TAF1B_ARATH
ID TAF1B_ARATH Reviewed; 1786 AA.
AC Q6PUA2; Q9LJ62;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Transcription initiation factor TFIID subunit 1b;
DE AltName: Full=TAFII250-B;
DE AltName: Full=TBP-associated factor 1b;
DE Short=AtTAF1b;
DE AltName: Full=Transcription initiation factor TFIID subunit 1-B;
GN Name=TAF1B; Synonyms=HAF2; OrderedLocusNames=At3g19040;
GN ORFNames=K13E13.15, K13E13_16;
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], TISSUE SPECIFICITY, AND FUNCTION.
RC STRAIN=cv. Wassilewskija;
RX PubMed=15525647; DOI=10.1074/jbc.m409000200;
RA Bertrand C., Benhamed M., Li Y.-F., Ayadi M., Lemonnier G., Renou J.-P.,
RA Delarue M., Zhou D.-X.;
RT "Arabidopsis HAF2 gene encoding TATA-binding protein (TBP)-associated
RT factor TAF1, is required to integrate light signals to regulate gene
RT expression and growth.";
RL J. Biol. Chem. 280:1465-1473(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION, NOMENCLATURE, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
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 [3]
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 [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 IDENTIFICATION, AND NOMENCLATURE.
RX PubMed=12466527; DOI=10.1093/nar/gkf660;
RA Pandey R., Mueller A., Napoli C.A., Selinger D.A., Pikaard C.S.,
RA Richards E.J., Bender J., Mount D.W., Jorgensen R.A.;
RT "Analysis of histone acetyltransferase and histone deacetylase families of
RT Arabidopsis thaliana suggests functional diversification of chromatin
RT modification among multicellular eukaryotes.";
RL Nucleic Acids Res. 30:5036-5055(2002).
RN [6]
RP FUNCTION.
RX PubMed=17085686; DOI=10.1105/tpc.106.043489;
RA Benhamed M., Bertrand C., Servet C., Zhou D.X.;
RT "Arabidopsis GCN5, HD1, and TAF1/HAF2 interact to regulate histone
RT acetylation required for light-responsive gene expression.";
RL Plant Cell 18:2893-2903(2006).
CC -!- FUNCTION: TAFs are components of the transcription factor IID (TFIID)
CC complex that is essential for mediating regulation of RNA polymerase
CC transcription. Core scaffold of the TFIID complex. Acts as a histone
CC acetyltransferase involved in the light regulation of growth and gene
CC expression. Required for H3K9, H3K27, and H4K12 acetylation on the
CC target promoters. {ECO:0000269|PubMed:15525647,
CC ECO:0000269|PubMed:17085686}.
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.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, shoots, leaves and
CC inflorescences. {ECO:0000269|PubMed:15525647,
CC ECO:0000269|PubMed:15527982}.
CC -!- DISRUPTION PHENOTYPE: Plants show reduced acetylation of histone H3 in
CC light-responsive promoters, decreased chlorophyll accumulation and
CC altered expression of about 9% of genes in young leaves.
CC {ECO:0000269|PubMed:15527982}.
CC -!- SIMILARITY: Belongs to the TAF1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB01700.1; 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; AY579213; AAS90944.1; -; mRNA.
DR EMBL; AP000735; BAB01700.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE76187.1; -; Genomic_DNA.
DR RefSeq; NP_188534.2; NM_112790.3.
DR AlphaFoldDB; Q6PUA2; -.
DR SMR; Q6PUA2; -.
DR STRING; 3702.AT3G19040.1; -.
DR PaxDb; Q6PUA2; -.
DR PRIDE; Q6PUA2; -.
DR EnsemblPlants; AT3G19040.1; AT3G19040.1; AT3G19040.
DR GeneID; 821437; -.
DR Gramene; AT3G19040.1; AT3G19040.1; AT3G19040.
DR KEGG; ath:AT3G19040; -.
DR Araport; AT3G19040; -.
DR TAIR; locus:2085909; AT3G19040.
DR eggNOG; KOG0008; Eukaryota.
DR HOGENOM; CLU_236945_0_0_1; -.
DR InParanoid; Q6PUA2; -.
DR OMA; RCQEIWD; -.
DR PhylomeDB; Q6PUA2; -.
DR PRO; PR:Q6PUA2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q6PUA2; baseline and differential.
DR Genevisible; Q6PUA2; AT.
DR GO; GO:0005669; C:transcription factor TFIID complex; IBA:GO_Central.
DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:InterPro.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IBA:GO_Central.
DR GO; GO:0001091; F:RNA polymerase II general transcription initiation factor binding; IEA:InterPro.
DR GO; GO:0017025; F:TBP-class protein binding; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016573; P:histone acetylation; IMP:TAIR.
DR GO; GO:0009416; P:response to light stimulus; IEP:TAIR.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IBA:GO_Central.
DR Gene3D; 1.20.920.10; -; 1.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR040240; TAF1.
