AURKB_PIG
ID AURKB_PIG Reviewed; 344 AA.
AC Q9N0X0; Q7YRC7;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 151.
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 Short=AIM-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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zhou G., Li W., Yu L.;
RT "Cloning of Sus scrofa STK12.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 150-305.
RC TISSUE=Small intestine;
RX PubMed=12270407; DOI=10.1016/s0041-1345(02)03244-x;
RA Braun F., Hosseini S.M., Lorf T., Laabs S., Ringe B.;
RT "Differential gene expression during intestinal ischemia-reperfusion
RT injury.";
RL Transplant. Proc. 34:2301-2302(2002).
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. The CPC complex has essential functions at the centromere in
CC ensuring correct chromosome alignment and segregation and is required
CC for chromatin-induced microtubule stabilization and spindle assembly.
CC Involved in the bipolar attachment of spindle microtubules to
CC kinetochores and is a key regulator for the onset of cytokinesis during
CC mitosis. Required for central/midzone spindle assembly and cleavage
CC furrow formation. Key component of the cytokinesis checkpoint, a
CC process required to delay abscission to prevent both premature
CC resolution of intercellular chromosome bridges and accumulation of DNA
CC damage: phosphorylates CHMP4C, leading to retain abscission-competent
CC VPS4 (VPS4A and/or VPS4B) at the midbody ring until abscission
CC checkpoint signaling is terminated at late cytokinesis. AURKB
CC phosphorylates the CPC complex subunits BIRC5/survivin, CDCA8/borealin
CC and INCENP. Phosphorylation of INCENP leads to increased AURKB
CC activity. Other known AURKB substrates involved in centromeric
CC functions and mitosis are CENPA, DES/desmin, GPAF, KIF2C, NSUN2,
CC RACGAP1, SEPTIN1, VIM/vimentin, HASPIN, and histone H3. A positive
CC feedback loop involving HASPIN and AURKB contributes to localization of
CC CPC to centromeres. Phosphorylation of VIM controls vimentin filament
CC segregation in cytokinetic process, whereas histone H3 is
CC phosphorylated at 'Ser-10' and 'Ser-28' during mitosis (H3S10ph and
CC H3S28ph, respectively). A positive feedback between HASPIN and AURKB
CC contributes to CPC localization. AURKB is also required for kinetochore
CC localization of BUB1 and SGO1. 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 -!- 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-232-
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-232-
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 -!- PTM: The phosphorylation of Thr-232 requires the binding to INCENP and
CC occurs by means of an autophosphorylation mechanism. Thr-232
CC phosphorylation is indispensable for the AURKB kinase activity.
CC {ECO:0000250|UniProtKB:Q96GD4}.
CC -!- PTM: Acetylated at Lys-215 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; AY336974; AAQ16150.1; -; mRNA.
DR EMBL; AF244364; AAF61735.1; -; mRNA.
DR RefSeq; NP_999084.1; NM_213919.1.
DR AlphaFoldDB; Q9N0X0; -.
DR SMR; Q9N0X0; -.
DR STRING; 9823.ENSSSCP00000022968; -.
DR iPTMnet; Q9N0X0; -.
DR PaxDb; Q9N0X0; -.
DR PRIDE; Q9N0X0; -.
DR GeneID; 396955; -.
DR KEGG; ssc:396955; -.
DR CTD; 9212; -.
DR eggNOG; KOG0580; Eukaryota.
DR InParanoid; Q9N0X0; -.
DR OrthoDB; 954262at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0032133; C:chromosome passenger complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
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:0035174; F:histone serine kinase activity; IBA:GO_Central.
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:0034644; P:cellular response to UV; ISS:UniProtKB.
DR GO; GO:0036089; P:cleavage furrow formation; ISS:UniProtKB.
DR GO; GO:0043988; P:histone H3-S28 phosphorylation; IEA:InterPro.
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: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:0062033; P:positive regulation of mitotic sister chromatid segregation; ISS:UniProtKB.
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 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 2: Evidence at transcript 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..344
FT /note="Aurora kinase B"
FT /id="PRO_0000085658"
FT DOMAIN 77..327
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
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:0000250|UniProtKB:Q96GD4"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96GD4"
FT MOD_RES 64
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96GD4"
FT MOD_RES 215
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q96GD4"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96GD4"
FT MOD_RES 232
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q96GD4"
FT CONFLICT 234
FT /note="C -> R (in Ref. 2; AAF61735)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="G -> V (in Ref. 2; AAF61735)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 344 AA; 39222 MW; 5163244791BF7F0D CRC64;
MAQKENTYPW PYGRQTAQSG LNILPQRVLR KEAVTPSALV LMSRSNTQPT AAPGQKVVEN
SSGTPNFSTR SFTIDDFEIG RPLGKGKFGN VYLAREKKSH FIVALKVLFK SQIEKEGVEH
QLRREIEIQA HLQHPNILRL YNYFYDRRRI YLILEYAPRG ELYKELQKCR TFDEQRTATI
MEELADALIY CHGKKVIHRD IKPENLLLGL QGELKIADFG WSVHAPSLRR KTMCGTLDYL
PPEMIEGRTH NEKVDLWCIG VLCYELLVGN PPFESASHNE TYRRIGKVDL KFPPSVPAGA
QDLISKLLKH NPSDRLPLAQ VSAHPWVRAH SRRVLPPSAP QSVP
