ID BZP63_ARATH Reviewed; 314 AA.
AC B9DGI8; F4KA11; Q712P1; Q940U4; Q9FUD2; Q9LKT9;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 10-OCT-2018, entry version 88.
DE RecName: Full=Basic leucine zipper 63;
DE Short=AtbZIP63;
DE Short=bZIP protein 63;
DE AltName: Full=Basic leucine zipper OPAQUE 2 homolog 3;
DE Short=Basic leucine zipper O2 homolog 3;
GN Name=BZIP63; Synonyms=BZO2H3; OrderedLocusNames=At5g28770;
GN ORFNames=T32B20.4;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K.,
RA Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
RA Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
RA Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
RA Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
RA Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
RA Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
RA Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
RA Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
RA Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
RA Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
RA Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S.,
RA Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
RA Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
RA van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
RA Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
RA Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
RA Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis
RT thaliana.";
RL Nature 408:823-826(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
RT reference genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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.,
RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA Yuan S., Shinozaki K., Davis R.W., Theologis A., 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] (ISOFORM 1).
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M.,
RA Seki M., 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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-191 (ISOFORM 1/3), AND GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=12569427; DOI=10.1007/s00239-002-2386-1;
RA Vincentz M., Bandeira-Kobarg C., Gauer L., Schloegl P., Leite A.;
RT "Evolutionary pattern of angiosperm bZIP factors homologous to the
RT maize Opaque2 regulatory protein.";
RL J. Mol. Evol. 56:105-116(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-314 (ISOFORM 1), TISSUE SPECIFICITY,
RP AND GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=12657652; DOI=10.1074/jbc.M210538200;
RA Lara P., Onate-Sanchez L., Abraham Z., Ferrandiz C., Diaz I.,
RA Carbonero P., Vicente-Carbajosa J.;
RT "Synergistic activation of seed storage protein gene expression in
RT Arabidopsis by ABI3 and two bZIPs related to OPAQUE2.";
RL J. Biol. Chem. 278:21003-21011(2003).
RN [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11906833; DOI=10.1016/S1360-1385(01)02223-3;
RA Jakoby M., Weisshaar B., Droege-Laser W., Vicente-Carbajosa J.,
RA Tiedemann J., Kroj T., Parcy F.;
RT "bZIP transcription factors in Arabidopsis.";
RL Trends Plant Sci. 7:106-111(2002).
RN [8]
RP INTERACTION WITH LSD1.
RX PubMed=15469500; DOI=10.1111/j.1365-313X.2004.02219.x;
RA Walter M., Chaban C., Schuetze K., Batistic O., Weckermann K.,
RA Naeke C., Blazevic D., Grefen C., Schumacher K., Oecking C.,
RA Harter K., Kudla J.;
RT "Visualization of protein interactions in living plant cells using
RT bimolecular fluorescence complementation.";
RL Plant J. 40:428-438(2004).
RN [9]
RP INTERACTION WITH BZIP53.
RX PubMed=16810321; DOI=10.1038/sj.emboj.7601206;
RA Weltmeier F., Ehlert A., Mayer C.S., Dietrich K., Wang X.,
RA Schuetze K., Alonso R., Harter K., Vicente-Carbajosa J.,
RA Droege-Laser W.;
RT "Combinatorial control of Arabidopsis proline dehydrogenase
RT transcription by specific heterodimerisation of bZIP transcription
RT factors.";
RL EMBO J. 25:3133-3143(2006).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=16957775; DOI=10.1038/sj.emboj.7601312;
RA Kaminaka H., Naeke C., Epple P., Dittgen J., Schuetze K., Chaban C.,
RA Holt B.F. III, Merkle T., Schaefer E., Harter K., Dangl J.L.;
RT "bZIP10-LSD1 antagonism modulates basal defense and cell death in
RT Arabidopsis following infection.";
RL EMBO J. 25:4400-4411(2006).
RN [11]
RP SUBUNIT.
RX PubMed=16731568; DOI=10.1093/molbev/msl022;
RA Deppmann C.D., Alvania R.S., Taparowsky E.J.;
RT "Cross-species annotation of basic leucine zipper factor interactions:
RT Insight into the evolution of closed interaction networks.";
RL Mol. Biol. Evol. 23:1480-1492(2006).
RN [12]
RP INTERACTION WITH BZIP1; BZIP2; BZIP9; BZIP10; BZIP11; BZIP44 AND
RP BZIP53.
RX PubMed=16709202; DOI=10.1111/j.1365-313X.2006.02731.x;
RA Ehlert A., Weltmeier F., Wang X., Mayer C.S., Smeekens S.,
RA Vicente-Carbajosa J., Droege-Laser W.;
RT "Two-hybrid protein-protein interaction analysis in Arabidopsis
RT protoplasts: establishment of a heterodimerization map of group C and
RT group S bZIP transcription factors.";
RL Plant J. 46:890-900(2006).
