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Transcription factor MYC2 (AtMYC2) (Basic helix-loop-helix protein 6) (AtbHLH6) (bHLH 6) (Protein JASMONATE INSENSITIVE 1) (R-homologous Arabidopsis protein 1) (RAP-1) (Transcription factor EN 38) (Z-box binding factor 1 protein) (bHLH transcription factor bHLH006) (rd22BP1)

 MYC2_ARATH              Reviewed;         623 AA.
Q39204; O48644; Q5K1L7; Q8W2F4; Q9LPJ8;
22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
22-AUG-2003, sequence version 2.
25-OCT-2017, entry version 144.
RecName: Full=Transcription factor MYC2;
Short=AtMYC2;
AltName: Full=Basic helix-loop-helix protein 6;
Short=AtbHLH6;
Short=bHLH 6;
AltName: Full=Protein JASMONATE INSENSITIVE 1;
AltName: Full=R-homologous Arabidopsis protein 1;
Short=RAP-1;
AltName: Full=Transcription factor EN 38;
AltName: Full=Z-box binding factor 1 protein;
AltName: Full=bHLH transcription factor bHLH006;
AltName: Full=rd22BP1;
Name=MYC2; Synonyms=BHLH6, EN38, JAI1, JIN1, RAP1, RD22BP1, ZBF1;
OrderedLocusNames=At1g32640; ORFNames=F6N18.4;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. C24;
PubMed=9177323; DOI=10.1023/A:1005898823105;
de Pater S., Pham K., Memelink J., Kijne J.;
"RAP-1 is an Arabidopsis MYC-like R protein homologue, that binds to
G-box sequence motifs.";
Plant Mol. Biol. 34:169-174(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INDUCTION.
STRAIN=cv. Columbia;
PubMed=9368419; DOI=10.1105/tpc.9.10.1859;
Abe H., Yamaguchi-Shinozaki K., Urao T., Iwasaki T., Hosokawa D.,
Shinozaki K.;
"Role of Arabidopsis MYC and MYB homologs in drought- and abscisic
acid-regulated gene expression.";
Plant Cell 9:1859-1868(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
PubMed=15923349; DOI=10.1105/tpc.105.032060;
Yadav V., Mallappa C., Gangappa S.N., Bhatia S., Chattopadhyay S.;
"A basic helix-loop-helix transcription factor in Arabidopsis, MYC2,
acts as a repressor of blue light-mediated photomorphogenic growth.";
Plant Cell 17:1953-1966(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[5]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 12-458, TISSUE SPECIFICITY, INDUCTION BY
UV LIGHT, GENE FAMILY, AND NOMENCLATURE.
STRAIN=cv. Columbia;
PubMed=12679534; DOI=10.1093/molbev/msg088;
Heim M.A., Jakoby M., Werber M., Martin C., Weisshaar B., Bailey P.C.;
"The basic helix-loop-helix transcription factor family in plants: a
genome-wide study of protein structure and functional diversity.";
Mol. Biol. Evol. 20:735-747(2003).
[8]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=12509522; DOI=10.1105/tpc.006130;
Abe H., Urao T., Ito T., Seki M., Shinozaki K.,
Yamaguchi-Shinozaki K.;
"Arabidopsis AtMYC2 (bHLH) and AtMYB2 (MYB) function as
transcriptional activators in abscisic acid signaling.";
Plant Cell 15:63-78(2003).
[9]
GENE FAMILY.
PubMed=12897250; DOI=10.1105/tpc.013839;
Toledo-Ortiz G., Huq E., Quail P.H.;
"The Arabidopsis basic/helix-loop-helix transcription factor family.";
Plant Cell 15:1749-1770(2003).
[10]
GENE FAMILY, AND NOMENCLATURE.
PubMed=14600211; DOI=10.1105/tpc.151140;
Bailey P.C., Martin C., Toledo-Ortiz G., Quail P.H., Huq E.,
Heim M.A., Jakoby M., Werber M., Weisshaar B.;
"Update on the basic helix-loop-helix transcription factor gene family
in Arabidopsis thaliana.";
Plant Cell 15:2497-2502(2003).
