AURKC_HUMAN
ID AURKC_HUMAN Reviewed; 309 AA.
AC Q9UQB9; O60681; O75442; Q6AZY8; Q6DLZ0; Q9UPK5;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Aurora kinase C;
DE EC=2.7.11.1;
DE AltName: Full=Aurora 3;
DE AltName: Full=Aurora/IPL1-related kinase 3;
DE Short=ARK-3;
DE Short=Aurora-related kinase 3;
DE AltName: Full=Aurora/IPL1/Eg2 protein 2;
DE AltName: Full=Serine/threonine-protein kinase 13;
DE AltName: Full=Serine/threonine-protein kinase aurora-C;
GN Name=AURKC; Synonyms=AIE2, AIK3, AIRK3, ARK3, STK13;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBCELLULAR LOCATION.
RC TISSUE=Testis;
RX PubMed=9809744; DOI=10.1089/dna.1998.17.823;
RA Tseng T.-C., Chen S.-H., Hsu Y.-P.P., Tang T.K.;
RT "Protein kinase profile of sperm and eggs: cloning and characterization of
RT two novel testis-specific protein kinases (AIE1, AIE2) related to yeast and
RT fly chromosome segregation regulators.";
RL DNA Cell Biol. 17:823-833(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Placenta;
RX PubMed=9799611; DOI=10.1006/geno.1998.5522;
RA Bernard M., Sanseau P., Henry C., Couturier A., Prigent C.;
RT "Cloning of STK13, a third human protein kinase related to Drosophila
RT aurora and budding yeast Ipl1 that maps on chromosome 19q13.3-ter.";
RL Genomics 53:406-409(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Testis;
RX PubMed=10066797; DOI=10.1074/jbc.274.11.7334;
RA Kimura M., Matsuda Y., Yoshioka T., Okano Y.;
RT "Cell cycle-dependent expression and centrosome localization of a third
RT human Aurora/Ipl1-related protein kinase, AIK3.";
RL J. Biol. Chem. 274:7334-7340(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY, FUNCTION,
RP MUTAGENESIS OF THR-198, AND SUBCELLULAR LOCATION.
RX PubMed=15670791; DOI=10.1016/j.bbrc.2004.12.168;
RA Yan X., Wu Y., Li Q., Cao L., Liu X., Saiyin H., Yu L.;
RT "Cloning and characterization of a novel human Aurora C splicing variant.";
RL Biochem. Biophys. Res. Commun. 328:353-361(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP INDUCTION, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH INCENP, AND
RP MUTAGENESIS OF LYS-72.
RX PubMed=15499654; DOI=10.1002/cm.20039;
RA Sasai K., Katayama H., Stenoien D.L., Fujii S., Honda R., Kimura M.,
RA Okano Y., Tatsuka M., Suzuki F., Nigg E.A., Earnshaw W.C., Brinkley W.R.,
RA Sen S.;
RT "Aurora-C kinase is a novel chromosomal passenger protein that can
RT complement Aurora-B kinase function in mitotic cells.";
RL Cell Motil. Cytoskeleton 59:249-263(2004).
RN [9]
RP IDENTIFICATION IN THE CDC COMPLEX, SUBCELLULAR LOCATION, ACTIVITY
RP REGULATION, FUNCTION, AND MUTAGENESIS OF LYS-72 AND THR-198.
RX PubMed=15316025; DOI=10.1074/jbc.m403029200;
RA Li X., Sakashita G., Matsuzaki H., Sugimoto K., Kimura K., Hanaoka F.,
RA Taniguchi H., Furukawa K., Urano T.;
RT "Direct association with inner centromere protein (INCENP) activates the
RT novel chromosomal passenger protein, Aurora-C.";
RL J. Biol. Chem. 279:47201-47211(2004).
RN [10]
RP IDENTIFICATION IN THE CDC COMPLEX, INTERACTION WITH BIRC5, SUBCELLULAR
RP LOCATION, FUNCTION, AND MUTAGENESIS OF ASP-166.
RX PubMed=15938719; DOI=10.1111/j.1365-2443.2005.00863.x;
RA Yan X., Cao L., Li Q., Wu Y., Zhang H., Saiyin H., Liu X., Zhang X.,
RA Shi Q., Yu L.;
RT "Aurora C is directly associated with Survivin and required for
RT cytokinesis.";
RL Genes Cells 10:617-626(2005).
