2, related to Drosophila
RT aurora using the new tool: EST Blast.";
RL In Silico Biol. 1:123-128(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT THR-298.
RA Zhang Q., Yu L., Bi A.;
RT "Cloning of a novel human gene homologous to mouse STK-1.";
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), ALTERNATIVE SPLICING, AND
RP TISSUE SPECIFICITY.
RX PubMed=19134008; DOI=10.1111/j.1349-7006.2008.01068.x;
RA Yasen M., Mizushima H., Mogushi K., Obulhasim G., Miyaguchi K., Inoue K.,
RA Nakahara I., Ohta T., Aihara A., Tanaka S., Arii S., Tanaka H.;
RT "Expression of Aurora B and alternative variant forms in hepatocellular
RT carcinoma and adjacent tissue.";
RL Cancer Sci. 100:472-480(2009).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT THR-298.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), AND VARIANT THR-298.
RC TISSUE=Lung, Lymph, and Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [12]
RP IDENTIFICATION IN THE CPC COMPLEX, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=11516652; DOI=10.1016/s0960-9822(01)00238-x;
RA Wheatley S.P., Carvalho A., Vagnarelli P., Earnshaw W.C.;
RT "INCENP is required for proper targeting of Survivin to the centromeres and
RT the anaphase spindle during mitosis.";
RL Curr. Biol. 11:886-890(2001).
RN [13]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11756469; DOI=10.1083/jcb.200108125;
RA Zeitlin S.G., Shelby R.D., Sullivan K.F.;
RT "CENP-A is phosphorylated by Aurora B kinase and plays an unexpected role
RT in completion of cytokinesis.";
RL J. Cell Biol. 155:1147-1157(2001).
RN [14]
RP REVIEW.
RX PubMed=11413462; DOI=10.1038/35048096;
RA Nigg E.A.;
RT "Mitotic kinases as regulators of cell division and its checkpoints.";
RL Nat. Rev. Mol. Cell Biol. 2:21-32(2001).
RN [15]
RP FUNCTION IN PHOSPHORYLATION OF HISTONE H3.
RX PubMed=11856369; DOI=10.1046/j.1356-9597.2001.00498.x;
RA Goto H., Yasui Y., Nigg E.A., Inagaki M.;
RT "Aurora-B phosphorylates Histone H3 at serine28 with regard to the mitotic
RT chromosome condensation.";
RL Genes Cells 7:11-17(2002).
RN [16]
RP FUNCTION IN PHOSPHORYLATION OF HISTONE H3.
RX PubMed=11784863; DOI=10.1128/mcb.22.3.874-885.2002;
RA Crosio C., Fimia G.M., Loury R., Kimura M., Okano Y., Zhou H., Sen S.,
RA Allis C.D., Sassone-Corsi P.;
RT "Mitotic phosphorylation of histone H3: spatio-temporal regulation by
RT mammalian Aurora kinases.";
RL Mol. Cell. Biol. 22:874-885(2002).
RN [17]
RP FUNCTION, AND INTERACTION WITH RACGAP1.
RX PubMed=12689593; DOI=10.1016/s1534-5807(03)00089-3;
RA Minoshima Y., Kawashima T., Hirose K., Tonozuka Y., Kawajiri A., Bao Y.C.,
RA Deng X., Tatsuka M., Narumiya S., May W.S. Jr., Nosaka T., Semba K.,
RA Inoue T., Satoh T., Inagaki M., Kitamura T.;
RT "Phosphorylation by aurora B converts MgcRacGAP to a RhoGAP during
RT cytokinesis.";
RL Dev. Cell 4:549-560(2003).
RN [18]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12458200; DOI=10.1074/jbc.m210892200;
RA Goto H., Yasui Y., Kawajiri A., Nigg E.A., Terada Y., Tatsuka M.,
RA Nagata K., Inagaki M.;
RT "Aurora-B regulates the cleavage furrow-specific vimentin phosphorylation
RT in the cytokinetic process.";
RL J. Biol. Chem. 278:8526-8530(2003).
RN [19]
RP FUNCTION, AND MUTAGENESIS OF LYS-106.
RX PubMed=12686604; DOI=10.1091/mbc.e02-09-0612;
RA Kawajiri A., Yasui Y., Goto H., Tatsuka M., Takahashi M., Nagata K.,
RA Inagaki M.;
RT "Functional significance of the specific sites phosphorylated in desmin at
RT cleavage furrow: Aurora-B may phosphorylate and regulate type III
RT intermediate filaments during cytokinesis coordinatedly with Rho-kinase.";
RL Mol. Biol. Cell 14:1489-1500(2003).
RN [20]
RP IDENTIFICATION IN THE CPC COMPLEX, FUNCTION OF THE CPC COMPLEX, INDUCTION,
RP SUBCELLULAR LOCATION, ACTIVITY REGULATION, AND MUTAGENESIS OF LYS-106.
RX PubMed=12925766; DOI=10.1091/mbc.e02-11-0769;
RA Honda R., Korner R., Nigg E.A.;
RT "Exploring the functional interactions between Aurora B, INCENP, and
RT survivin in mitosis.";
RL Mol. Biol. Cell 14:3325-3341(2003).
RN [21]
RP INTERACTION WITH PSMA3.
RX PubMed=14674694; DOI=10.1023/a:1027317014159;
RA Shu F., Guo S., Dang Y., Qi M., Zhou G., Guo Z., Zhang Y., Wu C., Zhao S.,
RA Yu L.;
RT "Human Aurora-B binds to a proteasome alpha-subunit HC8 and undergoes
RT degradation in a proteasome-dependent manner.";
RL Mol. Cell. Biochem. 254:157-162(2003).
RN [22]
RP FUNCTION.
RX PubMed=14610074; DOI=10.1074/jbc.m311299200;
RA Wheatley S.P., Henzing A.J., Dodson H., Khaled W., Earnshaw W.C.;
RT "Aurora-B phosphorylation in vitro identifies a residue of survivin that is
RT essential for its localization and binding to inner centromere protein
RT (INCENP) in vivo.";
RL J. Biol. Chem. 279:5655-5660(2004).