[11]
FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND INDUCTION BY
ABSCISIC ACID AND JASMONIC ACID.
PubMed=15208388; DOI=10.1105/tpc.022319;
Lorenzo O., Chico J.M., Sanchez-Serrano J.J., Solano R.;
"JASMONATE-INSENSITIVE1 encodes a MYC transcription factor essential
to discriminate between different jasmonate-regulated defense
responses in Arabidopsis.";
Plant Cell 16:1938-1950(2004).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=cv. Columbia;
PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,
Andreasson E., Rathjen J.P., Peck S.C.;
"Phosphoproteomic analysis of nuclei-enriched fractions from
Arabidopsis thaliana.";
J. Proteomics 72:439-451(2009).
[13]
INTERACTION WITH TIFY10A/JAZ1; TIFY10B/JAZ2; TIFY6B/JAZ3; TIFY6A/JAZ4;
TIFY11A/JAZ5; TIFY11B/JAZ6; TIFY5A/JAZ8; TIFY7/JAZ9; TIFY9/JAZ10;
TIFY3A/JAZ11 AND TIFY3B/JAZ12.
PubMed=19309455; DOI=10.1111/j.1365-313X.2009.03852.x;
Chini A., Fonseca S., Chico J.M., Fernandez-Calvo P., Solano R.;
"The ZIM domain mediates homo- and heteromeric interactions between
Arabidopsis JAZ proteins.";
Plant J. 59:77-87(2009).
[14]
FUNCTION, AND INTERACTION WITH TIFY10A/JAZ1; TIFY6B/JAZ3 AND
TIFY7/JAZ9.
PubMed=21321051; DOI=10.1093/jxb/erq408;
Niu Y., Figueroa P., Browse J.;
"Characterization of JAZ-interacting bHLH transcription factors that
regulate jasmonate responses in Arabidopsis.";
J. Exp. Bot. 62:2143-2154(2011).
[15]
FUNCTION, INTERACTION WITH TIFY10A/JAZ1; TIFY10B/JAZ2; TIFY6B/JAZ3;
TIFY11A/JAZ5; TIFY11B/JAZ6; TIFY5A/JAZ8; TIFY7/JAZ9; TIFY9/JAZ10;
TIFY3A/JAZ11; TIFY3B/JAZ12; MYC3 AND AFPH2/NINJA, SUBUNIT, DOMAIN,
SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
PubMed=21335373; DOI=10.1105/tpc.110.080788;
Fernandez-Calvo P., Chini A., Fernandez-Barbero G., Chico J.M.,
Gimenez-Ibanez S., Geerinck J., Eeckhout D., Schweizer F., Godoy M.,
Franco-Zorrilla J.M., Pauwels L., Witters E., Puga M.I., Paz-Ares J.,
Goossens A., Reymond P., De Jaeger G., Solano R.;
"The Arabidopsis bHLH transcription factors MYC3 and MYC4 are targets
of JAZ repressors and act additively with MYC2 in the activation of
jasmonate responses.";
Plant Cell 23:701-715(2011).
[16]
FUNCTION.
PubMed=21954460; DOI=10.1105/tpc.111.089870;
Chen Q., Sun J., Zhai Q., Zhou W., Qi L., Xu L., Wang B., Chen R.,
Jiang H., Qi J., Li X., Palme K., Li C.;
"The basic helix-loop-helix transcription factor MYC2 directly
represses PLETHORA expression during jasmonate-mediated modulation of
the root stem cell niche in Arabidopsis.";
Plant Cell 23:3335-3352(2011).
[17]
INTERACTION WITH TIC.
PubMed=22693280; DOI=10.1105/tpc.111.095430;
Shin J., Heidrich K., Sanchez-Villarreal A., Parker J.E., Davis S.J.;
"TIME FOR COFFEE represses accumulation of the MYC2 transcription
factor to provide time-of-day regulation of jasmonate signaling in
Arabidopsis.";
Plant Cell 24:2470-2482(2012).
[18]
INTERACTION WITH MED25.
