TAF12_YEAST
ID TAF12_YEAST Reviewed; 539 AA.
AC Q03761; D6VSC8;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Transcription initiation factor TFIID subunit 12;
DE AltName: Full=TAFII-61;
DE Short=TAFII61;
DE AltName: Full=TAFII-68;
DE Short=TAFII68;
DE AltName: Full=TBP-associated factor 12;
DE AltName: Full=TBP-associated factor 61 kDa;
GN Name=TAF12; Synonyms=TAF61, TAF68; OrderedLocusNames=YDR145W;
GN ORFNames=YD8358.02;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION, AND TAF-TAF INTERACTION THROUGH HISTONE-FOLD DOMAIN.
RX PubMed=9695952; DOI=10.1016/s0092-8674(00)81423-3;
RA Birck C., Poch O., Romier C., Ruff M., Mengus G., Lavigne A.C.,
RA Davidson I., Moras D.;
RT "Human TAF(II)28 and TAF(II)18 interact through a histone fold encoded by
RT atypical evolutionary conserved motifs also found in the SPT3 family.";
RL Cell 94:239-249(1998).
RN [4]
RP FUNCTION, IDENTIFICATION IN THE SAGA COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=9674426; DOI=10.1016/s0092-8674(00)81220-9;
RA Grant P.A., Schieltz D., Pray-Grant M.G., Steger D.J., Reese J.C.,
RA Yates J.R. III, Workman J.L.;
RT "A subset of TAF(II)s are integral components of the SAGA complex required
RT for nucleosome acetylation and transcriptional stimulation.";
RL Cell 94:45-53(1998).
RN [5]
RP FUNCTION IN HISTONE ACETYLATION AT THE SAGA COMPLEX.
RX PubMed=10026213; DOI=10.1074/jbc.274.9.5895;
RA Grant P.A., Eberharter A., John S., Cook R.G., Turner B.M., Workman J.L.;
RT "Expanded lysine acetylation specificity of Gcn5 in native complexes.";
RL J. Biol. Chem. 274:5895-5900(1999).
RN [6]
RP FUNCTION, AND IDENTIFICATION IN THE TFIID COMPLEX.
RX PubMed=10788514; DOI=10.1074/jbc.275.18.13895;
RA Sanders S.L., Weil P.A.;
RT "Identification of two novel TAF subunits of the yeast Saccharomyces
RT cerevisiae TFIID complex.";
RL J. Biol. Chem. 275:13895-13900(2000).
RN [7]
RP FUNCTION, AND INTERACTION IN TFIID AND SAGA.
RX PubMed=11238921; DOI=10.1128/mcb.21.5.1841-1853.2001;
RA Gangloff Y.G., Sanders S.L., Romier C., Kirschner D.B., Weil P.A., Tora L.,
RA Davidson I.;
RT "Histone folds mediate selective heterodimerization of yeast TAF(II)25 with
RT TFIID components yTAF(II)47 and yTAF(II)65 and with SAGA component ySPT7.";
RL Mol. Cell. Biol. 21:1841-1853(2001).
RN [8]
RP FUNCTION, AND HISTONE-FOLD DOMAIN CHARACTERIZATION.
RX PubMed=11295558; DOI=10.1016/s0968-0004(00)01741-2;
RA Gangloff Y.G., Romier C., Thuault S., Werten S., Davidson I.;
RT "The histone fold is a key structural motif of transcription factor
RT TFIID.";
RL Trends Biochem. Sci. 26:250-257(2001).
RN [9]
RP FUNCTION, AND TAF OCTAMER FORMATION.
RX PubMed=11473260; DOI=10.1038/90408;
RA Selleck W., Howley R., Fang Q., Podolny V., Fried M.G., Buratowski S.,
RA Tan S.;
RT "A histone fold TAF octamer within the yeast TFIID transcriptional
RT coactivator.";
RL Nat. Struct. Biol. 8:695-700(2001).
RN [10]
RP IDENTIFICATION IN THE SALSA COMPLEX.
RX PubMed=12186975; DOI=10.1073/pnas.182021199;
RA Sterner D.E., Belotserkovskaya R., Berger S.L.;
RT "SALSA, a variant of yeast SAGA, contains truncated Spt7, which correlates
RT with activated transcription.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:11622-11627(2002).
RN [11]
RP FUNCTION, AND IDENTIFICATION IN THE SAGA COMPLEX.