RN [23]
RP PHOSPHORYLATION AT THR-232, FUNCTION, INTERACTION WITH INCENP, ACTIVITY
RP REGULATION, AND MUTAGENESIS OF LYS-106.
RX PubMed=14722118; DOI=10.1074/jbc.m311128200;
RA Yasui Y., Urano T., Kawajiri A., Nagata K., Tatsuka M., Saya H.,
RA Furukawa K., Takahashi T., Izawa I., Inagaki M.;
RT "Autophosphorylation of a newly identified site of Aurora-B is
RT indispensable for cytokinesis.";
RL J. Biol. Chem. 279:12997-13003(2004).
RN [24]
RP FUNCTION.
RX PubMed=15020684; DOI=10.1242/jcs.01006;
RA Johnson V.L., Scott M.I., Holt S.V., Hussein D., Taylor S.S.;
RT "Bub1 is required for kinetochore localization of BubR1, Cenp-E, Cenp-F and
RT Mad2, and chromosome congression.";
RL J. Cell Sci. 117:1577-1589(2004).
RN [25]
RP INTERACTION WITH CDCA8, ACTIVITY REGULATION, AND FUNCTION.
RX PubMed=15249581; DOI=10.1083/jcb.200404001;
RA Gassmann R., Carvalho A., Henzing A.J., Ruchaud S., Hudson D.F., Honda R.,
RA Nigg E.A., Gerloff D.L., Earnshaw W.C.;
RT "Borealin: a novel chromosomal passenger required for stability of the
RT bipolar mitotic spindle.";
RL J. Cell Biol. 166:179-191(2004).
RN [26]
RP FUNCTION, AND INTERACTION WITH CDCA1 AND NDC80.
RX PubMed=14602875; DOI=10.1074/mcp.m300072-mcp200;
RA Tien A.-C., Lin M.-H., Su L.-J., Hong Y.-R., Cheng T.-S., Lee Y.-C.G.,
RA Lin W.-J., Still I.H., Huang C.-Y.F.;
RT "Identification of the substrates and interaction proteins of aurora
RT kinases from a protein-protein interaction model.";
RL Mol. Cell. Proteomics 3:93-104(2004).
RN [27]
RP INTERACTION WITH TACC1.
RX PubMed=15064709; DOI=10.1038/sj.onc.1207593;
RA Delaval B., Ferrand A., Conte N., Larroque C., Hernandez-Verdun D.,
RA Prigent C., Birnbaum D.;
RT "Aurora B -TACC1 protein complex in cytokinesis.";
RL Oncogene 23:4516-4522(2004).
RN [28]
RP SUBCELLULAR LOCATION, INTERACTION WITH SEPTIN1, AND MUTAGENESIS OF LYS-106.
RX PubMed=16179162; DOI=10.1016/j.bbrc.2005.06.212;
RA Qi M., Yu W., Liu S., Jia H., Tang L., Shen M., Yan X., Saiyin H., Lang Q.,
RA Wan B., Zhao S., Yu L.;
RT "Septin1, a new interaction partner for human serine/threonine kinase
RT aurora-B.";
RL Biochem. Biophys. Res. Commun. 336:994-1000(2005).
RN [29]
RP FUNCTION.
RX PubMed=16103226; DOI=10.1083/jcb.200501097;
RA Yuce O., Piekny A., Glotzer M.;
RT "An ECT2-centralspindlin complex regulates the localization and function of
RT RhoA.";
RL J. Cell Biol. 170:571-582(2005).
RN [30]
RP INTERACTION WITH EVI5.
RX PubMed=16764853; DOI=10.1016/j.yexcr.2006.03.032;
RA Faitar S.L., Sossey-Alaoui K., Ranalli T.A., Cowell J.K.;
RT "EVI5 protein associates with the INCENP-aurora B kinase-survivin
RT chromosomal passenger complex and is involved in the completion of
RT cytokinesis.";
RL Exp. Cell Res. 312:2325-2335(2006).
RN [31]
RP FUNCTION.
RX PubMed=17617734; DOI=10.4161/cc.6.13.4442;
RA Pouwels J., Kukkonen A.M., Lan W., Daum J.R., Gorbsky G.J., Stukenberg T.,
RA Kallio M.J.;
RT "Shugoshin 1 plays a central role in kinetochore assembly and is required
RT for kinetochore targeting of Plk1.";
RL Cell Cycle 6:1579-1585(2007).
RN [32]
RP UBIQUITINATION.
RX PubMed=17543862; DOI=10.1016/j.devcel.2007.03.019;
RA Sumara I., Quadroni M., Frei C., Olma M.H., Sumara G., Ricci R., Peter M.;
RT "A Cul3-based E3 ligase removes Aurora B from mitotic chromosomes,
RT regulating mitotic progression and completion of cytokinesis in human
RT cells.";
RL Dev. Cell 12:887-900(2007).
RN [33]
RP INTERACTION WITH SIRT2, AND SUBCELLULAR LOCATION.
RX PubMed=17726514; DOI=10.1371/journal.pone.0000784;
RA North B.J., Verdin E.;
RT "Interphase nucleo-cytoplasmic shuttling and localization of SIRT2 during
RT mitosis.";
RL PLoS ONE 2:E784-E784(2007).
RN [34]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [35]
RP INTERACTION WITH BIRC5.
RX PubMed=18591255; DOI=10.1128/mcb.02039-07;
RA Xia F., Canovas P.M., Guadagno T.M., Altieri D.C.;
RT "A survivin-ran complex regulates spindle formation in tumor cells.";
RL Mol. Cell. Biol. 28:5299-5311(2008).
RN [36]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-35, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [37]
RP UBIQUITINATION.
