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   27-MAR-2024, entry version 217.
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}, Stk1
GN   {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). AURKB is also required for kinetochore localization
CC       of BUB1 and SGO1 (By similarity). Phosphorylation of p53/TP53
CC       negatively regulates its transcriptional activity (By similarity). Key
CC       regulator of active promoters in resting B- and T-lymphocytes: acts by
CC       mediating phosphorylation of H3S28ph at active promoters in resting B-
CC       cells, inhibiting RNF2/RING1B-mediated ubiquitination of histone H2A
CC       and enhancing binding and activity of the USP16 deubiquitinase at
CC       transcribed genes (PubMed:24034696). Acts as an inhibitor of CGAS
CC       during mitosis: catalyzes phosphorylation of the N-terminus of CGAS
CC       during the G2-M transition, blocking CGAS liquid phase separation and
CC       activation, and thereby preventing CGAS-induced autoimmunity (By
CC       similarity). Phosphorylates KRT5 during anaphase and telophase
CC       (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. Deubiquitinated by
CC       USP35; inhibiting CDH1-mediated degradation of AURKB.
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; 31.
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   GlyGen; O70126; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; O70126; -.
DR   PhosphoSitePlus; O70126; -.
DR   EPD; O70126; -.
DR   MaxQB; O70126; -.
DR   PaxDb; 10090-ENSMUSP00000021277; -.
DR   PeptideAtlas; O70126; -.
DR   ProteomicsDB; 273505; -.
DR   Pumba; O70126; -.
DR   Antibodypedia; 3128; 1314 antibodies from 46 providers.
DR   DNASU; 20877; -.
DR   Ensembl; ENSMUST00000021277.6; ENSMUSP00000021277.6; ENSMUSG00000020897.13.
DR   Ensembl; ENSMUST00000108666.8; ENSMUSP00000104306.2; ENSMUSG00000020897.13.
DR   GeneID; 20877; -.
DR   KEGG; mmu:20877; -.
DR   UCSC; uc007jpa.1; mouse.
DR   AGR; MGI:107168; -.
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; HGPFSEK; -.
DR   OrthoDB; 117459at2759; -.
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 83 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 181 other cell types or tissues.
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: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 H3S28 kinase activity; IDA:UniProtKB.
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:0044839; P:cell cycle G2/M phase transition; ISO:MGI.
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; 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: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:0160049; P:negative regulation of cGAS/STING signaling pathway; ISO:MGI.
DR   GO; GO:0032466; P:negative regulation of cytokinesis; ISS:UniProtKB.
DR   GO; GO:0045824; P:negative regulation of innate immune response; 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; NAS: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; 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; ISS:UniProtKB.
DR   GO; GO:1901970; P:positive regulation of mitotic sister chromatid separation; NAS:ComplexPortal.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; NAS:ComplexPortal.
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   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; O70126; MM.
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
//