ID Q5Y191_HUMAN Unreviewed; 306 AA. AC Q5Y191; DT 23-NOV-2004, integrated into UniProtKB/TrEMBL. DT 23-NOV-2004, sequence version 1. DT 29-MAY-2024, entry version 140. 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:ENSP00000469983.1}; 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:ENSP00000469983.1, 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:ENSP00000469983.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2024) 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; 571 antibodies from 30 providers. DR Ensembl; ENST00000599062.5; ENSP00000469983.1; ENSG00000105146.14. DR UCSC; uc010etv.4; human. DR HGNC; HGNC:11391; AURKC. DR VEuPathDB; HostDB:ENSG00000105146; -. DR GeneTree; ENSGT00940000161619; -. DR Proteomes; UP000005640; Chromosome 19. DR Bgee; ENSG00000105146; Expressed in oocyte and 101 other cell types or tissues. DR GO; GO:0032133; C:chromosome passenger complex; IEA:TreeGrafter. DR GO; GO:0000776; C:kinetochore; IEA:TreeGrafter. DR GO; GO:0005876; C:spindle microtubule; IEA:TreeGrafter. DR GO; GO:0051233; C:spindle midzone; IEA:TreeGrafter. DR GO; GO:0031616; C:spindle pole centrosome; IEA:TreeGrafter. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0007052; P:mitotic spindle organization; IEA:TreeGrafter. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0032465; P:regulation of cytokinesis; IEA:TreeGrafter. DR CDD; cd14117; STKc_Aurora-B_like; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR030616; Aur-like. 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:SF3; AURORA KINASE C; 1. DR PANTHER; PTHR24350; SERINE/THREONINE-PROTEIN KINASE IAL-RELATED; 1. DR Pfam; PF00069; Pkinase; 1. DR PIRSF; PIRSF000654; Integrin-linked_kinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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|PIRSR:PIRSR630616- KW 2}; Cell cycle {ECO:0000256|ARBA:ARBA00023306}; KW Cell division {ECO:0000256|ARBA:ARBA00022618}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00023212}; KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU367134}; KW Mitosis {ECO:0000256|ARBA:ARBA00022776}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, KW ECO:0000256|PIRSR:PIRSR630616-2}; KW Proteomics identification {ECO:0007829|EPD:Q5Y191, KW ECO:0007829|PeptideAtlas:Q5Y191}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527, KW 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 50 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR630616-2" FT BINDING 69 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR630616-2, FT ECO:0000256|PROSITE-ProRule:PRU10141" FT BINDING 118..120 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR630616-2" FT BINDING 167..168 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR630616-2" FT BINDING 181 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR630616-2" FT CROSSLNK 165 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000256|PIRSR:PIRSR630616-3" 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 //