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NFYB2_ARATH
ID   NFYB2_ARATH             Reviewed;         190 AA.
AC   Q9FGJ3; O23634; Q9FV58;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 139.
DE   RecName: Full=Nuclear transcription factor Y subunit B-2 {ECO:0000303|PubMed:11250072};
DE            Short=AtNF-YB-2 {ECO:0000303|PubMed:11250072};
DE            Short=AtNF-YB2 {ECO:0000303|PubMed:25490919};
DE   AltName: Full=Transcriptional activator HAP3B {ECO:0000303|PubMed:9662544};
GN   Name=NFYB2 {ECO:0000303|PubMed:11250072};
GN   Synonyms=HAP3B {ECO:0000303|PubMed:9662544};
GN   OrderedLocusNames=At5g47640 {ECO:0000312|Araport:AT5G47640};
GN   ORFNames=MNJ7.23 {ECO:0000312|EMBL:BAB09090.1};
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;
RA   Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL   Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
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=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 [MRNA] OF 5-190, AND TISSUE SPECIFICITY.
RX   PubMed=9662544; DOI=10.1104/pp.117.3.1015;
RA   Edwards D., Murray J.A.H., Smith A.G.;
RT   "Multiple genes encoding the conserved CCAAT-box transcription factor
RT   complex are expressed in Arabidopsis.";
RL   Plant Physiol. 117:1015-1022(1998).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 68-190.
RC   STRAIN=cv. Columbia;
RX   PubMed=10929106; DOI=10.1046/j.1365-313x.2000.00809.x;
RA   Kleinow T., Bhalerao R., Breuer F., Umeda M., Salchert K., Koncz C.;
RT   "Functional identification of an Arabidopsis Snf4 ortholog by screening for
RT   heterologous multicopy suppressors of snf4 deficiency in yeast.";
RL   Plant J. 23:115-122(2000).
RN   [6]
RP   TISSUE SPECIFICITY.
RX   PubMed=11250072; DOI=10.1016/s0378-1119(01)00323-7;
RA   Gusmaroli G., Tonelli C., Mantovani R.;
RT   "Regulation of the CCAAT-binding NF-Y subunits in Arabidopsis thaliana.";
RL   Gene 264:173-185(2001).
RN   [7]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=11867211; DOI=10.1016/s0378-1119(01)00833-2;
RA   Gusmaroli G., Tonelli C., Mantovani R.;
RT   "Regulation of novel members of the Arabidopsis thaliana CCAAT-binding
RT   nuclear factor Y subunits.";
RL   Gene 283:41-48(2002).
RN   [8]
RP   INTERACTION WITH DPB3-1, AND INDUCTION BY DEHYDRATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=25490919; DOI=10.1105/tpc.114.132928;
RA   Sato H., Mizoi J., Tanaka H., Maruyama K., Qin F., Osakabe Y., Morimoto K.,
RA   Ohori T., Kusakabe K., Nagata M., Shinozaki K., Yamaguchi-Shinozaki K.;
RT   "Arabidopsis DPB3-1, a DREB2A interactor, specifically enhances heat
RT   stress-induced gene expression by forming a heat stress-specific
RT   transcriptional complex with NF-Y subunits.";
RL   Plant Cell 26:4954-4973(2014).
RN   [9]
RP   REVIEW.
RX   PubMed=28119722; DOI=10.3389/fpls.2016.02045;
RA   Zhao H., Wu D., Kong F., Lin K., Zhang H., Li G.;
RT   "The Arabidopsis thaliana Nuclear Factor Y Transcription Factors.";
RL   Front. Plant Sci. 7:2045-2045(2016).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 24-116, AND SUBUNIT.
RX   PubMed=33098724; DOI=10.1111/tpj.15038;
RA   Chaves-Sanjuan A., Gnesutta N., Gobbini A., Martignago D., Bernardini A.,
RA   Fornara F., Mantovani R., Nardini M.;
RT   "Structural determinants for NF-Y subunit organization and NF-Y/DNA
RT   association in plants.";
RL   Plant J. 105:49-61(2021).
CC   -!- FUNCTION: Component of the NF-Y/HAP transcription factor complex (By
CC       similarity). The NF-Y complex stimulates the transcription of various
CC       genes by recognizing and binding to a CCAAT motif in promoters (By
CC       similarity). {ECO:0000250|UniProtKB:Q84W66}.
CC   -!- SUBUNIT: Heterotrimeric transcription factor composed of three
CC       components, NF-YA, NF-YB and NF-YC (PubMed:33098724). NF-YB and NF-YC
CC       must interact and dimerize for NF-YA association and DNA binding
CC       (PubMed:33098724). Binds directly with DPB3-1 (PubMed:25490919).
CC       {ECO:0000269|PubMed:25490919, ECO:0000269|PubMed:33098724}.
CC   -!- INTERACTION:
CC       Q9FGJ3; Q8VYU9: At2g46735; NbExp=3; IntAct=EBI-15192505, EBI-15193063;
CC       Q9FGJ3; Q9LN09: NF-YC10; NbExp=4; IntAct=EBI-15192505, EBI-4461992;
CC       Q9FGJ3; Q58CM8: NFYC10; NbExp=3; IntAct=EBI-15192505, EBI-15191737;
CC       Q9FGJ3; Q9FGP8: NFYC7; NbExp=3; IntAct=EBI-15192505, EBI-2466133;
CC       Q9FGJ3; Q4PSE2: NFYC8; NbExp=5; IntAct=EBI-15192505, EBI-15191571;
CC       Q9FGJ3; Q8L4B2: NFYC9; NbExp=5; IntAct=EBI-15192505, EBI-2466050;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Predominantly expressed in flowers and
CC       siliques. {ECO:0000269|PubMed:11250072, ECO:0000269|PubMed:9662544}.