RX PubMed=12052880; DOI=10.1128/mcb.22.13.4723-4738.2002;
RA Sanders S.L., Jennings J., Canutescu A., Link A.J., Weil P.A.;
RT "Proteomics of the eukaryotic transcription machinery: identification of
RT proteins associated with components of yeast TFIID by multidimensional mass
RT spectrometry.";
RL Mol. Cell. Biol. 22:4723-4738(2002).
RN [12]
RP FUNCTION, AND TFIID STOICHIOMETRY.
RX PubMed=12138208; DOI=10.1128/mcb.22.16.6000-6013.2002;
RA Sanders S.L., Garbett K.A., Weil P.A.;
RT "Molecular characterization of Saccharomyces cerevisiae TFIID.";
RL Mol. Cell. Biol. 22:6000-6013(2002).
RN [13]
RP IDENTIFICATION IN THE SLIK COMPLEX.
RX PubMed=12446794; DOI=10.1128/mcb.22.24.8774-8786.2002;
RA Pray-Grant M.G., Schieltz D., McMahon S.J., Wood J.M., Kennedy E.L.,
RA Cook R.G., Workman J.L., Yates J.R. III, Grant P.A.;
RT "The novel SLIK histone acetyltransferase complex functions in the yeast
RT retrograde response pathway.";
RL Mol. Cell. Biol. 22:8774-8786(2002).
RN [14]
RP FUNCTION.
RX PubMed=12516863; DOI=10.1023/a:1021258713850;
RA Martinez E.;
RT "Multi-protein complexes in eukaryotic gene transcription.";
RL Plant Mol. Biol. 50:925-947(2002).
RN [15]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [16]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [17]
RP IDENTIFICATION IN THE SLIK COMPLEX.
RX PubMed=15647753; DOI=10.1038/nature03242;
RA Pray-Grant M.G., Daniel J.A., Schieltz D., Yates J.R. III, Grant P.A.;
RT "Chd1 chromodomain links histone H3 methylation with SAGA- and SLIK-
RT dependent acetylation.";
RL Nature 433:434-438(2005).
RN [18]
RP 3D-STRUCTURE, AND ELECTRON MICROSCOPY OF TFIID.
RX PubMed=12093743; DOI=10.1093/emboj/cdf342;
RA Leurent C., Sanders S.L., Ruhlmann C., Mallouh V., Weil P.A.,
RA Kirschner D.B., Tora L., Schultz P.;
RT "Mapping histone fold TAFs within yeast TFIID.";
RL EMBO J. 21:3424-3433(2002).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-286, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129 AND SER-286, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [23]
RP 3D-STRUCTURE MODELING OF THE SAGA COMPLEX.
RX PubMed=15260971; DOI=10.1016/j.molcel.2004.06.005;
RA Wu P.Y., Ruhlmann C., Winston F., Schultz P.;
RT "Molecular architecture of the S. cerevisiae SAGA complex.";
RL Mol. Cell 15:199-208(2004).
CC -!- FUNCTION: Functions as a component of the DNA-binding general
CC transcription factor complex TFIID and the transcription regulatory
CC histone acetylation (HAT) complexes SAGA, SALSA and SLIK. Binding of
CC TFIID to a promoter (with or without TATA element) is the initial step
CC in preinitiation complex (PIC) formation. TFIID plays a key role in the
CC regulation of gene expression by RNA polymerase II through different
CC activities such as transcription activator interaction, core promoter
CC recognition and selectivity, TFIIA and TFIIB interaction, chromatin
CC modification (histone acetylation by TAF1), facilitation of DNA opening
CC and initiation of transcription. SAGA is involved in RNA polymerase II-
CC dependent transcriptional regulation of approximately 10% of yeast
CC genes. At the promoters, SAGA is required for recruitment of the basal
CC transcription machinery. It influences RNA polymerase II
CC transcriptional activity through different activities such as TBP
CC interaction (SPT3, SPT8 and SPT20) and promoter selectivity,
CC interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1),
CC and chromatin modification through histone acetylation (GCN5) and
CC deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some
CC extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts
CC with DNA via upstream activating sequences (UASs). SALSA, an altered
CC form of SAGA, may be involved in positive transcriptional regulation.
