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Aurora kinase B (EC 2.7.11.1) (Aurora 1) (Aurora- and IPL1-like midbody-associated protein 1) (AIM-1) (Aurora/IPL1-related kinase 2) (ARK-2) (Aurora-related kinase 2) (STK-1) (Serine/threonine-protein kinase 12) (Serine/threonine-protein kinase 5) (Serine/threonine-protein kinase aurora-B)

 AURKB_BOVIN             Reviewed;         344 AA.
Q7YRC6;
05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
01-OCT-2003, sequence version 1.
28-MAR-2018, entry version 116.
RecName: Full=Aurora kinase B;
EC=2.7.11.1;
AltName: Full=Aurora 1;
AltName: Full=Aurora- and IPL1-like midbody-associated protein 1;
Short=AIM-1;
AltName: Full=Aurora/IPL1-related kinase 2;
Short=ARK-2;
Short=Aurora-related kinase 2;
AltName: Full=STK-1;
AltName: Full=Serine/threonine-protein kinase 12;
AltName: Full=Serine/threonine-protein kinase 5;
AltName: Full=Serine/threonine-protein kinase aurora-B;
Name=AURKB; Synonyms=AIK2, AIM1, AIRK2, ARK2, STK1, STK12, STK5;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Zhou G., Li W., Yu L.;
"Cloning of Bos taurus serine/threonine kinase 12 (STK12).";
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
-!- 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 CHMP4C, leading to retain abscission-
competent VPS4 (VPS4A and/or VPS4B) at the midbody ring until
abscission checkpoint signaling is terminated at late cytokinesis.
AURKB phosphorylates the CPC complex subunits BIRC5/survivin,
CDCA8/borealin and INCENP. Phosphorylation of INCENP leads to
increased AURKB activity. Other known AURKB substrates involved in
centromeric functions and mitosis are CENPA, DES/desmin, GPAF,
KIF2C, NSUN2, RACGAP1, SEPT1, VIM/vimentin, HASPIN and histone H3.
A positive feedback loop involving HASPIN and AURKB contributes to
localization of CPC to centromeres. Phosphorylation of VIM
controls vimentin filament segregation in cytokinetic process,
whereas histone H3 is phosphorylated at 'Ser-10' and 'Ser-28'
during mitosis (H3S10ph and H3S28ph, respectively). AURKB is also
required for kinetochore localization of BUB1 and SGO1.
Phosphorylation of p53/TP53 negatively regulates its
transcriptional activity. Key regulator of active promoters in
resting B- and T-lymphocytes: acts by mediating phosphorylation of
H3S28ph at active promoters in resting B-cells, inhibiting
RNF2/RING1B-mediated ubiquitination of histone H2A and enhancing
binding and activity of the USP16 deubiquitinase at transcribed
genes (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- ENZYME REGULATION: Activity is greatly increased when AURKB is
within the CPC complex. In particular, AURKB-phosphorylated INCENP
acts as an activator of AURKB (By similarity). {ECO:0000250}.
-!- SUBUNIT: Component of the chromosomal passenger complex (CPC)
composed of at least BIRC5/survivin, CDCA8/borealin, INCENP, AURKB
or AURKC; predominantly independent AURKB- and AURKC-containing
complexes exist (By similarity). Associates with RACGAP1 during M
phase. Interacts with CDCA1, EVI5, JTB, NDC80, PSMA3, SEPT1, SIRT2
and TACC1 (By similarity). Interacts with SPDYC; this interaction
may be required for proper localization of active, Thr-232-
phosphorylated AURKB form during prometaphase and metaphase.
Interacts with p53/TP53. Interacts (via the middle kinase domain)
with NOC2L (via the N- and C-terminus domains) (By similarity).
Interacts with TTC28. Interacts with RNF2/RING1B (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome
{ECO:0000250}. Chromosome, centromere {ECO:0000250}. Cytoplasm,
cytoskeleton, spindle {ECO:0000250}. Midbody {ECO:0000250}.
Note=Localizes on chromosome arms and inner centromeres from
prophase through metaphase and then transferring to the spindle
midzone and midbody from anaphase through cytokinesis. Colocalized
with gamma tubulin in the mid-body (By similarity). Proper
localization of the active, Thr-232-phosphorylated form during
metaphase may be dependent upon interaction with SPDYC.
Colocalized with SIRT2 during cytokinesis with the midbody.
Localization (and probably targeting of the CPC) to the inner
centromere occurs predominantly in regions with overlapping
mitosis-specific histone phosphorylations H3pT3 and H2ApT12 (By
similarity). {ECO:0000250}.
-!- PTM: The phosphorylation of Thr-232 requires the binding to INCENP
and occurs by means of an autophosphorylation mechanism. Thr-232
phosphorylation is indispensable for the AURKB kinase activity (By
similarity). {ECO:0000250}.
