NFYB1_ARATH
ID NFYB1_ARATH Reviewed; 141 AA.
AC Q9SLG0; O23633;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Nuclear transcription factor Y subunit B-1 {ECO:0000303|PubMed:11250072};
DE Short=AtNF-YB-1 {ECO:0000303|PubMed:11250072};
DE Short=AtNF-YB1 {ECO:0000303|PubMed:25490919};
DE AltName: Full=Transcriptional activator HAP3A {ECO:0000303|PubMed:9662544};
GN Name=NFYB1 {ECO:0000303|PubMed:11250072};
GN Synonyms=HAP3A {ECO:0000303|PubMed:9662544};
GN OrderedLocusNames=At2g38880 {ECO:0000312|Araport:AT2G38880};
GN ORFNames=T7F6.5 {ECO:0000312|EMBL:AAC79602.2};
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 [MRNA], 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
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 [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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
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 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [9]
RP INTERACTION WITH DPB3-1, AND INDUCTION BY HEAT AND 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 [10]
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).
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 (By similarity). NF-YB and NF-YC
CC must interact and dimerize for NF-YA association and DNA binding (By
CC similarity). Binds directly with DPB3-1 (PubMed:25490919).
CC {ECO:0000250|UniProtKB:P23511, ECO:0000269|PubMed:25490919}.
CC -!- INTERACTION:
CC Q9SLG0; Q39057: CO; NbExp=6; IntAct=EBI-2126009, EBI-1639724;
CC Q9SLG0; Q58CM8: NFYC10; NbExp=3; IntAct=EBI-2126009, EBI-15191737;
CC Q9SLG0; Q9FGP8: NFYC7; NbExp=3; IntAct=EBI-2126009, EBI-2466133;
CC Q9SLG0; Q4PSE2: NFYC8; NbExp=3; IntAct=EBI-2126009, EBI-15191571;
CC Q9SLG0; Q8L4B2: NFYC9; NbExp=3; IntAct=EBI-2126009, EBI-2466050;
CC Q9SLG0; Q9M565: TAF11; NbExp=3; IntAct=EBI-2126009, EBI-1247587;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9SLG0-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Predominantly expressed in leaves,
CC flowers and siliques. {ECO:0000269|PubMed:11250072,
CC ECO:0000269|PubMed:9662544}.
CC -!- INDUCTION: Enhanced by dehydration stress but repressed by heat stress.
CC {ECO:0000269|PubMed:25490919}.
CC -!- SIMILARITY: Belongs to the NFYB/HAP3 subunit family. {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; Y13723; CAA74051.1; -; mRNA.
DR EMBL; AC005770; AAC79602.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC09598.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09600.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09602.1; -; Genomic_DNA.
DR EMBL; BT004266; AAO42268.1; -; mRNA.
DR EMBL; BT005536; AAO63956.1; -; mRNA.
DR EMBL; AY088554; AAM66086.1; -; mRNA.
DR PIR; E84810; E84810.
DR RefSeq; NP_001031511.1; NM_001036434.2. [Q9SLG0-1]
DR RefSeq; NP_030436.1; NM_129445.3. [Q9SLG0-1]
DR RefSeq; NP_850304.2; NM_179973.4. [Q9SLG0-1]
DR AlphaFoldDB; Q9SLG0; -.
DR SMR; Q9SLG0; -.
DR BioGRID; 3812; 20.
DR IntAct; Q9SLG0; 15.
DR iPTMnet; Q9SLG0; -.
DR EnsemblPlants; AT2G38880.1; AT2G38880.1; AT2G38880. [Q9SLG0-1]
DR EnsemblPlants; AT2G38880.2; AT2G38880.2; AT2G38880. [Q9SLG0-1]
DR EnsemblPlants; AT2G38880.5; AT2G38880.5; AT2G38880. [Q9SLG0-1]
DR GeneID; 818472; -.
DR Gramene; AT2G38880.1; AT2G38880.1; AT2G38880. [Q9SLG0-1]
DR Gramene; AT2G38880.2; AT2G38880.2; AT2G38880. [Q9SLG0-1]
DR Gramene; AT2G38880.5; AT2G38880.5; AT2G38880. [Q9SLG0-1]
DR KEGG; ath:AT2G38880; -.
DR Araport; AT2G38880; -.
DR InParanoid; Q9SLG0; -.
DR PhylomeDB; Q9SLG0; -.
DR PRO; PR:Q9SLG0; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SLG0; baseline and differential.
DR Genevisible; Q9SLG0; AT.
DR GO; GO:0016602; C:CCAAT-binding factor complex; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:InterPro.
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:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0009408; P:response to heat; IEP:UniProtKB.
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 Acetylation; Activator; Alternative splicing; DNA-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..141
FT /note="Nuclear transcription factor Y subunit B-1"
FT /id="PRO_0000204615"
FT DNA_BIND 26..32
FT /evidence="ECO:0000250|UniProtKB:P13434"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 53..64
FT /note="Subunit association domain (SAD)"
FT /evidence="ECO:0000250"
FT REGION 114..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 141 AA; 15181 MW; D33060B5AD21D9E0 CRC64;
MADTPSSPAG DGGESGGSVR EQDRYLPIAN ISRIMKKALP PNGKIGKDAK DTVQECVSEF
ISFITSEASD KCQKEKRKTV NGDDLLWAMA TLGFEDYLEP LKIYLARYRE LEGDNKGSGK
SGDGSNRDAG GGVSGEEMPS W
