AUKBA_XENLA
ID AUKBA_XENLA Reviewed; 361 AA.
AC Q6DE08; Q7ZYT9; Q8JG74; Q9DF70;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Aurora kinase B-A;
DE EC=2.7.11.1;
DE AltName: Full=Aurora/IPL1-related kinase 2-A;
DE Short=AIRK2-A;
DE Short=XAIRK2-A;
DE AltName: Full=Serine/threonine-protein kinase 12-A;
DE AltName: Full=Serine/threonine-protein kinase aurora-B-A;
DE Short=xAurora-B;
GN Name=aurkb-a; Synonyms=airk2-a;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH INCENP, AND SUBCELLULAR
RP LOCATION.
RX PubMed=10996078; DOI=10.1016/s0960-9822(00)00673-4;
RA Adams R.R., Wheatleya S.P., Gouldsworthy A.M., Kandels-Lewis S.E.,
RA Carmena M., Smythe C., Gerloff D.L., Earnshaw W.C.;
RT "INCENP binds the Aurora-related kinase AIRK2 and is required to target it
RT to chromosomes, the central spindle and cleavage furrow.";
RL Curr. Biol. 10:1075-1078(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, INTERACTION WITH INCENP, PUTATIVE INTERACTION WITH BIRC5.1,
RP IDENTIFICATION IN A COMPLEX WITH BIRC5.1 AND INCENP, AND PHOSPHORYLATION.
RX PubMed=12221116; DOI=10.1091/mbc.e02-02-0092;
RA Bolton M.A., Lan W., Powers S.E., McCleland M.L., Kuang J.,
RA Stukenberg P.T.;
RT "Aurora B kinase exists in a complex with survivin and INCENP and its
RT kinase activity is stimulated by survivin binding and phosphorylation.";
RL Mol. Biol. Cell 13:3064-3077(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=11350965; DOI=10.1074/jbc.m102288200;
RA Murnion M.E., Adams R.R., Callister D.M., Allis C.D., Earnshaw W.C.,
RA Swedlow J.R.;
RT "Chromatin-associated protein phosphatase 1 regulates aurora-B and histone
RT H3 phosphorylation.";
RL J. Biol. Chem. 276:26656-26665(2001).
RN [5]
RP IDENTIFICATION IN A COMPLEX WITH BIRC5.1 AND INCENP, AND SUBCELLULAR
RP LOCATION.
RX PubMed=12464631; DOI=10.1101/gad.249202;
RA Losada A., Hirano M., Hirano T.;
RT "Cohesin release is required for sister chromatid resolution, but not for
RT condensin-mediated compaction, at the onset of mitosis.";
RL Genes Dev. 16:3004-3016(2002).
RN [6]
RP INTERACTION WITH MTUS1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=12919681; DOI=10.1016/s1534-5807(03)00229-6;
RA Ohi R., Coughlin M.L., Lane W.S., Mitchison T.J.;
RT "An inner centromere protein that stimulates the microtubule depolymerizing
RT activity of a KinI kinesin.";
RL Dev. Cell 5:309-321(2003).
RN [7]
RP IDENTIFICATION IN A COMPLEX WITH BIRC5.1; INCENP AND CDCA9.
RX PubMed=15260989; DOI=10.1016/j.cell.2004.06.026;
RA Sampath S.C., Ohi R., Leismann O., Salic A., Pozniakovski A., Funabiki H.;
RT "The chromosomal passenger complex is required for chromatin-induced
RT microtubule stabilization and spindle assembly.";
RL Cell 118:187-202(2004).
RN [8]
RP IDENTIFICATION IN A COMPLEX WITH BIRC5.1 AND INCENP.
RX PubMed=16322459; DOI=10.1126/science.1120160;
RA Vong Q.P., Cao K., Li H.Y., Iglesias P.A., Zheng Y.;
RT "Chromosome alignment and segregation regulated by ubiquitination of
RT survivin.";
RL Science 310:1499-1504(2005).
RN [9]
RP FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH CDCA8; CDCA9; BIRC5.1;
RP BIRC5.2 AND INCENP.
RX PubMed=17199039; DOI=10.1016/j.devcel.2006.11.001;
RA Kelly A.E., Sampath S.C., Maniar T.A., Woo E.M., Chait B.T., Funabiki H.;
RT "Chromosomal enrichment and activation of the aurora B pathway are coupled
RT to spatially regulate spindle assembly.";
RL Dev. Cell 12:31-43(2007).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 88-371 IN COMPLEX WITH INCENP AND
RP HESPERADIN.