RN [11]
RP INVOLVEMENT IN SPGF5.
RX PubMed=17435757; DOI=10.1038/ng2027;
RA Dieterich K., Soto Rifo R., Faure A.K., Hennebicq S., Ben Amar B., Zahi M.,
RA Perrin J., Martinez D., Sele B., Jouk P.-S., Ohlmann T., Rousseaux S.,
RA Lunardi J., Ray P.F.;
RT "Homozygous mutation of AURKC yields large-headed polyploid spermatozoa and
RT causes male infertility.";
RL Nat. Genet. 39:661-665(2007).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TACC1.
RX PubMed=21531210; DOI=10.1016/j.bbrc.2011.04.078;
RA Gabillard J.C., Ulisse S., Baldini E., Sorrenti S., Cremet J.Y.,
RA Coccaro C., Prigent C., D'Armiento M., Arlot-Bonnemains Y.;
RT "Aurora-C interacts with and phosphorylates the transforming acidic coiled-
RT coil 1 protein.";
RL Biochem. Biophys. Res. Commun. 408:647-653(2011).
RN [13]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21493633; DOI=10.1093/humrep/der111;
RA Avo Santos M., van de Werken C., de Vries M., Jahr H., Vromans M.J.,
RA Laven J.S., Fauser B.C., Kops G.J., Lens S.M., Baart E.B.;
RT "A role for Aurora C in the chromosomal passenger complex during human
RT preimplantation embryo development.";
RL Hum. Reprod. 26:1868-1881(2011).
RN [14]
RP INVOLVEMENT IN SPGF5.
RX PubMed=21733974; DOI=10.1093/molehr/gar050;
RA Ben Khelifa M., Zouari R., Harbuz R., Halouani L., Arnoult C., Lunardi J.,
RA Ray P.F.;
RT "A new AURKC mutation causing macrozoospermia: implications for human
RT spermatogenesis and clinical diagnosis.";
RL Mol. Hum. Reprod. 17:762-768(2011).
RN [15]
RP INTERACTION WITH BIRC5, SUBUNIT, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=27332895; DOI=10.1371/journal.pone.0157305;
RA Sasai K., Katayama H., Hawke D.H., Sen S.;
RT "Aurora-C interactions with survivin and INCENP reveal shared and distinct
RT features compared with Aurora-B chromosome passenger protein complex.";
RL PLoS ONE 11:E0157305-E0157305(2016).
RN [16]
RP VARIANTS [LARGE SCALE ANALYSIS] GLU-52; GLN-148 AND GLN-244.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
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 Also plays a role in meiosis and more particularly in spermatogenesis.
CC Has redundant cellular functions with AURKB and can rescue an AURKB
CC knockdown. Like AURKB, AURKC phosphorylates histone H3 at 'Ser-10' and
CC 'Ser-28'. AURKC phosphorylates the CPC complex subunits BIRC5/survivin
CC and INCENP leading to increased AURKC activity. Phosphorylates TACC1,
CC another protein involved in cell division, at 'Ser-228'.
CC {ECO:0000269|PubMed:15316025, ECO:0000269|PubMed:15499654,
CC ECO:0000269|PubMed:15670791, ECO:0000269|PubMed:15938719,
CC ECO:0000269|PubMed:21493633, ECO:0000269|PubMed:21531210,
CC ECO:0000269|PubMed:27332895}.
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 -!- ACTIVITY REGULATION: Okadaic acid, an inhibitor of protein phosphatase
CC 1 (PP1), protein phosphatase 2A (PP2A) and protein phosphatase 5 (PP5),
CC increases AURKC activity. AURKC is also stabilized through its
CC interaction with INCENP, which acts also as an activator.
CC {ECO:0000269|PubMed:15316025}.
CC -!- SUBUNIT: Component of the chromosomal passenger complex (CPC) composed
CC of at least BIRC5/survivin, CDCA8/borealin, INCENP, AURKB or AURKC;
CC predominantly independent AURKB- and AURKC-containing complexes exist;
CC in the complex interacts directly with BIRC5/survivin and INCENP.
