TA14B_ARATH
ID TA14B_ARATH Reviewed; 268 AA.
AC Q9FH40; F4KEK5;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Transcription initiation factor TFIID subunit 14b {ECO:0000303|PubMed:15527982};
DE AltName: Full=GAS 41-like protein {ECO:0000303|PubMed:10913114};
DE AltName: Full=Protein AF-9 homolog a {ECO:0000303|PubMed:23017898};
DE AltName: Full=TBP-associated factor 14b {ECO:0000303|PubMed:15527982};
DE Short=AtTAF14b {ECO:0000303|PubMed:15527982};
GN Name=TAF14B {ECO:0000303|PubMed:15527982};
GN Synonyms=GAS41 {ECO:0000303|PubMed:10913114},
GN YAF9A {ECO:0000303|PubMed:23017898};
GN OrderedLocusNames=At5g45600 {ECO:0000312|Araport:AT5G45600};
GN ORFNames=K2N11.8 {ECO:0000312|EMBL:BAB11199.1};
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 [MRNA], IDENTIFICATION, NOMENCLATURE, AND TISSUE
RP SPECIFICITY.
RX PubMed=15527982; DOI=10.1016/j.gene.2004.08.023;
RA Lago C., Clerici E., Mizzi L., Colombo L., Kater M.M.;
RT "TBP-associated factors in Arabidopsis.";
RL Gene 342:231-241(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH TAF1; TAF4B
RP AND TAF12B.
RC STRAIN=cv. Columbia;
RX PubMed=17340043; DOI=10.1007/s11103-007-9135-1;
RA Lawit S.J., O'Grady K., Gurley W.B., Czarnecka-Verner E.;
RT "Yeast two-hybrid map of Arabidopsis TFIID.";
RL Plant Mol. Biol. 64:73-87(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP IDENTIFICATION.
RX PubMed=10913114; DOI=10.1074/jbc.m000994200;
RA Harborth J., Weber K., Osborn M.;
RT "GAS41, a highly conserved protein in eukaryotic nuclei, binds to NuMA.";
RL J. Biol. Chem. 275:31979-31985(2000).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH FLX, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=21282526; DOI=10.1105/tpc.110.075911;
RA Choi K., Kim J., Hwang H.J., Kim S., Park C., Kim S.Y., Lee I.;
RT "The FRIGIDA complex activates transcription of FLC, a strong flowering
RT repressor in Arabidopsis, by recruiting chromatin modification factors.";
RL Plant Cell 23:289-303(2011).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=23017898; DOI=10.1016/j.plantsci.2012.07.010;
RA Zacharaki V., Benhamed M., Poulios S., Latrasse D., Papoutsoglou P.,
RA Delarue M., Vlachonasios K.E.;
RT "The Arabidopsis ortholog of the YEATS domain containing protein YAF9a
RT regulates flowering by controlling H4 acetylation levels at the FLC
RT locus.";
RL Plant Sci. 196:44-52(2012).
RN [9]
RP FUNCTION, IDENTIFICATION IN THE NUA4/SWR1 COMPLEX, INTERACTION WITH SWC4;
RP EAF1A AND EAF1B, AND DISRUPTION PHENOTYPE.
RX DOI=10.1186/s12870-015-0461-1;
RA Bieluszewski T., Galganski L., Sura W., Bieluszewska A., Abram M.,
RA Ludwikow A., Ziolkowski P., Sadowski J.;
RT "AtEAF1 is a potential platform protein for Arabidopsis NuA4
RT acetyltransferase complex.";
RL BMC Plant Biol. 15:0-0(2015).
CC -!- FUNCTION: Negative regulator of flowering controlling the H4K5
CC acetylation levels in the FLC and FT chromatin. Positively regulates
CC FLC expression. Component of the transcription factor IID (TFIID)
CC complex that is essential for mediating regulation of RNA polymerase
CC transcription. Component of the SWR1 complex which mediates the ATP-
CC dependent exchange of histone H2A for the H2A variant HZT1 leading to
CC transcriptional regulation of selected genes by chromatin remodeling.
CC Component of a NuA4 histone acetyltransferase complex which is involved
CC in transcriptional activation of selected genes principally by
CC acetylation of nucleosomal histones H4 and H2A.
CC {ECO:0000269|PubMed:23017898, ECO:0000269|Ref.9}.
CC -!- SUBUNIT: Component of the TFIID complex. TFIID is composed of TATA
CC binding protein (TBP) and a number of TBP-associated factors (TAFs)
CC whose MWs range from 14-217 kDa. Interacts with TAF1, TAF4B and TAF12B.
