AURKB_MOUSE
ID AURKB_MOUSE Reviewed; 345 AA.
AC O70126; Q61882; Q8C6C1;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Aurora kinase B {ECO:0000303|PubMed:11784863};
DE EC=2.7.11.1 {ECO:0000269|PubMed:24034696};
DE AltName: Full=Aurora 1;
DE AltName: Full=Aurora- and IPL1-like midbody-associated protein 1;
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 {ECO:0000303|PubMed:8647446};
DE AltName: Full=Serine/threonine-protein kinase 12;
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, Aim1, Airk2, Ark2 {ECO:0000303|PubMed:9514916},
GN Stk1 {ECO:0000303|PubMed:8647446}, Stk12, Stk5;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=8647446; DOI=10.1016/0378-1119(95)00809-8;
RA Niwa H., Abe K., Kunisada T., Yamamura K.;
RT "Cell-cycle-dependent expression of the STK-1 gene encoding a novel murine
RT putative protein kinase.";
RL Gene 169:197-201(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RX PubMed=9514916; DOI=10.1006/bbrc.1998.8250;
RA Shindo M., Nakano H., Kuroyanagi H., Shirasawa T., Mihara M., Gilbert D.J.,
RA Jenkins N.A., Copeland N.G., Yagita H., Okumura K.;
RT "cDNA cloning, expression, subcellular localization, and chromosomal
RT assignment of mammalian aurora homologues, aurora-related kinase (ARK) 1
RT and 2.";
RL Biochem. Biophys. Res. Commun. 244:285-292(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Embryonic stem cell;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland;
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 [7]
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH RNF2.
RX PubMed=24034696; DOI=10.1016/j.molcel.2013.08.022;
RA Frangini A., Sjoberg M., Roman-Trufero M., Dharmalingam G., Haberle V.,
RA Bartke T., Lenhard B., Malumbres M., Vidal M., Dillon N.;
RT "The Aurora B kinase and the Polycomb protein Ring1B combine to regulate
RT active promoters in quiescent lymphocytes.";
RL Mol. Cell 51:647-661(2013).
RN [10]
RP FUNCTION.
RX PubMed=29518391; DOI=10.1016/j.bbrc.2018.03.016;
RA Inaba H., Yamakawa D., Tomono Y., Enomoto A., Mii S., Kasahara K., Goto H.,
RA Inagaki M.;
RT "Regulation of keratin 5/14 intermediate filaments by CDK1, Aurora-B, and
RT Rho-kinase.";
RL Biochem. Biophys. Res. Commun. 498:544-550(2018).
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 (By similarity). 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 (By similarity). Involved in the bipolar attachment of spindle
CC microtubules to kinetochores and is a key regulator for the onset of
CC cytokinesis during mitosis (By similarity). Required for
CC central/midzone spindle assembly and cleavage furrow formation (By
CC similarity). Key component of the cytokinesis checkpoint, a process
CC required to delay abscission to prevent both premature resolution of
CC intercellular chromosome bridges and accumulation of DNA damage:
CC phosphorylates CHMP4C, leading to retain abscission-competent VPS4
CC (VPS4A and/or VPS4B) at the midbody ring until abscission checkpoint
CC signaling is terminated at late cytokinesis (By similarity). AURKB
CC phosphorylates the CPC complex subunits BIRC5/survivin, CDCA8/borealin
CC and INCENP (By similarity). Phosphorylation of INCENP leads to
CC increased AURKB activity (By similarity). 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 (By similarity). A positive feedback loop involving HASPIN and AURKB
CC contributes to localization of CPC to centromeres (By similarity).
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). A positive feedback between HASPIN and AURKB
CC contributes to CPC localization (By similarity). AURKB is also required
CC for kinetochore localization of BUB1 and SGO1 (By similarity).
CC Phosphorylation of p53/TP53 negatively regulates its transcriptional
CC activity (By similarity). Key regulator of active promoters in resting
CC B- and T-lymphocytes: acts by mediating phosphorylation of H3S28ph at
CC active 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 (PubMed:24034696). 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 (By similarity). Phosphorylates KRT5 during anaphase and
CC telophase (PubMed:29518391). {ECO:0000250|UniProtKB:Q96GD4,
CC ECO:0000269|PubMed:11784863, ECO:0000269|PubMed:24034696,
CC ECO:0000269|PubMed:29518391}.
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:24034696};
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:24034696};
CC -!- ACTIVITY REGULATION: Activity is greatly increased when AURKB is within
CC the CPC complex. In particular, AURKB-phosphorylated INCENP acts as an
CC activator of AURKB. Positive feedback between HASPIN and AURKB
CC contributes to CPC localization. {ECO:0000250|UniProtKB:Q96GD4}.
