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 29-MAY-2024, entry version 116. 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; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; 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., Kohara M., RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K., RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., RA Baker J., 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., Langham S.-A., RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., RA Bevan M., Fransz P.F.; RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis 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 reference RT 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., 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] (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., 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 [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 maize RT Opaque2 regulatory protein."; RL J. Mol. Evol. 56:105-116(2003). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-314 (ISOFORM 1), TISSUE SPECIFICITY, AND RP 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., Carbonero P., RA 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., Naeke C., RA Blazevic D., Grefen C., Schumacher K., Oecking C., 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., Schuetze K., RA Alonso R., Harter K., Vicente-Carbajosa J., Droege-Laser W.; RT "Combinatorial control of Arabidopsis proline dehydrogenase transcription RT by specific heterodimerisation of bZIP transcription 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 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 group RT 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., Wang X., RA Chaban C., Hanson J., Teige M., Harter K., Vicente-Carbajosa J., RA Smeekens S., Droege-Laser W.; RT "Expression patterns within the Arabidopsis C/S1 bZIP transcription factor RT network: availability of heterodimerization partners controls gene RT 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 domain of RT 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 signaling, RT protein networking, and DNA binding."; RL Mol. Plant 3:361-373(2010). RN [16] RP INTERACTION WITH KIN10; SNF4; BZIP1 AND BZIP11, SUBUNIT, PHOSPHORYLATION AT RP SER-29; SER-294 AND SER-300, MUTAGENESIS OF SER-29; SER-294 AND SER-300, RP FUNCTION, DISRUPTION PHENOTYPE, AND ACTIVITY REGULATION. RX PubMed=26263501; DOI=10.7554/elife.05828; RA Mair A., Pedrotti L., Wurzinger B., Anrather D., Simeunovic A., Weiste C., RA Valerio C., Dietrich K., Kirchler T., Naegele T., Vicente Carbajosa J., RA Hanson J., Baena-Gonzalez E., Chaban C., Weckwerth W., Droege-Laser W., RA 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 alternative RT mitochondrial metabolic pathways to ensure plant survival in extended RT darkness."; RL Plant Cell 30:495-509(2018). CC -!- FUNCTION: Transcription factor involved in controlling responses to CC starvation (PubMed:26263501). BZIP2-BZIP63-KIN10 complex binds to the CC ETFQO promoter to up-regulate its transcription (PubMed:29348240). CC {ECO:0000269|PubMed:26263501, ECO:0000269|PubMed:29348240}. CC -!- ACTIVITY REGULATION: Up-regulated by KIN10 under a phosphorylation- CC dependent manner. {ECO:0000269|PubMed:26263501}. CC -!- SUBUNIT: Homodimer. Forms a heterodimer with LSD1, BZIP1, BZIP2, BZIP9, CC BZIP10, BZIP11, BZIP25, BZIP44 and BZIP53. Interacts with KIN10 and CC SNF4 (PubMed:26263501). Component of a ternary complex composed of CC 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 B9DGI8; O22286: BPM3; NbExp=3; IntAct=EBI-942713, EBI-540923; CC B9DGI8; Q9FGX2: BZIP1; NbExp=4; IntAct=EBI-942713, EBI-942623; CC B9DGI8; O65683: BZIP11; NbExp=4; IntAct=EBI-942713, EBI-942769; CC B9DGI8; Q9SI15: BZIP2; NbExp=4; IntAct=EBI-942713, EBI-942735; CC B9DGI8; C0Z2L5: BZIP44; NbExp=4; IntAct=EBI-942713, EBI-942804; CC B9DGI8; Q9LZP8: BZIP53; NbExp=8; IntAct=EBI-942713, EBI-942845; CC B9DGI8; B9DGI8: BZIP63; NbExp=2; IntAct=EBI-942713, EBI-942713; CC B9DGI8; Q9LQT8: GAI; NbExp=3; IntAct=EBI-942713, EBI-963606; CC B9DGI8; Q8GXW1: RGL2; NbExp=5; IntAct=EBI-942713, EBI-963665; CC B9DGI8; Q9LF53: RGL3; NbExp=3; IntAct=EBI-942713, EBI-15681313; CC B9DGI8-2; C0SUZ3: At1g35490; NbExp=3; IntAct=EBI-15191817, EBI-15192249; CC B9DGI8-2; O22763-3: BZIP10; NbExp=3; IntAct=EBI-15191817, EBI-15191815; CC B9DGI8-2; C0Z2L5: BZIP44; NbExp=3; IntAct=EBI-15191817, EBI-942804; CC B9DGI8-2; O81002: BZIP6; NbExp=3; IntAct=EBI-15191817, EBI-3133475; CC B9DGI8-2; Q9SSE5: COL9; NbExp=3; IntAct=EBI-15191817, EBI-15197469; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978, CC 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 Name=3; CC IsoId=B9DGI8-3; Sequence=VSP_042642, VSP_042643; CC -!