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 27-MAR-2024, entry version 234. 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}, AIM1 GN {ECO:0000303|PubMed:9809983}, AIRK2, ARK2 GN {ECO:0000303|PubMed:9514916}, STK1, STK12 GN {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 DEUBIQUITINATION BY USP35. RX PubMed=29449677; DOI=10.1038/s41467-018-03107-0; RA Park J., Kwon M.S., Kim E.E., Lee H., Song E.J.; RT "USP35 regulates mitotic progression by modulating the stability of Aurora RT B."; RL Nat. Commun. 9:688-688(2018). RN [54] 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 [55] 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 [56] 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 [57] 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, PubMed:29449677). The CPC complex has essential CC functions at the centromere in ensuring correct chromosome alignment CC and segregation and is required for chromatin-induced microtubule CC stabilization and spindle assembly (PubMed:11516652, PubMed:12925766, CC PubMed:14610074, PubMed:14722118, PubMed:26829474). Involved in the CC bipolar attachment of spindle microtubules to kinetochores and is a key CC regulator for the onset of cytokinesis during mitosis CC (PubMed:15249581). Required for central/midzone spindle assembly and CC cleavage furrow formation (PubMed:12458200, PubMed:12686604). Key CC component of the cytokinesis checkpoint, a process required to delay CC abscission to prevent both premature resolution of intercellular CC chromosome bridges and accumulation of DNA damage: phosphorylates CC CHMP4C, leading to retain abscission-competent VPS4 (VPS4A and/or CC VPS4B) at the midbody ring until abscission checkpoint signaling is CC terminated at late cytokinesis (PubMed:22422861, PubMed:24814515). CC AURKB phosphorylates the CPC complex subunits BIRC5/survivin, CC CDCA8/borealin and INCENP (PubMed:11516652, PubMed:12925766, CC PubMed:14610074). Phosphorylation of INCENP leads to increased AURKB CC activity (PubMed:11516652, PubMed:12925766, PubMed:14610074). Other CC known AURKB substrates involved in centromeric functions and mitosis CC are CENPA, DES/desmin, GPAF, KIF2C, NSUN2, RACGAP1, SEPTIN1, CC VIM/vimentin, HASPIN, and histone H3 (PubMed:11784863, PubMed:12689593, CC PubMed:14602875, PubMed:11856369, PubMed:16103226, PubMed:21658950, CC PubMed:11756469). A positive feedback loop involving HASPIN and AURKB CC contributes to localization of CPC to centromeres (PubMed:21658950). CC Phosphorylation of VIM controls vimentin filament segregation in CC cytokinetic process, whereas histone H3 is phosphorylated at 'Ser-10' CC and 'Ser-28' during mitosis (H3S10ph and H3S28ph, respectively) CC (PubMed:11784863, PubMed:11856369). AURKB is also required for CC kinetochore localization of BUB1 and SGO1 (PubMed:15020684, CC PubMed:17617734). Phosphorylation of p53/TP53 negatively regulates its CC transcriptional activity (PubMed:20959462). Key regulator of active CC promoters in resting B- and T-lymphocytes: acts by mediating CC phosphorylation of H3S28ph at active promoters in resting B-cells, CC inhibiting RNF2/RING1B-mediated ubiquitination of histone H2A and CC enhancing binding and activity of the USP16 deubiquitinase at CC transcribed genes (By similarity). Acts as an inhibitor of CGAS during CC mitosis: catalyzes phosphorylation of the N-terminus of CGAS during the CC G2-M transition, blocking CGAS liquid phase separation and activation, CC and thereby preventing CGAS-induced autoimmunity (PubMed:33542149). CC Phosphorylates KRT5 during anaphase and telophase (By similarity). CC {ECO:0000250|UniProtKB:O70126, ECO:0000269|PubMed:11516652, CC ECO:0000269|PubMed:11756469, ECO:0000269|PubMed:11784863, CC ECO:0000269|PubMed:11856369, ECO:0000269|PubMed:12458200, CC