CC Interacts with TACC1. {ECO:0000269|PubMed:15316025,
CC ECO:0000269|PubMed:15499654, ECO:0000269|PubMed:15938719,
CC ECO:0000269|PubMed:21531210, ECO:0000269|PubMed:27332895}.
CC -!- INTERACTION:
CC Q9UQB9; O15392: BIRC5; NbExp=10; IntAct=EBI-3926851, EBI-518823;
CC Q9UQB9; Q96CA5: BIRC7; NbExp=3; IntAct=EBI-3926851, EBI-517623;
CC Q9UQB9; A2RRN7: CADPS; NbExp=3; IntAct=EBI-3926851, EBI-10179719;
CC Q9UQB9; Q9NQS7: INCENP; NbExp=17; IntAct=EBI-3926851, EBI-307907;
CC Q9UQB9; P32243-2: OTX2; NbExp=4; IntAct=EBI-3926851, EBI-9087860;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Chromosome, centromere
CC {ECO:0000269|PubMed:27332895}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:15938719}. Note=Distributes in the condensed
CC chromosomes during prophase to metaphase. After entering anaphase,
CC there is a dissociation from separated chromosomes and a redistribution
CC to midzone microtubules, and finally remains in the midbody during
CC cytokinesis. {ECO:0000269|PubMed:21531210}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9UQB9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UQB9-2; Sequence=VSP_004872;
CC Name=3; Synonyms=Aurora C-SV;
CC IsoId=Q9UQB9-3; Sequence=VSP_041095;
CC -!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in testis.
CC Elevated expression levels were seen only in a subset of cancer cell
CC lines such as Hep-G2, Huh-7 and HeLa. Expression is maximum at M phase.
CC {ECO:0000269|PubMed:15670791}.
CC -!- INDUCTION: Expression is cell cycle-regulated, with an increase during
CC G2 and M phases. {ECO:0000269|PubMed:10066797,
CC ECO:0000269|PubMed:15499654}.
CC -!- DISEASE: Spermatogenic failure 5 (SPGF5) [MIM:243060]: An infertility
CC disorder caused by spermatogenesis defects. Semen from affected men
CC show close to 100% morphologically abnormal multiflagellar spermatozoa
CC with low motility, oversized irregular heads, and abnormal midpiece and
CC acrosome. {ECO:0000269|PubMed:17435757, ECO:0000269|PubMed:21733974}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. Aurora subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; AF054621; AAC25955.1; -; mRNA.
DR EMBL; AF059681; AAC77369.1; -; mRNA.
DR EMBL; AB017332; BAA76292.1; -; mRNA.
DR EMBL; AY661554; AAT64422.1; -; mRNA.
DR EMBL; AC005261; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471135; EAW72485.1; -; Genomic_DNA.
DR EMBL; BC075064; AAH75064.2; -; mRNA.
DR CCDS; CCDS33128.1; -. [Q9UQB9-1]
DR CCDS; CCDS46205.1; -. [Q9UQB9-3]
DR CCDS; CCDS46206.1; -. [Q9UQB9-2]
DR RefSeq; NP_001015878.1; NM_001015878.1. [Q9UQB9-1]
DR RefSeq; NP_001015879.1; NM_001015879.1. [Q9UQB9-3]
DR RefSeq; NP_003151.2; NM_003160.2. [Q9UQB9-2]
DR PDB; 6GR8; X-ray; 1.75 A; A=36-305.
DR PDB; 6GR9; X-ray; 2.25 A; A=36-305.
DR PDBsum; 6GR8; -.
DR PDBsum; 6GR9; -.
DR AlphaFoldDB; Q9UQB9; -.
DR SMR; Q9UQB9; -.
DR BioGRID; 112671; 34.
DR IntAct; Q9UQB9; 30.
DR STRING; 9606.ENSP00000302898; -.
DR BindingDB; Q9UQB9; -.
DR ChEMBL; CHEMBL3935; -.
DR DrugBank; DB12010; Fostamatinib.
DR DrugBank; DB06134; SNS-314.
DR DrugCentral; Q9UQB9; -.
DR GuidetoPHARMACOLOGY; 1938; -.
DR iPTMnet; Q9UQB9; -.
