BZR2_ARATH
ID BZR2_ARATH Reviewed; 335 AA.
AC Q9LN63; Q8LCX8; Q94JU1; Q9SEG5;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Protein BRASSINAZOLE-RESISTANT 2 {ECO:0000303|PubMed:11970900};
DE AltName: Full=Protein 107;
DE AltName: Full=Protein BIN2 SUBSTRATE 1 {ECO:0000303|PubMed:12427989};
DE AltName: Full=Protein BRI1-EMS-SUPPRESSOR 1 {ECO:0000303|PubMed:12007405};
GN Name=BZR2 {ECO:0000303|PubMed:11970900};
GN Synonyms=BES1 {ECO:0000303|PubMed:12007405},
GN BIS1 {ECO:0000303|PubMed:12427989};
GN OrderedLocusNames=At1g19350 {ECO:0000312|Araport:AT1G19350};
GN ORFNames=F18O14_4 {ECO:0000312|EMBL:AAF79422.1};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Kwon H.-B.;
RT "Molecular cloning and characterization of a gibberellin-responsive gene
RT from Arabidopsis thaliana.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
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 [4]
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 [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 IDENTIFICATION.
RX PubMed=11970900; DOI=10.1016/s1534-5807(02)00153-3;
RA Wang Z.-Y., Nakano T., Gendron J., He J., Chen M., Vafeados D., Yang Y.,
RA Fujioka S., Yoshida S., Asami T., Chory J.;
RT "Nuclear-localized BZR1 mediates brassinosteroid-induced growth and
RT feedback suppression of brassinosteroid biosynthesis.";
RL Dev. Cell 2:505-513(2002).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION, SUBCELLULAR LOCATION, AND
RP MUTANT BES1-D.
RX PubMed=12007405; DOI=10.1016/s0092-8674(02)00721-3;
RA Yin Y., Wang Z.Y., Mora-Garcia S., Li J., Yoshida S., Asami T., Chory J.;
RT "BES1 accumulates in the nucleus in response to brassinosteroids to
RT regulate gene expression and promote stem elongation.";
RL Cell 109:181-191(2002).
RN [8]
RP PHOSPHORYLATION, SUBCELLULAR LOCATION, MUTANT BES1-101, AND INTERACTION
RP WITH ASK7/BIN2.
RX PubMed=12427989; DOI=10.1104/pp.102.010918;
RA Zhao J., Peng P., Schmitz R.J., Decker A.D., Tax F.E., Li J.;
RT "Two putative BIN2 substrates are nuclear components of brassinosteroid
RT signaling.";
RL Plant Physiol. 130:1221-1229(2002).
RN [9]
RP FUNCTION, DNA-BINDING, AND INTERACTION WITH ASK7/BIN2; BIM1; BIM2 AND BIM3.
RX PubMed=15680330; DOI=10.1016/j.cell.2004.11.044;
RA Yin Y., Vafeados D., Tao Y., Yoshida S., Asami T., Chory J.;
RT "A new class of transcription factors mediates brassinosteroid-regulated
RT gene expression in Arabidopsis.";
RL Cell 120:249-259(2005).
RN [10]
RP FUNCTION, AND INTERACTION WITH ELF6 AND REF6.
RX PubMed=18467490; DOI=10.1073/pnas.0802254105;
RA Yu X., Li L., Li L., Guo M., Chory J., Yin Y.;
RT "Modulation of brassinosteroid-regulated gene expression by Jumonji domain-
RT containing proteins ELF6 and REF6 in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:7618-7623(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-175, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [12]
RP FUNCTION, INTERACTION WITH MYB30, AND DOMAIN.
RX PubMed=19170933; DOI=10.1111/j.1365-313x.2008.03778.x;
RA Li L., Yu X., Thompson A., Guo M., Yoshida S., Asami T., Chory J., Yin Y.;
RT "Arabidopsis MYB30 is a direct target of BES1 and cooperates with BES1 to
RT regulate brassinosteroid-induced gene expression.";
RL Plant J. 58:275-286(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [14]
RP FUNCTION, AND INTERACTION WITH IWS1.
RX PubMed=20139304; DOI=10.1073/pnas.0909198107;
RA Li L., Ye H., Guo H., Yin Y.;
RT "Arabidopsis IWS1 interacts with transcription factor BES1 and is involved
RT in plant steroid hormone brassinosteroid regulated gene expression.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:3918-3923(2010).
RN [15]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH MYB56, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=24981610; DOI=10.1016/j.devcel.2014.05.020;
RA Vilarrasa-Blasi J., Gonzalez-Garcia M.P., Frigola D., Fabregas N.,
RA Alexiou K.G., Lopez-Bigas N., Rivas S., Jauneau A., Lohmann J.U.,
RA Benfey P.N., Ibanes M., Cano-Delgado A.I.;
RT "Regulation of plant stem cell quiescence by a brassinosteroid signaling
RT module.";
RL Dev. Cell 30:36-47(2014).
RN [16]
RP FUNCTION, INTERACTION WITH ASHH2/SDG8, AND SUBCELLULAR LOCATION.
