TAF6_DROME
ID TAF6_DROME Reviewed; 606 AA.
AC P49847; Q961B6; Q9VW16;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-JAN-2003, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Transcription initiation factor TFIID subunit 6;
DE AltName: Full=TAFII-60;
DE AltName: Full=TAFII-62;
DE AltName: Full=Transcription initiation factor TFIID 62 kDa subunit;
DE Short=p62;
GN Name=Taf6; Synonyms=Taf60; ORFNames=CG32211;
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-606, AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=7545910; DOI=10.1038/367484a0;
RA Kokubo T., Gong D.-W., Wootton J.C., Horikoshi M., Roeder R.G.,
RA Nakatani Y.;
RT "Molecular cloning of Drosophila TFIID subunits.";
RL Nature 367:484-487(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 7-606, PARTIAL PROTEIN SEQUENCE, FUNCTION,
RP AND INTERACTION WITH TAF1.
RC STRAIN=Oregon-R;
RX PubMed=8262073; DOI=10.1002/j.1460-2075.1993.tb06226.x;
RA Weinzierl R.O., Ruppert S., Dynlacht B.D., Tanese N., Tjian R.;
RT "Cloning and expression of Drosophila TAFII60 and human TAFII70 reveal
RT conserved interactions with other subunits of TFIID.";
RL EMBO J. 12:5303-5309(1993).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-546; SER-547 AND SER-550, 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).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 15-84, AND INTERACTION WITH E(Y)1.
RX PubMed=8598927; DOI=10.1038/380316a0;
RA Xie X., Kokubo T., Cohen S.L., Mirza U.A., Hoffmann A., Chait B.T.,
RA Roeder R.G., Nakatani Y., Burley S.K.;
RT "Structural similarity between TAFs and the heterotetrameric core of the
RT histone octamer.";
RL Nature 380:316-322(1996).
CC -!- FUNCTION: TFIID is a multimeric protein complex that plays a central
CC role in mediating promoter responses to various activators and
CC repressors. {ECO:0000269|PubMed:8262073}.
CC -!- SUBUNIT: Belongs to the TFIID complex which is composed of TATA binding
CC protein (Tbp) and a number of TBP-associated factors (TAFs). E(y)1 and
CC Taf6 exist as a heterotetramer. Interacts with Taf1.
CC {ECO:0000269|PubMed:8262073, ECO:0000269|PubMed:8598927}.
CC -!- INTERACTION:
CC P49847; Q27272: e(y)1; NbExp=2; IntAct=EBI-136204, EBI-174260;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the TAF6 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA16536.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAC46480.1; Type=Erroneous initiation; 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; AE014296; AAF49139.2; -; Genomic_DNA.
DR EMBL; AY051702; AAK93126.1; -; mRNA.
DR EMBL; U06459; AAC46480.1; ALT_INIT; mRNA.
DR EMBL; L25443; AAA16536.1; ALT_INIT; mRNA.
DR RefSeq; NP_524161.2; NM_079437.4.
DR PDB; 1TAF; X-ray; 2.00 A; B=15-84.
DR PDBsum; 1TAF; -.
DR AlphaFoldDB; P49847; -.
DR SMR; P49847; -.
DR BioGRID; 65404; 33.
DR DIP; DIP-778N; -.
DR IntAct; P49847; 7.
DR STRING; 7227.FBpp0074709; -.
DR iPTMnet; P49847; -.
DR PaxDb; P49847; -.
DR PRIDE; P49847; -.
DR EnsemblMetazoa; FBtr0074941; FBpp0074709; FBgn0010417.
DR GeneID; 40134; -.
DR KEGG; dme:Dmel_CG32211; -.
DR CTD; 6878; -.
DR FlyBase; FBgn0010417; Taf6.
DR VEuPathDB; VectorBase:FBgn0010417; -.
DR eggNOG; KOG2549; Eukaryota.
DR GeneTree; ENSGT00640000091486; -.
