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Aurora kinase B-A (EC 2.7.11.1) (Aurora/IPL1-related kinase 2-A) (AIRK2-A) (XAIRK2-A) (Serine/threonine-protein kinase 12-A) (Serine/threonine-protein kinase aurora-B-A) (xAurora-B)

 AUKBA_XENLA             Reviewed;         361 AA.
Q6DE08; Q7ZYT9; Q8JG74; Q9DF70;
20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
16-AUG-2004, sequence version 1.
28-MAR-2018, entry version 105.
RecName: Full=Aurora kinase B-A;
EC=2.7.11.1;
AltName: Full=Aurora/IPL1-related kinase 2-A;
Short=AIRK2-A;
Short=XAIRK2-A;
AltName: Full=Serine/threonine-protein kinase 12-A;
AltName: Full=Serine/threonine-protein kinase aurora-B-A;
Short=xAurora-B;
Name=aurkb-a; Synonyms=airk2-a;
Xenopus laevis (African clawed frog).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
Xenopus.
NCBI_TaxID=8355;
[1]
NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH INCENP, AND SUBCELLULAR
LOCATION.
PubMed=10996078; DOI=10.1016/S0960-9822(00)00673-4;
Adams R.R., Wheatleya S.P., Gouldsworthy A.M., Kandels-Lewis S.E.,
Carmena M., Smythe C., Gerloff D.L., Earnshaw W.C.;
"INCENP binds the Aurora-related kinase AIRK2 and is required to
target it to chromosomes, the central spindle and cleavage furrow.";
Curr. Biol. 10:1075-1078(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ENZYME
REGULATION, INTERACTION WITH INCENP, PUTATIVE INTERACTION WITH
BIRC5.1, IDENTIFICATION IN A COMPLEX WITH BIRC5.1 AND INCENP, AND
PHOSPHORYLATION.
PubMed=12221116; DOI=10.1091/mbc.E02-02-0092;
Bolton M.A., Lan W., Powers S.E., McCleland M.L., Kuang J.,
Stukenberg P.T.;
"Aurora B kinase exists in a complex with survivin and INCENP and its
kinase activity is stimulated by survivin binding and
phosphorylation.";
Mol. Biol. Cell 13:3064-3077(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Ovary;
NIH - Xenopus Gene Collection (XGC) project;
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
[4]
FUNCTION, CATALYTIC ACTIVITY, AND ENZYME REGULATION.
PubMed=11350965; DOI=10.1074/jbc.M102288200;
Murnion M.E., Adams R.R., Callister D.M., Allis C.D., Earnshaw W.C.,
Swedlow J.R.;
"Chromatin-associated protein phosphatase 1 regulates aurora-B and
histone H3 phosphorylation.";
J. Biol. Chem. 276:26656-26665(2001).
[5]
IDENTIFICATION IN A COMPLEX WITH BIRC5.1 AND INCENP, AND SUBCELLULAR
LOCATION.
PubMed=12464631; DOI=10.1101/gad.249202;
Losada A., Hirano M., Hirano T.;
"Cohesin release is required for sister chromatid resolution, but not
for condensin-mediated compaction, at the onset of mitosis.";
Genes Dev. 16:3004-3016(2002).
[6]
INTERACTION WITH MTUS1, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=12919681; DOI=10.1016/S1534-5807(03)00229-6;
Ohi R., Coughlin M.L., Lane W.S., Mitchison T.J.;
"An inner centromere protein that stimulates the microtubule
depolymerizing activity of a KinI kinesin.";
Dev. Cell 5:309-321(2003).
[7]
IDENTIFICATION IN A COMPLEX WITH BIRC5.1; INCENP AND CDCA9.
PubMed=15260989; DOI=10.1016/j.cell.2004.06.026;
Sampath S.C., Ohi R., Leismann O., Salic A., Pozniakovski A.,
Funabiki H.;
"The chromosomal passenger complex is required for chromatin-induced
microtubule stabilization and spindle assembly.";
Cell 118:187-202(2004).
[8]
IDENTIFICATION IN A COMPLEX WITH BIRC5.1 AND INCENP.
PubMed=16322459; DOI=10.1126/science.1120160;
Vong Q.P., Cao K., Li H.Y., Iglesias P.A., Zheng Y.;
"Chromosome alignment and segregation regulated by ubiquitination of
survivin.";
Science 310:1499-1504(2005).
[9]
FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH CDCA8; CDCA9; BIRC5.1;
BIRC5.2 AND INCENP.
PubMed=17199039; DOI=10.1016/j.devcel.2006.11.001;
Kelly A.E., Sampath S.C., Maniar T.A., Woo E.M., Chait B.T.,
Funabiki H.;
"Chromosomal enrichment and activation of the aurora B pathway are
coupled to spatially regulate spindle assembly.";
Dev. Cell 12:31-43(2007).
