AURAB_XENLA
ID AURAB_XENLA Reviewed; 408 AA.
AC Q91819; Q6DJK0;
DT 27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 3.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Aurora kinase A-B;
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-B;
DE AltName: Full=Serine/threonine-protein kinase Eg2-B;
DE AltName: Full=Serine/threonine-protein kinase aurora-A;
DE AltName: Full=p46XlEg22;
GN Name=aurka-b; 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].
RC TISSUE=Egg;
RA Roghi C., Le Guellec R., Paris J., Couturier A., Philippe M.;
RT "Eg2, selected by differential screening encodes a new Xenopus protein
RT kinase family.";
RL Submitted (OCT-1992) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Mitotic serine/threonine kinases that contributes to the
CC regulation of cell cycle progression (By similarity). Associates with
CC the centrosome and the spindle microtubules during mitosis and plays a
CC critical role in various mitotic events including the establishment of
CC mitotic spindle, centrosome duplication, centrosome separation as well
CC as maturation, chromosomal alignment, spindle assembly checkpoint, and
CC cytokinesis (By similarity). Phosphorylates numerous target proteins
CC (By similarity). Important for microtubule formation and/or
CC stabilization (By similarity). {ECO:0000250|UniProtKB:Q91820}.
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:0000250|UniProtKB:Q91820};
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:0000250|UniProtKB:Q91820};
CC -!- SUBUNIT: Interacts with kif2c and kif11.
CC {ECO:0000250|UniProtKB:Q91820}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000250|UniProtKB:Q91820}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:Q91820}.
CC Note=Localizes to the spindle pole during mitosis especially from
CC prophase through anaphase (By similarity). Partially colocalized with
CC gamma tubulin in the centrosome, from S to M phase (By similarity).
CC {ECO:0000250|UniProtKB:Q91820}.
CC -!- PTM: Phosphorylated (By similarity). Autophosphorylated on a serine
CC residue (By similarity). {ECO:0000250|UniProtKB:Q91820}.
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=CAA78914.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; Z17206; CAA78914.1; ALT_INIT; mRNA.
DR EMBL; BC075177; AAH75177.1; -; mRNA.
DR RefSeq; NP_001082272.1; NM_001088803.1.
DR AlphaFoldDB; Q91819; -.
DR SMR; Q91819; -.
DR BioGRID; 99681; 1.
DR IntAct; Q91819; 1.
DR iPTMnet; Q91819; -.
DR GeneID; 398349; -.
DR KEGG; xla:398349; -.
DR CTD; 398349; -.
DR Xenbase; XB-GENE-17337404; aurka.S.
DR OrthoDB; 954262at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10S.
DR Bgee; 398349; Expressed in egg cell and 19 other tissues.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005876; C:spindle microtubule; ISS:UniProtKB.
DR GO; GO:0000922; C:spindle pole; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019894; F:kinesin binding; ISS:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; ISS:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS: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; ISS:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISS:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; ISS: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 2: Evidence at transcript 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..408
FT /note="Aurora kinase A-B"
FT /id="PRO_0000086696"
FT DOMAIN 140..390
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..128
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 28..117
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:0000255|PROSITE-ProRule:PRU00159"
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 CONFLICT 211
FT /note="C -> S (in Ref. 1; CAA78914)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 408 AA; 46477 MW; FD4855CC6708E5E7 CRC64;
MERAVKENHK PSNVKVFHPM TEGPKRIPVS QPPSTQVRPP VTGVSAQRIL GPSNVPQRVM
MQAQKPVLSN QKPTAQGLLR PATHGHQTSK PQGPNENRNP QQTSHSSTPN MEKKGSTDQG
KTLAVPKEEG KKKQWCLEDF EIGRPLGKGK FGNVYLARER ESKFILALKV LFKSQLEKAG
VEHQLRREVE IQSHLRHPNI LRLYGYFHDA CRVYLILDYA PGGELFRELQ KCTRFDDQRS
ALYIKQLAEA LLYCHSKKVI HRDIKPENLL LGSNGELKIA DFGWSVHAPS SRRTTLCGTL
DYLPPEMIEG RMHDEKVDLW SLGVLCYEFL VGKPPFETDT HQETYRRISK VEFQYPPYVS
EEAKDLVSKL LKHNPNHRLP LKGVLEHPWI VKNSQQPKKK DEPLAGAQ