RX PubMed=19995937; DOI=10.1083/jcb.200906117;
RA Maerki S., Olma M.H., Staubli T., Steigemann P., Gerlich D.W., Quadroni M.,
RA Sumara I., Peter M.;
RT "The Cul3-KLHL21 E3 ubiquitin ligase targets aurora B to midzone
RT microtubules in anaphase and is required for cytokinesis.";
RL J. Cell Biol. 187:791-800(2009).
RN [38]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [39]
RP INTERACTION WITH SPDYC, AND SUBCELLULAR LOCATION.
RX PubMed=20605920; DOI=10.1242/jcs.059964;
RA Mouron S., de Carcer G., Seco E., Fernandez-Miranda G., Malumbres M.,
RA Nebreda A.R.;
RT "RINGO C is required to sustain the spindle-assembly checkpoint.";
RL J. Cell Sci. 123:2586-2595(2010).
RN [40]
RP INTERACTION WITH INCENP.
RX PubMed=20562864; DOI=10.1038/ncb2075;
RA Nozawa R.S., Nagao K., Masuda H.T., Iwasaki O., Hirota T., Nozaki N.,
RA Kimura H., Obuse C.;
RT "Human POGZ modulates dissociation of HP1alpha from mitotic chromosome arms
RT through Aurora B activation.";
RL Nat. Cell Biol. 12:719-727(2010).
RN [41]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62 AND THR-64, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [42]
RP SUBCELLULAR LOCATION.
RX PubMed=20929775; DOI=10.1126/science.1194498;
RA Yamagishi Y., Honda T., Tanno Y., Watanabe Y.;
RT "Two histone marks establish the inner centromere and chromosome bi-
RT orientation.";
RL Science 330:239-243(2010).
RN [43]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [44]
RP FUNCTION IN PHOSPHORYLATION OF HASPIN.
RX PubMed=21658950; DOI=10.1016/j.cub.2011.05.016;
RA Wang F., Ulyanova N.P., van der Waal M.S., Patnaik D., Lens S.M.,
RA Higgins J.M.;
RT "A positive feedback loop involving Haspin and Aurora B promotes CPC
RT accumulation at centromeres in mitosis.";
RL Curr. Biol. 21:1061-1069(2011).
RN [45]
RP FUNCTION IN PHOSPHORYLATION OF TP53, INTERACTION WITH NOC2L AND TP53, AND
RP SUBCELLULAR LOCATION.
RX PubMed=20959462; DOI=10.1074/jbc.m110.174755;
RA Wu L., Ma C.A., Zhao Y., Jain A.;
RT "Aurora B interacts with NIR-p53, leading to p53 phosphorylation in its
RT DNA-binding domain and subsequent functional suppression.";
RL J. Biol. Chem. 286:2236-2244(2011).
RN [46]
RP INTERACTION WITH JTB.
RX PubMed=21225229; DOI=10.3892/ijo.2011.900;
RA Platica M., Ionescu A., Ivan E., Holland J.F., Mandeli J., Platica O.;
RT "PAR, a protein involved in the cell cycle, is functionally related to
RT chromosomal passenger proteins.";
RL Int. J. Oncol. 38:777-785(2011).
RN [47]
RP INTERACTION WITH TTC28, AND SUBCELLULAR LOCATION.
RX PubMed=23036704; DOI=10.1016/j.gene.2012.09.061;
RA Izumiyama T., Minoshima S., Yoshida T., Shimizu N.;
RT "A novel big protein TPRBK possessing 25 units of TPR motif is essential
RT for the progress of mitosis and cytokinesis.";
RL Gene 511:202-217(2012).
RN [48]
RP FUNCTION.
RX PubMed=22422861; DOI=10.1126/science.1217180;
RA Carlton J.G., Caballe A., Agromayor M., Kloc M., Martin-Serrano J.;
RT "ESCRT-III governs the Aurora B-mediated abscission checkpoint through
RT CHMP4C.";
RL Science 336:220-225(2012).
RN [49]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [50]
RP FUNCTION.
RX PubMed=24814515; DOI=10.1038/ncb2959;
RA Thoresen S.B., Campsteijn C., Vietri M., Schink K.O., Liestoel K.,
RA Andersen J.S., Raiborg C., Stenmark H.;
RT "ANCHR mediates Aurora-B-dependent abscission checkpoint control through
RT retention of VPS4.";
RL Nat. Cell Biol. 16:550-560(2014).
RN [51]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, PHOSPHORYLATION AT
RP THR-232, ACETYLATION AT LYS-215, AND MUTAGENESIS OF LYS-215.
RX PubMed=26829474; DOI=10.1038/nchembio.2017;
RA Mo F., Zhuang X., Liu X., Yao P.Y., Qin B., Su Z., Zang J., Wang Z.,
RA Zhang J., Dou Z., Tian C., Teng M., Niu L., Hill D.L., Fang G., Ding X.,
RA Fu C., Yao X.;
RT "Acetylation of Aurora B by TIP60 ensures accurate chromosomal
RT segregation.";
RL Nat. Chem. Biol. 12:226-232(2016).
RN [52]
RP SUBUNIT.
RX PubMed=27332895; DOI=10.1371/journal.pone.0157305;
RA Sasai K., Katayama H., Hawke D.H., Sen S.;
RT "Aurora-C interactions with survivin and INCENP reveal shared and distinct
RT features compared with Aurora-B chromosome passenger protein complex.";
RL PLoS ONE 11:E0157305-E0157305(2016).
RN [53]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=33542149; DOI=10.1126/science.abc5386;
RA Li T., Huang T., Du M., Chen X., Du F., Ren J., Chen Z.J.;
RT "Phosphorylation and chromatin tethering prevent cGAS activation during
RT mitosis.";
RL Science 371:0-0(2021).
RN [54]
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 55-344 IN COMPLEX WITH INCENP.
RX PubMed=22920039; DOI=10.1021/jm3008954;
RA Elkins J.M., Santaguida S., Musacchio A., Knapp S.;
RT "Crystal structure of human aurora B in complex with INCENP and VX-680.";
RL J. Med. Chem. 55:7841-7848(2012).
