TAF1_ARATH
ID TAF1_ARATH Reviewed; 1919 AA.
AC Q8LRK9; Q9LPI9;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Transcription initiation factor TFIID subunit 1;
DE AltName: Full=TAFII250-A;
DE AltName: Full=TBP-associated factor 1;
DE Short=AtTAF1;
DE AltName: Full=Transcription initiation factor TFIID subunit 1-A;
GN Name=TAF1; Synonyms=GTD1, HAC13, HAF1, TAF1A; OrderedLocusNames=At1g32750;
GN ORFNames=F6N18.13;
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 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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 INTERACTION WITH TAF7; TAF14B; TBP1 AND TBP2.
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).
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 (By similarity).
CC {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 TAF7 and TAF14B, and
CC (via N-terminus) with TBP1 and TBP2. {ECO:0000269|PubMed:17340043}.
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 TAF1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF25977.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF510669; AAM34782.1; -; mRNA.
DR EMBL; AC017118; AAF25977.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE31524.1; -; Genomic_DNA.
DR PIR; D86452; D86452.
DR RefSeq; NP_174552.1; NM_103009.4.
DR AlphaFoldDB; Q8LRK9; -.
DR SMR; Q8LRK9; -.
DR BioGRID; 25403; 10.
DR IntAct; Q8LRK9; 10.
DR STRING; 3702.AT1G32750.1; -.
DR iPTMnet; Q8LRK9; -.
DR PaxDb; Q8LRK9; -.
DR PRIDE; Q8LRK9; -.
DR ProteomicsDB; 245284; -.
DR EnsemblPlants; AT1G32750.1; AT1G32750.1; AT1G32750.
DR GeneID; 840169; -.
DR Gramene; AT1G32750.1; AT1G32750.1; AT1G32750.
DR KEGG; ath:AT1G32750; -.
DR Araport; AT1G32750; -.
DR TAIR; locus:2035574; AT1G32750.
DR eggNOG; KOG0008; Eukaryota.
DR HOGENOM; CLU_236945_0_0_1; -.
DR InParanoid; Q8LRK9; -.
DR OMA; KHEFRDD; -.
DR OrthoDB; 103411at2759; -.
DR PhylomeDB; Q8LRK9; -.
DR PRO; PR:Q8LRK9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8LRK9; baseline and differential.
DR Genevisible; Q8LRK9; 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:0009294; P:DNA-mediated transformation; IMP:TAIR.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IBA:GO_Central.
DR Gene3D; 1.10.1100.10; -; 1.
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; IPR009067; TAF_II_230-bd.
DR InterPro; IPR036741; TAFII-230_TBP-bd_sf.
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; PF09247; TBP-binding; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF47055; SSF47055; 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 1: Evidence at protein level;
KW Activator; Bromodomain; Chromatin regulator; Coiled coil; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..1919
FT /note="Transcription initiation factor TFIID subunit 1"
FT /id="PRO_0000269753"
FT DOMAIN 661..737
