AURKB_DROME
ID AURKB_DROME Reviewed; 329 AA.
AC Q9VKN7; Q9XTQ0;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Aurora kinase B {ECO:0000305};
DE EC=2.7.11.1;
DE AltName: Full=IPL1/Aurora-like protein kinase {ECO:0000303|PubMed:11266459};
DE AltName: Full=Serine/threonine-protein kinase Ial {ECO:0000303|PubMed:10433558};
DE AltName: Full=Serine/threonine-protein kinase aurora-B {ECO:0000303|PubMed:11266459};
GN Name=aurB {ECO:0000312|FlyBase:FBgn0024227};
GN Synonyms=ial {ECO:0000303|PubMed:10433558};
GN ORFNames=CG6620 {ECO:0000312|FlyBase:FBgn0024227};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC STRAIN=Canton-S;
RX PubMed=10433558; DOI=10.1089/104454999315141;
RA Reich A., Yanai A., Mesilaty-Gross S., Chen-Moses A., Wides R., Motro B.;
RT "Cloning, mapping, and expression of ial, a novel Drosophila member of the
RT Ipl1/aurora mitotic control kinase family.";
RL DNA Cell Biol. 18:593-603(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DEVELOPMENTAL STAGE.
RC STRAIN=Canton-S;
RX PubMed=10231582; DOI=10.1016/s0378-1119(99)00053-0;
RA Mesilaty-Gross S., Reich A., Motro B., Wides R.;
RT "The Drosophila STAM gene homolog is in a tight gene cluster, and its
RT expression correlates to that of the adjacent gene ial.";
RL Gene 231:173-186(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11266459; DOI=10.1083/jcb.152.4.669;
RA Giet R., Glover D.M.;
RT "Drosophila aurora B kinase is required for histone H3 phosphorylation and
RT condensin recruitment during chromosome condensation and to organize the
RT central spindle during cytokinesis.";
RL J. Cell Biol. 152:669-682(2001).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH INCENP.
RX PubMed=11352945; DOI=10.1083/jcb.153.4.865;
RA Adams R.R., Maiato H., Earnshaw W.C., Carmena M.;
RT "Essential roles of Drosophila inner centromere protein (INCENP) and aurora
RT B in histone H3 phosphorylation, metaphase chromosome alignment,
RT kinetochore disjunction, and chromosome segregation.";
RL J. Cell Biol. 153:865-880(2001).
RN [8]
RP INTERACTION WITH CDC37.
RX PubMed=12374737; DOI=10.1093/emboj/cdf531;
RA Lange B.M.H., Rebollo E., Herold A., Gonzalez C.;
RT "Cdc37 is essential for chromosome segregation and cytokinesis in higher
RT eukaryotes.";
RL EMBO J. 21:5364-5374(2002).
RN [9]
RP FUNCTION.
RX PubMed=16824953; DOI=10.1016/j.devcel.2006.04.021;
RA Resnick T.D., Satinover D.L., MacIsaac F., Stukenberg P.T., Earnshaw W.C.,
RA Orr-Weaver T.L., Carmena M.;
RT "INCENP and Aurora B promote meiotic sister chromatid cohesion through
RT localization of the Shugoshin MEI-S332 in Drosophila.";
RL Dev. Cell 11:57-68(2006).
CC -!- FUNCTION: Serine/threonine-protein kinase which mediates both meiotic
CC and mitotic chromosome segregation. Required for histone H3 'Ser-10'
CC phosphorylation. Phosphorylates mei-S332 within residues 124-126 and
CC stabilizes its association with centromeres during meiosis.
CC {ECO:0000269|PubMed:11266459, ECO:0000269|PubMed:11352945,
CC ECO:0000269|PubMed:16824953}.
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 -!- 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;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBUNIT: Interacts with Incenp and Cdc37. {ECO:0000269|PubMed:11352945,
CC ECO:0000269|PubMed:12374737}.
CC -!- SUBCELLULAR LOCATION: Chromosome. Cytoplasm, cytoskeleton. Midbody.
CC Note=Meiotic and mitotic chromosomes. During each division, relocates
CC to the midbody microtubules.
CC -!- DEVELOPMENTAL STAGE: Ubiquitously expressed at very high levels in
CC embryo. Expressed at low levels during larval stages, and at higher
CC levels in female adults (at protein level).
CC {ECO:0000269|PubMed:10231582, ECO:0000269|PubMed:10433558}.
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=AAD34349.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAD37504.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF121358; AAD34349.1; ALT_FRAME; mRNA.