RN [55]
RP VARIANT THR-298.
RX PubMed=16762494; DOI=10.1016/j.canlet.2006.05.002;
RA Tchatchou S., Wirtenberger M., Hemminki K., Sutter C., Meindl A.,
RA Wappenschmidt B., Kiechle M., Bugert P., Schmutzler R.K., Bartram C.R.,
RA Burwinkel B.;
RT "Aurora kinases A and B and familial breast cancer risk.";
RL Cancer Lett. 247:266-272(2007).
RN [56]
RP VARIANTS [LARGE SCALE ANALYSIS] VAL-52 AND MET-179.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Serine/threonine-protein kinase component of the chromosomal
CC passenger complex (CPC), a complex that acts as a key regulator of
CC mitosis (PubMed:11516652, PubMed:12925766, PubMed:14610074,
CC PubMed:14722118). The CPC complex has essential functions at the
CC centromere in ensuring correct chromosome alignment and segregation and
CC is required for chromatin-induced microtubule stabilization and spindle
CC assembly (PubMed:11516652, PubMed:12925766, PubMed:14610074,
CC PubMed:14722118, PubMed:26829474). Involved in the bipolar attachment
CC of spindle microtubules to kinetochores and is a key regulator for the
CC onset of cytokinesis during mitosis (PubMed:15249581). Required for
CC central/midzone spindle assembly and cleavage furrow formation
CC (PubMed:12458200, PubMed:12686604). Key component of the cytokinesis
CC checkpoint, a process required to delay abscission to prevent both
CC premature resolution of intercellular chromosome bridges and
CC accumulation of DNA damage: phosphorylates CHMP4C, leading to retain
CC abscission-competent VPS4 (VPS4A and/or VPS4B) at the midbody ring
CC until abscission checkpoint signaling is terminated at late cytokinesis
CC (PubMed:22422861, PubMed:24814515). AURKB phosphorylates the CPC
CC complex subunits BIRC5/survivin, CDCA8/borealin and INCENP
CC (PubMed:11516652, PubMed:12925766, PubMed:14610074). Phosphorylation of
CC INCENP leads to increased AURKB activity (PubMed:11516652,
CC PubMed:12925766, PubMed:14610074). Other known AURKB substrates
CC involved in centromeric functions and mitosis are CENPA, DES/desmin,
CC GPAF, KIF2C, NSUN2, RACGAP1, SEPTIN1, VIM/vimentin, HASPIN, and histone
CC H3 (PubMed:11784863, PubMed:12689593, PubMed:14602875, PubMed:11856369,
CC PubMed:16103226, PubMed:21658950, PubMed:11756469). A positive feedback
CC loop involving HASPIN and AURKB contributes to localization of CPC to
CC centromeres (PubMed:21658950). Phosphorylation of VIM controls vimentin
CC filament segregation in cytokinetic process, whereas histone H3 is
CC phosphorylated at 'Ser-10' and 'Ser-28' during mitosis (H3S10ph and
CC H3S28ph, respectively) (PubMed:11784863, PubMed:11856369). A positive
CC feedback between HASPIN and AURKB contributes to CPC localization
CC (PubMed:21658950). AURKB is also required for kinetochore localization
CC of BUB1 and SGO1 (PubMed:15020684, PubMed:17617734). Phosphorylation of
CC p53/TP53 negatively regulates its transcriptional activity
CC (PubMed:20959462). Key regulator of active promoters in resting B- and
CC T-lymphocytes: acts by mediating phosphorylation of H3S28ph at active
CC promoters in resting B-cells, inhibiting RNF2/RING1B-mediated
CC ubiquitination of histone H2A and enhancing binding and activity of the
CC USP16 deubiquitinase at transcribed genes (By similarity). Acts as an
CC inhibitor of CGAS during mitosis: catalyzes phosphorylation of the N-
CC terminus of CGAS during the G2-M transition, blocking CGAS liquid phase
CC separation and activation, and thereby preventing CGAS-induced
CC autoimmunity (PubMed:33542149). Phosphorylates KRT5 during anaphase and
CC telophase (By similarity). {ECO:0000250|UniProtKB:O70126,
CC ECO:0000269|PubMed:11516652, ECO:0000269|PubMed:11756469,
CC ECO:0000269|PubMed:11784863, ECO:0000269|PubMed:11856369,
CC ECO:0000269|PubMed:12458200, ECO:0000269|PubMed:12686604,
CC ECO:0000269|PubMed:12689593, ECO:0000269|PubMed:12925766,
CC ECO:0000269|PubMed:14602875, ECO:0000269|PubMed:14610074,
CC ECO:0000269|PubMed:14722118, ECO:0000269|PubMed:15020684,
CC ECO:0000269|PubMed:15249581, ECO:0000269|PubMed:16103226,
CC ECO:0000269|PubMed:17617734, ECO:0000269|PubMed:20959462,
CC ECO:0000269|PubMed:21658950, ECO:0000269|PubMed:22422861,
CC ECO:0000269|PubMed:24814515, ECO:0000269|PubMed:26829474,
CC ECO:0000269|PubMed:33542149}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000269|PubMed:11784863, ECO:0000269|PubMed:11856369,
CC ECO:0000269|PubMed:26829474, ECO:0000269|PubMed:33542149};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000269|PubMed:14722118,
CC ECO:0000269|PubMed:26829474, ECO:0000269|PubMed:33542149};
CC -!- ACTIVITY REGULATION: Activity is greatly increased when AURKB is within
CC the CPC complex (PubMed:12925766, PubMed:14722118, PubMed:15249581). In
CC particular, AURKB-phosphorylated INCENP acts as an activator of AURKB
CC (PubMed:14722118, PubMed:15249581). Positive feedback between HASPIN
CC and AURKB contributes to CPC localization (PubMed:14722118,
CC PubMed:15249581). {ECO:0000269|PubMed:12925766,
CC ECO:0000269|PubMed:14722118, ECO:0000269|PubMed:15249581}.
