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Serine/threonine-protein kinase Aurora-1 (AtAur1) (EC 2.7.11.1) (Aurora-like kinase 1)

 AUR1_ARATH              Reviewed;         294 AA.
Q9M077; Q8LBX4;
09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
25-APR-2018, entry version 139.
RecName: Full=Serine/threonine-protein kinase Aurora-1;
Short=AtAur1;
EC=2.7.11.1;
AltName: Full=Aurora-like kinase 1;
Name=AUR1; OrderedLocusNames=At4g32830; ORFNames=T16I18.40;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
STRAIN=cv. Columbia;
PubMed=16028112; DOI=10.1007/s11103-005-3454-x;
Kawabe A., Matsunaga S., Nakagawa K., Kurihara D., Yoneda A.,
Hasezawa S., Uchiyama S., Fukui K.;
"Characterization of plant Aurora kinases during mitosis.";
Plant Mol. Biol. 58:1-13(2005).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION,
DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
STRAIN=cv. Columbia;
PubMed=15722465; DOI=10.1105/tpc.104.029710;
Demidov D., Van Damme D., Geelen D., Blattner F.R., Houben A.;
"Identification and dynamics of two classes of aurora-like kinases in
Arabidopsis and other plants.";
Plant Cell 17:836-848(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
Langham S.-A., McCullagh B., Bilham L., Robben J.,
van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[7]
SUBCELLULAR LOCATION.
PubMed=15469496; DOI=10.1111/j.1365-313X.2004.02222.x;
Van Damme D., Bouget F.-Y., Van Poucke K., Inze D., Geelen D.;
"Molecular dissection of plant cytokinesis and phragmoplast structure:
a survey of GFP-tagged proteins.";
Plant J. 40:386-398(2004).
[8]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TPX2.
PubMed=22150830; DOI=10.1111/j.1469-8137.2011.03989.x;
Petrovska B., Cenklova V., Pochylova Z., Kourova H., Doskocilova A.,
Plihal O., Binarova L., Binarova P.;
"Plant Aurora kinases play a role in maintenance of primary meristems
and control of endoreduplication.";
New Phytol. 193:590-604(2012).
-!- FUNCTION: Phosphorylates specifically 'Ser-10' of histone H3 in
vitro and colocalizes with phosphorylated histone H3 during
mitosis. Associates with cytoskeletal structures that are
necessary for cytokinesis and with the microtubule spindle.
Colocalizes also with gamma-tubulin and function in microtubule
organizing centers (MTOCs). In contrast with the mammalian B-type
Aurora, AUR1 has no kinase activity toward 'Ser-28' of histone H3.
{ECO:0000269|PubMed:15722465, ECO:0000269|PubMed:16028112,
ECO:0000269|PubMed:22150830}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- SUBUNIT: Interacts with TPX2. {ECO:0000269|PubMed:22150830}.
-!- SUBCELLULAR LOCATION: Nucleus membrane. Cytoplasm, cytoskeleton,
spindle. Cytoplasm, cytoskeleton, spindle pole. Cytoplasm,
cytoskeleton, phragmoplast. Note=Nuclear membrane in interphase
cells, spindle poles at prophase, mitotic spindle from metaphase
to telophase and equatorial cell plate at telophase.
-!- TISSUE SPECIFICITY: Abundant in roots, flowers and flower buds,
low or absent in expanded leaves, stems and siliques.
{ECO:0000269|PubMed:15722465}.
-!- DEVELOPMENTAL STAGE: Peak of expression at mitosis.
{ECO:0000269|PubMed:15722465}.
-!- PTM: Phosphorylation at Thr-185 may regulate activity and
degradation of AUR1 in a cell cycle dependent manner.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. Aurora subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
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EMBL; AB196733; BAE00019.1; -; Genomic_DNA.
EMBL; AJ854183; CAH69532.1; -; mRNA.
EMBL; AL161582; CAB80000.1; -; Genomic_DNA.
EMBL; CP002687; AEE86124.1; -; Genomic_DNA.
EMBL; AY086942; AAM64506.1; -; mRNA.
EMBL; AK221608; BAD95178.1; -; mRNA.
PIR; T10690; T10690.
RefSeq; NP_195009.1; NM_119436.3.
UniGene; At.24046; -.
UniGene; At.28037; -.
ProteinModelPortal; Q9M077; -.
SMR; Q9M077; -.
BioGrid; 14704; 2.
STRING; 3702.AT4G32830.1; -.
PaxDb; Q9M077; -.
EnsemblPlants; AT4G32830.1; AT4G32830.1; AT4G32830.
GeneID; 829419; -.
Gramene; AT4G32830.1; AT4G32830.1; AT4G32830.
KEGG; ath:AT4G32830; -.
Araport; AT4G32830; -.
TAIR; locus:2134103; AT4G32830.
eggNOG; KOG0580; Eukaryota.
eggNOG; ENOG410XNRB; LUCA.
HOGENOM; HOG000233016; -.
InParanoid; Q9M077; -.
KO; K08850; -.
OMA; WVQAHSR; -.
OrthoDB; EOG09360G97; -.
PhylomeDB; Q9M077; -.
PRO; PR:Q9M077; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; Q9M077; baseline and differential.
Genevisible; Q9M077; AT.
GO; GO:0009504; C:cell plate; IDA:TAIR.
GO; GO:0032133; C:chromosome passenger complex; IBA:GO_Central.
GO; GO:0000780; C:condensed nuclear chromosome, centromeric region; IBA:GO_Central.
GO; GO:0005874; C:microtubule; IDA:TAIR.
GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
GO; GO:0005730; C:nucleolus; IDA:TAIR.
GO; GO:0005634; C:nucleus; IDA:TAIR.
GO; GO:0009524; C:phragmoplast; IEA:UniProtKB-SubCell.
GO; GO:0005819; C:spindle; IDA:TAIR.
GO; GO:0005876; C:spindle microtubule; IBA:GO_Central.
GO; GO:0051233; C:spindle midzone; IBA:GO_Central.
GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0035175; F:histone kinase activity (H3-S10 specific); IDA:TAIR.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:TAIR.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0016572; P:histone phosphorylation; IDA:TAIR.
GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
GO; GO:0032465; P:regulation of cytokinesis; IBA:GO_Central.
InterPro; IPR030616; Aur.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
PANTHER; PTHR24350; PTHR24350; 1.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
ATP-binding; Cell cycle; Cell division; Complete proteome; Cytoplasm;
Cytoskeleton; Kinase; Membrane; Microtubule; Mitosis;
Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
Serine/threonine-protein kinase; Transferase.
CHAIN 1 294 Serine/threonine-protein kinase Aurora-1.
/FTId=PRO_0000270792.
DOMAIN 31 282 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 37 45 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
COMPBIAS 17 22 Poly-Ala.
ACT_SITE 154 154 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 60 60 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 176 176 Phosphoserine.
{ECO:0000250|UniProtKB:Q93V58}.
MOD_RES 185 185 Phosphothreonine.
{ECO:0000250|UniProtKB:Q38997}.
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


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