ID   AURKB_RAT               Reviewed;         343 AA.
AC   O55099; Q4V8N1;
DT   17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   27-MAR-2024, entry version 197.
DE   RecName: Full=Aurora kinase B;
DE            EC=2.7.11.1 {ECO:0000250|UniProtKB:Q96GD4};
DE   AltName: Full=Aurora 1;
DE   AltName: Full=Aurora- and IPL1-like midbody-associated protein 1;
DE   AltName: Full=Aurora/IPL1-related kinase 2;
DE            Short=ARK-2;
DE            Short=Aurora-related kinase 2;
DE   AltName: Full=STK-1;
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;
GN   Name=Aurkb; Synonyms=Aik2, Aim1, Airk2, Ark2, Stk1, Stk12, Stk5;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS
RP   OF LYS-109.
RC   TISSUE=Kidney;
RX   PubMed=9450992; DOI=10.1093/emboj/17.3.667;
RA   Terada Y., Tatsuka M., Suzuki F., Yasuda Y., Fujita S., Otsu M.;
RT   "AIM-1: a mammalian midbody-associated protein required for cytokinesis.";
RL   EMBO J. 17:667-676(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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).
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 (PubMed:9450992). 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) (By
CC       similarity). AURKB is also required for kinetochore localization of
CC       BUB1 and SGO1 (By similarity). Phosphorylation of p53/TP53 negatively
CC       regulates its transcriptional activity (By similarity). Key regulator
CC       of active 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 (By similarity).
CC       Phosphorylates KRT5 during anaphase and telophase (By similarity).
CC       {ECO:0000250|UniProtKB:O70126, ECO:0000250|UniProtKB:Q96GD4,
CC       ECO:0000269|PubMed:9450992}.
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:0000250|UniProtKB:Q96GD4};
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:0000250|UniProtKB:Q96GD4};
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-235-
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 (By similarity).
CC       {ECO:0000250|UniProtKB:O70126, ECO:0000250|UniProtKB:Q96GD4}.
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-235-
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: High level expression seen in the testis. It is
CC       also expressed in the spleen, lung and heart. Expressed in the G2/M
CC       phase of the cell cycle. {ECO:0000269|PubMed:9450992}.
CC   -!- PTM: The phosphorylation of Thr-235 requires the binding to INCENP and
CC       occurs by means of an autophosphorylation mechanism. Thr-235
CC       phosphorylation is indispensable for the AURKB kinase activity.
CC       {ECO:0000250|UniProtKB:Q96GD4}.
CC   -!- PTM: Acetylated at Lys-218 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; D89731; BAA23794.1; -; mRNA.
DR   EMBL; BC097297; AAH97297.1; -; mRNA.
DR   RefSeq; NP_446201.1; NM_053749.1.
DR   RefSeq; XP_006246631.1; XM_006246569.3.
DR   RefSeq; XP_008765979.1; XM_008767757.2.
DR   RefSeq; XP_008765980.1; XM_008767758.1.
DR   AlphaFoldDB; O55099; -.
DR   SMR; O55099; -.
DR   ELM; O55099; -.
DR   STRING; 10116.ENSRNOP00000072371; -.
DR   iPTMnet; O55099; -.
DR   PhosphoSitePlus; O55099; -.
DR   PaxDb; 10116-ENSRNOP00000008492; -.
DR   Ensembl; ENSRNOT00000008492.7; ENSRNOP00000008492.3; ENSRNOG00000005659.7.
DR   Ensembl; ENSRNOT00065043008; ENSRNOP00065035207; ENSRNOG00065025020.
DR   GeneID; 114592; -.
DR   KEGG; rno:114592; -.
DR   UCSC; RGD:621625; rat.
DR   AGR; RGD:621625; -.
DR   CTD; 9212; -.
DR   RGD; 621625; Aurkb.
DR   eggNOG; KOG0580; Eukaryota.
DR   GeneTree; ENSGT00940000158980; -.
DR   HOGENOM; CLU_000288_63_0_1; -.
DR   InParanoid; O55099; -.
DR   OrthoDB; 117459at2759; -.
DR   PhylomeDB; O55099; -.
DR   TreeFam; TF351439; -.
DR   Reactome; R-RNO-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR   Reactome; R-RNO-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR   Reactome; R-RNO-2467813; Separation of Sister Chromatids.