CC -!- SUBUNIT: Component of the chromosomal passenger complex (CPC) composed
CC of at least BIRC5/survivin, CDCA8/borealin, INCENP, AURKB or AURKC;
CC predominantly independent AURKB- and AURKC-containing complexes exist
CC (PubMed:11516652, PubMed:12925766, PubMed:14722118, PubMed:15249581,
CC PubMed:18591255, PubMed:27332895, PubMed:20562864). Associates with
CC RACGAP1 during M phase (PubMed:12689593). Interacts with CDCA1, EVI5,
CC JTB, NDC80, PSMA3, SEPTIN1, SIRT2 and TACC1 (PubMed:14602875,
CC PubMed:14674694, PubMed:15064709, PubMed:16179162, PubMed:16764853,
CC PubMed:17726514, PubMed:21225229). Interacts with SPDYC; this
CC interaction may be required for proper localization of active, Thr-232-
CC phosphorylated AURKB form during prometaphase and metaphase
CC (PubMed:20605920). Interacts with p53/TP53 (PubMed:20959462). Interacts
CC (via the middle kinase domain) with NOC2L (via the N- and C-terminus
CC domains) (PubMed:20959462). Interacts with TTC28 (PubMed:23036704).
CC Interacts with RNF2/RING1B (By similarity).
CC {ECO:0000250|UniProtKB:O70126, ECO:0000269|PubMed:11516652,
CC ECO:0000269|PubMed:12689593, ECO:0000269|PubMed:12925766,
CC ECO:0000269|PubMed:14602875, ECO:0000269|PubMed:14674694,
CC ECO:0000269|PubMed:14722118, ECO:0000269|PubMed:15064709,
CC ECO:0000269|PubMed:15249581, ECO:0000269|PubMed:16179162,
CC ECO:0000269|PubMed:16764853, ECO:0000269|PubMed:17726514,
CC ECO:0000269|PubMed:18591255, ECO:0000269|PubMed:20562864,
CC ECO:0000269|PubMed:20605920, ECO:0000269|PubMed:20959462,
CC ECO:0000269|PubMed:21225229, ECO:0000269|PubMed:23036704,
CC ECO:0000269|PubMed:27332895}.
CC -!- INTERACTION:
CC Q96GD4; O15392: BIRC5; NbExp=13; IntAct=EBI-624291, EBI-518823;
CC Q96GD4; O15392-1: BIRC5; NbExp=2; IntAct=EBI-624291, EBI-518838;
CC Q96GD4; O15392-2: BIRC5; NbExp=2; IntAct=EBI-624291, EBI-518842;
CC Q96GD4; Q16543: CDC37; NbExp=5; IntAct=EBI-624291, EBI-295634;
CC Q96GD4; Q53HL2: CDCA8; NbExp=9; IntAct=EBI-624291, EBI-979174;
CC Q96GD4; Q86XJ1: GAS2L3; NbExp=4; IntAct=EBI-624291, EBI-9248152;
CC Q96GD4; Q16695: H3-4; NbExp=8; IntAct=EBI-624291, EBI-358900;
CC Q96GD4; P08238: HSP90AB1; NbExp=5; IntAct=EBI-624291, EBI-352572;
CC Q96GD4; Q9NQS7: INCENP; NbExp=19; IntAct=EBI-624291, EBI-307907;
CC Q96GD4; Q9NQS7-1: INCENP; NbExp=2; IntAct=EBI-624291, EBI-15767972;
CC Q96GD4; Q92993: KAT5; NbExp=4; IntAct=EBI-624291, EBI-399080;
CC Q96GD4; Q15691: MAPRE1; NbExp=5; IntAct=EBI-624291, EBI-1004115;
CC Q96GD4; P06748: NPM1; NbExp=5; IntAct=EBI-624291, EBI-78579;
CC Q96GD4; P30153: PPP2R1A; NbExp=3; IntAct=EBI-624291, EBI-302388;
CC Q96GD4; Q8WYJ6: SEPTIN1; NbExp=6; IntAct=EBI-624291, EBI-693002;
CC Q96GD4; O75410-6: TACC1; NbExp=2; IntAct=EBI-624291, EBI-624278;
CC Q96GD4; Q99986: VRK1; NbExp=14; IntAct=EBI-624291, EBI-1769146;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20959462}. Chromosome
CC {ECO:0000269|PubMed:20929775}. Chromosome, centromere
CC {ECO:0000269|PubMed:11756469, ECO:0000269|PubMed:12925766,
CC ECO:0000269|PubMed:20929775}. Chromosome, centromere, kinetochore
CC {ECO:0000269|PubMed:26829474}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:11516652, ECO:0000269|PubMed:12458200,
CC ECO:0000269|PubMed:12925766, ECO:0000269|PubMed:20605920}. Midbody
CC {ECO:0000269|PubMed:16179162, ECO:0000269|PubMed:17726514,
CC ECO:0000269|PubMed:23036704}. Note=Localizes on chromosome arms and
CC inner centromeres from prophase through metaphase and then transferring
CC to the spindle midzone and midbody from anaphase through cytokinesis
CC (PubMed:20929775). Colocalized with gamma tubulin in the midbody
CC (PubMed:17726514). Proper localization of the active, Thr-232-
CC phosphorylated form during metaphase may be dependent upon interaction
CC with SPDYC (PubMed:20605920). Colocalized with SIRT2 during cytokinesis
CC with the midbody (PubMed:17726514). Localization (and probably
CC targeting of the CPC) to the inner centromere occurs predominantly in
CC regions with overlapping mitosis-specific histone phosphorylations
CC H3pT3 and H2ApT12 (PubMed:20929775). {ECO:0000269|PubMed:17726514,
CC ECO:0000269|PubMed:20605920, ECO:0000269|PubMed:20929775}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q96GD4-1; Sequence=Displayed;
CC Name=2; Synonyms=aurkb-sv1;
CC IsoId=Q96GD4-2; Sequence=VSP_044385;
CC Name=3; Synonyms=aurkb-sv2;
CC IsoId=Q96GD4-3; Sequence=VSP_044384, VSP_044386, VSP_044387;
CC Name=4;
CC IsoId=Q96GD4-4; Sequence=VSP_047103;
CC Name=5;
CC IsoId=Q96GD4-5; Sequence=VSP_044384;
CC -!- TISSUE SPECIFICITY: High level expression seen in the thymus. It is
CC also expressed in the spleen, lung, testis, colon, placenta and fetal
CC liver. Expressed during S and G2/M phase and expression is up-regulated
CC in cancer cells during M phase. {ECO:0000269|PubMed:9809983,
CC ECO:0000269|PubMed:9858806}.