CC Component of the SWR1 chromatin-remodeling complex. Interacts with FLX,
CC a component of the transcription activator complex FRI-C
CC (PubMed:17340043, PubMed:21282526). Interacts with SWC4, and with EAF1A
CC and EAF1B (via HSA domain) (Ref.9). {ECO:0000269|PubMed:17340043,
CC ECO:0000269|PubMed:21282526, ECO:0000269|Ref.9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9FH40-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FH40-2; Sequence=VSP_053264;
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, inflorescence and
CC flowering tissues. {ECO:0000269|PubMed:15527982,
CC ECO:0000269|PubMed:23017898}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, due to the redundancy with
CC TAF14. Modest early flowering. Taf14 and taf14b double mutants show a
CC pleiotropic phenotype that includes small size and abnormal leaf
CC morphology (PubMed:21282526, PubMed:23017898). Taf14 and taf14b double
CC mutants show a reduced H4K5 acetylation in the promoter region of major
CC flowering regulator genes including FLC, CO and SOC1, and a more
CC pronounced early flowering (Ref.9). {ECO:0000269|PubMed:21282526,
CC ECO:0000269|PubMed:23017898, ECO:0000269|Ref.9}.
CC -!- SIMILARITY: Belongs to the YAF9 family. {ECO:0000305}.
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DR EMBL; AY463617; AAR28019.1; -; mRNA.
DR EMBL; AB022213; BAB11199.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95273.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95274.1; -; Genomic_DNA.
DR EMBL; AY072123; AAL59945.1; -; mRNA.
DR EMBL; AY096486; AAM20126.1; -; mRNA.
DR RefSeq; NP_001190475.1; NM_001203546.1. [Q9FH40-2]
DR RefSeq; NP_199373.1; NM_123928.4. [Q9FH40-1]
DR AlphaFoldDB; Q9FH40; -.
DR SMR; Q9FH40; -.
DR BioGRID; 19848; 19.
DR IntAct; Q9FH40; 11.
DR STRING; 3702.AT5G45600.1; -.
DR iPTMnet; Q9FH40; -.
DR PaxDb; Q9FH40; -.
DR PRIDE; Q9FH40; -.
DR ProteomicsDB; 232998; -. [Q9FH40-1]
DR EnsemblPlants; AT5G45600.1; AT5G45600.1; AT5G45600. [Q9FH40-1]
DR EnsemblPlants; AT5G45600.2; AT5G45600.2; AT5G45600. [Q9FH40-2]
DR GeneID; 834599; -.
DR Gramene; AT5G45600.1; AT5G45600.1; AT5G45600. [Q9FH40-1]
DR Gramene; AT5G45600.2; AT5G45600.2; AT5G45600. [Q9FH40-2]
DR KEGG; ath:AT5G45600; -.
DR Araport; AT5G45600; -.
DR TAIR; locus:2157156; AT5G45600.
DR eggNOG; KOG3149; Eukaryota.
DR HOGENOM; CLU_051385_1_1_1; -.
DR InParanoid; Q9FH40; -.
DR OMA; QINLIDG; -.
DR OrthoDB; 1482359at2759; -.
DR PhylomeDB; Q9FH40; -.
DR PRO; PR:Q9FH40; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FH40; baseline and differential.
DR Genevisible; Q9FH40; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000812; C:Swr1 complex; IDA:TAIR.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0009908; P:flower development; IEA:UniProtKB-KW.
DR GO; GO:0016573; P:histone acetylation; IBA:GO_Central.
DR GO; GO:0043981; P:histone H4-K5 acetylation; IMP:UniProtKB.
DR GO; GO:0009909; P:regulation of flower development; IMP:UniProtKB.
DR GO; GO:0090239; P:regulation of histone H4 acetylation; IMP:TAIR.
DR GO; GO:2000028; P:regulation of photoperiodism, flowering; IGI:TAIR.
DR GO; GO:0048510; P:regulation of timing of transition from vegetative to reproductive phase; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 2.60.40.1970; -; 1.
DR InterPro; IPR038704; YEAST_sf.
DR InterPro; IPR005033; YEATS.
DR PANTHER; PTHR23195; PTHR23195; 1.
DR Pfam; PF03366; YEATS; 1.
DR PROSITE; PS51037; YEATS; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Chromatin regulator; Coiled coil;
KW Cytoplasm; Developmental protein; Differentiation; DNA damage; DNA repair;
KW Flowering; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..268
FT /note="Transcription initiation factor TFIID subunit 14b"
FT /id="PRO_0000423726"
FT DOMAIN 38..182
FT /note="YEATS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00376"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 229..263
FT /evidence="ECO:0000255"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 36
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_053264"
SQ SEQUENCE 268 AA; 30232 MW; 6CACDFB4BCC94977 CRC64;
MTNSSSSKKQ AQDQPETSEP TLKSLKTKMT KSDEKQKKLK DIEISVPIVY GNVAFWLGKK
ASEYQSHKWA VYVRGATNED ISVVVKKVVF QLHSSFNSPT RVIEEPPFEV SESGWGEFEI
AMTLHFHSDV CDKPLSLYHH LKLYPEDESG PLTMKKPVVV ESYDEIVFPD PSESFLARVQ
NHPALTFPRL PSGYNLPAPM QVEDTGKKKR GDTKDHSLGQ WFMSFSEADE LLQLAAARQQ
VQAHIAKLRR QISLLEGQNQ TVKTGSDL