PubMed=22822206; DOI=10.1105/tpc.112.098277;
Chen R., Jiang H., Li L., Zhai Q., Qi L., Zhou W., Liu X., Li H.,
Zheng W., Sun J., Li C.;
"The Arabidopsis mediator subunit MED25 differentially regulates
jasmonate and abscisic acid signaling through interacting with the
MYC2 and ABI5 transcription factors.";
Plant Cell 24:2898-2916(2012).
[19]
FUNCTION, AND INTERACTION WITH RGA.
PubMed=22669881; DOI=10.1105/tpc.112.098749;
Hong G.J., Xue X.Y., Mao Y.B., Wang L.J., Chen X.Y.;
"Arabidopsis MYC2 interacts with DELLA proteins in regulating
sesquiterpene synthase gene expression.";
Plant Cell 24:2635-2648(2012).
[20]
SUBCELLULAR LOCATION, AND DOMAIN.
PubMed=23169619; DOI=10.1073/pnas.1210054109;
Withers J., Yao J., Mecey C., Howe G.A., Melotto M., He S.Y.;
"Transcription factor-dependent nuclear localization of a
transcriptional repressor in jasmonate hormone signaling.";
Proc. Natl. Acad. Sci. U.S.A. 109:20148-20153(2012).
[21]
FUNCTION, AND REVIEW.
PubMed=23142764; DOI=10.1093/mp/sss128;
Kazan K., Manners J.M.;
"MYC2: the master in action.";
Mol. Plant 6:686-703(2013).
[22]
FUNCTION, INDUCTION BY METHYL JASMONATE, PHOSPHORYLATION AT THR-328,
DOMAIN, AND MUTAGENESIS OF THR-328; SER-330; SER-334 AND THR-336.
PubMed=23593022; DOI=10.1371/journal.pgen.1003422;
Zhai Q., Yan L., Tan D., Chen R., Sun J., Gao L., Dong M.Q., Wang Y.,
Li C.;
"Phosphorylation-coupled proteolysis of the transcription factor MYC2
is important for jasmonate-signaled plant immunity.";
PLoS Genet. 9:E1003422-E1003422(2013).
[23]
FUNCTION, DISRUPTION PHENOTYPE, DOMAIN, INTERACTION WITH MYB28; MYB29;
MYB34; MYB51; MYB76 AND MYB122, AND INDUCTION BY HERBIVORY.
PubMed=23943862; DOI=10.1105/tpc.113.115139;
Schweizer F., Fernandez-Calvo P., Zander M., Diez-Diaz M., Fonseca S.,
Glauser G., Lewsey M.G., Ecker J.R., Solano R., Reymond P.;
"Arabidopsis basic helix-loop-helix transcription factors MYC2, MYC3,
and MYC4 regulate glucosinolate biosynthesis, insect performance, and
feeding behavior.";
Plant Cell 25:3117-3132(2013).
[24]
INTERACTION WITH JAZ13.
PubMed=25846245; DOI=10.1111/tpj.12841;
Thireault C., Shyu C., Yoshida Y., St Aubin B., Campos M.L.,
Howe G.A.;
"Repression of jasmonate signaling by a non-TIFY JAZ protein in
Arabidopsis.";
Plant J. 82:669-679(2015).
-!- FUNCTION: Transcriptional activator. Common transcription factor
of light, abscisic acid (ABA), and jasmonic acid (JA) signaling
pathways. With MYC3 and MYC4, controls additively subsets of JA-
dependent responses. In cooperation with MYB2 is involved in the
regulation of ABA-inducible genes under drought stress conditions.
Can form complexes with all known glucosinolate-related MYBs to
regulate glucosinolate biosynthesis. Binds to the MYC recognition
site (5'-CACATG-3'), and to the G-box (5'-CACNTG-3') and Z-box
(5'-ATACGTGT-3') of promoters. Binds directly to the promoters of
the transcription factors PLETHORA1 (PLT1) and PLT2 and represses
their expression. Negative regulator of blue light-mediated
photomorphogenic growth and blue- and far-red-light regulated gene
expression. Activates multiple TIFY/JAZ promoters. Positive
regulator of lateral root formation. Regulates sesquiterpene
biosynthesis. Subjected to proteasome-dependent proteolysis. The
presence of the destruction element (DE) involved in turnover is
required for the function to regulate gene transcription.