CC -!- TISSUE SPECIFICITY: [Isoform 3]: Not expressed in normal liver, high
CC expression in metastatic liver. {ECO:0000269|PubMed:19134008}.
CC -!- INDUCTION: Expression is cell cycle-regulated, with a low in G1/S, an
CC increase during G2 and M. Expression decreases again after M phase.
CC {ECO:0000269|PubMed:12925766}.
CC -!- PTM: The phosphorylation of Thr-232 requires the binding to INCENP and
CC occurs by means of an autophosphorylation mechanism (PubMed:14722118).
CC Thr-232 phosphorylation is indispensable for the AURKB kinase activity
CC (PubMed:14722118, PubMed:26829474). {ECO:0000269|PubMed:14722118,
CC ECO:0000269|PubMed:26829474}.
CC -!- PTM: Acetylated at Lys-215 by KAT5 at kinetochores, increasing AURKB
CC activity and promoting accurate chromosome segregation in mitosis.
CC {ECO:0000269|PubMed:26829474}.
CC -!- PTM: Ubiquitinated by different BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase
CC complexes (PubMed:17543862, PubMed:19995937). Ubiquitinated by the
CC BCR(KLHL9-KLHL13) E3 ubiquitin ligase complex, ubiquitination leads to
CC removal from mitotic chromosomes and is required for cytokinesis
CC (PubMed:17543862). During anaphase, the BCR(KLHL21) E3 ubiquitin ligase
CC complex recruits the CPC complex from chromosomes to the spindle
CC midzone and mediates the ubiquitination of AURKB (PubMed:17543862).
CC Ubiquitination of AURKB by BCR(KLHL21) E3 ubiquitin ligase complex may
CC not lead to its degradation by the proteasome (PubMed:19995937).
CC {ECO:0000269|PubMed:17543862, ECO:0000269|PubMed:19995937}.
CC -!- DISEASE: Note=Disruptive regulation of expression is a possible
CC mechanism of the perturbation of chromosomal integrity in cancer cells
CC through its dominant-negative effect on cytokinesis.
CC {ECO:0000305|PubMed:9809983}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. Aurora subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH13300.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF008552; AAC12709.1; -; mRNA.
DR EMBL; AB011450; BAA32136.1; -; mRNA.
DR EMBL; AB011446; BAA82709.1; -; mRNA.
DR EMBL; AF004022; AAB65786.1; -; mRNA.
DR EMBL; AF015254; AAC98891.1; -; mRNA.
DR EMBL; AB519677; BAI23190.1; -; mRNA.
DR EMBL; AB519678; BAI23191.1; -; mRNA.
DR EMBL; AB519679; BAI23192.1; -; mRNA.
DR EMBL; BT019534; AAV38341.1; -; mRNA.
DR EMBL; AK297976; BAG60286.1; -; mRNA.
DR EMBL; AC135178; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471108; EAW90075.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW90077.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW90078.1; -; Genomic_DNA.
DR EMBL; BC000442; AAH00442.3; -; mRNA.
DR EMBL; BC009751; AAH09751.1; -; mRNA.
DR EMBL; BC013300; AAH13300.2; ALT_INIT; mRNA.
DR EMBL; BC080581; AAH80581.1; -; mRNA.
DR CCDS; CCDS11134.1; -. [Q96GD4-1]
DR CCDS; CCDS58514.1; -. [Q96GD4-4]
DR CCDS; CCDS67162.1; -. [Q96GD4-5]
DR CCDS; CCDS82065.1; -. [Q96GD4-2]
DR RefSeq; NP_001243763.1; NM_001256834.2. [Q96GD4-4]
DR RefSeq; NP_001271455.1; NM_001284526.1. [Q96GD4-5]
DR RefSeq; NP_001300879.1; NM_001313950.1. [Q96GD4-1]
DR RefSeq; NP_001300880.1; NM_001313951.1. [Q96GD4-4]
DR RefSeq; NP_001300881.1; NM_001313952.1.
DR RefSeq; NP_001300882.1; NM_001313953.1. [Q96GD4-2]
DR RefSeq; NP_001300883.1; NM_001313954.1.
DR RefSeq; NP_001300884.1; NM_001313955.1.
DR RefSeq; NP_004208.2; NM_004217.3. [Q96GD4-1]
DR RefSeq; XP_011522372.1; XM_011524070.2.
DR RefSeq; XP_011522374.1; XM_011524072.2. [Q96GD4-4]
DR RefSeq; XP_016880796.1; XM_017025307.1. [Q96GD4-4]
DR PDB; 4AF3; X-ray; 2.75 A; A=55-344.
DR PDBsum; 4AF3; -.
DR AlphaFoldDB; Q96GD4; -.
DR SMR; Q96GD4; -.
DR BioGRID; 114646; 711.
DR ComplexPortal; CPX-116; Chromosomal passenger complex.
DR CORUM; Q96GD4; -.
DR DIP; DIP-34530N; -.
DR ELM; Q96GD4; -.
DR IntAct; Q96GD4; 199.
DR MINT; Q96GD4; -.
DR STRING; 9606.ENSP00000313950; -.
DR BindingDB; Q96GD4; -.
DR ChEMBL; CHEMBL2185; -.
DR DrugBank; DB05169; AT9283.
DR DrugBank; DB06486; Enzastaurin.