RX PubMed=15866179; DOI=10.1016/j.molcel.2005.03.031;
RA Sessa F., Mapelli M., Ciferri C., Tarricone C., Areces L.B.,
RA Schneider T.R., Stukenberg P.T., Musacchio A.;
RT "Mechanism of Aurora B activation by INCENP and inhibition by hesperadin.";
RL Mol. Cell 18:379-391(2005).
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 'Ser-10' of histone H3 during mitosis.
CC {ECO:0000269|PubMed:11350965, ECO:0000269|PubMed:12221116,
CC ECO:0000269|PubMed:17199039}.
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:11350965, ECO:0000269|PubMed:12221116};
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:11350965,
CC ECO:0000269|PubMed:12221116};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Kinase activity is stimulated by both
CC birc5/survivin-binding and cell-cycle specific phosphorylation.
CC {ECO:0000269|PubMed:11350965, ECO:0000269|PubMed:12221116}.
CC -!- SUBUNIT: Component of the CPC at least composed of survivin/birc5,
CC incenp, cdca8/borealin and/or cdca9/dasra-A, and aurkb/aurora-B.
CC Interacts directly (via N-terminus and kinase domain) with incenp (via
CC C terminus), and may weakly interact (via N-terminus) with birc5.1 to
CC stabilize the complex. Interacts with mtus1.
CC {ECO:0000269|PubMed:10996078, ECO:0000269|PubMed:12221116,
CC ECO:0000269|PubMed:12464631, ECO:0000269|PubMed:12919681,
CC ECO:0000269|PubMed:15260989, ECO:0000269|PubMed:15866179,
CC ECO:0000269|PubMed:16322459, ECO:0000269|PubMed:17199039}.
CC -!- INTERACTION:
CC Q6DE08; O13024: incenp-a; NbExp=2; IntAct=EBI-1042262, EBI-1042275;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Chromosomal until
CC metaphase but transfers to the midzone microtubule array and the
CC equatorial cortex during anaphase.
CC -!- PTM: Phosphorylated, stimulates kinase activity.
CC {ECO:0000269|PubMed:12221116}.
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=AAH41288.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF292096; AAG10787.1; -; mRNA.
DR EMBL; AY115554; AAM76715.1; -; mRNA.
DR EMBL; BC041288; AAH41288.1; ALT_INIT; mRNA.
DR EMBL; BC077339; AAH77339.1; -; mRNA.
DR RefSeq; NP_001082418.1; NM_001088949.1.
DR RefSeq; XP_018106316.1; XM_018250827.1.
DR PDB; 2BFX; X-ray; 1.80 A; A/B=78-361.
DR PDB; 2BFY; X-ray; 1.80 A; A/B=78-361.
DR PDB; 2VGO; X-ray; 1.70 A; A/B=78-361.
DR PDB; 2VGP; X-ray; 1.70 A; A/B=78-361.
DR PDB; 2VRX; X-ray; 1.86 A; A/B=77-361.
DR PDB; 3ZTX; X-ray; 1.95 A; A/B=78-361.
DR PDB; 4B8L; X-ray; 3.00 A; A=78-361.
DR PDB; 4B8M; X-ray; 1.85 A; A/B=78-361.
DR PDB; 4C2V; X-ray; 1.49 A; A/B=76-360.
DR PDB; 4C2W; X-ray; 1.70 A; A/B=78-356.
DR PDB; 5EYK; X-ray; 1.93 A; A/B=81-356.
DR PDB; 5K3Y; X-ray; 1.60 A; A/B=78-356.
DR PDBsum; 2BFX; -.
DR PDBsum; 2BFY; -.
DR PDBsum; 2VGO; -.
DR PDBsum; 2VGP; -.
DR PDBsum; 2VRX; -.
DR PDBsum; 3ZTX; -.
DR PDBsum; 4B8L; -.
DR PDBsum; 4B8M; -.
DR PDBsum; 4C2V; -.
DR PDBsum; 4C2W; -.
DR PDBsum; 5EYK; -.
DR PDBsum; 5K3Y; -.
DR AlphaFoldDB; Q6DE08; -.