[10]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 88-371 IN COMPLEX WITH INCENP
AND HESPERADIN.
PubMed=15866179; DOI=10.1016/j.molcel.2005.03.031;
Sessa F., Mapelli M., Ciferri C., Tarricone C., Areces L.B.,
Schneider T.R., Stukenberg P.T., Musacchio A.;
"Mechanism of Aurora B activation by INCENP and inhibition by
hesperadin.";
Mol. Cell 18:379-391(2005).
-!- FUNCTION: Serine/threonine-protein kinase component of the
chromosomal passenger complex (CPC), a complex that acts as a key
regulator of mitosis. The CPC complex has essential functions at
the centromere in ensuring correct chromosome alignment and
segregation and is required for chromatin-induced microtubule
stabilization and spindle assembly. Involved in the bipolar
attachment of spindle microtubules to kinetochores and is a key
regulator for the onset of cytokinesis during mitosis. Required
for central/midzone spindle assembly and cleavage furrow
formation. Key component of the cytokinesis checkpoint, a process
required to delay abscission to prevent both premature resolution
of intercellular chromosome bridges and accumulation of DNA
damage. Phosphorylates 'Ser-10' of histone H3 during mitosis.
{ECO:0000269|PubMed:11350965, ECO:0000269|PubMed:12221116,
ECO:0000269|PubMed:17199039}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:11350965, ECO:0000269|PubMed:12221116}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
-!- ENZYME REGULATION: Kinase activity is stimulated by both
birc5/survivin-binding and cell-cycle specific phosphorylation.
{ECO:0000269|PubMed:11350965, ECO:0000269|PubMed:12221116}.
-!- SUBUNIT: Component of the CPC at least composed of survivin/birc5,
incenp, cdca8/borealin and/or cdca9/dasra-A, and aurkb/aurora-B.
Interacts directly (via N-terminus and kinase domain) with incenp
(via C terminus), and may weakly interact (via N-terminus) with
birc5.1 to stabilize the complex. Interacts with mtus1.
{ECO:0000269|PubMed:10996078, ECO:0000269|PubMed:12221116,
ECO:0000269|PubMed:12464631, ECO:0000269|PubMed:12919681,
ECO:0000269|PubMed:15260989, ECO:0000269|PubMed:15866179,
ECO:0000269|PubMed:16322459, ECO:0000269|PubMed:17199039}.
-!- INTERACTION:
O13024:incenp-a; NbExp=2; IntAct=EBI-1042262, EBI-1042275;
-!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Chromosomal until
metaphase but transfers to the midzone microtubule array and the
equatorial cortex during anaphase.
-!- PTM: Phosphorylated, stimulates kinase activity.
{ECO:0000269|PubMed:12221116}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. Aurora subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-!- SEQUENCE CAUTION:
Sequence=AAH41288.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF292096; AAG10787.1; -; mRNA.
EMBL; AY115554; AAM76715.1; -; mRNA.
EMBL; BC041288; AAH41288.1; ALT_INIT; mRNA.
EMBL; BC077339; AAH77339.1; -; mRNA.
RefSeq; NP_001082418.1; NM_001088949.1.
RefSeq; XP_018106316.1; XM_018250827.1.
UniGene; Xl.6652; -.
PDB; 2BFX; X-ray; 1.80 A; A/B=78-361.
PDB; 2BFY; X-ray; 1.80 A; A/B=78-361.
PDB; 2VGO; X-ray; 1.70 A; A/B=78-361.
PDB; 2VGP; X-ray; 1.70 A; A/B=78-361.
PDB; 2VRX; X-ray; 1.86 A; A/B=77-361.
PDB; 3ZTX; X-ray; 1.95 A; A/B=78-361.
PDB; 4B8L; X-ray; 3.00 A; A=78-361.
PDB; 4B8M; X-ray; 1.85 A; A/B=78-361.
PDB; 4C2V; X-ray; 1.49 A; A/B=76-360.
PDB; 4C2W; X-ray; 1.70 A; A/B=78-356.
PDB; 5EYK; X-ray; 1.93 A; A/B=81-356.
PDB; 5K3Y; X-ray; 1.60 A; A/B=78-356.
PDBsum; 2BFX; -.
PDBsum; 2BFY; -.
PDBsum; 2VGO; -.
PDBsum; 2VGP; -.
PDBsum; 2VRX; -.
PDBsum; 3ZTX; -.
PDBsum; 4B8L; -.
PDBsum; 4B8M; -.
PDBsum; 4C2V; -.
PDBsum; 4C2W; -.
PDBsum; 5EYK; -.
PDBsum; 5K3Y; -.