{ECO:0000269|PubMed:12509522, ECO:0000269|PubMed:15208388,
ECO:0000269|PubMed:15923349, ECO:0000269|PubMed:21321051,
ECO:0000269|PubMed:21335373, ECO:0000269|PubMed:21954460,
ECO:0000269|PubMed:22669881, ECO:0000269|PubMed:23142764,
ECO:0000269|PubMed:23593022, ECO:0000269|PubMed:23943862,
ECO:0000269|PubMed:9368419}.
-!- SUBUNIT: Homo- and heterodimer. Efficient DNA binding requires
dimerization with another bHLH protein (By similarity). Interacts
(via N-terminus) with RGA, (via TAD domain) with the mediator
subunit MED25, with TIC, MYC3, AFPH2/NINJA and the JAZ repressors
TIFY10A/JAZ1, TIFY10B/JAZ2, TIFY6B/JAZ3, TIFY6A/JAZ4,
TIFY11A/JAZ5, TIFY11B/JAZ6, TIFY5A/JAZ8, TIFY7/JAZ9, TIFY9/JAZ10,
TIFY3A/JAZ11 and TIFY3B/JAZ12. Interacts with JAZ13 (via jas
motif) (PubMed:25846245). Interacts with MYB28, MYB29, MYB34,
MYB51, MYB76, MYB122 and mybe MYB2. {ECO:0000250,
ECO:0000269|PubMed:19309455, ECO:0000269|PubMed:21321051,
ECO:0000269|PubMed:21335373, ECO:0000269|PubMed:22669881,
ECO:0000269|PubMed:22693280, ECO:0000269|PubMed:22822206,
ECO:0000269|PubMed:23943862, ECO:0000269|PubMed:25846245}.
-!- INTERACTION:
Q9LMA8:TIFY10A; NbExp=10; IntAct=EBI-1792336, EBI-1388539;
Q9S7M2:TIFY10B; NbExp=5; IntAct=EBI-1792336, EBI-1792563;
Q9LDU5:TIFY11A; NbExp=5; IntAct=EBI-1792336, EBI-2312095;
Q9C9E3:TIFY11B; NbExp=7; IntAct=EBI-1792336, EBI-2312120;
Q9M246:TIFY3A; NbExp=5; IntAct=EBI-1792336, EBI-2312209;
Q9C5K8:TIFY3B; NbExp=7; IntAct=EBI-1792336, EBI-2312231;
Q8LBM2:TIFY5A; NbExp=7; IntAct=EBI-1792336, EBI-2312143;
Q9LVI4:TIFY6B; NbExp=6; IntAct=EBI-1792336, EBI-1792431;
Q8W4J8:TIFY7; NbExp=13; IntAct=EBI-1792336, EBI-1792583;
Q93ZM9:TIFY9; NbExp=2; IntAct=EBI-1792336, EBI-2312172;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00981, ECO:0000269|PubMed:15208388,
ECO:0000269|PubMed:21335373, ECO:0000269|PubMed:23169619}.
-!- TISSUE SPECIFICITY: Widely expressed in the whole plant with the
highest expression in stem. Constitutively expressed in dark- and
light-grown seedlings. {ECO:0000269|PubMed:12679534,
ECO:0000269|PubMed:15923349}.
-!- INDUCTION: Detected early after abscisic acid (ABA) treatment or
after dehydration and high-salt stresses. Induced by UV treatment.
Up-regulated by methyl jasmonate and herbivory.
{ECO:0000269|PubMed:12679534, ECO:0000269|PubMed:15208388,
ECO:0000269|PubMed:23593022, ECO:0000269|PubMed:23943862,
ECO:0000269|PubMed:9368419}.
-!- DOMAIN: The transcriptional activation domain (TAD) (149-188)
overlaps with the destruction element (DE) (154-165).
{ECO:0000269|PubMed:23593022}.
