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CDKA2_ORYSJ
ID   CDKA2_ORYSJ             Reviewed;         292 AA.
AC   P29619; B7ERM3; Q0E4E3; Q6Z721; Q6Z722;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 149.
DE   RecName: Full=Cyclin-dependent kinase A-2;
DE            Short=CDKA;2;
DE            EC=2.7.11.22;
DE            EC=2.7.11.23;
DE   AltName: Full=CDC2Os-2;
DE   AltName: Full=Cell division control protein 2 homolog 2;
GN   Name=CDKA-2; Synonyms=CDC2-2;
GN   OrderedLocusNames=Os02g0123100, LOC_Os02g03060;
GN   ORFNames=P0575F10.10-1, P0575F10.10-2;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=1376401; DOI=10.1007/bf00587555;
RA   Hashimoto J., Hirabayashi T., Hayano Y., Hata S., Ohashi Y., Suzuka I.,
RA   Utsugi T., Toh-e A., Kikuchi Y.;
RT   "Isolation and characterization of cDNA clones encoding cdc2 homologues
RT   from Oryza sativa: a functional homologue and cognate variants.";
RL   Mol. Gen. Genet. 233:10-16(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
RN   [6]
RP   TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=7742859; DOI=10.1046/j.1365-313x.1995.7040623.x;
RA   Sauter M., Mekhedov S.L., Kende H.;
RT   "Gibberellin promotes histone H1 kinase activity and the expression of cdc2
RT   and cyclin genes during the induction of rapid growth in deepwater rice
RT   internodes.";
RL   Plant J. 7:623-632(1995).
RN   [7]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=9076986; DOI=10.1046/j.1365-313x.1997.11020181.x;
RA   Sauter M.;
RT   "Differential expression of a CAK (cdc2-activating kinase)-like protein
RT   kinase, cyclins and cdc2 genes from rice during the cell cycle and in
RT   response to gibberellin.";
RL   Plant J. 11:181-190(1997).
RN   [8]
RP   INDUCTION.
RX   PubMed=9880342; DOI=10.1104/pp.119.1.21;
RA   Lorbiecke R., Sauter M.;
RT   "Adventitious root growth and cell-cycle induction in deepwater rice.";
RL   Plant Physiol. 119:21-30(1999).
RN   [9]
RP   TISSUE SPECIFICITY.
RX   PubMed=9880343; DOI=10.1104/pp.119.1.31;
RA   Umeda M., Umeda-Hara C., Yamaguchi M., Hashimoto J., Uchimiya H.;
RT   "Differential expression of genes for cyclin-dependent protein kinases in
RT   rice plants.";
RL   Plant Physiol. 119:31-40(1999).
RN   [10]
RP   INDUCTION AND GENE FAMILY.
RX   PubMed=17443292; DOI=10.1007/s11103-007-9154-y;
RA   Guo J., Song J., Wang F., Zhang X.S.;
RT   "Genome-wide identification and expression analysis of rice cell cycle
RT   genes.";
RL   Plant Mol. Biol. 64:349-360(2007).
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=2.7.11.22;
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=2.7.11.22;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho-
CC         [DNA-directed RNA polymerase]; Xref=Rhea:RHEA:10216, Rhea:RHEA-
CC         COMP:11321, Rhea:RHEA-COMP:11322, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546,
CC         ChEBI:CHEBI:456216; EC=2.7.11.23;
CC   -!- TISSUE SPECIFICITY: Expressed in the dividing region of the root apex
CC       and in differentiated cells such as those in the sclerenchyma,
CC       pericycle and parenchyma of the central cylinder. Expressed in the
CC       intercalary meristem and the elongation zone of internodes.
CC       {ECO:0000269|PubMed:7742859, ECO:0000269|PubMed:9880343}.
CC   -!- DEVELOPMENTAL STAGE: Expression reaches a peak in the G1/S phases and
CC       then decreases in the G2/M phases. {ECO:0000269|PubMed:9076986}.
CC   -!- INDUCTION: By gibberellic acid (GA3) and submergence. Down-regulated by
CC       auxin. {ECO:0000269|PubMed:17443292, ECO:0000269|PubMed:7742859,
CC       ECO:0000269|PubMed:9880342}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC       protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD07950.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; X60375; CAA42923.1; -; mRNA.
DR   EMBL; AP004885; BAD07949.1; -; Genomic_DNA.
DR   EMBL; AP004885; BAD07950.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP008208; BAF07645.1; -; Genomic_DNA.
DR   EMBL; AP014958; BAS76730.1; -; Genomic_DNA.
DR   EMBL; AK101344; BAG95020.1; -; mRNA.
DR   PIR; S22441; S22441.
DR   RefSeq; XP_015623588.1; XM_015768102.1.
DR   AlphaFoldDB; P29619; -.
DR   SMR; P29619; -.
DR   STRING; 4530.OS02T0123100-01; -.
DR   PaxDb; P29619; -.
DR   PRIDE; P29619; -.
DR   EnsemblPlants; Os02t0123100-03; Os02t0123100-03; Os02g0123100.
DR   GeneID; 4328135; -.
DR   Gramene; Os02t0123100-03; Os02t0123100-03; Os02g0123100.
DR   KEGG; osa:4328135; -.
DR   eggNOG; KOG0594; Eukaryota.
DR   HOGENOM; CLU_000288_181_6_1; -.
DR   InParanoid; P29619; -.
DR   PlantReactome; R-OSA-9640760; G1 phase.
DR   PlantReactome; R-OSA-9640887; G1/S transition.
DR   Proteomes; UP000000763; Chromosome 2.
DR   Proteomes; UP000059680; Chromosome 2.
DR   ExpressionAtlas; P29619; baseline and differential.
DR   Genevisible; P29619; OS.
DR   GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0030332; F:cyclin binding; IBA:GO_Central.
DR   GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IBA:GO_Central.
DR   GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR   GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; IBA:GO_Central.
DR   GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR   GO; GO:0051445; P:regulation of meiotic cell cycle; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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   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; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..292
FT                   /note="Cyclin-dependent kinase A-2"
FT                   /id="PRO_0000085756"
FT   DOMAIN          4..286
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        126
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         10..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         33
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         14
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         15
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         160
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   292 AA;  33693 MW;  C7791576349DFE22 CRC64;
     MEQYEKVEKI GEGTYGVVYK GKHRHTNETI ALKKIRLEQE DEGVPSTAIR EISLLKEMQH
     RNIVRLQDVV HKEKCIYLVF EYLDLDLKKH MDSSPDFKNH RIVKSFLYQI LRGIAYCHSH
     RVLHRDLKPQ NLLIDRRTNS LKLADFGLAR AFGIPVRTFT HEVVTLWYRA PEILLGARHY
     STPVDMWSVG CIFAEMVNQK PLFPGDSEID ELFKIFSIMG TPNEETWPGV ASLPDYISTF
     PKWPSVDLAT VVPTLDSSGL DLLSKMLRLD PSKRINARAA LEHEYFKDLE VA
 
 
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