ProteinModelPortal; Q6DE08; -.
SMR; Q6DE08; -.
BioGrid; 99789; 3.
IntAct; Q6DE08; 3.
BindingDB; Q6DE08; -.
ChEMBL; CHEMBL2176838; -.
GeneID; 398457; -.
KEGG; xla:398457; -.
CTD; 398457; -.
Xenbase; XB-GENE-1019634; aurkb.
HOVERGEN; HBG108519; -.
KO; K11479; -.
EvolutionaryTrace; Q6DE08; -.
PRO; PR:Q6DE08; -.
GO; GO:0000785; C:chromatin; IDA:UniProtKB.
GO; GO:0005694; C:chromosome; IDA:UniProtKB.
GO; GO:0032133; C:chromosome passenger complex; IPI:UniProtKB.
GO; GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB.
GO; GO:0030496; C:midbody; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0035175; F:histone kinase activity (H3-S10 specific); IDA:UniProtKB.
GO; GO:0035174; F:histone serine kinase activity; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
GO; GO:0009838; P:abscission; ISS:UniProtKB.
GO; GO:0034644; P:cellular response to UV; ISS:UniProtKB.
GO; GO:0036089; P:cleavage furrow formation; ISS:UniProtKB.
GO; GO:0043987; P:histone H3-S10 phosphorylation; IDA:UniProtKB.
GO; GO:0043988; P:histone H3-S28 phosphorylation; ISS:UniProtKB.
GO; GO:0044878; P:mitotic cytokinesis checkpoint; ISS:UniProtKB.
GO; GO:0051256; P:mitotic spindle midzone assembly; ISS:UniProtKB.
GO; GO:0002903; P:negative regulation of B cell apoptotic process; ISS:UniProtKB.
GO; GO:0032466; P:negative regulation of cytokinesis; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0032467; P:positive regulation of cytokinesis; ISS:UniProtKB.
GO; GO:0034501; P:protein localization to kinetochore; ISS:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
GO; GO:0051225; P:spindle assembly; IMP:UniProtKB.
InterPro; IPR030616; Aur.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
PANTHER; PTHR24350; PTHR24350; 1.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Cell cycle; Cell division; Chromosome;
Chromosome partition; Kinase; Magnesium; Metal-binding; Mitosis;
Nucleotide-binding; Nucleus; Phosphoprotein;
Serine/threonine-protein kinase; Transferase.
CHAIN 1 361 Aurora kinase B-A.
/FTId=PRO_0000281015.
DOMAIN 93 343 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 99 107 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 216 216 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 122 122 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
CONFLICT 2 2 S -> E (in Ref. 1; AAG10787 and 2;
AAM76715). {ECO:0000305}.
CONFLICT 87 87 K -> Q (in Ref. 1; AAG10787).
{ECO:0000305}.
TURN 78 80 {ECO:0000244|PDB:4C2V}.
HELIX 90 92 {ECO:0000244|PDB:4C2V}.
STRAND 93 100 {ECO:0000244|PDB:4C2V}.
TURN 103 105 {ECO:0000244|PDB:2VGP}.
STRAND 106 112 {ECO:0000244|PDB:4C2V}.
TURN 113 116 {ECO:0000244|PDB:4C2V}.
STRAND 117 125 {ECO:0000244|PDB:4C2V}.
HELIX 126 131 {ECO:0000244|PDB:4C2V}.
TURN 132 134 {ECO:0000244|PDB:4B8L}.
HELIX 135 146 {ECO:0000244|PDB:4C2V}.
STRAND 156 161 {ECO:0000244|PDB:4C2V}.
STRAND 163 170 {ECO:0000244|PDB:4C2V}.
HELIX 178 185 {ECO:0000244|PDB:4C2V}.
HELIX 190 208 {ECO:0000244|PDB:4C2V}.
TURN 209 211 {ECO:0000244|PDB:4C2V}.
HELIX 219 221 {ECO:0000244|PDB:4C2V}.
STRAND 222 224 {ECO:0000244|PDB:4C2V}.
STRAND 230 232 {ECO:0000244|PDB:4C2V}.
STRAND 242 244 {ECO:0000244|PDB:2VGO}.
HELIX 253 255 {ECO:0000244|PDB:4C2V}.
HELIX 258 261 {ECO:0000244|PDB:4C2V}.
HELIX 270 284 {ECO:0000244|PDB:4C2V}.
HELIX 294 302 {ECO:0000244|PDB:4C2V}.
HELIX 314 323 {ECO:0000244|PDB:4C2V}.
HELIX 328 330 {ECO:0000244|PDB:4C2V}.
HELIX 334 338 {ECO:0000244|PDB:4C2V}.
HELIX 341 346 {ECO:0000244|PDB:4C2V}.
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


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