DR InterPro; IPR022591; TAF1_HAT_dom.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR13900; PTHR13900; 2.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF12157; DUF3591; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF47370; SSF47370; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 2: Evidence at transcript level;
KW Activator; Bromodomain; Chromatin regulator; Coiled coil; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..1786
FT /note="Transcription initiation factor TFIID subunit 1b"
FT /id="PRO_0000269754"
FT DOMAIN 574..650
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 1679..1749
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT REGION 54..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1303..1382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1397..1471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1596..1634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1591..1620
FT /evidence="ECO:0000255"
FT COILED 1752..1786
FT /evidence="ECO:0000255"
FT COMPBIAS 350..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1322..1341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1358..1382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1433..1468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1596..1617
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1786 AA; 202252 MW; C66C722F48B7B1CF CRC64;
MICRVDYGSN DEEYDGPELQ VVTEEDHLLP KREYLSAAFA LSGLNSRASV FDDEDYDEQG
GQEKEHVPVE KSFDSEEREP VVLKEEKPVK HEKEASILGN KNQMDTGDVQ EELVVGLSEA
TLDEKRVTPL PTLYLEDDGM VILQFSEIFA IQEPQKKRQK REIRCITYRD KYISMDISEL
IEDDEEVLLK SHGRIDTHGK KTDQIQLDVP LPIRERSQLV KSGIVRDTTS ESREFTKLGR
DSCIMGELLK QDLKDDNSSL CQSQLTMEVF PLDQQEWEHL ILWEISPQFS ANCCEGFKSG
LESAGIMVQV RASNSVTEQE SLNVMNSGGQ TQGDNNNMLE PFFVNPLESF GSRGSQSTNE
STNKSRHHPQ LLRLESQWDE DHYRENGDAG RENLKQLNSD ARGRLSGLAL QDRDMWDESW
LDSIIWESDK DLSRSKLIFD LQDEQMIFEV PNNKERKYLQ LHAGSRIVSR SSKSKDGSFQ
EGCGSNSGWQ FNISNDKFYM NGKSAQKLQG NAKKSTVHSL RVFHSAPAIK LQTMKIKLSN
KERANFHRPK ALWYPHDNEL AIKQQKILPT QGSMTIVVKS LGGKGSLLTV GREESVSSLK
AKASRKLDFK ETEAVKMFYM GKELEDEKSL AEQNVQPNSL VHLLRTKVHL WPWAQKLPGE
NKSLRPPGAF KKKSDLSNQD GHVFLMEYCE ERPLMLSNAG MGANLCTYYQ KSSPEDQHGN
LLRNQSDTLG SVIILEHGNK SPFLGEVHGG CSQSSVETNM YKAPVFPHRL QSTDYLLVRS
AKGKLSLRRI NKIVAVGQQE PRMEIMSPAS KNLHAYLVNR MMAYVYREFK HRDRIAADEL
SFSFSNISDA TVRKYMQVCS DLERDANGKA CWSKKRKFDK IPLGLNTLVA PEDVCSYESM
LAGLFRLKHL GITRFTLPAS ISTALAQLPD ERIAAASHIA RELQITPWNL SSSFVTCATQ
GRENIERLEI TGVGDPSGRG LGFSYVRVAP KSSAASEHKK KKAAACRGVP TVTGTDADPR
RLSMEAAREV LLKFNVPDEI IAKQTQRHRT AMIRKISSEQ AASGGKVGPT TVGMFSRSQR
MSFLQLQQQA REMCHEIWDR QRLSLSACDD DGNESENEAN SDLDSFVGDL EDLLDAEDGG
EGEESNKSMN EKLDGVKGLK MRRWPSQVEK DEEIEDEAAE YVELCRLLMQ DENDKKKKKL
KDVGEGIGSF PPPRSNFEPF IDKKYIATEP DASFLIVNES TVKHTKNVDK ATSKSPKDKQ
VKEIGTPICQ MKKILKENQK VFMGKKTARA NFVCGACGQH GHMKTNKHCP KYRRNTESQP
ESMDMKKSTG KPSSSDLSGE VWLTPIDNKK PAPKSATKIS VNEATKVGDS TSKTPGSSDV
AAVSEIDSGT KLTSRKLKIS SKAKPKASKV ESDSPFHSLM PAYSRERGES ELHNPSVSGQ
LLPSTETDQA ASSRYTTSVP QPSLSIDKDQ AESCRPHRVI WPPTGKEHSQ KKLVIKRLKE
ITDHDSGSLE ETPQFESRKT KRMAELADFQ RQQRLRLSEN FLDWGPKDDR KWRKEQDIST
ELHREGKVRR AYDDSTVSEE RSEIAESRRY REVIRSEREE EKRRKAKQKK KLQRGILENY
PPRRNDGISS ESGQNINSLC VSDFERNRTE YAPQPKRRKK GQVGLANILE SIVDTLRVKE
VNVSYLFLKP VTKKEAPNYL EIVKCPMDLS TIRDKVRRME YRDRQQFRHD VWQIKFNAHL
YNDGRNLSIP PLADELLVKC DRLLDEYRDE LKEAEKGIVD SSDSLR