RN [13]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION BY GLUCOSE.
RC STRAIN=cv. Columbia;
RX PubMed=18841482; DOI=10.1007/s11103-008-9410-9;
RA Weltmeier F., Rahmani F., Ehlert A., Dietrich K., Schuetze K.,
RA Wang X., Chaban C., Hanson J., Teige M., Harter K.,
RA Vicente-Carbajosa J., Smeekens S., Droege-Laser W.;
RT "Expression patterns within the Arabidopsis C/S1 bZIP transcription
RT factor network: availability of heterodimerization partners controls
RT gene expression during stress response and development.";
RL Plant Mol. Biol. 69:107-119(2009).
RN [14]
RP PHOSPHORYLATION, AND MUTAGENESIS OF SER-160; SER-164 AND SER-168.
RX PubMed=20047775; DOI=10.1016/j.ejcb.2009.11.023;
RA Kirchler T., Briesemeister S., Singer M., Schuetze K., Keinath M.,
RA Kohlbacher O., Vicente-Carbajosa J., Teige M., Harter K., Chaban C.;
RT "The role of phosphorylatable serine residues in the DNA-binding
RT domain of Arabidopsis bZIP transcription factors.";
RL Eur. J. Cell Biol. 89:175-183(2010).
RN [15]
RP INTERACTION WITH BZIP1; BZIP10 AND BZIP25, AND SUBUNIT.
RX PubMed=20080816; DOI=10.1093/mp/ssp115;
RA Kang S.G., Price J., Lin P.-C., Hong J.C., Jang J.-C.;
RT "The arabidopsis bZIP1 transcription factor is involved in sugar
RT signaling, protein networking, and DNA binding.";
RL Mol. Plant 3:361-373(2010).
RN [16]
RP INTERACTION WITH KIN10; SNF4; BZIP1 AND BZIP11, SUBUNIT,
RP PHOSPHORYLATION AT SER-29; SER-294 AND SER-300, MUTAGENESIS OF SER-29;
RP SER-294 AND SER-300, FUNCTION, DISRUPTION PHENOTYPE, AND ACTIVITY
RP REGULATION.
RX PubMed=26263501; DOI=10.7554/eLife.05828;
RA Mair A., Pedrotti L., Wurzinger B., Anrather D., Simeunovic A.,
RA Weiste C., Valerio C., Dietrich K., Kirchler T., Naegele T.,
RA Vicente Carbajosa J., Hanson J., Baena-Gonzalez E., Chaban C.,
RA Weckwerth W., Droege-Laser W., Teige M.;
RT "SnRK1-triggered switch of bZIP63 dimerization mediates the low-energy
RT response in plants.";
RL Elife 4:0-0(2015).
RN [17]
RP MUTAGENESIS OF SER-29; SER-294 AND SER-300, INTERACTION WITH KIN10 AND
RP BZIP2, AND FUNCTION.
RX PubMed=29348240; DOI=10.1105/tpc.17.00414;
RA Pedrotti L., Weiste C., Naegele T., Wolf E., Lorenzin F., Dietrich K.,
RA Mair A., Weckwerth W., Teige M., Baena-Gonzalez E., Droege-Laser W.;
RT "Snf1-RELATED KINASE1-controlled C/S1-bZIP signaling activates
RT alternative mitochondrial metabolic pathways to ensure plant survival
RT in extended darkness.";
RL Plant Cell 30:495-509(2018).
CC -!- FUNCTION: Transcription factor involved in controlling responses
CC to starvation (PubMed:26263501). BZIP2-BZIP63-KIN10 complex binds
CC to the ETFQO promoter to up-regulate its transcription
CC (PubMed:29348240). {ECO:0000269|PubMed:26263501,
CC ECO:0000269|PubMed:29348240}.
CC -!- ACTIVITY REGULATION: Up-regulated by KIN10 under a
CC phosphorylation-dependent manner. {ECO:0000269|PubMed:26263501}.
CC -!- SUBUNIT: Homodimer. Forms a heterodimer with LSD1, BZIP1, BZIP2,
CC BZIP9, BZIP10, BZIP11, BZIP25, BZIP44 and BZIP53. Interacts with
CC KIN10 and SNF4 (PubMed:26263501). Component of a ternary complex
CC composed of BZIP2-BZIP63 heterodimer and KIN10 (PubMed:29348240).
CC {ECO:0000269|PubMed:16709202, ECO:0000269|PubMed:16731568,
CC ECO:0000269|PubMed:16810321, ECO:0000269|PubMed:20080816,
CC ECO:0000269|PubMed:26263501, ECO:0000269|PubMed:29348240}.