ECO:0000269|PubMed:12686604, ECO:0000269|PubMed:12689593, CC ECO:0000269|PubMed:12925766, ECO:0000269|PubMed:14602875, CC ECO:0000269|PubMed:14610074, ECO:0000269|PubMed:14722118, CC ECO:0000269|PubMed:15020684, ECO:0000269|PubMed:15249581, CC ECO:0000269|PubMed:16103226, ECO:0000269|PubMed:17617734, CC ECO:0000269|PubMed:20959462, ECO:0000269|PubMed:21658950, CC ECO:0000269|PubMed:22422861, ECO:0000269|PubMed:24814515, CC ECO:0000269|PubMed:26829474, ECO:0000269|PubMed:29449677, 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; Q9P2N7: KLHL13; NbExp=2; IntAct=EBI-624291, EBI-1996321; CC Q96GD4; Q9P2J3: KLHL9; NbExp=2; IntAct=EBI-624291, EBI-2510152; 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 Deubiquitinated by USP35; inhibiting CDH1-mediated degradation of AURKB CC (PubMed:29449677). {ECO:0000269|PubMed:17543862, CC ECO:0000269|PubMed:19995937, ECO:0000269|PubMed:29449677}. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; 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. DR PDB; 4AF3; X-ray; 2.75 A; A=55-344. DR PDBsum; 4AF3; -. DR AlphaFoldDB; Q96GD4; -. DR SMR; Q96GD4; -. DR BioGRID; 114646; 824. DR ComplexPortal; CPX-116; Chromosomal passenger complex. DR CORUM; Q96GD4; -. DR DIP; DIP-34530N; -. DR ELM; Q96GD4; -. DR IntAct; Q96GD4; 204. 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 DrugBank; DB12756; TAK-901. 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 CPTAC; CPTAC-3030; -. DR CPTAC; CPTAC-3031; -. DR EPD; Q96GD4; -. DR jPOST; Q96GD4; -. DR MassIVE; Q96GD4; -. DR MaxQB; Q96GD4; -. DR PaxDb; 9606-ENSP00000313950; -. DR PeptideAtlas; Q96GD4; -. DR ProteomicsDB; 4709; -. DR ProteomicsDB; 7611; -. DR ProteomicsDB; 76623; -. [Q96GD4-1] DR Pumba; Q96GD4; -. DR Antibodypedia; 3128; 1314 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 AGR; HGNC:11390; -. 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; HGPFSEK; -. DR OrthoDB; 117459at2759; -. 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; 863 hits in 1220 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 125 other cell types or tissues. DR ExpressionAtlas; Q96GD4; baseline and differential. 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:HPA. 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: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:0008608; P:attachment of spindle microtubules to kinetochore; TAS:UniProtKB. DR GO; GO:0044839; P:cell cycle G2/M phase transition; IDA:UniProt. DR GO; GO:0034644; P:cellular response to UV; IDA:UniProtKB. DR GO; GO:0036089; P:cleavage furrow formation; IDA:UniProtKB. DR GO; GO:0016570; P:histone modification; TAS:UniProtKB. DR GO; GO:0000278; P:mitotic cell cycle; NAS:ComplexPortal. DR GO; GO:0000281; P:mitotic cytokinesis; NAS:ComplexPortal. DR GO; GO:0044878; P:mitotic cytokinesis checkpoint signaling; ISS:UniProtKB. DR GO; GO:0090307; P:mitotic spindle assembly; NAS:ComplexPortal. 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:0160049; P:negative regulation of cGAS/STING signaling pathway; IDA:UniProt. DR GO; GO:0032466; P:negative regulation of cytokinesis; ISS:UniProtKB. DR GO; GO:0045824; P:negative regulation of innate immune response; IDA:UniProt. 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; NAS: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; NAS:ComplexPortal. DR GO; GO:1903490; P:positive regulation of mitotic cytokinesis; NAS: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; NAS: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 Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR030616; Aur-like. 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:SF4; AURORA KINASE B; 1. DR PANTHER; PTHR24350; SERINE/THREONINE-PROTEIN KINASE IAL-RELATED; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR Genevisible; Q96GD4; HS. 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 //