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 Associates with RACGAP1 during M phase. Interacts with CDCA1, EVI5,
CC JTB, NDC80, PSMA3, SEPTIN1, SIRT2 and TACC1. Interacts with SPDYC; this
CC interaction may be required for proper localization of active, Thr-237-
CC phosphorylated AURKB form during prometaphase and metaphase. Interacts
CC with p53/TP53. Interacts (via the middle kinase domain) with NOC2L (via
CC the N- and C-terminus domains). Interacts with TTC28 (By similarity).
CC Interacts with RNF2/RING1B (PubMed:24034696).
CC {ECO:0000250|UniProtKB:Q96GD4, ECO:0000269|PubMed:24034696}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96GD4}.
CC Chromosome {ECO:0000250|UniProtKB:Q96GD4}. Chromosome, centromere
CC {ECO:0000250|UniProtKB:Q96GD4}. Chromosome, centromere, kinetochore
CC {ECO:0000250|UniProtKB:Q96GD4}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:Q96GD4}. Midbody {ECO:0000250|UniProtKB:Q96GD4}.
CC Note=Localizes on chromosome arms and inner centromeres from prophase
CC through metaphase and then transferring to the spindle midzone and
CC midbody from anaphase through cytokinesis. Colocalized with gamma
CC tubulin in the midbody. Proper localization of the active, Thr-237-
CC phosphorylated form during metaphase may be dependent upon interaction
CC with SPDYC. Colocalized with SIRT2 during cytokinesis with the midbody.
CC Localization (and probably targeting of the CPC) to the inner
CC centromere occurs predominantly in regions with overlapping mitosis-
CC specific histone phosphorylations H3pT3 and H2ApT12.
CC {ECO:0000250|UniProtKB:Q96GD4}.
CC -!- TISSUE SPECIFICITY: Expressed in testis, intestine and spleen. All of
CC them are tissues that contain a large number of proliferating cells.
CC Expressed during S phase, in a cell-cycle-dependent fashion.
CC {ECO:0000269|PubMed:8647446}.
CC -!- DEVELOPMENTAL STAGE: Strongly expressed in 8.5 and 12.5 dpc.
CC {ECO:0000269|PubMed:8647446}.
CC -!- PTM: The phosphorylation of Thr-237 requires the binding to INCENP and
CC occurs by means of an autophosphorylation mechanism. Thr-237
CC phosphorylation is indispensable for the AURKB kinase activity.
CC {ECO:0000250|UniProtKB:Q96GD4}.
CC -!- PTM: Acetylated at Lys-220 by KAT5 at kinetochores, increasing AURKB
CC activity and promoting accurate chromosome segregation in mitosis.
CC {ECO:0000250|UniProtKB:Q96GD4}.
CC -!- PTM: Ubiquitinated by different BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase
CC complexes. Ubiquitinated by the BCR(KLHL9-KLHL13) E3 ubiquitin ligase
CC complex, ubiquitination leads to removal from mitotic chromosomes and
CC is required for cytokinesis. During anaphase, the BCR(KLHL21) E3
CC ubiquitin ligase complex recruits the CPC complex from chromosomes to
CC the spindle midzone and mediates the ubiquitination of AURKB.
CC Ubiquitination of AURKB by BCR(KLHL21) E3 ubiquitin ligase complex may
CC not lead to its degradation by the proteasome.
CC {ECO:0000250|UniProtKB:Q96GD4}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. Aurora subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; D21099; BAA04658.1; -; mRNA.
DR EMBL; U69107; AAC12683.1; -; mRNA.
DR EMBL; AK075951; BAC36078.1; -; mRNA.
DR EMBL; AK132006; BAE20935.1; -; mRNA.
DR EMBL; AL645902; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466601; EDL10472.1; -; Genomic_DNA.
DR EMBL; BC003261; AAH03261.1; -; mRNA.
DR CCDS; CCDS24877.1; -.
DR PIR; JC4665; JC4665.
DR RefSeq; NP_035626.1; NM_011496.2.
DR AlphaFoldDB; O70126; -.
DR SMR; O70126; -.
DR BioGRID; 203547; 29.
DR ComplexPortal; CPX-119; Chromosomal passenger complex.
DR IntAct; O70126; 15.
DR MINT; O70126; -.
DR STRING; 10090.ENSMUSP00000021277; -.
DR BindingDB; O70126; -.
DR ChEMBL; CHEMBL1075275; -.
DR CarbonylDB; O70126; -.
DR iPTMnet; O70126; -.
DR PhosphoSitePlus; O70126; -.
DR EPD; O70126; -.
DR MaxQB; O70126; -.
DR PaxDb; O70126; -.
DR PeptideAtlas; O70126; -.
DR PRIDE; O70126; -.
DR ProteomicsDB; 273505; -.
DR Antibodypedia; 3128; 1133 antibodies from 46 providers.
DR DNASU; 20877; -.
DR Ensembl; ENSMUST00000021277; ENSMUSP00000021277; ENSMUSG00000020897.
DR Ensembl; ENSMUST00000108666; ENSMUSP00000104306; ENSMUSG00000020897.