DR   Reactome; R-RNO-2500257; Resolution of Sister Chromatid Cohesion.
DR   Reactome; R-RNO-4615885; SUMOylation of DNA replication proteins.
DR   Reactome; R-RNO-5663220; RHO GTPases Activate Formins.
DR   Reactome; R-RNO-6804756; Regulation of TP53 Activity through Phosphorylation.
DR   Reactome; R-RNO-68877; Mitotic Prometaphase.
DR   Reactome; R-RNO-9648025; EML4 and NUDC in mitotic spindle formation.
DR   PRO; PR:O55099; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Bgee; ENSRNOG00000005659; Expressed in thymus and 19 other cell types or tissues.
DR   GO; GO:0010369; C:chromocenter; ISO:RGD.
DR   GO; GO:0005694; C:chromosome; ISO:RGD.
DR   GO; GO:0032133; C:chromosome passenger complex; ISO:RGD.
DR   GO; GO:0000775; C:chromosome, centromeric region; ISO:RGD.
DR   GO; GO:0000779; C:condensed chromosome, centromeric region; ISO:RGD.
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:RGD.
DR   GO; GO:0030496; C:midbody; IDA:RGD.
DR   GO; GO:1990023; C:mitotic spindle midzone; ISO:RGD.
DR   GO; GO:0097431; C:mitotic spindle pole; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; ISS: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:0044022; F:histone H3S28 kinase activity; ISO:RGD.
DR   GO; GO:0019900; F:kinase binding; ISO:RGD.
DR   GO; GO:0004672; F:protein kinase activity; IMP:RGD.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR   GO; GO:0009838; P:abscission; ISS:UniProtKB.
DR   GO; GO:0044839; P:cell cycle G2/M phase transition; ISO:RGD.
DR   GO; GO:0034644; P:cellular response to UV; ISS:UniProtKB.
DR   GO; GO:0036089; P:cleavage furrow formation; IMP:RGD.
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:RGD.
DR   GO; GO:0032466; P:negative regulation of cytokinesis; ISS:UniProtKB.
DR   GO; GO:0045824; P:negative regulation of innate immune response; ISO:RGD.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
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:RGD.
DR   GO; GO:0062033; P:positive regulation of mitotic sister chromatid segregation; ISS:UniProtKB.
DR   GO; GO:1904355; P:positive regulation of telomere capping; ISO:RGD.
DR   GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; ISO:RGD.
DR   GO; GO:0043687; P:post-translational protein modification; ISS: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:RGD.
DR   CDD; cd14117; STKc_Aurora-B_like; 1.
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; O55099; RN.
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..343
FT                   /note="Aurora kinase B"
FT                   /id="PRO_0000085659"
FT   DOMAIN          80..330
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   REGION          36..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..57
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        203
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         86..94
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         109
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   MOD_RES         218
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96GD4"
FT   MOD_RES         230
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96GD4"
FT   MOD_RES         235
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250|UniProtKB:Q96GD4"
FT   MUTAGEN         109
FT                   /note="K->R: Loss of kinase activity, disruption of
FT                   cleavage furrow formation, failure of cytokinesis leading
FT                   to cell polyploidy death."
FT                   /evidence="ECO:0000269|PubMed:9450992"
SQ   SEQUENCE   343 AA;  39234 MW;  27B740D20E287598 CRC64;
     MAQKENVYPW PYGSKTSQSG LNTLPQRVLR KEPAVTPAQA LMNRSNSQST AVPGQKLTEN
     KGATALQGSQ SRQPFTIDNF EIGRPLGKGK FGNVYLAREK KSRFIVALKI LFKSQIEKEG
     VEHQLRREIE IQAHLKHPNI LQLYNYFYDQ QRIYLILEYA PRGELYKELQ KSGTFDEQRT
     ATIMEELSDA LMYCHKKKVI HRDIKPENLL LGLQGELKIA DFGWSVHAPS LRRKTMCGTL
     DYLPPEMIEG RMHNEMVDLW CIGVLCYELM VGNPPFESPS HSETYRRIVK VDLKFPSSMP
     LGAKDLISKL LKHNPSQRLP LEQVSAHPWV RANSRRVLPP SAL
//