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RBBP_ARATH
ID   RBBP_ARATH              Reviewed;         547 AA.
AC   Q5E915; B9DHL4; Q84W60; Q9LJC6;
DT   04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Protein RBL {ECO:0000303|PubMed:21423667};
DE   AltName: Full=COMPASS-like H3K4 histone methylation complex component RBL {ECO:0000303|PubMed:21423667};
DE   AltName: Full=RBBP5-like protein {ECO:0000303|PubMed:21423667};
DE            Short=AtRbBp5 {ECO:0000303|PubMed:23284292};
DE   AltName: Full=Retinoblastoma-binding protein-like {ECO:0000303|PubMed:21423667};
GN   Name=RBL {ECO:0000303|PubMed:21423667};
GN   OrderedLocusNames=At3g21060 {ECO:0000312|Araport:AT3G21060};
GN   ORFNames=MSA6.10 {ECO:0000312|EMBL:BAB01449.1};
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 {ECO:0000312|EMBL:AAX12875.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA   Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT   features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT   clones.";
RL   DNA Res. 7:217-221(2000).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Cheuk R., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 266-547.
RC   STRAIN=cv. Columbia;
RX   PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA   Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA   Shinozaki K.;
RT   "Analysis of multiple occurrences of alternative splicing events in
RT   Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL   DNA Res. 16:155-164(2009).
RN   [6]
RP   FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH TRO AND WDR5A, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=21423667; DOI=10.1371/journal.pgen.1001330;
RA   Jiang D., Kong N.C., Gu X., Li Z., He Y.;
RT   "Arabidopsis COMPASS-like complexes mediate histone H3 lysine-4
RT   trimethylation to control floral transition and plant development.";
RL   PLoS Genet. 7:E1001330-E1001330(2011).
RN   [7]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=cv. Wassilewskija;
RX   PubMed=23284292; DOI=10.1371/journal.pgen.1003111;
RA   Ding Y., Ndamukong I., Xu Z., Lapko H., Fromm M., Avramova Z.;
RT   "ATX1-generated H3K4me3 is required for efficient elongation of
RT   transcription, not initiation, at ATX1-regulated genes.";
RL   PLoS Genet. 8:E1003111-E1003111(2012).
CC   -!- FUNCTION: Promotes the expression of FLC and FLC homologs to repress
CC       the floral transition (PubMed:21423667). Promotes WRKY70 and LTP7 genes
CC       epigenetic methylation (e.g. H3K4me3) and subsequent expression
CC       (PubMed:23284292). {ECO:0000269|PubMed:21423667,
CC       ECO:0000269|PubMed:23284292}.
CC   -!- SUBUNIT: Part of a complex composed of TRO, RBL and WDR5A. Interacts
CC       with TRO and WDR5A, but not with WDR5B. This complex is formed during
CC       both vegetative and reproductive development.
CC       {ECO:0000269|PubMed:21423667}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21423667}.
CC   -!- TISSUE SPECIFICITY: Strongly expressed in root tips, shoot apices,
CC       vascular tissues, developing embryos and endosperms.
CC       {ECO:0000269|PubMed:21423667}.
CC   -!- DISRUPTION PHENOTYPE: Eearly flowering (PubMed:23284292). Significantly
CC       reduced trimethylated 'Lys-4' of histone H3 (H3K4me3) levels at the 5'-
CC       ends of WRKY70 and LTP7 genes leading to reduced transcript
CC       accumulation (PubMed:23284292). {ECO:0000269|PubMed:23284292}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB01449.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AP000604; BAB01449.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002686; AEE76455.1; -; Genomic_DNA.
DR   EMBL; BT004200; AAO42218.1; -; mRNA.
DR   EMBL; BT021105; AAX12875.1; -; mRNA.
DR   EMBL; AK317567; BAH20231.1; -; mRNA.
DR   RefSeq; NP_188743.3; NM_113000.6.
DR   AlphaFoldDB; Q5E915; -.
DR   SMR; Q5E915; -.
DR   STRING; 3702.AT3G21060.1; -.
DR   iPTMnet; Q5E915; -.
DR   PaxDb; Q5E915; -.
DR   PRIDE; Q5E915; -.
DR   ProteomicsDB; 236506; -.
DR   EnsemblPlants; AT3G21060.1; AT3G21060.1; AT3G21060.
DR   GeneID; 821658; -.
DR   Gramene; AT3G21060.1; AT3G21060.1; AT3G21060.
DR   KEGG; ath:AT3G21060; -.
DR   Araport; AT3G21060; -.
DR   TAIR; locus:2092930; AT3G21060.
DR   eggNOG; KOG1273; Eukaryota.
DR   HOGENOM; CLU_032142_2_2_1; -.
DR   InParanoid; Q5E915; -.
DR   OMA; DYEDDIM; -.
DR   OrthoDB; 1001705at2759; -.
DR   PhylomeDB; Q5E915; -.
DR   PRO; PR:Q5E915; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q5E915; baseline and differential.
DR   Genevisible; Q5E915; AT.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0048188; C:Set1C/COMPASS complex; IBA:GO_Central.
DR   GO; GO:0051568; P:histone H3-K4 methylation; IBA:GO_Central.
DR   GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IMP:TAIR.
DR   Gene3D; 2.130.10.10; -; 2.
DR   InterPro; IPR037850; RBBP5/Swd1.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR44040; PTHR44040; 1.
DR   Pfam; PF00400; WD40; 4.
DR   SMART; SM00320; WD40; 5.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 3.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Nucleus; Reference proteome; Repeat; WD repeat.
FT   CHAIN           1..547
FT                   /note="Protein RBL"
FT                   /id="PRO_0000431781"
FT   REPEAT          21..60
FT                   /note="WD 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          65..104
FT                   /note="WD 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          214..253
FT                   /note="WD 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          285..332
FT                   /note="WD 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          334..373
FT                   /note="WD 5"
FT                   /evidence="ECO:0000255"
FT   REGION          466..547
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        467..481
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        487..508
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        220
FT                   /note="K -> E (in Ref. 3; AAO42218)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   547 AA;  60142 MW;  7D2B3C5ACBF23375 CRC64;
     MNAPIIDPLQ GDFPEVIEEY LEHGVIKCVA FNHRGSLLAA GCADGGCVIW DFETRGIAKE
     IRDNDCSAAI TSVSWSKYGH RLLVSAADKS LTLWDVSTGE KIARTILQQT PLQARLNPGL
     SSPSLCLACP LSSAPMIVDF DIDCTTLLPV SVPEMPDVLA PPQRSKCPES NPPFSPAAAC
     FNKCGDLVYI GNSKGEILIV DYKSVRVLAL VSASGAAPVK NIVFSRNGQY LLTNSHDRTI
     RIYENLLPAK NVLKSLEDLG KNIDGLDGIE KMKTVGSKCL TLFREFQDSV TKMHWKAPCF
     SGDGEWVVGG SACKGEHKIY IWDRAGHLVK ILEGPKEALI DLAWHPVHPI IVSVSLAGLV
     YIWAKDYTEN WSAFAPDFKE LEENEEYVER EDEFDLIPET EKVKVLDVNE DEEVDIDTVE
     KDAFSDSDMS VEELRYLPAE PIPDTNDQQD NLVESIKLIE GQISASPASE EAGQNGHHAS
     SPQAEEMGET RGKRKRKPSE KAMELQAEKA KPLKGSGKTV RAKNRAAFDQ ETDDSINGGD
     DDDDAYY
 
 
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