-!- DOMAIN: The JAZ-interaction domain (JID) (93-160) is sufficient
for interaction with MYB proteins and most of the TIFY/JAZ
proteins (PubMed:21335373 and PubMed:23943862).
-!- DOMAIN: The C-terminal half contains an active nuclear
localization signal (NLS). {ECO:0000269|PubMed:23169619}.
-!- PTM: The phosphorylation at Thr-328 is increased by methyl
jasmonate treatment, facilitates the proteolysis of the protein
and is coupled to transcription activity.
{ECO:0000269|PubMed:23593022}.
-!- DISRUPTION PHENOTYPE: Minor effect on jasmonic acid response and
no effect on glucosinolate biosynthesis, but decreased abscisic
acid sensitivity. Myc2 and myc3 double mutant has an increased
insensitivity to jasmonic acid. Myc2 and myc4 double mutant has an
increased insensitivity to jasmonic acid. Myc2, myc3 and myc4
triple mutant has no jasmonate-related defense response, is devoid
of glucosinolates and is extremely susceptible to generalist
herbivores. {ECO:0000269|PubMed:12509522,
ECO:0000269|PubMed:15208388, ECO:0000269|PubMed:21335373,
ECO:0000269|PubMed:23943862}.
-!- SEQUENCE CAUTION:
Sequence=BAA25078.1; Type=Frameshift; Positions=353, 360; Evidence={ECO:0000305};
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EMBL; X99548; CAA67885.2; -; mRNA.
EMBL; AB000875; BAA25078.1; ALT_FRAME; mRNA.
EMBL; AJ843256; CAH58735.1; -; mRNA.
EMBL; AC017118; AAF25980.1; -; Genomic_DNA.
EMBL; CP002684; AEE31513.1; -; Genomic_DNA.
EMBL; AY037203; AAK59788.1; -; mRNA.
EMBL; BT003042; AAO23607.1; -; mRNA.
EMBL; AF251691; AAL55713.1; -; mRNA.
PIR; T52293; T52293.
RefSeq; NP_174541.1; NM_102998.4.
UniGene; At.22648; -.
PDB; 5GNJ; X-ray; 2.70 A; A/B/E/F/G/I/M/N=446-525.
PDBsum; 5GNJ; -.
ProteinModelPortal; Q39204; -.
SMR; Q39204; -.
BioGrid; 25392; 48.
DIP; DIP-40533N; -.
IntAct; Q39204; 17.
STRING; 3702.AT1G32640.1; -.
iPTMnet; Q39204; -.
PaxDb; Q39204; -.
EnsemblPlants; AT1G32640.1; AT1G32640.1; AT1G32640.
GeneID; 840158; -.
Gramene; AT1G32640.1; AT1G32640.1; AT1G32640.
KEGG; ath:AT1G32640; -.
Araport; AT1G32640; -.
TAIR; locus:2035609; AT1G32640.
eggNOG; ENOG410IGFU; Eukaryota.
eggNOG; ENOG410YCJJ; LUCA.
HOGENOM; HOG000238207; -.
InParanoid; Q39204; -.
KO; K13422; -.
OMA; PSMWIND; -.
OrthoDB; EOG093607T9; -.
PhylomeDB; Q39204; -.
PRO; PR:Q39204; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q39204; baseline and differential.
Genevisible; Q39204; AT.
GO; GO:0005634; C:nucleus; IDA:TAIR.
GO; GO:0003677; F:DNA binding; IDA:TAIR.
GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:TAIR.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; ISS:TAIR.
GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0009963; P:positive regulation of flavonoid biosynthetic process; IEP:TAIR.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:TAIR.
GO; GO:2000068; P:regulation of defense response to insect; IMP:TAIR.
GO; GO:0051090; P:regulation of sequence-specific DNA binding transcription factor activity; IMP:TAIR.
GO; GO:0043619; P:regulation of transcription from RNA polymerase II promoter in response to oxidative stress; IMP:TAIR.
GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
GO; GO:0010200; P:response to chitin; IEP:TAIR.
GO; GO:0009269; P:response to desiccation; IEP:TAIR.
