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AUR1_ARATH
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   03-AUG-2022, entry version 159.
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.AT4G32830.1; -.
DR   PaxDb; Q9M077; -.
DR   PRIDE; Q9M077; -.
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; locus:2134103; AT4G32830.
DR   eggNOG; KOG0580; Eukaryota.
DR   HOGENOM; CLU_000288_63_0_1; -.
DR   InParanoid; Q9M077; -.
DR   OMA; EKEGMEH; -.
DR   OrthoDB; 954262at2759; -.
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:0032133; C:chromosome passenger complex; IBA:GO_Central.
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: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:0004674; F:protein serine/threonine kinase activity; IDA:TAIR.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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   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
 
 
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