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 1816..1886
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1287..1314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1408..1679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1726..1746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1713..1750
FT /evidence="ECO:0000255"
FT COMPBIAS 144..158
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1502..1529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1531..1564
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1565..1598
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1599..1656
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1919 AA; 217194 MW; EDB5443616D371BF CRC64;
MAESNGKGSH NETSSDDDDE YEDNSRGFNL GFIFGNVDNS GDLDADYLDE DAKEHLSALA
DKLGSSLPDI NLLAKSERTA SDPAEQDYDR KAEDAVDYED IDEEYDGPEV QVVSEEDHLL
PKKEYFSTAV ALGSLKSRAS VFDDEDYDEE EEQEEEQAPV EKSLETEKRE PVVLKEDKAL
EYEEEASILD KEDHMDTEDV QEEEVDELLE GTLDDKGATP LPTLYVEDGM VILQFSEIFA
IHEPPQKRDR RENRYVTCRD KYKSMDISEL VEDDEEVLLK SHGRIDTHVE QADLIQLDVP
FPIREGLQLV KASTIGGITP ESREFTKLGR DSCIMGELLK QDFIDDNSSL CQSQLSMQVF
PLDQHEWERR IIWEHSPEIS GNSGEIFEPG LEPEGMLVKG TNSETEQESL NVVNSRVQVQ
ADNNMFVPFS ANLLESFGSR GSQSTNESTN KSRHHPQLLR LESQWDENHL SGNDEAGVKK
IKRLEKDALG RFSRLVLRER DLGDEAWLDS IIWDSEKELS RSKLIFDLQD EQMVFEIFDN
EESKNLQLHA GAMIVSRSSK SKDETFQEGC ESNSGWQFNL SNDKFYMNGK SSQQLQANTN
KSSVHSLRVF HSVPAIKLQT MKSKLSNKDI ANFHRPKALW YPHDNELAIK QQGKLPTRGS
MKIIVKSLGG KGSKLHVGIE ESVSSLRAKA SRKLDFKETE AVKMFYKGKE LDDEKSLAAQ
NVQPNSLVHL IRTKVHLWPW AQKLPGENKS LRPPGAFKKK SDLSTKDGHV FLMEYCEERP
LMLSNAGMGA NLCTYYQKSS PEDQRGNLLR NQSDTLGNVM ILEPGDKSPF LGEIHAGCSQ
SSVETNMYKA PIFPQRLQST DYLLVRSPKG KLSLRRIDKI VVVGQQEPRM EVMSPGSKNL
QTYLVNRMLV YVYREFFKRG GGEHPIAADE LSFLFSNLTD AIIKKNMKII ACWKRDKNGQ
SYWTKKDSLL EPPESELKKL VAPEHVCSYE SMLAGLYRLK HLGITRFTLP ASISNALAQL
PDEAIALAAA SHIERELQIT PWNLSSNFVA CTNQDRANIE RLEITGVGDP SGRGLGFSYV
RAAPKAPAAA GHMKKKAAAG RGAPTVTGTD ADLRRLSMEA AREVLIKFNV PDEIIAKQTR
WHRIAMIRKL SSEQAASGVK VDPTTIGKYA RGQRMSFLQM QQQAREKCQE IWDRQLLSLS
AFDGDENESE NEANSDLDSF AGDLENLLDA EEGGEGEESN ISKNDKLDGV KGLKMRRRPS
QVETDEEIED EATEYAELCR LLMQDEDQKK KKKKMKGVGE GMGSYPPPRP NIALQSGEPV
RKANAMDKKP IAIQPDASFL VNESTIKDNR NVDSIIKTPK GKQVKENSNS LGQLKKVKIL
NENLKVFKEK KSARENFVCG ACGQHGHMRT NKHCPRYREN TESQPEGIDM DKSAGKPSSS
EPSGLPKLKP IKNSKAAPKS AMKTSVDEAL KGDKLSSKTG GLPLKFRYGI PAGDLSDKPV
SEAPGSSEQA VVSDIDTGIK STSKISKLKI SSKAKPKESK GESERRSHSL MPTFSRERGE
SESHKPSVSG QPLSSTERNQ AASSRHTISI PRPSLSMDTD QAESRRPHLV IRPPTEREQP
QKKLVIKRSK EMNDHDMSSL EESPRFESRK TKRMAELAGF QRQQSFRLSE NSLERRPKED
RVWWEEEEIS TGRHREVRAR RDYDDMSVSE EPNEIAEIRR YEEVIRSERE EEERQKAKKK
KKKKKLQPEI VEGYLEDYPP RKNDRRLSER GRNVRSRYVS DFERDGAEYA PQPKRRKKGE
VGLANILERI VDTLRLKEEV SRLFLKPVSK KEAPDYLDIV ENPMDLSTIR DKVRKIEYRN
REQFRHDVWQ IKYNAHLYND GRNPGIPPLA DQLLEICDYL LDDYEDQLKE AEKGIDPND