DR SMR; Q6DE08; -.
DR BioGRID; 99789; 4.
DR IntAct; Q6DE08; 3.
DR BindingDB; Q6DE08; -.
DR ChEMBL; CHEMBL2176838; -.
DR DNASU; 398457; -.
DR GeneID; 398457; -.
DR KEGG; xla:398457; -.
DR CTD; 398457; -.
DR Xenbase; XB-GENE-1019634; aurkb.L.
DR OMA; PYGRQTT; -.
DR OrthoDB; 954262at2759; -.
DR EvolutionaryTrace; Q6DE08; -.
DR PRO; PR:Q6DE08; -.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 398457; Expressed in egg cell and 16 other tissues.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0005694; C:chromosome; IDA:UniProtKB.
DR GO; GO:0032133; C:chromosome passenger complex; IPI:UniProtKB.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB.
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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0035175; F:histone kinase activity (H3-S10 specific); IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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: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; 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:0051225; P:spindle assembly; IMP:UniProtKB.
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 3D-structure; ATP-binding; Cell cycle; Cell division; Chromosome;
KW Chromosome partition; Kinase; Magnesium; Metal-binding; Mitosis;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..361
FT /note="Aurora kinase B-A"
FT /id="PRO_0000281015"
FT DOMAIN 93..343
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 216
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 99..107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 122
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 2
FT /note="S -> E (in Ref. 1; AAG10787 and 2; AAM76715)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="K -> Q (in Ref. 1; AAG10787)"
FT /evidence="ECO:0000305"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:4C2V"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:4C2V"
FT STRAND 93..100
FT /evidence="ECO:0007829|PDB:4C2V"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:2VGP"
FT STRAND 106..112
FT /evidence="ECO:0007829|PDB:4C2V"
FT TURN 113..116
FT /evidence="ECO:0007829|PDB:4C2V"
FT STRAND 117..125
FT /evidence="ECO:0007829|PDB:4C2V"
FT HELIX 126..131
FT /evidence="ECO:0007829|PDB:4C2V"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:4B8L"
FT HELIX 135..146
FT /evidence="ECO:0007829|PDB:4C2V"
FT STRAND 156..161
FT /evidence="ECO:0007829|PDB:4C2V"
FT STRAND 163..170
FT /evidence="ECO:0007829|PDB:4C2V"
FT HELIX 178..185
FT /evidence="ECO:0007829|PDB:4C2V"
FT HELIX 190..208
FT /evidence="ECO:0007829|PDB:4C2V"
FT TURN 209..211
FT /evidence="ECO:0007829|PDB:4C2V"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:4C2V"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:4C2V"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:4C2V"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:2VGO"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:4C2V"
FT HELIX 258..261
FT /evidence="ECO:0007829|PDB:4C2V"
FT HELIX 270..284
FT /evidence="ECO:0007829|PDB:4C2V"
FT HELIX 294..302
FT /evidence="ECO:0007829|PDB:4C2V"
FT HELIX 314..323
FT /evidence="ECO:0007829|PDB:4C2V"
FT HELIX 328..330
FT /evidence="ECO:0007829|PDB:4C2V"
FT HELIX 334..338
FT /evidence="ECO:0007829|PDB:4C2V"
FT HELIX 341..346
FT /evidence="ECO:0007829|PDB:4C2V"
SQ SEQUENCE 361 AA; 41735 MW; 384803072040015B CRC64;
MSYKENLNPS SYTSKFTTPS SATAAQRVLR KEPYVSTFTT PSDNLLAQRT QLSRITPSAS
SSVPGRVAVS TEMPSQNTAL AEMPKRKFTI DDFDIGRPLG KGKFGNVYLA REKQNKFIMA
LKVLFKSQLE KEGVEHQLRR EIEIQSHLRH PNILRMYNYF HDRKRIYLML EFAPRGELYK
ELQKHGRFDE QRSATFMEEL ADALHYCHER KVIHRDIKPE NLLMGYKGEL KIADFGWSVH
APSLRRRTMC GTLDYLPPEM IEGKTHDEKV DLWCAGVLCY EFLVGMPPFD SPSHTETHRR
IVNVDLKFPP FLSDGSKDLI SKLLRYHPPQ RLPLKGVMEH PWVKANSRRV LPPVYQSTQS
K
