ID AUR1_ARATH Reviewed; 294 AA.
AC Q9M077; Q8LBX4;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 168.
DE RecName: Full=Serine/threonine-protein kinase Aurora-1;
DE Short=AtAur1;
DE EC=2.7.11.1;
DE AltName: Full=Aurora-like kinase 1;
GN Name=AUR1; OrderedLocusNames=At4g32830; ORFNames=T16I18.40;
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], FUNCTION, AND SUBCELLULAR 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], FUNCTION, 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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=15469496; DOI=10.1111/j.1365-313x.2004.02222.x;
RA Van Damme D., Bouget F.-Y., Van Poucke K., Inze D., Geelen D.;
RT "Molecular dissection of plant cytokinesis and phragmoplast structure: a
RT survey of GFP-tagged proteins.";
RL Plant J. 40:386-398(2004).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TPX2.
RX PubMed=22150830; DOI=10.1111/j.1469-8137.2011.03989.x;
RA Petrovska B., Cenklova V., Pochylova Z., Kourova H., Doskocilova A.,
RA Plihal O., Binarova L., Binarova P.;
RT "Plant Aurora kinases play a role in maintenance of primary meristems and
RT control of endoreduplication.";
RL New Phytol. 193:590-604(2012).
CC -!- FUNCTION: Phosphorylates specifically 'Ser-10' of histone H3 in vitro
CC and colocalizes with phosphorylated histone H3 during mitosis.
CC Associates with cytoskeletal structures that are necessary for
CC cytokinesis and with the microtubule spindle. Colocalizes also with
CC gamma-tubulin and function in microtubule organizing centers (MTOCs).
CC In contrast with the mammalian B-type Aurora, AUR1 has no kinase
CC activity toward 'Ser-28' of histone H3. {ECO:0000269|PubMed:15722465,
CC ECO:0000269|PubMed:16028112, ECO:0000269|PubMed:22150830}.
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 -!- SUBUNIT: Interacts with TPX2. {ECO:0000269|PubMed:22150830}.
CC -!- SUBCELLULAR LOCATION: Nucleus membrane. Cytoplasm, cytoskeleton,
CC spindle. Cytoplasm, cytoskeleton, spindle pole. Cytoplasm,
CC cytoskeleton, phragmoplast. Note=Nuclear membrane in interphase cells,
CC spindle poles at prophase, mitotic spindle from metaphase to telophase
CC and equatorial cell plate at telophase.
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: Peak of expression at mitosis.
CC {ECO:0000269|PubMed:15722465}.
CC -!- PTM: Phosphorylation at Thr-185 may regulate activity and degradation
CC of AUR1 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; AB196733; BAE00019.1; -; Genomic_DNA.
DR EMBL; AJ854183; CAH69532.1; -; mRNA.
DR EMBL; AL161582; CAB80000.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86124.1; -; Genomic_DNA.
DR EMBL; AY086942; AAM64506.1; -; mRNA.
DR EMBL; AK221608; BAD95178.1; -; mRNA.
DR PIR; T10690; T10690.
DR RefSeq; NP_195009.1; NM_119436.3.
DR AlphaFoldDB; Q9M077; -.
DR SMR; Q9M077; -.
DR BioGRID; 14704; 2.
DR STRING; 3702.Q9M077; -.
DR PaxDb; 3702-AT4G32830-1; -.
DR ProteomicsDB; 241150; -.
DR EnsemblPlants; AT4G32830.1; AT4G32830.1; AT4G32830.
DR GeneID; 829419; -.
DR Gramene; AT4G32830.1; AT4G32830.1; AT4G32830.
DR KEGG; ath:AT4G32830; -.
DR Araport; AT4G32830; -.
DR TAIR; AT4G32830; AUR1.
DR eggNOG; KOG0580; Eukaryota.
DR HOGENOM; CLU_000288_63_0_1; -.
DR InParanoid; Q9M077; -.
DR OMA; DSHFIVA; -.
DR OrthoDB; 117459at2759; -.
DR PhylomeDB; Q9M077; -.
DR PRO; PR:Q9M077; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9M077; baseline and differential.
DR Genevisible; Q9M077; AT.
DR GO; GO:0009504; C:cell plate; IDA:TAIR.
DR GO; GO:0005874; C:microtubule; IDA:TAIR.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0009524; C:phragmoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; HDA:TAIR.
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 H3S10 kinase activity; IDA:TAIR.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:TAIR.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14007; STKc_Aurora; 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; SERINE/THREONINE-PROTEIN KINASE IAL-RELATED; 1.
DR PANTHER; PTHR24350:SF32; SERINE_THREONINE-PROTEIN KINASE AURORA-1-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; Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Kinase;
KW Membrane; Microtubule; Mitosis; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..294
FT /note="Serine/threonine-protein kinase Aurora-1"
FT /id="PRO_0000270792"
FT DOMAIN 31..282
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 154
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 37..45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 60
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q93V58"
FT MOD_RES 185
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q38997"
SQ SEQUENCE 294 AA; 33972 MW; B6669E1799083BE4 CRC64;
MAIPTETQHQ EKEASDASAA AAQKRWTLSD FDIGKPLGRG KFGHVYLARE KRSNHVVALK
VLFKSQLQQS QVEHQLRREV EIQSHLRHPN ILRLYGYFYD QKRVYLILEY AARGELYKDL
QKCKYFSERR AATYVASLAR ALIYCHGKHV IHRDIKPENL LIGAQGELKI ADFGWSVHTF
NRRRTMCGTL DYLPPEMVES VEHDASVDIW SLGILCYEFL YGVPPFEAME HSDTYRRIVQ
VDLKFPPKPI ISASAKDLIS QMLVKESSQR LPLHKLLEHP WIVQNADPSG IYRV
//