CC -!- INTERACTION:
CC Self; NbExp=2; IntAct=EBI-942713, EBI-942713;
CC C0SUZ3:At1g35490; NbExp=3; IntAct=EBI-15191817, EBI-15192249;
CC Q9FGX2:BZIP1; NbExp=4; IntAct=EBI-942713, EBI-942623;
CC O22763-3:BZIP10; NbExp=3; IntAct=EBI-15191817, EBI-15191815;
CC O65683:BZIP11; NbExp=4; IntAct=EBI-942713, EBI-942769;
CC Q9SI15:BZIP2; NbExp=4; IntAct=EBI-942713, EBI-942735;
CC C0Z2L5:BZIP44; NbExp=4; IntAct=EBI-942713, EBI-942804;
CC Q9LZP8:BZIP53; NbExp=8; IntAct=EBI-942713, EBI-942845;
CC O81002:bZIP6; NbExp=3; IntAct=EBI-15191817, EBI-3133475;
CC Q9SSE5:COL9; NbExp=3; IntAct=EBI-15191817, EBI-15197469;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
CC ProRule:PRU00978, ECO:0000269|PubMed:16957775}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=B9DGI8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=B9DGI8-2; Sequence=VSP_042641;
CC Note=No experimental confirmation available.;
CC Name=3;
CC IsoId=B9DGI8-3; Sequence=VSP_042642, VSP_042643;
CC Note=Derived from EST data. No experimental confirmation
CC available.;
CC -!- TISSUE SPECIFICITY: Expressed in roots, shoots, young leaves,
CC pollen, and flowers. {ECO:0000269|PubMed:12657652,
CC ECO:0000269|PubMed:18841482}.
CC -!- DEVELOPMENTAL STAGE: Present in silique valves, vasculature and
CC funiculi. {ECO:0000269|PubMed:18841482}.
CC -!- INDUCTION: Strongly repressed by glucose.
CC {ECO:0000269|PubMed:18841482}.
CC -!- PTM: Phosphorylated. The phosphorylation at Ser-29, Ser-294 and
CC Ser-300 by KIN10 strongly enhances its ability to form homo- as
CC well as hetero-dimers and are then essential for its
CC transcriptional activity (PubMed:26263501).
CC {ECO:0000269|PubMed:20047775, ECO:0000269|PubMed:26263501}.
CC -!- DISRUPTION PHENOTYPE: Starvation-related phenotype with reduced
CC growth and accumulation of anthocyanins.
CC {ECO:0000269|PubMed:26263501}.
CC -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF67360.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAC79656.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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DR EMBL; AF262041; AAF67360.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED93832.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93833.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93834.1; -; Genomic_DNA.
DR EMBL; AF446876; AAL38609.1; -; mRNA.
DR EMBL; AY052688; AAK96592.1; -; mRNA.
DR EMBL; AK317169; BAH19855.1; -; mRNA.
DR EMBL; AF310224; AAG25729.1; -; mRNA.
DR EMBL; AJ010858; CAC79656.1; ALT_INIT; mRNA.
DR RefSeq; NP_001031962.1; NM_001036885.2. [B9DGI8-3]
DR RefSeq; NP_568508.2; NM_122760.4. [B9DGI8-1]
DR RefSeq; NP_851088.1; NM_180757.3. [B9DGI8-2]
DR UniGene; At.15754; -.
DR ProteinModelPortal; B9DGI8; -.
DR SMR; B9DGI8; -.
DR BioGrid; 18262; 12.
DR IntAct; B9DGI8; 28.
DR MINT; B9DGI8; -.
DR STRING; 3702.AT5G28770.2; -.
DR iPTMnet; B9DGI8; -.
DR PaxDb; B9DGI8; -.
DR PRIDE; B9DGI8; -.
DR EnsemblPlants; AT5G28770.1; AT5G28770.1; AT5G28770. [B9DGI8-2]
DR EnsemblPlants; AT5G28770.2; AT5G28770.2; AT5G28770. [B9DGI8-1]
DR EnsemblPlants; AT5G28770.3; AT5G28770.3; AT5G28770. [B9DGI8-3]
DR GeneID; 832990; -.
DR Gramene; AT5G28770.1; AT5G28770.1; AT5G28770. [B9DGI8-2]
DR Gramene; AT5G28770.2; AT5G28770.2; AT5G28770. [B9DGI8-1]
DR Gramene; AT5G28770.3; AT5G28770.3; AT5G28770. [B9DGI8-3]
DR KEGG; ath:AT5G28770; -.
DR Araport; AT5G28770; -.
DR TAIR; locus:2184251; AT5G28770.
DR eggNOG; ENOG410IIE6; Eukaryota.
DR eggNOG; ENOG4111S51; LUCA.
DR HOGENOM; HOG000240492; -.
DR InParanoid; B9DGI8; -.
DR OMA; PMMSSAI; -.
DR OrthoDB; EOG09360JUP; -.