DR EMBL; AF121361; AAD37504.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AE014134; AAF53026.1; -; Genomic_DNA.
DR EMBL; AY118562; AAM49931.1; -; mRNA.
DR RefSeq; NP_477336.1; NM_057988.4.
DR AlphaFoldDB; Q9VKN7; -.
DR SMR; Q9VKN7; -.
DR BioGRID; 60576; 9.
DR IntAct; Q9VKN7; 1.
DR STRING; 7227.FBpp0079769; -.
DR ChEMBL; CHEMBL3308999; -.
DR PaxDb; Q9VKN7; -.
DR PRIDE; Q9VKN7; -.
DR DNASU; 34504; -.
DR EnsemblMetazoa; FBtr0080180; FBpp0079769; FBgn0024227.
DR GeneID; 34504; -.
DR KEGG; dme:Dmel_CG6620; -.
DR CTD; 34504; -.
DR FlyBase; FBgn0024227; aurB.
DR VEuPathDB; VectorBase:FBgn0024227; -.
DR eggNOG; KOG0580; Eukaryota.
DR HOGENOM; CLU_000288_63_0_1; -.
DR InParanoid; Q9VKN7; -.
DR OMA; YVDHWCL; -.
DR OrthoDB; 954262at2759; -.
DR PhylomeDB; Q9VKN7; -.
DR Reactome; R-DME-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-DME-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-DME-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
DR Reactome; R-DME-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-DME-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR SignaLink; Q9VKN7; -.
DR BioGRID-ORCS; 34504; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 34504; -.
DR PRO; PR:Q9VKN7; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0024227; Expressed in secondary oocyte and 30 other tissues.
DR Genevisible; Q9VKN7; DM.
DR GO; GO:0032133; C:chromosome passenger complex; IDA:FlyBase.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:FlyBase.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000776; C:kinetochore; IDA:FlyBase.
DR GO; GO:1990385; C:meiotic spindle midzone; IDA:FlyBase.
DR GO; GO:0030496; C:midbody; IDA:FlyBase.
DR GO; GO:0005819; C:spindle; IDA:FlyBase.
DR GO; GO:0005876; C:spindle microtubule; IBA:GO_Central.
DR GO; GO:0051233; C:spindle midzone; IDA:FlyBase.
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: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:FlyBase.
DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IDA:FlyBase.
DR GO; GO:0006325; P:chromatin organization; IMP:FlyBase.
DR GO; GO:0030261; P:chromosome condensation; IMP:FlyBase.
DR GO; GO:0048132; P:female germ-line stem cell asymmetric division; IGI:FlyBase.
DR GO; GO:0043988; P:histone H3-S28 phosphorylation; IEA:InterPro.
DR GO; GO:0016572; P:histone phosphorylation; IMP:FlyBase.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0061952; P:midbody abscission; IMP:FlyBase.
DR GO; GO:0007076; P:mitotic chromosome condensation; IMP:FlyBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:FlyBase.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:FlyBase.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IEA:InterPro.
DR GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
DR GO; GO:0032467; P:positive regulation of cytokinesis; IEA:InterPro.
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:SF24; PTHR24350:SF24; 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 ATP-binding; Cell cycle; Cell division; Chromatin regulator; Chromosome;
KW Chromosome partition; Cytoplasm; Cytoskeleton; Kinase; Magnesium; Meiosis;
KW Metal-binding; Mitosis; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..329
FT /note="Aurora kinase B"
FT /id="PRO_0000280545"
FT DOMAIN 53..305
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 178
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 320
FT /note="E -> D (in Ref. 1; AAD34349 and 2; AAD37504)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 329 AA; 38301 MW; B489A0A33A4F2128 CRC64;
MTLSRAKHAN RNHLPHLLAK VPEEHQEPIK NMCLKMMSHD AYGQPYDWSP RDFEMGAHLG
RGKFGRVYLA RERHSHYLVA MKVMFKEELR KGCVQRQVLR EIEIQSRLKH PHILRLLTWF
HDESRIYLAL EIASEGELFK HLRGAPNHRF DEPRSAKYTY QVANALNYCH LNNVIHRDLK
PENILLTSTD DLKLADFGWS AHTPNNKRRT LCGTLDYLPP EMVDGNSYDD SVDQWCLGIL
CYEFVVGCPP FESNSTESTY SKIRRMEISY PSHLSKGCKE LIGGLLRKES KGRITLVDVM
THYWVKAGMA ERELQLQKRE RGKENTARN
