TAF11_DROME
ID TAF11_DROME Reviewed; 196 AA.
AC P49906; Q9VL90;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Transcription initiation factor TFIID subunit 11;
DE AltName: Full=TAFII30 beta;
DE AltName: Full=Transcription initiation factor TFIID 28 kDa subunit beta;
DE Short=p28-beta;
GN Name=Taf11; Synonyms=TAF30-BETA; ORFNames=CG4079;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH TAF2 AND TAF4.
RX PubMed=8276241; DOI=10.1101/gad.7.12b.2587;
RA Yokomori K., Chen J.L., Admon A., Zhou S., Tjian R.;
RT "Molecular cloning and characterization of dTAFII30 alpha and dTAFII30
RT beta: two small subunits of Drosophila TFIID.";
RL Genes Dev. 7:2587-2597(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Nakatani Y.;
RT "Molecular cloning of the 28 kDa subunit (p28b) of Drosophila transcription
RT initiation factor TFIID.";
RL Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-16, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: TFIID is a multimeric protein complex that plays a central
CC role in mediating promoter responses to various activators and
CC repressors.
CC -!- SUBUNIT: Belongs to the TFIID complex which is composed of TATA binding
CC protein (Tbp) and a number of TBP-associated factors (TAFs). Interacts
CC with Taf2 and Taf4. {ECO:0000269|PubMed:8276241}.
CC -!- INTERACTION:
CC P49906; Q9VJQ5: NC2beta; NbExp=3; IntAct=EBI-187533, EBI-176193;
CC P49906; Q9VIP1: Taf13; NbExp=4; IntAct=EBI-187533, EBI-90043;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the TAF11 family. {ECO:0000305}.
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DR EMBL; S67660; AAB29541.1; -; mRNA.
DR EMBL; U06457; AAB19245.1; -; mRNA.
DR EMBL; AE014134; AAF52806.1; -; Genomic_DNA.
DR PIR; B49453; B49453.
DR RefSeq; NP_723484.1; NM_164871.3.
DR AlphaFoldDB; P49906; -.
DR SMR; P49906; -.
DR BioGRID; 60390; 20.
DR DIP; DIP-18832N; -.
DR IntAct; P49906; 11.
DR STRING; 7227.FBpp0079514; -.
DR iPTMnet; P49906; -.
DR PaxDb; P49906; -.
DR DNASU; 34293; -.
DR EnsemblMetazoa; FBtr0079924; FBpp0079514; FBgn0011291.
DR GeneID; 34293; -.
DR KEGG; dme:Dmel_CG4079; -.
DR CTD; 6882; -.
DR FlyBase; FBgn0011291; Taf11.
DR VEuPathDB; VectorBase:FBgn0011291; -.
DR eggNOG; KOG3219; Eukaryota.
DR GeneTree; ENSGT00390000013228; -.
DR HOGENOM; CLU_088696_0_1_1; -.
DR InParanoid; P49906; -.
DR OMA; PTQQKNN; -.
DR OrthoDB; 1418543at2759; -.
DR PhylomeDB; P49906; -.
DR Reactome; R-DME-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-DME-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-DME-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-DME-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-DME-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-DME-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-DME-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR SignaLink; P49906; -.
DR BioGRID-ORCS; 34293; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 34293; -.
DR PRO; PR:P49906; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0011291; Expressed in eye disc (Drosophila) and 20 other tissues.
DR ExpressionAtlas; P49906; baseline and differential.
DR Genevisible; P49906; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0070578; C:RISC-loading complex; IDA:FlyBase.
DR GO; GO:0005669; C:transcription factor TFIID complex; IDA:FlyBase.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR GO; GO:1900370; P:positive regulation of post-transcriptional gene silencing by RNA; IMP:FlyBase.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IBA:GO_Central.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; ISS:FlyBase.
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 Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..196
FT /note="Transcription initiation factor TFIID subunit 11"
FT /id="PRO_0000118906"
FT REGION 1..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
SQ SEQUENCE 196 AA; 22091 MW; E852855E3F598AC9 CRC64;
MDEILFPTQQ KSNSLSDGDD VDLKFFQSAS GERKDSDTSD PGNDADRDGK DADGDNDNKN
TDGDGDSGEP AHKKLKTKKE LEEEERERMQ VLVSNFTEEQ LDRYEMYRRS AFPKAAVKRL
MQTITGCSVS QNVVIAMSGI AKVFVGEVVE EALDVMEAQG ESGALQPKFI REAVRRLRTK
DRMPIGRYQQ PYFRLN
