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BH123_ARATH
ID   BH123_ARATH             Reviewed;         454 AA.
AC   Q8GXT3; Q9LHQ8;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 119.
DE   RecName: Full=Transcription factor bHLH123;
DE   AltName: Full=Basic helix-loop-helix protein 123;
DE            Short=AtbHLH123;
DE            Short=bHLH 123;
DE   AltName: Full=Transcription factor EN 63;
DE   AltName: Full=bHLH transcription factor bHLH123;
GN   Name=BHLH123; Synonyms=EN63; OrderedLocusNames=At3g20640; ORFNames=F3H11.2;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA   Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT   features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT   clones.";
RL   DNA Res. 7:217-221(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].
RC   STRAIN=cv. Columbia;
RX   PubMed=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
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   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=12679534; DOI=10.1093/molbev/msg088;
RA   Heim M.A., Jakoby M., Werber M., Martin C., Weisshaar B., Bailey P.C.;
RT   "The basic helix-loop-helix transcription factor family in plants: a
RT   genome-wide study of protein structure and functional diversity.";
RL   Mol. Biol. Evol. 20:735-747(2003).
RN   [6]
RP   GENE FAMILY.
RX   PubMed=12897250; DOI=10.1105/tpc.013839;
RA   Toledo-Ortiz G., Huq E., Quail P.H.;
RT   "The Arabidopsis basic/helix-loop-helix transcription factor family.";
RL   Plant Cell 15:1749-1770(2003).
RN   [7]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=14600211; DOI=10.1105/tpc.151140;
RA   Bailey P.C., Martin C., Toledo-Ortiz G., Quail P.H., Huq E., Heim M.A.,
RA   Jakoby M., Werber M., Weisshaar B.;
RT   "Update on the basic helix-loop-helix transcription factor gene family in
RT   Arabidopsis thaliana.";
RL   Plant Cell 15:2497-2502(2003).
CC   -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC   -!- INTERACTION:
CC       Q8GXT3; Q93Y00: BHLH7; NbExp=3; IntAct=EBI-15194527, EBI-4442198;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB02240.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AP002034; BAB02240.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002686; AEE76406.1; -; Genomic_DNA.
DR   EMBL; AK118054; BAC42685.1; -; mRNA.
DR   EMBL; BT008580; AAP40407.1; -; mRNA.
DR   RefSeq; NP_188700.1; NM_112955.3.
DR   AlphaFoldDB; Q8GXT3; -.
DR   SMR; Q8GXT3; -.
DR   BioGRID; 6943; 8.
DR   IntAct; Q8GXT3; 8.
DR   STRING; 3702.AT3G20640.1; -.
DR   iPTMnet; Q8GXT3; -.
DR   PaxDb; Q8GXT3; -.
DR   PRIDE; Q8GXT3; -.
DR   EnsemblPlants; AT3G20640.1; AT3G20640.1; AT3G20640.
DR   GeneID; 821611; -.
DR   Gramene; AT3G20640.1; AT3G20640.1; AT3G20640.
DR   KEGG; ath:AT3G20640; -.
DR   Araport; AT3G20640; -.
DR   TAIR; locus:2083460; AT3G20640.
DR   eggNOG; ENOG502QRNH; Eukaryota.
DR   HOGENOM; CLU_041735_1_1_1; -.
DR   InParanoid; Q8GXT3; -.
DR   OrthoDB; 890119at2759; -.
DR   PhylomeDB; Q8GXT3; -.
DR   PRO; PR:Q8GXT3; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q8GXT3; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd11393; bHLH_AtbHLH_like; 1.
DR   Gene3D; 4.10.280.10; -; 1.
DR   InterPro; IPR045239; bHLH95_bHLH.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
DR   SUPFAM; SSF47459; SSF47459; 1.
DR   PROSITE; PS50888; BHLH; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..454
FT                   /note="Transcription factor bHLH123"
FT                   /id="PRO_0000358808"
FT   DOMAIN          334..383
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          101..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          185..228
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          270..348
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          398..417
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        101..122
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        288..305
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        306..332
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   454 AA;  49064 MW;  FB2D717F168832B6 CRC64;
     MGDHHDFINS GSWWKVSSSS SPSSSSSMRA SSIESGGSAV FHDKLHHHSL ATDHHLQMIG
     LGLSSQSPVD QWNQSLLRGD SKAETSFGVM LQENLNLDAT SNANANTTSS TSSYQLQESD
     SSHHHQALWR DPQSDFKPQI LTSGGNRGFF LDHQFSPHGS SSTDSSTVTC QGFAVDNSSN
     AMYAATTTTP NSSSGMFHHQ QAGGFGSSDQ QPSRNHQQSS LGYSQFGSST GNYDQMASAL
     PSTWFLRSSP PPKPHSPLRF SNNATFWNPA AAGNAGAPPP HDASSNFFPA LQPPQIHPQS
     FDEQPKNISE IRDSSSNEVK RGGNDHQPAA KRAKSEAASP SPAFKRKEKM GDRIAALQQL
     VSPFGKTDAA SVLSEAIEYI KFLHQQVSAL SNPYMKSGAS LQHQQSDHST ELEVSEEPDL
     RSRGLCLVPV SSTFPVTHDT TVDFWTPTFG GTFR
 
 
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