DR PhylomeDB; B9DGI8; -.
DR PRO; PR:B9DGI8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; B9DGI8; baseline and differential.
DR Genevisible; B9DGI8; AT.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
DR GO; GO:0071215; P:cellular response to abscisic acid stimulus; IEP:TAIR.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEP:UniProtKB.
DR GO; GO:0009267; P:cellular response to starvation; IMP:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR InterPro; IPR020983; Basic_leucine-zipper_C.
DR InterPro; IPR004827; bZIP.
DR Pfam; PF00170; bZIP_1; 1.
DR Pfam; PF12498; bZIP_C; 2.
DR SMART; SM00338; BRLZ; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation.
FT CHAIN 1 314 Basic leucine zipper 63.
FT /FTId=PRO_0000416560.
FT DOMAIN 151 214 bZIP. {ECO:0000255|PROSITE-
FT ProRule:PRU00978}.
FT REGION 153 172 Basic motif. {ECO:0000255|PROSITE-
FT ProRule:PRU00978}.
FT REGION 179 193 Leucine-zipper. {ECO:0000255|PROSITE-
FT ProRule:PRU00978}.
FT MOTIF 155 162 Nuclear localization signal 1.
FT {ECO:0000250}.
FT MOTIF 295 302 Nuclear localization signal 2.
FT {ECO:0000250}.
FT MOD_RES 29 29 Phosphoserine; by KIN10.
FT {ECO:0000269|PubMed:26263501}.
FT MOD_RES 294 294 Phosphoserine; by KIN10.
FT {ECO:0000269|PubMed:26263501}.
FT MOD_RES 300 300 Phosphoserine; by KIN10.
FT {ECO:0000269|PubMed:26263501}.
FT VAR_SEQ 90 96 Missing (in isoform 2).
FT {ECO:0000303|PubMed:14593172}.
FT /FTId=VSP_042641.
FT VAR_SEQ 227 250 MAEETVKRLTGFNPMFHNMPQIVS -> YFLLSLCLPKLAI
FT EACLFLAGENG (in isoform 3).
FT {ECO:0000305}.
FT /FTId=VSP_042642.
FT VAR_SEQ 251 314 Missing (in isoform 3). {ECO:0000305}.
FT /FTId=VSP_042643.
FT MUTAGEN 29 29 S->A: Reduces its activity. Abolishes the
FT formation of the BZIP2-BZIP63
FT heterodimer; when associated with A-294
FT and A-300. {ECO:0000269|PubMed:26263501,
FT ECO:0000269|PubMed:29348240}.
FT MUTAGEN 160 160 S->A: Normal DNA-binding.
FT {ECO:0000269|PubMed:20047775}.
FT MUTAGEN 160 160 S->D: Reduced DNA-binding to C-box motif.
FT {ECO:0000269|PubMed:20047775}.
FT MUTAGEN 164 164 S->A: Normal DNA-binding.
FT {ECO:0000269|PubMed:20047775}.
FT MUTAGEN 164 164 S->D: Impaired DNA-binding to C-box
FT motif. {ECO:0000269|PubMed:20047775}.
FT MUTAGEN 168 168 S->A: Normal DNA-binding.
FT {ECO:0000269|PubMed:20047775}.
FT MUTAGEN 168 168 S->D: Impaired DNA-binding to C-box
FT motif. {ECO:0000269|PubMed:20047775}.
FT MUTAGEN 294 294 S->A: Reduces activity. Abolishes the
FT formation of the BZIP2-BZIP63
FT heterodimer; when associated with A-29
FT and A-300. {ECO:0000269|PubMed:26263501,
FT ECO:0000269|PubMed:29348240}.
FT MUTAGEN 300 300 S->A: Reduces activity. Abolishes the
FT formation of the BZIP2-BZIP63
FT heterodimer; when associated with A-29
FT and A-294. {ECO:0000269|PubMed:26263501,
FT ECO:0000269|PubMed:29348240}.
SQ SEQUENCE 314 AA; 34311 MW; 37B85F20425DFF8B CRC64;
MEKVFSDEEI SGNHHWSVNG MTSLNRSASE WAFNRFIQES SAAADDGEST TACGVSVSSP
PNVPVDSEEY RAFLKSKLNL ACAAVAMKRG TFIKPQDTSG RSDNGGANES EQASLASSKA
TPMMSSAITS GSELSGDEEE ADGETNMNPT NVKRVKRMLS NRESARRSRR RKQAHLSELE
TQVSQLRVEN SKLMKGLTDV TQTFNDASVE NRVLKANIET LRAKVKMAEE TVKRLTGFNP
MFHNMPQIVS TVSLPSETSN SPDTTSSQVT TPEIISSGNK GKALIGCKMN RTASMRRVES
LEHLQKRIRS VGDQ
//