DR PhosphoSitePlus; Q9UQB9; -.
DR BioMuta; AURKC; -.
DR DMDM; 27805738; -.
DR EPD; Q9UQB9; -.
DR jPOST; Q9UQB9; -.
DR MassIVE; Q9UQB9; -.
DR MaxQB; Q9UQB9; -.
DR PaxDb; Q9UQB9; -.
DR PeptideAtlas; Q9UQB9; -.
DR PRIDE; Q9UQB9; -.
DR ProteomicsDB; 85538; -. [Q9UQB9-1]
DR ProteomicsDB; 85539; -. [Q9UQB9-2]
DR ProteomicsDB; 85540; -. [Q9UQB9-3]
DR Antibodypedia; 33237; 510 antibodies from 30 providers.
DR DNASU; 6795; -.
DR Ensembl; ENST00000302804.12; ENSP00000302898.6; ENSG00000105146.14. [Q9UQB9-1]
DR Ensembl; ENST00000415300.6; ENSP00000407162.1; ENSG00000105146.14. [Q9UQB9-3]
DR Ensembl; ENST00000598785.5; ENSP00000471830.1; ENSG00000105146.14. [Q9UQB9-2]
DR GeneID; 6795; -.
DR KEGG; hsa:6795; -.
DR MANE-Select; ENST00000302804.12; ENSP00000302898.6; NM_001015878.2; NP_001015878.1.
DR UCSC; uc002qoc.4; human. [Q9UQB9-1]
DR CTD; 6795; -.
DR DisGeNET; 6795; -.
DR GeneCards; AURKC; -.
DR HGNC; HGNC:11391; AURKC.
DR HPA; ENSG00000105146; Tissue enriched (testis).
DR MalaCards; AURKC; -.
DR MIM; 243060; phenotype.
DR MIM; 603495; gene.
DR neXtProt; NX_Q9UQB9; -.
DR OpenTargets; ENSG00000105146; -.
DR Orphanet; 137893; Male infertility due to large-headed multiflagellar polyploid spermatozoa.
DR PharmGKB; PA36200; -.
DR VEuPathDB; HostDB:ENSG00000105146; -.
DR eggNOG; KOG0580; Eukaryota.
DR GeneTree; ENSGT00940000161619; -.
DR HOGENOM; CLU_000288_63_0_1; -.
DR InParanoid; Q9UQB9; -.
DR OMA; EKEGMEH; -.
DR OrthoDB; 954262at2759; -.
DR PhylomeDB; Q9UQB9; -.
DR TreeFam; TF105331; -.
DR PathwayCommons; Q9UQB9; -.
DR SignaLink; Q9UQB9; -.
DR SIGNOR; Q9UQB9; -.
DR BioGRID-ORCS; 6795; 12 hits in 1111 CRISPR screens.
DR GeneWiki; AURKC; -.
DR GenomeRNAi; 6795; -.
DR Pharos; Q9UQB9; Tchem.
DR PRO; PR:Q9UQB9; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9UQB9; protein.
DR Bgee; ENSG00000105146; Expressed in oocyte and 99 other tissues.
DR ExpressionAtlas; Q9UQB9; baseline and differential.
DR Genevisible; Q9UQB9; HS.
DR GO; GO:0032133; C:chromosome passenger complex; IBA:GO_Central.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0000793; C:condensed chromosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; TAS:UniProtKB.
DR GO; GO:0005876; C:spindle microtubule; IBA:GO_Central.
DR GO; GO:0051233; C:spindle midzone; IDA:UniProtKB.
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:0004672; F:protein kinase activity; IDA:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; TAS:UniProtKB.
DR GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; TAS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0016570; P:histone modification; TAS:UniProtKB.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051256; P:mitotic spindle midzone assembly; TAS:UniProtKB.
DR GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
DR GO; GO:0048599; P:oocyte development; IEA:InterPro.
DR GO; GO:0032467; P:positive regulation of cytokinesis; TAS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0032465; P:regulation of cytokinesis; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IEA:InterPro.
DR InterPro; IPR030616; Aur.
DR InterPro; IPR030613; AURKC.