GO; GO:0009753; P:response to jasmonic acid; IMP:TAIR.
GO; GO:0009611; P:response to wounding; IEP:TAIR.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd00083; HLH; 1.
Gene3D; 4.10.280.10; -; 1.
InterPro; IPR011598; bHLH_dom.
InterPro; IPR036638; HLH_DNA-bd_sf.
InterPro; IPR025610; MYC/MYB_N.
Pfam; PF14215; bHLH-MYC_N; 1.
Pfam; PF00010; HLH; 1.
SMART; SM00353; HLH; 1.
SUPFAM; SSF47459; SSF47459; 1.
PROSITE; PS50888; BHLH; 1.
1: Evidence at protein level;
3D-structure; Abscisic acid signaling pathway; Activator;
Complete proteome; DNA-binding; Jasmonic acid signaling pathway;
Nucleus; Phosphoprotein; Reference proteome; Transcription;
Transcription regulation.
CHAIN 1 623 Transcription factor MYC2.
/FTId=PRO_0000127427.
DOMAIN 448 497 bHLH. {ECO:0000255|PROSITE-
ProRule:PRU00981}.
REGION 93 160 JAZ-interaction domain.
MOTIF 434 442 Nuclear localization signal.
{ECO:0000255}.
MOD_RES 328 328 Phosphothreonine.
{ECO:0000269|PubMed:23593022}.
MUTAGEN 328 328 T->A: Jasmonate-insensitive phenotype and
increased stability of the protein.
{ECO:0000269|PubMed:23593022}.
MUTAGEN 330 330 S->A: No effect.
{ECO:0000269|PubMed:23593022}.
MUTAGEN 334 334 S->A: No effect.
{ECO:0000269|PubMed:23593022}.
MUTAGEN 336 336 T->A: No effect.
{ECO:0000269|PubMed:23593022}.
CONFLICT 258 258 A -> D (in Ref. 2; BAA25078).
{ECO:0000305}.
CONFLICT 526 526 K -> R (in Ref. 4; AAL55713).
{ECO:0000305}.
CONFLICT 529 529 A -> P (in Ref. 2; BAA25078).
{ECO:0000305}.
CONFLICT 612 612 E -> D (in Ref. 2; BAA25078).
{ECO:0000305}.
HELIX 454 472 {ECO:0000244|PDB:5GNJ}.
HELIX 483 522 {ECO:0000244|PDB:5GNJ}.
SEQUENCE 623 AA; 67950 MW; 4A8D4DE34C5928F6 CRC64;
MTDYRLQPTM NLWTTDDNAS MMEAFMSSSD ISTLWPPAST TTTTATTETT PTPAMEIPAQ
AGFNQETLQQ RLQALIEGTH EGWTYAIFWQ PSYDFSGASV LGWGDGYYKG EEDKANPRRR
SSSPPFSTPA DQEYRKKVLR ELNSLISGGV APSDDAVDEE VTDTEWFFLV SMTQSFACGA
GLAGKAFATG NAVWVSGSDQ LSGSGCERAK QGGVFGMHTI ACIPSANGVV EVGSTEPIRQ
SSDLINKVRI LFNFDGGAGD LSGLNWNLDP DQGENDPSMW INDPIGTPGS NEPGNGAPSS
SSQLFSKSIQ FENGSSSTIT ENPNLDPTPS PVHSQTQNPK FNNTFSRELN FSTSSSTLVK
PRSGEILNFG DEGKRSSGNP DPSSYSGQTQ FENKRKRSMV LNEDKVLSFG DKTAGESDHS
DLEASVVKEV AVEKRPKKRG RKPANGREEP LNHVEAERQR REKLNQRFYA LRAVVPNVSK
MDKASLLGDA IAYINELKSK VVKTESEKLQ IKNQLEEVKL ELAGRKASAS GGDMSSSCSS
IKPVGMEIEV KIIGWDAMIR VESSKRNHPA ARLMSALMDL ELEVNHASMS VVNDLMIQQA
TVKMGFRIYT QEQLRASLIS KIG


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