DR GeneID; 20877; -.
DR KEGG; mmu:20877; -.
DR UCSC; uc007jpa.1; mouse.
DR CTD; 9212; -.
DR MGI; MGI:107168; Aurkb.
DR VEuPathDB; HostDB:ENSMUSG00000020897; -.
DR eggNOG; KOG0580; Eukaryota.
DR GeneTree; ENSGT00940000158980; -.
DR HOGENOM; CLU_000288_63_0_1; -.
DR InParanoid; O70126; -.
DR OMA; PYGRQTT; -.
DR OrthoDB; 954262at2759; -.
DR PhylomeDB; O70126; -.
DR TreeFam; TF351439; -.
DR Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-MMU-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-MMU-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-MMU-68877; Mitotic Prometaphase.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR BioGRID-ORCS; 20877; 26 hits in 77 CRISPR screens.
DR ChiTaRS; Aurkb; mouse.
DR PRO; PR:O70126; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; O70126; protein.
DR Bgee; ENSMUSG00000020897; Expressed in embryonic post-anal tail and 178 other tissues.
DR Genevisible; O70126; MM.
DR GO; GO:0010369; C:chromocenter; IDA:MGI.
DR GO; GO:0005694; C:chromosome; IDA:MGI.
DR GO; GO:0032133; C:chromosome passenger complex; IDA:MGI.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:MGI.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0030496; C:midbody; IDA:MGI.
DR GO; GO:1990023; C:mitotic spindle midzone; IDA:MGI.
DR GO; GO:0097431; C:mitotic spindle pole; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005819; C:spindle; ISO:MGI.
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:0044022; F:histone kinase activity (H3-S28 specific); IDA:UniProtKB.
DR GO; GO:0035174; F:histone serine kinase activity; IBA:GO_Central.
DR GO; GO:0019900; F:kinase binding; ISO:MGI.
DR GO; GO:0004672; F:protein kinase activity; ISO:MGI.
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:0009838; P:abscission; ISS:UniProtKB.
DR GO; GO:0034644; P:cellular response to UV; ISS:UniProtKB.
DR GO; GO:0036089; P:cleavage furrow formation; ISS: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; ISS:UniProtKB.
DR GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
DR GO; GO:0002903; P:negative regulation of B cell apoptotic process; ISS:UniProtKB.
DR GO; GO:0032466; P:negative regulation of cytokinesis; ISS:UniProtKB.
DR GO; GO:0032091; P:negative regulation of protein binding; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS: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; ISS:UniProtKB.
DR GO; GO:1905116; P:positive regulation of lateral attachment of mitotic spindle microtubules to kinetochore; ISO:MGI.
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; ISS: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; ISO:MGI.
DR GO; GO:1904355; P:positive regulation of telomere capping; ISO:MGI.
DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; ISO:MGI.
DR GO; GO:0043687; P:post-translational protein modification; IDA:UniProtKB.
DR GO; GO:0034501; P:protein localization to kinetochore; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0032465; P:regulation of cytokinesis; IBA:GO_Central.
DR GO; GO:0007051; P:spindle organization; ISO:MGI.
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 Acetylation; ATP-binding; Cell cycle; Cell division; Centromere;
KW Chromosome; Cytoplasm; Cytoskeleton; Kinase; Kinetochore; Mitosis;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Ubl conjugation.
FT CHAIN 1..345
FT /note="Aurora kinase B"
FT /id="PRO_0000085657"
FT DOMAIN 82..332
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 50..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 205
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 88..96
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 111
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:0000250|UniProtKB:Q96GD4"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96GD4"
FT MOD_RES 220
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q96GD4"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96GD4"
FT MOD_RES 237
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q96GD4"
FT CONFLICT 44
FT /note="R -> W (in Ref. 1; BAA04658)"
FT /evidence="ECO:0000305"
FT CONFLICT 45
FT /note="F -> S (in Ref. 1; BAA04658, 2; AAC12683 and 6;
FT AAH03261)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 345 AA; 39384 MW; D204D8B91CFF00A4 CRC64;
MAQKENAYPW PYGSKTSQSG LNTLSQRVLR KEPATTSALA LVNRFNSQST AAPGQKLAEN
KSQGSTASQG SQNKQPFTID NFEIGRPLGK GKFGNVYLAR EKKSRFIVAL KILFKSQIEK
EGVEHQLRRE IEIQAHLKHP NILQLYNYFY DQQRIYLILE YAPRGELYKE LQKSRTFDEQ
RTATIMEELS DALTYCHKKK VIHRDIKPEN LLLGLQGELK IADFGWSVHA PSLRRKTMCG
TLDYLPPEMI EGRMHNEMVD LWCIGVLCYE LMVGNPPFES PSHSETYRRI VKVDLKFPSS
VPSGAQDLIS KLLKHNPWQR LPLAEVAAHP WVRANSRRVL PPSAL
