AURAA_XENLA
ID AURAA_XENLA Reviewed; 407 AA.
AC Q91820; Q6INY9;
DT 27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Aurora kinase A-A;
DE EC=2.7.11.1;
DE AltName: Full=Aurora/IPL1-related kinase 1;
DE Short=ARK-1;
DE Short=Aurora-related kinase 1;
DE AltName: Full=Serine/threonine-protein kinase 6-A;
DE AltName: Full=Serine/threonine-protein kinase Eg2-A;
DE Short=pEg2;
DE AltName: Full=Serine/threonine-protein kinase aurora-A;
DE AltName: Full=p46Eg265;
GN Name=aurka-a; Synonyms=aurka, eg2, stk6;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP AUTOPHOSPHORYLATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND MUTAGENESIS OF LYS-169.
RC TISSUE=Egg;
RX PubMed=9454730; DOI=10.1242/jcs.111.5.557;
RA Roghi C., Giet R., Uzbekov R., Morin N., Chartrain I., Le Guellec R.,
RA Couturier A., Doree M., Phillippe M., Prigent C.;
RT "The Xenopus protein kinase pEg2 associates with the centrosome in a cell
RT cycle-dependent manner, binds to the spindle microtubules and is involved
RT in bipolar mitotic spindle assembly.";
RL J. Cell Sci. 111:557-572(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH KIF11, AND SUBCELLULAR
RP LOCATION.
RX PubMed=10329703; DOI=10.1074/jbc.274.21.15005;
RA Giet R., Uzbekov R., Cubizolles F., Le Guellec K., Prigent C.;
RT "The Xenopus laevis aurora-related protein kinase pEg2 associates with and
RT phosphorylates the kinesin-related protein XlEg5.";
RL J. Biol. Chem. 274:15005-15013(1999).
RN [4]
RP FUNCTION, AND INTERACTION WITH KIF2C.
RX PubMed=18434591; DOI=10.1091/mbc.e08-02-0198;
RA Zhang X., Ems-McClung S.C., Walczak C.E.;
RT "Aurora A phosphorylates MCAK to control ran-dependent spindle
RT bipolarity.";
RL Mol. Biol. Cell 19:2752-2765(2008).
CC -!- FUNCTION: Mitotic serine/threonine kinases that contributes to the
CC regulation of cell cycle progression. Associates with the centrosome
CC and the spindle microtubules during mitosis and plays a critical role
CC in various mitotic events including the establishment of mitotic
CC spindle, centrosome duplication, centrosome separation as well as
CC maturation, chromosomal alignment, spindle assembly checkpoint, and
CC cytokinesis. Phosphorylates numerous target proteins. Important for
CC microtubule formation and/or stabilization.
CC {ECO:0000269|PubMed:10329703, ECO:0000269|PubMed:18434591,
CC ECO:0000269|PubMed:9454730}.
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:0000269|PubMed:10329703, ECO:0000269|PubMed:9454730};
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:0000269|PubMed:10329703,
CC ECO:0000269|PubMed:9454730};
CC -!- SUBUNIT: Interacts with kif2c and kif11. {ECO:0000269|PubMed:10329703,
CC ECO:0000269|PubMed:18434591}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:10329703, ECO:0000269|PubMed:9454730}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:10329703, ECO:0000269|PubMed:9454730}.
CC Note=Localizes to the spindle pole during mitosis especially from
CC prophase through anaphase. Partially colocalized with gamma tubulin in
CC the centrosome, from S to M phase. {ECO:0000269|PubMed:9454730}.
CC -!- TISSUE SPECIFICITY: Highly expressed in ovary and testis.
CC {ECO:0000269|PubMed:9454730}.
CC -!- DEVELOPMENTAL STAGE: Expressed maternally in oocytes, unfertilized eggs
CC and embryos up to the mid-blastula transition (MBT).
CC {ECO:0000269|PubMed:9454730}.
CC -!- PTM: Phosphorylated (PubMed:9454730). Autophosphorylated on a serine
CC residue (PubMed:9454730). {ECO:0000269|PubMed:9454730}.
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; Z17207; CAA78915.1; -; mRNA.
DR EMBL; BC072133; AAH72133.1; -; mRNA.
DR PIR; S52243; S52243.
DR RefSeq; NP_001081565.1; NM_001088096.1.
DR RefSeq; XP_018089632.1; XM_018234143.1.
DR AlphaFoldDB; Q91820; -.
DR SMR; Q91820; -.
DR BioGRID; 99261; 2.
DR ELM; Q91820; -.
DR IntAct; Q91820; 4.
DR iPTMnet; Q91820; -.
DR PRIDE; Q91820; -.
DR DNASU; 397925; -.
DR GeneID; 397925; -.
DR KEGG; xla:397925; -.
DR CTD; 397925; -.
DR Xenbase; XB-GENE-866460; aurka.L.
DR OMA; PHTKNVD; -.
DR OrthoDB; 954262at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 397925; Expressed in egg cell and 16 other tissues.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005876; C:spindle microtubule; IDA:UniProtKB.
DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019894; F:kinesin binding; IPI:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000212; P:meiotic spindle organization; IEA:InterPro.
DR GO; GO:0007100; P:mitotic centrosome separation; IEA:InterPro.
DR GO; GO:0090307; P:mitotic spindle assembly; IMP:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IMP:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IMP:UniProtKB.
DR CDD; cd14116; STKc_Aurora-A; 1.
DR InterPro; IPR030616; Aur.
DR InterPro; IPR030611; AURKA.
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 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; Cytoplasm; Cytoskeleton; Kinase;
KW Microtubule; Mitosis; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..407
FT /note="Aurora kinase A-A"
FT /id="PRO_0000086695"
FT DOMAIN 140..390
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..300
FT /note="Activation segment"
FT /evidence="ECO:0000250|UniProtKB:O14965"
FT COMPBIAS 27..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 263
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 150
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 169
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT BINDING 217..220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 281
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MUTAGEN 169
FT /note="K->R: Lacks kinase activity. Disrupts mitotic
FT spindle assembly."
FT /evidence="ECO:0000269|PubMed:9454730"
SQ SEQUENCE 407 AA; 46372 MW; DE1628A2C6D11277 CRC64;
MERAVKENHK PSNVKIFHPM TEGAKRIPVN QPQSTQFRPP GTAVSAQRIL GPSNVPQRVL
AQAQKPILSS QKPTTQIPLR PATQGHQSSK PQGPNENRNP QQTSHSSTPN VEKKGSTDQG
KTSAVPKEEG KKKQWCLEDF EIGRPLGKGK FGNVYLARER ESKFILALKV LFKSQLEKAG
VEHQLRREVE IQSHLRHPNI LRLYGYFHDA SRVYLILDYA PGGELFRELQ KCTRFDDQRS
AMYIKQLAEA LLYCHSKKVI HRDIKPENLL LGSNGELKIA DFGWSVHAPS SRRTTLCGTL
DYLPPEMIEG RMHDETVDLW SLGVLCYEFL VGKPPFETDT HQETYRRISK VEFQYPPYVS
EEARDLVSKL LKHNPNHRLP LKGVLEHPWI IKNSQLKKKD EPLPGAQ
