AURKB_DANRE
ID AURKB_DANRE Reviewed; 320 AA.
AC Q6NW76; Q8JGS8;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Aurora kinase B;
DE EC=2.7.11.1;
DE AltName: Full=Serine/threonine kinase A;
DE AltName: Full=Serine/threonine-protein kinase 12;
DE AltName: Full=Serine/threonine-protein kinase aurora-B;
GN Name=aurkb; Synonyms=stka;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND DISRUPTION PHENOTYPE.
RC TISSUE=Embryo;
RX PubMed=12006978; DOI=10.1038/ng896;
RA Golling G., Amsterdam A., Sun Z., Antonelli M., Maldonado E., Chen W.,
RA Burgess S., Haldi M., Artzt K., Farrington S., Lin S.-Y., Nissen R.M.,
RA Hopkins N.;
RT "Insertional mutagenesis in zebrafish rapidly identifies genes essential
RT for early vertebrate development.";
RL Nat. Genet. 31:135-140(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). 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 (By
CC similarity). Phosphorylates 'Ser-10' of histone H3 during mitosis (By
CC similarity). {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: Kinase activity is stimulated by cell-cycle
CC specific phosphorylation. {ECO:0000250|UniProtKB:Q96GD4}.
CC -!- SUBUNIT: Component of the chromosomal passenger complex (CPC).
CC {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}. 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. Localization (and probably
CC targeting of the CPC) to the inner centromere occurs predominantly in
CC regions with overlapping mitosis-specific histone phosphorylations
CC H3pT3 and H2ApT12. {ECO:0000250|UniProtKB:Q96GD4}.
CC -!- DISRUPTION PHENOTYPE: Embryos show severe brain necrosis.
CC {ECO:0000269|PubMed:12006978}.
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=AAM28206.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY099518; AAM28206.1; ALT_FRAME; mRNA.
DR EMBL; BC067695; AAH67695.1; -; mRNA.
DR AlphaFoldDB; Q6NW76; -.
DR SMR; Q6NW76; -.
DR STRING; 7955.ENSDARP00000054822; -.
DR PaxDb; Q6NW76; -.
DR ZFIN; ZDB-GENE-020419-40; aurkb.
DR eggNOG; KOG0580; Eukaryota.
DR InParanoid; Q6NW76; -.
DR PhylomeDB; Q6NW76; -.
DR Reactome; R-DRE-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-DRE-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-DRE-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
DR Reactome; R-DRE-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-DRE-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-DRE-8854518; AURKA Activation by TPX2.
DR Reactome; R-DRE-8854521; Interaction between PHLDA1 and AURKA.
DR PRO; PR:Q6NW76; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; 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:0007059; P:chromosome segregation; IMP:ZFIN.
DR GO; GO:0036089; P:cleavage furrow formation; IMP:ZFIN.
DR GO; GO:0043988; P:histone H3-S28 phosphorylation; IEA:InterPro.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:ZFIN.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:ZFIN.
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 ATP-binding; Centromere; Chromosome; Chromosome partition; Cytoplasm;
KW Cytoskeleton; Developmental protein; Kinase; Nucleotide-binding; Nucleus;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..320
FT /note="Aurora kinase B"
FT /id="PRO_0000259599"
FT DOMAIN 53..303
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 176
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 59..67
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 82
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 147
FT /note="R -> H (in Ref. 1; AAM28206)"
FT /evidence="ECO:0000305"
FT CONFLICT 252..253
FT /note="AS -> RQ (in Ref. 1; AAM28206)"
FT /evidence="ECO:0000305"
FT CONFLICT 301..302
FT /note="PW -> RG (in Ref. 1; AAM28206)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="E -> D (in Ref. 1; AAM28206)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 320 AA; 36947 MW; D1D9EC08556D1CF1 CRC64;
MQNKENREPR VQQTPSAGVG PLRVEMNPDT HAVSGPGRVP VKSNSKVLSI DDFDIGRPLG
KGKFGNVYLA RERKLKVVIA LKVLFKSQMV KEGVEHQLRR EIEIQSHLRH PNILRFYNYF
HDDTRVFLIL EYAPRGEMYK ELQRYGRFDD QRTATYMEEV SDALQYCHEK KVIHRDIKPE
NLLLGYRGEL KIADFGWSVH APSLRRRTMC GTLDYLPPEM IEGHSHDEKV DLWSIGVLCY
ECLVGNPPFE TASHAETYKR ITKVDLQFPK LVSEGARDLI SKLLRHSPSM RLPLRSVMEH
PWVKANSRRV LPPVCSSEPH