-!- PTM: Ubiquitinated by different BCR (BTB-CUL3-RBX1) E3 ubiquitin
ligase complexes. Ubiquitinated by the BCR(KLHL9-KLHL13) E3
ubiquitin ligase complex, ubiquitination leads to removal from
mitotic chromosomes and is required for cytokinesis. During
anaphase, the BCR(KLHL21) E3 ubiquitin ligase complex recruits the
CPC complex from chromosomes to the spindle midzone and mediates
the ubiquitination of AURKB. Ubiquitination of AURKB by
BCR(KLHL21) E3 ubiquitin ligase complex may not lead to its
degradation by the proteasome (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. Aurora subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
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EMBL; AY336975; AAQ16151.1; -; mRNA.
UniGene; Bt.7331; -.
ProteinModelPortal; Q7YRC6; -.
SMR; Q7YRC6; -.
STRING; 9913.ENSBTAP00000002250; -.
PaxDb; Q7YRC6; -.
PRIDE; Q7YRC6; -.
eggNOG; KOG0580; Eukaryota.
eggNOG; ENOG410XNRB; LUCA.
HOGENOM; HOG000233016; -.
HOVERGEN; HBG108519; -.
InParanoid; Q7YRC6; -.
Proteomes; UP000009136; Unplaced.
GO; GO:0005694; C:chromosome; IDA:AgBase.
GO; GO:0032133; C:chromosome passenger complex; IBA:GO_Central.
GO; GO:0000775; C:chromosome, centromeric region; IDA:AgBase.
GO; GO:0000780; C:condensed nuclear chromosome, centromeric region; IBA:GO_Central.
GO; GO:0070938; C:contractile ring; IDA:AgBase.
GO; GO:0005737; C:cytoplasm; IDA:AgBase.
GO; GO:0042585; C:germinal vesicle; IDA:AgBase.
GO; GO:1990385; C:meiotic spindle midzone; IDA:AgBase.
GO; GO:0030496; C:midbody; IDA:AgBase.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005876; C:spindle microtubule; IBA:GO_Central.
GO; GO:0031616; C:spindle pole centrosome; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IDA:UniProtKB.
GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IBA:GO_Central.
GO; GO:0009838; P:abscission; IMP:UniProtKB.
GO; GO:0034644; P:cellular response to UV; ISS:UniProtKB.
GO; GO:0036089; P:cleavage furrow formation; ISS:UniProtKB.
GO; GO:0043988; P:histone H3-S28 phosphorylation; ISS:UniProtKB.
GO; GO:0044878; P:mitotic cytokinesis checkpoint; IMP:UniProtKB.
GO; GO:0051256; P:mitotic spindle midzone assembly; ISS:UniProtKB.
GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
GO; GO:0002903; P:negative regulation of B cell apoptotic process; ISS:UniProtKB.
GO; GO:0032466; P:negative regulation of cytokinesis; IMP: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; IDA:UniProtKB.
GO; GO:0031577; P:spindle checkpoint; IEA:InterPro.
InterPro; IPR030616; Aur.
InterPro; IPR028772; AURKB.
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.
PANTHER; PTHR24350:SF4; PTHR24350:SF4; 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.
2: Evidence at transcript level;
ATP-binding; Cell cycle; Cell division; Centromere; Chromosome;
Complete proteome; Cytoplasm; Cytoskeleton; Kinase; Magnesium;
Metal-binding; Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein;
Reference proteome; Serine/threonine-protein kinase; Transferase;
Ubl conjugation.
CHAIN 1 344 Aurora kinase B.
/FTId=PRO_0000248282.
DOMAIN 77 327 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 83 91 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 200 200 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 106 106 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 35 35 Phosphothreonine.
{ECO:0000250|UniProtKB:Q96GD4}.
MOD_RES 62 62 Phosphoserine.
{ECO:0000250|UniProtKB:Q96GD4}.
MOD_RES 64 64 Phosphothreonine.
{ECO:0000250|UniProtKB:Q96GD4}.
MOD_RES 227 227 Phosphoserine.
{ECO:0000250|UniProtKB:Q96GD4}.
MOD_RES 232 232 Phosphothreonine; by autocatalysis.
{ECO:0000250|UniProtKB:Q96GD4}.
SEQUENCE 344 AA; 39442 MW; 4DD7158CF2F5D047 CRC64;
MAQKENAYPW PYGRQTAQPG LNTLPQRVLR KEPVTPSALV LMSRSNAQPT AAPGQKVVEN
SSGTPNIPKR SFTIDDFEIG RPLGKGKFGN VYLAREKKSH FIVALKVLFK SQIEKEGVEH
QLRREIEIQA HLQHPNILRL YNYFYDRRRI YLILEYAPRG ELYKELQKSR TFDEQRTATI
MEELADALTY CHAKKVIHRD IKPENLLLGL RGELKIADFG WSVHAPSLRR KTMCGTLDYL
PPEMIEGRTH NEKVDLWCIG VLCYELLVGN PPFESASHNE TYRRIVKVDL KFPPSVPLGA
QDFIYKLLKH NPSERLPLAQ VSAHPWVRTH SRRVLPPSAP QSVP


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