DR DrugBank; DB12010; Fostamatinib.
DR DrugBank; DB04703; Hesperidin.
DR DrugBank; DB07340; Reversine.
DR DrugCentral; Q96GD4; -.
DR GuidetoPHARMACOLOGY; 1937; -.
DR GlyGen; Q96GD4; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96GD4; -.
DR MetOSite; Q96GD4; -.
DR PhosphoSitePlus; Q96GD4; -.
DR SwissPalm; Q96GD4; -.
DR BioMuta; AURKB; -.
DR DMDM; 317373473; -.
DR CPTAC; CPTAC-1219; -.
DR CPTAC; CPTAC-1228; -.
DR CPTAC; CPTAC-1340; -.
DR EPD; Q96GD4; -.
DR jPOST; Q96GD4; -.
DR MassIVE; Q96GD4; -.
DR MaxQB; Q96GD4; -.
DR PaxDb; Q96GD4; -.
DR PeptideAtlas; Q96GD4; -.
DR PRIDE; Q96GD4; -.
DR ProteomicsDB; 4709; -.
DR ProteomicsDB; 7611; -.
DR ProteomicsDB; 76623; -. [Q96GD4-1]
DR Antibodypedia; 3128; 1133 antibodies from 46 providers.
DR DNASU; 9212; -.
DR Ensembl; ENST00000316199.10; ENSP00000313950.6; ENSG00000178999.13. [Q96GD4-5]
DR Ensembl; ENST00000534871.5; ENSP00000443869.1; ENSG00000178999.13. [Q96GD4-4]
DR Ensembl; ENST00000578549.5; ENSP00000462207.1; ENSG00000178999.13. [Q96GD4-2]
DR Ensembl; ENST00000585124.6; ENSP00000463999.1; ENSG00000178999.13. [Q96GD4-1]
DR GeneID; 9212; -.
DR KEGG; hsa:9212; -.
DR MANE-Select; ENST00000585124.6; ENSP00000463999.1; NM_004217.4; NP_004208.2.
DR UCSC; uc002gkm.5; human. [Q96GD4-1]
DR CTD; 9212; -.
DR DisGeNET; 9212; -.
DR GeneCards; AURKB; -.
DR HGNC; HGNC:11390; AURKB.
DR HPA; ENSG00000178999; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 604970; gene.
DR neXtProt; NX_Q96GD4; -.
DR OpenTargets; ENSG00000178999; -.
DR PharmGKB; PA36199; -.
DR VEuPathDB; HostDB:ENSG00000178999; -.
DR eggNOG; KOG0580; Eukaryota.
DR GeneTree; ENSGT00940000158980; -.
DR InParanoid; Q96GD4; -.
DR OMA; PYGRQTT; -.
DR OrthoDB; 954262at2759; -.
DR PhylomeDB; Q96GD4; -.
DR TreeFam; TF351439; -.
DR PathwayCommons; Q96GD4; -.
DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-HSA-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-HSA-68877; Mitotic Prometaphase.
DR Reactome; R-HSA-9022692; Regulation of MECP2 expression and activity.
DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR SignaLink; Q96GD4; -.
DR SIGNOR; Q96GD4; -.
DR BioGRID-ORCS; 9212; 827 hits in 1132 CRISPR screens.
DR GeneWiki; Aurora_B_kinase; -.
DR GenomeRNAi; 9212; -.
DR Pharos; Q96GD4; Tchem.
DR PRO; PR:Q96GD4; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q96GD4; protein.
DR Bgee; ENSG00000178999; Expressed in ventricular zone and 124 other tissues.
DR ExpressionAtlas; Q96GD4; baseline and differential.
DR Genevisible; Q96GD4; HS.
DR GO; GO:0010369; C:chromocenter; IEA:Ensembl.
DR GO; GO:0032133; C:chromosome passenger complex; IPI:UniProtKB.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:ComplexPortal.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:1990023; C:mitotic spindle midzone; IEA:Ensembl.
DR GO; GO:0097431; C:mitotic spindle pole; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005819; C:spindle; TAS:UniProtKB.
DR GO; GO:0005876; C:spindle microtubule; IBA:GO_Central.
DR GO; GO:0051233; C:spindle midzone; IBA:GO_Central.
DR GO; GO:0031616; C:spindle pole centrosome; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0035174; F:histone serine kinase activity; IBA:GO_Central.
DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; TAS:UniProtKB.
DR GO; GO:0009838; P:abscission; ISS:UniProtKB.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; TAS:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; IEA:Ensembl.
DR GO; GO:0034644; P:cellular response to UV; IDA:UniProtKB.
DR GO; GO:0036089; P:cleavage furrow formation; IDA:UniProtKB.
DR GO; GO:0043988; P:histone H3-S28 phosphorylation; IEA:InterPro.
DR GO; GO:0016570; P:histone modification; TAS:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; IC:ComplexPortal.
DR GO; GO:0000281; P:mitotic cytokinesis; IC:ComplexPortal.
DR GO; GO:0044878; P:mitotic cytokinesis checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IEA:InterPro.
DR GO; GO:0051256; P:mitotic spindle midzone assembly; IMP:UniProtKB.
DR GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
DR GO; GO:0002903; P:negative regulation of B cell apoptotic process; IDA:UniProtKB.
DR GO; GO:0032466; P:negative regulation of cytokinesis; ISS:UniProtKB.
DR GO; GO:0032091; P:negative regulation of protein binding; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:1902425; P:positive regulation of attachment of mitotic spindle microtubules to kinetochore; IC:ComplexPortal.
DR GO; GO:0032467; P:positive regulation of cytokinesis; IMP:UniProtKB.
DR GO; GO:1905116; P:positive regulation of lateral attachment of mitotic spindle microtubules to kinetochore; IDA:CACAO.
DR GO; GO:0090267; P:positive regulation of mitotic cell cycle spindle assembly checkpoint; IC:ComplexPortal.