DR InParanoid; P49847; -.
DR OMA; QDSAKFM; -.
DR OrthoDB; 384329at2759; -.
DR PhylomeDB; P49847; -.
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; P49847; -.
DR BioGRID-ORCS; 40134; 1 hit in 1 CRISPR screen.
DR EvolutionaryTrace; P49847; -.
DR GenomeRNAi; 40134; -.
DR PRO; PR:P49847; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0010417; Expressed in wing disc and 23 other tissues.
DR ExpressionAtlas; P49847; baseline and differential.
DR Genevisible; P49847; DM.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0000124; C:SAGA complex; IEA:InterPro.
DR GO; GO:0046695; C:SLIK (SAGA-like) complex; IEA:InterPro.
DR GO; GO:0005669; C:transcription factor TFIID complex; IDA:FlyBase.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor 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 GO; GO:0006366; P:transcription by RNA polymerase II; IDA:FlyBase.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; ISS:FlyBase.
DR CDD; cd08050; TAF6C; 1.
DR Gene3D; 1.10.20.10; -; 1.
DR Gene3D; 1.25.40.770; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR037796; TAF6.
DR InterPro; IPR011442; TAF6_C.
DR InterPro; IPR046344; TAF6_C_sf.
DR InterPro; IPR004823; TAF_TATA-bd_Histone-like_dom.
DR PANTHER; PTHR10221; PTHR10221; 1.
DR Pfam; PF02969; TAF; 1.
DR Pfam; PF07571; TAF6_C; 1.
DR SMART; SM00803; TAF; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..606
FT /note="Transcription initiation factor TFIID subunit 6"
FT /id="PRO_0000118877"
FT MOD_RES 546
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 547
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 550
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 3
FT /note="G -> K (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="F -> L (in Ref. 5; AAA16536)"
FT /evidence="ECO:0000305"
FT CONFLICT 582
FT /note="D -> E (in Ref. 4; AAC46480 and 5; AAA16536)"
FT /evidence="ECO:0000305"
FT HELIX 23..32
FT /evidence="ECO:0007829|PDB:1TAF"
FT HELIX 40..67
FT /evidence="ECO:0007829|PDB:1TAF"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:1TAF"
FT HELIX 75..82
FT /evidence="ECO:0007829|PDB:1TAF"
SQ SEQUENCE 606 AA; 65654 MW; 9D93C3496A23C0A3 CRC64;
MSGKPSKPSS PSSSMLYGSS ISAESMKVIA ESIGVGSLSD DAAKELAEDV SIKLKRIVQD
AAKFMNHAKR QKLSVRDIDM SLKVRNVEPQ YGFVAKDFIP FRFASGGGRE LHFTEDKEID
LGEITSTNSV KIPLDLTLRS HWFVVEGVQP TVPENPPPLS KDSQLLDSVN PVIKMDQGLN
KDAAGKPTTG KIHKLKNVET IHVKQLATHE LSVEQQLYYK EITEACVGSD EPRRGEALQS
LGSDPGLHEM LPRMCTFIAE GVKVNVVQNN LALLIYLMRM VRALLDNPSL FLEKYLHELI
PSVMTCIVSK QLCMRPELDN HWALRDFASR LMAQICKNFN TLTNNLQTRV TRIFSKALQN
DKTHLSSLYG SIAGLSELGG EVIKVFIIPR LKFISERIEP HLLGTSISNT DKTAAGHIRA
MLQKCCPPIL RQMRSAPDTA EDYKNDFGFL GPSLCQAVVK VRNAPASSIV TLSSNTINTA
PITSAAQTAT TIGRVSMPTT QRQGSPGVSS LPQIRAIQAN QPAQKFVIVT QNSPQQGQAK
VVRRGSSPHS VVLSAASNAA SASNSNSSSS GSLLAAAQRS SDNVCVIAGS EAPAVDGITV
QSFRAS