BZP63_ARATH
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 03-AUG-2022, entry version 108.
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};
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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 AlphaFoldDB; B9DGI8; -.
DR BioGRID; 18262; 34.
DR IntAct; B9DGI8; 32.
DR MINT; B9DGI8; -.
DR STRING; 3702.AT5G28770.2; -.
DR iPTMnet; B9DGI8; -.
DR PaxDb; B9DGI8; -.
DR PRIDE; B9DGI8; -.
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; locus:2184251; AT5G28770.
DR eggNOG; ENOG502QS0A; Eukaryota.
DR InParanoid; B9DGI8; -.
DR OMA; MKRGAFS; -.
DR OrthoDB; 1008484at2759; -.
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:0009649; P:entrainment of circadian clock; IMP:TAIR.
DR InterPro; IPR020983; Basic_leucine-zipper_C.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR Pfam; PF00170; bZIP_1; 1.
DR Pfam; PF12498; bZIP_C; 2.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 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