DR GO; GO:1903490; P:positive regulation of mitotic cytokinesis; IC:ComplexPortal.
DR GO; GO:0062033; P:positive regulation of mitotic sister chromatid segregation; IDA:UniProtKB.
DR GO; GO:1901970; P:positive regulation of mitotic sister chromatid separation; IC:ComplexPortal.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IC:ComplexPortal.
DR GO; GO:0051973; P:positive regulation of telomerase activity; IMP:BHF-UCL.
DR GO; GO:1904355; P:positive regulation of telomere capping; IMP:BHF-UCL.
DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; IMP:BHF-UCL.
DR GO; GO:0043687; P:post-translational protein modification; ISS:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; TAS:UniProtKB.
DR GO; GO:0034501; P:protein localization to kinetochore; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0051983; P:regulation of chromosome segregation; TAS:UniProtKB.
DR GO; GO:0032465; P:regulation of cytokinesis; IBA:GO_Central.
DR GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
DR GO; GO:0007051; P:spindle organization; IMP:UniProtKB.
DR DisProt; DP02389; -.
DR InterPro; IPR030616; Aur.
DR InterPro; IPR028772; AURKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24350; PTHR24350; 1.
DR PANTHER; PTHR24350:SF4; PTHR24350:SF4; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; Cell cycle;
KW Cell division; Centromere; Chromosome; Cytoplasm; Cytoskeleton; Kinase;
KW Kinetochore; Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Ubl conjugation.
FT CHAIN 1..344
FT /note="Aurora kinase B"
FT /id="PRO_0000085656"
FT DOMAIN 77..327
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 200
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 83..91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 35
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 64
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 215
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:26829474"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 232
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:14722118,
FT ECO:0000269|PubMed:26829474"
FT VAR_SEQ 1..41
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047103"
FT VAR_SEQ 69
FT /note="T -> TR (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:19134008"
FT /id="VSP_044384"
FT VAR_SEQ 86..134
FT /note="GKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHH ->
FT ALLCLWPEASSVSSPSH (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19134008"
FT /id="VSP_044385"
FT VAR_SEQ 133..141
FT /note="HHPNILRLY -> QSWRSWQML (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:19134008"
FT /id="VSP_044386"
FT VAR_SEQ 142..344
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:19134008"
FT /id="VSP_044387"
FT VARIANT 52
FT /note="A -> V (in dbSNP:rs55878091)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040383"
FT VARIANT 100
FT /note="H -> Q (in dbSNP:rs3027254)"
FT /id="VAR_027970"
FT VARIANT 179
FT /note="T -> M (in dbSNP:rs55871613)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040384"
FT VARIANT 298
FT /note="M -> T (in dbSNP:rs1059476)"
FT /evidence="ECO:0000269|PubMed:11471245,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16762494,
FT ECO:0000269|PubMed:9514916, ECO:0000269|PubMed:9809983,
FT ECO:0000269|PubMed:9858806, ECO:0000269|Ref.5,
FT ECO:0000269|Ref.7"
FT /id="VAR_027971"
FT MUTAGEN 106
FT /note="K->R: Leads to loss of kinase activity and severely
FT impairs mitotic progression."
FT /evidence="ECO:0000269|PubMed:12686604,
FT ECO:0000269|PubMed:12925766, ECO:0000269|PubMed:14722118,
FT ECO:0000269|PubMed:16179162"
FT MUTAGEN 215
FT /note="K->Q: Mimics acetylation, promoting accurate
FT chromosome segregation."
FT /evidence="ECO:0000269|PubMed:26829474"
FT MUTAGEN 215
FT /note="K->R: Abolished acetylation by KAT5, leading to
FT impaired chromosome segregation."
FT /evidence="ECO:0000269|PubMed:26829474"
FT CONFLICT 14..15
FT /note="RQ -> DK (in Ref. 5; AAC98891)"
FT /evidence="ECO:0000305"
FT CONFLICT 161
FT /note="E -> M (in Ref. 4; AAB65786 and 5; AAC98891)"
FT /evidence="ECO:0000305"
FT CONFLICT 167..169
FT /note="QKS -> HKT (in Ref. 4; AAB65786)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="T -> TVRR (in Ref. 4; AAB65786)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="I -> VRAV (in Ref. 5; AAC98891)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="P -> T (in Ref. 3; BAA82709)"
FT /evidence="ECO:0000305"
FT CONFLICT 249..250
FT /note="MH -> ID (in Ref. 3; BAA82709)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="Missing (in Ref. 3; BAA82709)"
FT /evidence="ECO:0000305"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:4AF3"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:4AF3"
FT STRAND 89..96
FT /evidence="ECO:0007829|PDB:4AF3"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:4AF3"
FT STRAND 102..109
FT /evidence="ECO:0007829|PDB:4AF3"
FT HELIX 110..116
FT /evidence="ECO:0007829|PDB:4AF3"
FT HELIX 119..130
FT /evidence="ECO:0007829|PDB:4AF3"
FT STRAND 140..145
FT /evidence="ECO:0007829|PDB:4AF3"
FT STRAND 147..155
FT /evidence="ECO:0007829|PDB:4AF3"
FT HELIX 162..169
FT /evidence="ECO:0007829|PDB:4AF3"
FT HELIX 174..193
FT /evidence="ECO:0007829|PDB:4AF3"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:4AF3"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:4AF3"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:4AF3"
FT HELIX 242..245
FT /evidence="ECO:0007829|PDB:4AF3"
FT HELIX 253..268
FT /evidence="ECO:0007829|PDB:4AF3"
FT HELIX 278..286
FT /evidence="ECO:0007829|PDB:4AF3"
FT HELIX 298..307
FT /evidence="ECO:0007829|PDB:4AF3"
FT HELIX 312..314
FT /evidence="ECO:0007829|PDB:4AF3"
FT HELIX 318..322
FT /evidence="ECO:0007829|PDB:4AF3"
FT HELIX 325..330
FT /evidence="ECO:0007829|PDB:4AF3"
SQ 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