RX PubMed=24838002; DOI=10.1093/mp/ssu056;
RA Wang X., Chen J., Xie Z., Liu S., Nolan T., Ye H., Zhang M., Guo H.,
RA Schnable P.S., Li Z., Yin Y.;
RT "Histone lysine methyltransferase SDG8 is involved in brassinosteroid-
RT regulated gene expression in Arabidopsis thaliana.";
RL Mol. Plant 7:1303-1315(2014).
RN [17]
RP INTERACTION WITH WRKY46; WRKY54 AND WRKY70.
RC STRAIN=cv. Columbia;
RX PubMed=28576847; DOI=10.1105/tpc.17.00364;
RA Chen J., Nolan T.M., Ye H., Zhang M., Tong H., Xin P., Chu J., Chu C.,
RA Li Z., Yin Y.;
RT "Arabidopsis WRKY46, WRKY54, and WRKY70 transcription factors are involved
RT in brassinosteroid-regulated plant growth and drought responses.";
RL Plant Cell 29:1425-1439(2017).
CC -!- FUNCTION: Positive regulator of brassinosteroid (BR) signaling.
CC Transcription factor that activates target gene expression by binding
CC specifically to the DNA sequence 5'-CANNTG-3'(E box) through its N-
CC terminal domain. Can bind individually to the promoter as a homodimer
CC or synergistically as a heterodimer with BIM1, BIM2 or BIM3. The C-
CC terminal domain is probably involved in transcriptional activation
CC (PubMed:12007405, PubMed:15680330, PubMed:18467490, PubMed:19170933).
CC Recruits the transcription elongation factor IWS1 to control BR-
CC regulated gene expression (PubMed:20139304). Forms a trimeric complex
CC with IWS1 and ASHH2/SDG8 to regulate BR-regulated gene expression
CC (PubMed:24838002). Promotes quiescent center (QC) self-renewal by cell
CC divisions in the primary root. Binds to the E-boxes of the BRAVO
CC promoter to repress its expression (PubMed:24981610).
CC {ECO:0000269|PubMed:12007405, ECO:0000269|PubMed:15680330,
CC ECO:0000269|PubMed:18467490, ECO:0000269|PubMed:19170933,
CC ECO:0000269|PubMed:20139304, ECO:0000269|PubMed:24838002,
CC ECO:0000269|PubMed:24981610}.
CC -!- SUBUNIT: Interacts with ASK7/BIN2 through its C-terminal domain and
CC with the bHLH transcription factors BIM1, BIM2 and BIM3 through its
CC C- and N-terminal domains. Interacts (via N-terminus) with REF6 and
CC ELF6 (PubMed:12427989, PubMed:15680330, PubMed:18467490). Interacts
CC with MYB30 (PubMed:19170933). Interacts with IWS1 (PubMed:20139304).
CC Interacts with ASHH2/SDG8 (PubMed:24838002). Binds to MYB56 when
CC dephosphorylated in the nucleus of quiescent center (QC) cells
CC (PubMed:24981610). Binds to WRKY46, WRKY54 and WRKY70 to cooperatively
CC regulate the expression of target genes (PubMed:28576847).
CC {ECO:0000269|PubMed:12427989, ECO:0000269|PubMed:15680330,
CC ECO:0000269|PubMed:18467490, ECO:0000269|PubMed:19170933,
CC ECO:0000269|PubMed:20139304, ECO:0000269|PubMed:24838002,
CC ECO:0000269|PubMed:24981610, ECO:0000269|PubMed:28576847}.
CC -!- INTERACTION:
CC Q9LN63; Q9C9A5: ARABIDOPSIS MYB-LIKE 2; NbExp=5; IntAct=EBI-617078, EBI-1546577;
CC Q9LN63; Q39011: ASK7; NbExp=2; IntAct=EBI-617078, EBI-1798250;
CC Q9LN63; Q9LEZ3: BIM1; NbExp=2; IntAct=EBI-617078, EBI-617095;
CC Q9LN63; Q6BDA0: ELF6; NbExp=3; IntAct=EBI-617078, EBI-1798417;
CC Q9LN63; O49413: IWS2; NbExp=3; IntAct=EBI-617078, EBI-15834301;
CC Q9LN63; Q9STM3: REF6; NbExp=2; IntAct=EBI-617078, EBI-1798387;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12007405,
CC ECO:0000269|PubMed:12427989, ECO:0000269|PubMed:24838002,
CC ECO:0000269|PubMed:24981610}. Cytoplasm {ECO:0000269|PubMed:12007405}.
CC Note=Brassinosteroid treatment triggers nuclear accumulation.
CC {ECO:0000269|PubMed:12007405}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9LN63-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in cotyledons, leaves,
CC hypocotyls and roots. {ECO:0000269|PubMed:12007405}.
CC -!- DOMAIN: The central part (140-272) is important for interaction with
CC MYB30. {ECO:0000269|PubMed:19170933}.
CC -!- PTM: Phosphorylated by ASK7/BIN2. Phosphorylation increases protein
CC degradation and/or interferes with the nuclear localization.