- TISSUE SPECIFICITY: Expressed in roots, shoots, young leaves, pollen, CC 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 Ser-300 CC by KIN10 strongly enhances its ability to form homo- as well as CC heterodimers and are then essential for its transcriptional activity CC (PubMed:26263501). {ECO:0000269|PubMed:20047775, CC ECO:0000269|PubMed:26263501}. CC -!- DISRUPTION PHENOTYPE: Starvation-related phenotype with reduced growth CC and accumulation of anthocyanins. {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=Truncated N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 AlphaFoldDB; B9DGI8; -. DR BioGRID; 18262; 34. DR IntAct; B9DGI8; 32. DR MINT; B9DGI8; -. DR STRING; 3702.B9DGI8; -. DR iPTMnet; B9DGI8; -. DR PaxDb; 3702-AT5G28770-2; -. DR ProteomicsDB; 240445; -. [B9DGI8-1] 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; AT5G28770; BZO2H3. DR eggNOG; ENOG502QS0A; Eukaryota. DR InParanoid; B9DGI8; -. DR OMA; DIAGHFW; -. DR OrthoDB; 393915at2759; -. DR PhylomeDB; B9DGI8; -. DR PRO; PR:B9DGI8; -. DR Proteomes; UP000006548; Chromosome 5. DR ExpressionAtlas; B9DGI8; baseline and differential. 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:0009649; P:entrainment of circadian clock; IMP:TAIR. DR Gene3D; 1.20.5.170; -; 1. DR InterPro; IPR020983; Basic_leucine-zipper_C. DR InterPro; IPR004827; bZIP. DR InterPro; IPR046347; bZIP_sf. DR PANTHER; PTHR46408; BASIC LEUCINE ZIPPER 63; 1. DR PANTHER; PTHR46408:SF10; BASIC LEUCINE ZIPPER 63; 1. DR Pfam; PF00170; bZIP_1; 1. DR Pfam; PF12498; bZIP_C; 2. DR SMART; SM00338; BRLZ; 1. DR SUPFAM; SSF57959; Leucine zipper domain; 1. DR PROSITE; PS50217; BZIP; 1. DR PROSITE; PS00036; BZIP_BASIC; 1. PE 1: Evidence at protein level; KW Alternative splicing; DNA-binding; Nucleus; Phosphoprotein; KW Reference proteome; Repeat; Transcription; Transcription regulation. FT CHAIN 1..314 FT /note="Basic leucine zipper 63" FT /id="PRO_0000416560" FT DOMAIN 151..214 FT /note="bZIP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978" FT REGION 94..177 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 153..172 FT /note="Basic motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978" FT REGION 179..193 FT /note="Leucine-zipper" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978" FT REGION 253..274 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 155..162 FT /note="Nuclear localization signal 1" FT /evidence="ECO:0000250" FT MOTIF 295..302 FT /note="Nuclear localization signal 2" FT /evidence="ECO:0000250" FT COMPBIAS 95..133 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 29 FT /note="Phosphoserine; by KIN10" FT /evidence="ECO:0000269|PubMed:26263501" FT MOD_RES 294 FT /note="Phosphoserine; by KIN10" FT /evidence="ECO:0000269|PubMed:26263501" FT MOD_RES 300 FT /note="Phosphoserine; by KIN10" FT /evidence="ECO:0000269|PubMed:26263501" FT VAR_SEQ 90..96 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14593172" FT /id="VSP_042641" FT VAR_SEQ 227..250 FT /note="MAEETVKRLTGFNPMFHNMPQIVS -> YFLLSLCLPKLAIEACLFLAGENG FT (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_042642" FT VAR_SEQ 251..314 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_042643" FT MUTAGEN 29 FT /note="S->A: Reduces its activity. Abolishes the formation FT of the BZIP2-BZIP63 heterodimer; when associated with A-294 FT and A-300." FT /evidence="ECO:0000269|PubMed:26263501, FT ECO:0000269|PubMed:29348240" FT MUTAGEN 160 FT /note="S->A: Normal DNA-binding." FT /evidence="ECO:0000269|PubMed:20047775" FT MUTAGEN 160 FT /note="S->D: Reduced DNA-binding to C-box motif." FT /evidence="ECO:0000269|PubMed:20047775" FT MUTAGEN 164 FT /note="S->A: Normal DNA-binding." FT /evidence="ECO:0000269|PubMed:20047775" FT MUTAGEN 164 FT /note="S->D: Impaired DNA-binding to C-box motif." FT /evidence="ECO:0000269|PubMed:20047775" FT MUTAGEN 168 FT /note="S->A: Normal DNA-binding." FT /evidence="ECO:0000269|PubMed:20047775" FT MUTAGEN 168 FT /note="S->D: Impaired DNA-binding to C-box motif." FT /evidence="ECO:0000269|PubMed:20047775" FT MUTAGEN 294 FT /note="S->A: Reduces activity. Abolishes the formation of FT the BZIP2-BZIP63 heterodimer; when associated with A-29 and FT A-300." FT /evidence="ECO:0000269|PubMed:26263501, FT ECO:0000269|PubMed:29348240" FT MUTAGEN 300 FT /note="S->A: Reduces activity. Abolishes the formation of FT the BZIP2-BZIP63 heterodimer; when associated with A-29 and FT A-294." FT /evidence="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 //