CC SLIK is proposed to have partly overlapping functions with SAGA. It
CC preferentially acetylates methylated histone H3, at least after
CC activation at the GAL1-10 locus. {ECO:0000269|PubMed:10026213,
CC ECO:0000269|PubMed:10788514, ECO:0000269|PubMed:11238921,
CC ECO:0000269|PubMed:11295558, ECO:0000269|PubMed:11473260,
CC ECO:0000269|PubMed:12052880, ECO:0000269|PubMed:12138208,
CC ECO:0000269|PubMed:12516863, ECO:0000269|PubMed:9674426,
CC ECO:0000269|PubMed:9695952}.
CC -!- SUBUNIT: In TFIID, TAF12 heterodimerizes with TAF4, forming ultimately
CC an octamer consisting of a TAF6/TAF9 heterotetramer core flanked by
CC TAF4/TAF12 dimers on either side, similar to the histone H2A/H2B/H3/H4
CC octamer. The 1.2 MDa TFIID complex is composed of TATA binding protein
CC (TBP) and the 14 TBP-associated factors. One copy of each TAF1, TAF2,
CC TAF3, TAF7, TAF8, TAF11, TAF13, two copies of each TAF4, TAF5, TAF6,
CC TAF9, TAF10, TAF12, and three copies of TAF14. Component of the 1.8 MDa
CC SAGA complex, which consists of at least TRA1, CHD1, SPT7, TAF5, ADA3,
CC SGF73, SPT20/ADA5, SPT8, TAF12, TAF6, HFI1/ADA1, UBP8, GCN5, ADA2,
CC SPT3, SGF29, TAF10, TAF9, SGF11 and SUS1. TAF5, TAF6, TAF9, TAF19,
CC TAF12 and ADA1 seem to be present in 2 copies. SAGA is built of 5
CC distinct domains with specialized functions. Domain I (containing TRA1)
CC probably represents the activator interaction surface. Domain II
CC (containing TAF5 and TAF6, and probably TAF9 and TAF10), domain III
CC (containing GCN5, TAF10, SPT7, TAF5 and ADA1, and probably ADA2, ADA3
CC and TAF12), and domain IV (containing HFI1/ADA1 and TAF6, and probably
CC TAF9) are believed to play primarily an architectural role. Domain III
CC also harbors the HAT activity. Domain V (containing SPT3 and SPT20, and
CC probably SPT8) represents the TBP-interacting module, which may be
CC associated transiently with SAGA. Component of the SALSA complex, which
CC consists of at least TRA1, SPT7 (C-terminal truncated form), TAF5,
CC ADA3, SPT20, TAF12, TAF6, HFI1, GCN5, ADA2 and SPT3. Component of the
CC SLIK complex, which consists of at least TRA1, CHD1, SPT7, TAF5, ADA3,
CC SPT20, RTG2, TAF12, TAF6, HFI1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10
CC and TAF9. {ECO:0000269|PubMed:10788514, ECO:0000269|PubMed:12052880,
CC ECO:0000269|PubMed:12186975, ECO:0000269|PubMed:12446794,
CC ECO:0000269|PubMed:15647753, ECO:0000269|PubMed:9674426}.
CC -!- INTERACTION:
CC Q03761; P35817: BDF1; NbExp=2; IntAct=EBI-35097, EBI-3493;
CC Q03761; Q12060: HFI1; NbExp=10; IntAct=EBI-35097, EBI-8287;
CC Q03761; Q12030: TAF10; NbExp=10; IntAct=EBI-35097, EBI-18889;
CC Q03761; Q03761: TAF12; NbExp=4; IntAct=EBI-35097, EBI-35097;
CC Q03761; P50105: TAF4; NbExp=13; IntAct=EBI-35097, EBI-11231;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 930 (+/-45) molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TAF12 family. {ECO:0000305}.
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DR EMBL; Z50046; CAA90368.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11988.1; -; Genomic_DNA.
DR PIR; S57972; S57972.
DR RefSeq; NP_010429.1; NM_001180452.1.
DR PDB; 6T9I; EM; 3.90 A; I=1-539.
DR PDB; 6T9J; EM; 3.40 A; I=1-539.
DR PDB; 6T9K; EM; 3.30 A; I=1-539.
DR PDBsum; 6T9I; -.
DR PDBsum; 6T9J; -.
DR PDBsum; 6T9K; -.
DR AlphaFoldDB; Q03761; -.
DR SMR; Q03761; -.
DR BioGRID; 32199; 778.
DR ComplexPortal; CPX-1642; General transcription factor complex TFIID.
DR ComplexPortal; CPX-656; SAGA complex.