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:SF3; PTHR24350:SF3; 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; Alternative splicing; ATP-binding; Cell cycle; Cell division;
KW Centromere; Chromosome; Cytoplasm; Cytoskeleton; Kinase; Meiosis; Mitosis;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..309
FT /note="Aurora kinase C"
FT /id="PRO_0000085660"
FT DOMAIN 43..293
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..309
FT /note="Interaction with BIRC5"
FT /evidence="ECO:0000269|PubMed:27332895"
FT COMPBIAS 19..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 166
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 49..57
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 198
FT /note="Phosphothreonine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:O88445"
FT VAR_SEQ 1..34
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9799611"
FT /id="VSP_004872"
FT VAR_SEQ 1..20
FT /note="MSSPRAVVQLGKAQPAGEEL -> M (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15670791"
FT /id="VSP_041095"
FT VARIANT 52
FT /note="G -> E (in a lung adenocarcinoma sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040385"
FT VARIANT 148
FT /note="E -> Q (in a lung squamous cell carcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040386"
FT VARIANT 244
FT /note="H -> Q (in a lung adenocarcinoma sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040387"
FT MUTAGEN 72
FT /note="K->R: Impairs kinase activity."
FT /evidence="ECO:0000269|PubMed:15316025,
FT ECO:0000269|PubMed:15499654"
FT MUTAGEN 166
FT /note="D->Y: Impairs kinase activity, and keeps AURKC with
FT the chromosomes until the end of mitosis."
FT /evidence="ECO:0000269|PubMed:15938719"
FT MUTAGEN 198
FT /note="T->A: Impairs kinase activity."
FT /evidence="ECO:0000269|PubMed:15316025,
FT ECO:0000269|PubMed:15670791"
FT CONFLICT 109
FT /note="Y -> H (in Ref. 1; AAC25955)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="L -> V (in Ref. 2; AAC77369)"
FT /evidence="ECO:0000305"
FT CONFLICT 193..195
FT /note="SLR -> LPE (in Ref. 2; AAC77369)"
FT /evidence="ECO:0000305"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:6GR8"
FT STRAND 43..52
FT /evidence="ECO:0007829|PDB:6GR8"
FT STRAND 55..62
FT /evidence="ECO:0007829|PDB:6GR8"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:6GR8"
FT STRAND 68..75
FT /evidence="ECO:0007829|PDB:6GR8"
FT HELIX 76..82
FT /evidence="ECO:0007829|PDB:6GR8"
FT HELIX 85..97
FT /evidence="ECO:0007829|PDB:6GR8"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:6GR8"
FT STRAND 113..120
FT /evidence="ECO:0007829|PDB:6GR8"
FT HELIX 128..135
FT /evidence="ECO:0007829|PDB:6GR8"
FT HELIX 140..159
FT /evidence="ECO:0007829|PDB:6GR8"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:6GR8"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:6GR8"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:6GR8"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:6GR8"
FT HELIX 208..211
FT /evidence="ECO:0007829|PDB:6GR8"
FT HELIX 220..234
FT /evidence="ECO:0007829|PDB:6GR8"
FT HELIX 244..252
FT /evidence="ECO:0007829|PDB:6GR8"
FT HELIX 264..273
FT /evidence="ECO:0007829|PDB:6GR8"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:6GR8"
FT HELIX 284..289
FT /evidence="ECO:0007829|PDB:6GR8"
FT HELIX 291..296
FT /evidence="ECO:0007829|PDB:6GR8"
SQ SEQUENCE 309 AA; 35591 MW; 41B7DFCA91704201 CRC64;
MSSPRAVVQL GKAQPAGEEL ATANQTAQQP SSPAMRRLTV DDFEIGRPLG KGKFGNVYLA
RLKESHFIVA LKVLFKSQIE KEGLEHQLRR EIEIQAHLQH PNILRLYNYF HDARRVYLIL
EYAPRGELYK ELQKSEKLDE QRTATIIEEL ADALTYCHDK KVIHRDIKPE NLLLGFRGEV
KIADFGWSVH TPSLRRKTMC GTLDYLPPEM IEGRTYDEKV DLWCIGVLCY ELLVGYPPFE
SASHSETYRR ILKVDVRFPL SMPLGARDLI SRLLRYQPLE RLPLAQILKH PWVQAHSRRV
LPPCAQMAS