CC   -!- INDUCTION: Enhanced by dehydration stress.
CC       {ECO:0000269|PubMed:25490919}.
CC   -!- SIMILARITY: Belongs to the NFYB/HAP3 subunit family. {ECO:0000305}.
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DR   EMBL; AB025628; BAB09090.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED95545.1; -; Genomic_DNA.
DR   EMBL; AF385744; AAK60334.1; -; mRNA.
DR   EMBL; AY078026; AAL77727.1; -; mRNA.
DR   EMBL; Y13724; CAA74052.1; -; mRNA.
DR   EMBL; AF250338; AAG10144.1; -; mRNA.
DR   RefSeq; NP_199575.1; NM_124138.2.
DR   PDB; 6R0M; X-ray; 2.30 A; A/C=24-116.
DR   PDB; 6R0N; X-ray; 2.10 A; A=24-116.
DR   PDB; 6R2V; X-ray; 2.50 A; B=24-116.
DR   PDB; 7CVQ; X-ray; 3.30 A; B/G/L/Q=24-120.
DR   PDBsum; 6R0M; -.
DR   PDBsum; 6R0N; -.
DR   PDBsum; 6R2V; -.
DR   PDBsum; 7CVQ; -.
DR   AlphaFoldDB; Q9FGJ3; -.
DR   SMR; Q9FGJ3; -.
DR   BioGRID; 20063; 31.
DR   IntAct; Q9FGJ3; 14.
DR   STRING; 3702.AT5G47640.1; -.
DR   iPTMnet; Q9FGJ3; -.
DR   PaxDb; Q9FGJ3; -.
DR   PRIDE; Q9FGJ3; -.
DR   ProteomicsDB; 251296; -.
DR   EnsemblPlants; AT5G47640.1; AT5G47640.1; AT5G47640.
DR   GeneID; 834815; -.
DR   Gramene; AT5G47640.1; AT5G47640.1; AT5G47640.
DR   KEGG; ath:AT5G47640; -.
DR   Araport; AT5G47640; -.
DR   TAIR; locus:2168983; AT5G47640.
DR   eggNOG; KOG0869; Eukaryota.
DR   HOGENOM; CLU_066247_1_1_1; -.
DR   InParanoid; Q9FGJ3; -.
DR   OMA; FRWRAGE; -.
DR   OrthoDB; 1529111at2759; -.
DR   PhylomeDB; Q9FGJ3; -.
DR   PRO; PR:Q9FGJ3; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FGJ3; baseline and differential.
DR   Genevisible; Q9FGJ3; AT.
DR   GO; GO:0016602; C:CCAAT-binding factor complex; IBA:GO_Central.
DR   GO; GO:0009536; C:plastid; HDA:TAIR.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:InterPro.
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:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR   GO; GO:0003712; F:transcription coregulator activity; IDA:TAIR.
DR   GO; GO:0048574; P:long-day photoperiodism, flowering; IMP:TAIR.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0009414; P:response to water deprivation; IEP:UniProtKB.
DR   Gene3D; 1.10.20.10; -; 1.
DR   InterPro; IPR003958; CBFA_NFYB_domain.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR027113; Transc_fact_NFYB/HAP3.
DR   InterPro; IPR003956; Transcrpt_fac_NFYB/HAP3_CS.
DR   PANTHER; PTHR11064; PTHR11064; 1.
DR   Pfam; PF00808; CBFD_NFYB_HMF; 1.
DR   SUPFAM; SSF47113; SSF47113; 1.
DR   PROSITE; PS00685; NFYB_HAP3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; DNA-binding; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..190
FT                   /note="Nuclear transcription factor Y subunit B-2"
FT                   /id="PRO_0000204616"
FT   DNA_BIND        32..38
FT                   /evidence="ECO:0000250|UniProtKB:P13434"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          59..70
FT                   /note="Subunit association domain (SAD)"
FT                   /evidence="ECO:0000250"
FT   REGION          168..190
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..27
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   HELIX           25..28
FT                   /evidence="ECO:0007829|PDB:6R0M"
FT   HELIX           34..44
FT                   /evidence="ECO:0007829|PDB:6R0N"
FT   HELIX           53..80
FT                   /evidence="ECO:0007829|PDB:6R0N"
FT   HELIX           88..97
FT                   /evidence="ECO:0007829|PDB:6R0N"
FT   HELIX           101..115
FT                   /evidence="ECO:0007829|PDB:6R0N"
SQ   SEQUENCE   190 AA;  20529 MW;  D8E5CE0F42247C02 CRC64;
     MGDSDRDSGG GQNGNNQNGQ SSLSPREQDR FLPIANVSRI MKKALPANAK ISKDAKETMQ
     ECVSEFISFV TGEASDKCQK EKRKTINGDD LLWAMTTLGF EDYVEPLKVY LQRFREIEGE
     RTGLGRPQTG GEVGEHQRDA VGDGGGFYGG GGGMQYHQHH QFLHQQNHMY GATGGGSDSG
     GGAASGRTRT
 
 
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