DR ComplexPortal; CPX-675; SLIK (SAGA-like) complex.
DR DIP; DIP-1302N; -.
DR IntAct; Q03761; 120.
DR MINT; Q03761; -.
DR STRING; 4932.YDR145W; -.
DR iPTMnet; Q03761; -.
DR MaxQB; Q03761; -.
DR PaxDb; Q03761; -.
DR PRIDE; Q03761; -.
DR EnsemblFungi; YDR145W_mRNA; YDR145W; YDR145W.
DR GeneID; 851723; -.
DR KEGG; sce:YDR145W; -.
DR SGD; S000002552; TAF12.
DR VEuPathDB; FungiDB:YDR145W; -.
DR eggNOG; KOG1142; Eukaryota.
DR GeneTree; ENSGT00390000002144; -.
DR HOGENOM; CLU_021602_0_0_1; -.
DR InParanoid; Q03761; -.
DR OMA; ADDFITN; -.
DR BioCyc; YEAST:G3O-29742-MON; -.
DR Reactome; R-SCE-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-SCE-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-SCE-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-SCE-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-SCE-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR PRO; PR:Q03761; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q03761; protein.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0000124; C:SAGA complex; IDA:SGD.
DR GO; GO:0046695; C:SLIK (SAGA-like) complex; IDA:SGD.
DR GO; GO:0005669; C:transcription factor TFIID complex; IDA:SGD.
DR GO; GO:0003682; F:chromatin binding; IDA:SGD.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0060090; F:molecular adaptor activity; IMP:SGD.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IDA:SGD.
DR GO; GO:0017025; F:TBP-class protein binding; IDA:SGD.
DR GO; GO:0006325; P:chromatin organization; IDA:SGD.
DR GO; GO:0016573; P:histone acetylation; IDA:SGD.
DR GO; GO:0016578; P:histone deubiquitination; IC:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IMP:SGD.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:SGD.
DR CDD; cd07981; TAF12; 1.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR037794; TAF12.
DR InterPro; IPR003228; TFIID_TAF12_dom.
DR PANTHER; PTHR12264; PTHR12264; 1.
DR Pfam; PF03847; TFIID_20kDa; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Coiled coil; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..539
FT /note="Transcription initiation factor TFIID subunit 12"
FT /id="PRO_0000118909"
FT DOMAIN 413..490
FT /note="Histone-fold"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 153..202
FT /evidence="ECO:0000255"
FT COILED 239..285
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT STRAND 387..392
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 394..398
FT /evidence="ECO:0007829|PDB:6T9J"
FT STRAND 400..402
FT /evidence="ECO:0007829|PDB:6T9J"
FT HELIX 419..427
FT /evidence="ECO:0007829|PDB:6T9K"
FT STRAND 436..438
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 440..467
FT /evidence="ECO:0007829|PDB:6T9K"
FT STRAND 471..473
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 475..484
FT /evidence="ECO:0007829|PDB:6T9K"
FT STRAND 492..494
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 508..523
FT /evidence="ECO:0007829|PDB:6T9K"
SQ SEQUENCE 539 AA; 61073 MW; A8FC84E46F8370D3 CRC64;
MSSNPENSGV NANNNTGTGN ADAITGAQQN MVLQPRQLQE MAAKFRTLLT EARNVGETTP
RGKELMFQAA KIKQVYDALT LNRRRQQAAQ AYNNTSNSNS SNPASIPTEN VPNSSQQQQQ
QQQQTRNNSN KFSNMIKQVL TPEENQEYEK LWQNFQVRHT SIKEKETYLK QNIDRLEQEI
NKQTDEGPKQ QLQEKKIELL NDWKVLKIEY TKLFNNYQNS KKTFYVECAR HNPALHKFLQ
ESTQQQRVQQ QRVQQQQQQQ QQQQQQQQQQ QQQQQQRQGQ NQRKISSSNS TEIPSVTGPD
ALKSQQQQQN TITATNNPRG NVNTSQTEQS KAKVTNVNAT ASMLNNISSS KSAIFKQTEP
AIPISENIST KTPAPVAYRS NRPTITGGSA MNASALNTPA TTKLPPYEMD TQRVMSKRKL
RELVKTVGID EGDGETVIDG DVEELLLDLA DDFVTNVTAF SCRLAKHRKS DNLEARDIQL
HLERNWNIRI PGYSADEIRS TRKWNPSQNY NQKLQSITSD KVAAAKNNGN NVASLNTKK
