AUR2_ARATH
ID AUR2_ARATH Reviewed; 282 AA.
AC Q683C9; O82309;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Serine/threonine-protein kinase Aurora-2;
DE Short=AtAur2;
DE EC=2.7.11.1;
DE AltName: Full=Aurora-like kinase 2;
GN Name=AUR2; OrderedLocusNames=At2g25880; ORFNames=F17H15.9;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), FUNCTION, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=16028112; DOI=10.1007/s11103-005-3454-x;
RA Kawabe A., Matsunaga S., Nakagawa K., Kurihara D., Yoneda A., Hasezawa S.,
RA Uchiyama S., Fukui K.;
RT "Characterization of plant Aurora kinases during mitosis.";
RL Plant Mol. Biol. 58:1-13(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=15722465; DOI=10.1105/tpc.104.029710;
RA Demidov D., Van Damme D., Geelen D., Blattner F.R., Houben A.;
RT "Identification and dynamics of two classes of aurora-like kinases in
RT Arabidopsis and other plants.";
RL Plant Cell 17:836-848(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Carninci P., Hayashizaki Y.,
RA Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA Shinozaki K., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Phosphorylates specifically 'Ser-10' of histone H3 in vitro.
CC Associates with cytoskeletal structures that are necessary for
CC cytokinesis and with the microtubule spindle. Might colocalize with
CC gamma-tubulin and function in microtubule organizing centers (MTOCs).
CC {ECO:0000269|PubMed:16028112}.
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 -!- INTERACTION:
CC Q683C9; O23160: MYB73; NbExp=3; IntAct=EBI-25517163, EBI-25506855;
CC Q683C9; Q9SSA8: RAP2-12; NbExp=3; IntAct=EBI-25517163, EBI-4441057;
CC -!- SUBCELLULAR LOCATION: Nucleus membrane. Cytoplasm, cytoskeleton,
CC spindle. Cytoplasm, cytoskeleton, spindle pole. Note=Nuclear membrane
CC in interphase cells, spindle poles at prophase and mitotic spindle from
CC metaphase to telophase.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q683C9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q683C9-2; Sequence=VSP_022228;
CC -!- TISSUE SPECIFICITY: Abundant in roots, flowers and flower buds, low or
CC absent in expanded leaves, stems and siliques.
CC {ECO:0000269|PubMed:15722465}.
CC -!- DEVELOPMENTAL STAGE: Expression peaks at mitosis.
CC {ECO:0000269|PubMed:15722465}.
CC -!- PTM: Phosphorylation at Thr-173 may regulate activity and degradation
CC of AUR2 in a cell cycle dependent manner. {ECO:0000250}.
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; AB196734; BAE00020.1; -; Genomic_DNA.
DR EMBL; AJ854184; CAH69533.1; -; mRNA.
DR EMBL; AC005395; AAC42257.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07766.1; -; Genomic_DNA.
DR EMBL; BT010653; AAR07517.1; -; mRNA.
DR EMBL; AK175188; BAD42951.1; -; mRNA.
DR PIR; H84653; H84653.
DR RefSeq; NP_180159.2; NM_128148.4. [Q683C9-2]
DR AlphaFoldDB; Q683C9; -.
DR SMR; Q683C9; -.
DR BioGRID; 2481; 2.
DR IntAct; Q683C9; 2.
DR STRING; 3702.AT2G25880.1; -.
DR PaxDb; Q683C9; -.
DR PeptideAtlas; Q683C9; -.
DR ProteomicsDB; 241104; -. [Q683C9-1]
DR EnsemblPlants; AT2G25880.1; AT2G25880.1; AT2G25880. [Q683C9-2]
DR GeneID; 817129; -.
DR Gramene; AT2G25880.1; AT2G25880.1; AT2G25880. [Q683C9-2]
DR KEGG; ath:AT2G25880; -.
DR Araport; AT2G25880; -.
DR TAIR; locus:2043485; AT2G25880.
DR eggNOG; KOG0580; Eukaryota.
DR HOGENOM; CLU_000288_63_0_1; -.
DR InParanoid; Q683C9; -.
DR PhylomeDB; Q683C9; -.
DR PRO; PR:Q683C9; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q683C9; baseline and differential.
DR Genevisible; Q683C9; AT.
DR GO; GO:0032133; C:chromosome passenger complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005876; C:spindle microtubule; IBA:GO_Central.
DR GO; GO:0051233; C:spindle midzone; IBA:GO_Central.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0035175; F:histone kinase activity (H3-S10 specific); IDA:TAIR.
DR GO; GO:0035174; F:histone serine kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0016572; P:histone phosphorylation; IDA:TAIR.
DR GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
DR GO; GO:0032465; P:regulation of cytokinesis; IBA:GO_Central.
DR InterPro; IPR030616; Aur.
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 Alternative splicing; ATP-binding; Cytoplasm; Cytoskeleton; Kinase;
KW Membrane; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..282
FT /note="Serine/threonine-protein kinase Aurora-2"
FT /id="PRO_0000270793"
FT DOMAIN 19..270
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 142
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 25..33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q93V58"
FT MOD_RES 173
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q38997"
FT VAR_SEQ 1..4
FT /note="MLYQ -> MGISTETQQI (in isoform 2)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_022228"
SQ SEQUENCE 282 AA; 32757 MW; 3475F9C04D166B7E CRC64;
MLYQAASEAA QKRWTTSDFD IGKPLGRGKF GHVYLAREKR SDHIVALKVL FKAQLQQSQV
EHQLRREVEI QSHLRHPNIL RLYGYFYDQK RVYLILEYAV RGELYKELQK CKYFSERRAA
TYVASLARAL IYCHGKHVIH RDIKPENLLI GAQGELKIAD FGWSVHTFNR RRTMCGTLDY
LPPEMVESVE HDASVDIWSL GILCYEFLYG VPPFEAREHS ETYKRIVQVD LKFPPKPIVS
SSAKDLISQM LVKESTQRLA LHKLLEHPWI VQNADPSGLY RG
