ID Q5Y191_HUMAN Unreviewed; 306 AA. AC Q5Y191; DT 23-NOV-2004, integrated into UniProtKB/TrEMBL. DT 23-NOV-2004, sequence version 1. DT 19-JAN-2022, entry version 128. DE RecName: Full=Aurora kinase {ECO:0000256|RuleBase:RU367134}; DE EC=2.7.11.1 {ECO:0000256|RuleBase:RU367134}; GN Name=AURKC {ECO:0000313|EMBL:AAU04399.1, GN ECO:0000313|Ensembl:ENSP00000469983}; 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 {ECO:0000313|EMBL:AAU04399.1}; RN [1] {ECO:0000313|EMBL:AAU04399.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Testis {ECO:0000313|EMBL:AAU04399.1}; 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 [2] {ECO:0000313|Ensembl:ENSP00000469983, ECO:0000313|Proteomes:UP000005640} 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 [3] {ECO:0000313|Ensembl:ENSP00000469983} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2013) to UniProtKB. 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:0000256|ARBA:ARBA00001433, CC ECO:0000256|RuleBase:RU367134}; 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:0000256|ARBA:ARBA00000775, CC ECO:0000256|RuleBase:RU367134}; CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein CC kinase family. Aurora subfamily. {ECO:0000256|RuleBase:RU367134}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AC005261; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AY714054; AAU04399.1; -; mRNA. DR Antibodypedia; 33237; 504 antibodies from 30 providers. DR Ensembl; ENST00000599062; ENSP00000469983; ENSG00000105146. DR UCSC; uc010etv.4; human. DR HGNC; HGNC:11391; AURKC. DR OpenTargets; ENSG00000105146; -. DR VEuPathDB; HostDB:ENSG00000105146; -. DR GeneTree; ENSGT00940000161619; -. DR Proteomes; UP000005640; Chromosome 19. DR Bgee; ENSG00000105146; Expressed in oocyte and 120 other tissues. DR GO; GO:0032133; C:chromosome passenger complex; IEA:InterPro. DR GO; GO:0005819; C:spindle; IEA:UniProt. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:RHEA. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0051321; P:meiotic cell cycle; IEA:InterPro. DR GO; GO:0048599; P:oocyte development; IEA:InterPro. DR GO; GO:0007283; P:spermatogenesis; IEA:InterPro. DR GO; GO:0051255; P:spindle midzone assembly; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Cell cycle {ECO:0000256|ARBA:ARBA00023306}; KW Cell division {ECO:0000256|ARBA:ARBA00022618}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU367134}; KW Mitosis {ECO:0000256|ARBA:ARBA00022776}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; KW Proteomics identification {ECO:0007829|PeptideAtlas:Q5Y191}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU000304}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU367134}. FT DOMAIN 40..290 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 1..31 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 15..31 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 163 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR630616-1" FT BINDING 69 FT /note="ATP" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 306 AA; 35322 MW; 869FC07D176B45CE CRC64; MSSPRAVVQL GKAQPAGEES NQTAQQPSSP AMRRLTVDDF EIGRPLGKGK FGNVYLARLK ESHFIVALKV LFKSQIEKEG LEHQLRREIE IQAHLQHPNI LRLYNYFHDA RRVYLILEYA PRGELYKELQ KSEKLDEQRT ATIIEELADA LTYCHDKKVI HRDIKPENLL LGFRGEVKIA DFGWSVHTPS LRRKTMCGTL DYLPPEMIEG RTYDEKVDLW CIGVLCYELL VGYPPFESAS HSETYRRILK VDVRFPLSMP LGARDLISRL LRYQPLERLP LAQILKHPWV QAHSRRVLPP CAQMAS //