TAF11_ARATH
ID TAF11_ARATH Reviewed; 210 AA.
AC Q9M565; O65441;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Transcription initiation factor TFIID subunit 11;
DE AltName: Full=TBP-associated factor 11;
DE Short=AtTAF11;
GN Name=TAF11; OrderedLocusNames=At4g20280; ORFNames=F1C12.195;
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], AND INTERACTION WITH TAF12; TAF12B AND TAF13.
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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].
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).
CC -!- FUNCTION: TAFs are components of the transcription factor IID (TFIID)
CC complex that is essential for mediating regulation of RNA polymerase
CC transcription. {ECO:0000250}.
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 TAF12, TAF12B and
CC TAF13. {ECO:0000269|PubMed:17340043}.
CC -!- INTERACTION:
CC Q9M565; Q9SLG0: NFYB1; NbExp=3; IntAct=EBI-1247587, EBI-2126009;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves and inflorescences.
CC {ECO:0000269|PubMed:15527982}.
CC -!- SIMILARITY: Belongs to the TAF11 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA18253.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79028.1; Type=Erroneous gene model prediction; Evidence={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; AY463612; AAR28014.1; -; mRNA.
DR EMBL; AF238326; AAF65405.1; -; mRNA.
DR EMBL; AL022224; CAA18253.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161552; CAB79028.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84298.1; -; Genomic_DNA.
DR EMBL; AF370141; AAK43956.1; -; mRNA.
DR EMBL; AY051084; AAK93761.1; -; mRNA.
DR PIR; T05336; T05336.
DR RefSeq; NP_193761.1; NM_118147.5.
DR AlphaFoldDB; Q9M565; -.
DR SMR; Q9M565; -.
DR BioGRID; 13067; 14.
DR IntAct; Q9M565; 15.
DR STRING; 3702.AT4G20280.1; -.
DR iPTMnet; Q9M565; -.
DR PaxDb; Q9M565; -.
DR PRIDE; Q9M565; -.
DR ProteomicsDB; 233005; -.
DR EnsemblPlants; AT4G20280.1; AT4G20280.1; AT4G20280.
DR GeneID; 827775; -.
DR Gramene; AT4G20280.1; AT4G20280.1; AT4G20280.
DR KEGG; ath:AT4G20280; -.
DR Araport; AT4G20280; -.
DR TAIR; locus:2120422; AT4G20280.
DR eggNOG; KOG3219; Eukaryota.
DR HOGENOM; CLU_088696_1_0_1; -.
DR InParanoid; Q9M565; -.
DR OMA; PIRPCHV; -.
DR OrthoDB; 1528461at2759; -.
DR PhylomeDB; Q9M565; -.
DR PRO; PR:Q9M565; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9M565; baseline and differential.
DR Genevisible; Q9M565; AT.
DR GO; GO:0005669; C:transcription factor TFIID complex; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IBA:GO_Central.
DR CDD; cd08048; TAF11; 1.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR045127; TAF11-like.
DR InterPro; IPR006809; TAFII28_dom.
DR PANTHER; PTHR13218; PTHR13218; 1.
DR Pfam; PF04719; TAFII28; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 1: Evidence at protein level;
KW Activator; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..210
FT /note="Transcription initiation factor TFIID subunit 11"
FT /id="PRO_0000424048"
FT DOMAIN 112..201
FT /note="Histone-fold"
FT REGION 1..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 210 AA; 23700 MW; DA16EFDF21D65A4D CRC64;
MKHSKDPFEA AIEEEQEESP PESPVGGGGG GDGSEDGRIE IDQTQDEDER PVDVRRPMKK
AKTSVVVTEA KNKDKDEDDE EEEENMDVEL TKYPTSSDPA KMAKMQTILS QFTEDQMSRY
ESFRRSALQR PQMKKLLIGV TGSQKIGMPM IIVACGIAKM FVGELVETAR VVMAERKESG
PIRPCHIRES YRRLKLEGKV PKRSVPRLFR