CC {ECO:0000269|PubMed:12007405, ECO:0000269|PubMed:12427989}.
CC -!- DISRUPTION PHENOTYPE: Reduced brassinosteroid (BR)-mediated quiescent
CC center (QC) cells division. {ECO:0000269|PubMed:24981610}.
CC -!- SIMILARITY: Belongs to the BZR/LAT61 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK50077.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF134217; AAF22161.1; -; mRNA.
DR EMBL; AC025808; AAF79422.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29834.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29836.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29837.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29838.1; -; Genomic_DNA.
DR EMBL; AY065041; AAL57677.1; -; mRNA.
DR EMBL; AF372937; AAK50077.1; ALT_INIT; mRNA.
DR EMBL; AY074829; AAL69527.1; -; mRNA.
DR EMBL; AY086340; AAM64408.1; -; mRNA.
DR EMBL; BK000396; DAA00023.1; -; mRNA.
DR PIR; G86326; G86326.
DR RefSeq; NP_001077562.1; NM_001084093.1. [Q9LN63-1]
DR RefSeq; NP_564081.1; NM_101792.4. [Q9LN63-1]
DR RefSeq; NP_973864.1; NM_202135.3. [Q9LN63-1]
DR RefSeq; NP_973865.1; NM_202136.1. [Q9LN63-1]
DR AlphaFoldDB; Q9LN63; -.
DR SMR; Q9LN63; -.
DR BioGRID; 23757; 29.
DR DIP; DIP-34780N; -.
DR IntAct; Q9LN63; 21.
DR STRING; 3702.AT1G19350.3; -.
DR iPTMnet; Q9LN63; -.
DR PaxDb; Q9LN63; -.
DR PRIDE; Q9LN63; -.
DR ProteomicsDB; 222825; -. [Q9LN63-1]
DR EnsemblPlants; AT1G19350.1; AT1G19350.1; AT1G19350. [Q9LN63-1]
DR EnsemblPlants; AT1G19350.4; AT1G19350.4; AT1G19350. [Q9LN63-1]
DR EnsemblPlants; AT1G19350.5; AT1G19350.5; AT1G19350. [Q9LN63-1]
DR EnsemblPlants; AT1G19350.6; AT1G19350.6; AT1G19350. [Q9LN63-1]
DR GeneID; 838518; -.
DR Gramene; AT1G19350.1; AT1G19350.1; AT1G19350. [Q9LN63-1]
DR Gramene; AT1G19350.4; AT1G19350.4; AT1G19350. [Q9LN63-1]
DR Gramene; AT1G19350.5; AT1G19350.5; AT1G19350. [Q9LN63-1]
DR Gramene; AT1G19350.6; AT1G19350.6; AT1G19350. [Q9LN63-1]
DR KEGG; ath:AT1G19350; -.
DR Araport; AT1G19350; -.
DR eggNOG; ENOG502QUKX; Eukaryota.
DR HOGENOM; CLU_036256_0_0_1; -.
DR InParanoid; Q9LN63; -.
DR PhylomeDB; Q9LN63; -.
DR PRO; PR:Q9LN63; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LN63; baseline and differential.
DR Genevisible; Q9LN63; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0071367; P:cellular response to brassinosteroid stimulus; IMP:UniProtKB.
DR GO; GO:1904961; P:quiescent center organization; IMP:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR InterPro; IPR008540; BES1_N.
DR InterPro; IPR033264; BZR.
DR PANTHER; PTHR31506; PTHR31506; 1.
DR Pfam; PF05687; BES1_N; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Brassinosteroid signaling pathway; Cytoplasm;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..335
FT /note="Protein BRASSINAZOLE-RESISTANT 2"
FT /id="PRO_0000113272"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 22..103
FT /note="Required for DNA-binding"
FT /evidence="ECO:0000250"
FT REGION 85..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..251
FT /note="PEST-like"
FT COMPBIAS 22..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 175
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19245862"
FT MUTAGEN 233
FT /note="P->L: In bes1-101/bes1-D; insensitive to
FT brassinazole; increased stability of the protein but no
FT effect on its phosphorylation."
FT CONFLICT 186
FT /note="P -> S (in Ref. 5; AAM64408)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="S -> F (in Ref. 1; AAF22161)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 335 AA; 36486 MW; 7B0AA929FED4748B CRC64;
MTSDGATSTS AAAAAAAMAT RRKPSWRERE NNRRRERRRR AVAAKIYTGL RAQGNYNLPK
HCDNNEVLKA LCSEAGWVVE EDGTTYRKGH KPLPGDMAGS SSRATPYSSH NQSPLSSTFD
SPILSYQVSP SSSSFPSPSR VGDPHNISTI FPFLRNGGIP SSLPPLRISN SAPVTPPVSS
PTSRNPKPLP TWESFTKQSM SMAAKQSMTS LNYPFYAVSA PASPTHHRQF HAPATIPECD
ESDSSTVDSG HWISFQKFAQ QQPFSASMVP TSPTFNLVKP APQQLSPNTA AIQEIGQSSE
FKFENSQVKP WEGERIHDVA MEDLELTLGN GKAHS
