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TAF6_YEAST
ID   TAF6_YEAST              Reviewed;         516 AA.
AC   P53040; D6VU35;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 193.
DE   RecName: Full=Transcription initiation factor TFIID subunit 6;
DE   AltName: Full=TBP-associated factor 6;
DE   AltName: Full=TBP-associated factor 60 kDa;
DE            Short=TAFII-60;
DE            Short=TAFII60;
GN   Name=TAF6; Synonyms=TAF60; OrderedLocusNames=YGL112C; ORFNames=G2985;
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 [GENOMIC DNA], AND PROTEIN SEQUENCE OF 72-92; 99-132
RP   AND 222-229.
RC   STRAIN=ATCC 76621 / YPH252;
RX   PubMed=7667272; DOI=10.1073/pnas.92.18.8224;
RA   Poon D., Bai Y., Campbell A.M., Bjorklund S., Kim Y.-J., Zhou S.,
RA   Kornberg R.D., Weil P.A.;
RT   "Identification and characterization of a TFIID-like multiprotein complex
RT   from Saccharomyces cerevisiae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:8224-8228(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9046090;
RX   DOI=10.1002/(sici)1097-0061(199701)13:1<85::aid-yea53>3.0.co;2-e;
RA   Paoluzi S., Minenkova O., Castagnoli L.;
RT   "The genes encoding the transcription factor yTAFII60, the G4p1 protein and
RT   a putative glucose transporter are contained in a 12.3 kb DNA fragment on
RT   the left arm of Saccharomyces cerevisiae chromosome VII.";
RL   Yeast 13:85-91(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(1997).
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [6]
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   [7]
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   [8]
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   [9]
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   [10]
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   [11]
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   [12]
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   [13]
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   [14]
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   [15]
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   [16]
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   [17]
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   [18]
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   [19]
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   [20]
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   [21]
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 regulatory transcription
CC       regulatory histone acetylation (HAT) complexes SAGA, SALSA and SLIK.
CC       Binding of TFIID to a promoter (with or without TATA element) is the
CC       initial step in preinitiation complex (PIC) formation. TFIID plays a
CC       key role in the regulation of gene expression by RNA polymerase II
CC       through different activities such as transcription activator
CC       interaction, core promoter recognition and selectivity, TFIIA and TFIIB
CC       interaction, chromatin modification (histone acetylation by TAF1),
CC       facilitation of DNA opening and initiation of transcription. SAGA is
CC       involved in RNA polymerase II-dependent transcriptional regulation of
CC       approximately 10% of yeast genes. At the promoters, SAGA is required
CC       for recruitment of the basal transcription machinery. It influences RNA
CC       polymerase II transcriptional activity through different activities
CC       such as TBP interaction (SPT3, SPT8 and SPT20) and promoter
CC       selectivity, interaction with transcription activators (GCN5, ADA2,
CC       ADA3 and TRA1), and chromatin modification through histone acetylation
CC       (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone
CC       H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA
CC       interacts with DNA via upstream activating sequences (UASs). SALSA, an
CC       altered form of SAGA, may be involved in positive transcriptional
CC       regulation. SLIK is proposed to have partly overlapping functions with
CC       SAGA. It preferentially acetylates methylated histone H3, at least
CC       after 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, TAF6 heterodimerizes with TAF9, 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       P53040; P35817: BDF1; NbExp=2; IntAct=EBI-18876, EBI-3493;
CC       P53040; Q12060: HFI1; NbExp=9; IntAct=EBI-18876, EBI-8287;
CC       P53040; P46677: TAF1; NbExp=6; IntAct=EBI-18876, EBI-18855;
CC       P53040; Q12030: TAF10; NbExp=8; IntAct=EBI-18876, EBI-18889;
CC       P53040; P38129: TAF5; NbExp=12; IntAct=EBI-18876, EBI-18868;
CC       P53040; P53040: TAF6; NbExp=2; IntAct=EBI-18876, EBI-18876;
CC       P53040; Q05027: TAF9; NbExp=11; IntAct=EBI-18876, EBI-27500;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- MISCELLANEOUS: Present with 6506 (+/-1290) molecules/cell in log phase
CC       SD medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the TAF6 family. {ECO:0000305}.
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DR   EMBL; X97644; CAA66240.1; -; Genomic_DNA.
DR   EMBL; L40145; AAA83389.1; -; Genomic_DNA.
DR   EMBL; Z72634; CAA96819.1; -; Genomic_DNA.
DR   EMBL; AY723809; AAU09726.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA07996.1; -; Genomic_DNA.
DR   PIR; S64120; S64120.
DR   RefSeq; NP_011403.1; NM_001180977.1.
DR   PDB; 6T9I; EM; 3.90 A; E=1-516.
DR   PDB; 6T9K; EM; 3.30 A; E=1-516.
DR   PDBsum; 6T9I; -.
DR   PDBsum; 6T9K; -.
DR   AlphaFoldDB; P53040; -.
DR   SMR; P53040; -.
DR   BioGRID; 33139; 423.
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-981N; -.
DR   IntAct; P53040; 122.
DR   MINT; P53040; -.
DR   STRING; 4932.YGL112C; -.
DR   MaxQB; P53040; -.
DR   PaxDb; P53040; -.
DR   PRIDE; P53040; -.
DR   EnsemblFungi; YGL112C_mRNA; YGL112C; YGL112C.
DR   GeneID; 852766; -.
DR   KEGG; sce:YGL112C; -.
DR   SGD; S000003080; TAF6.
DR   VEuPathDB; FungiDB:YGL112C; -.
DR   eggNOG; KOG2549; Eukaryota.
DR   GeneTree; ENSGT00640000091486; -.
DR   HOGENOM; CLU_021711_3_1_1; -.
DR   InParanoid; P53040; -.
DR   OMA; YFVQFIA; -.
DR   BioCyc; YEAST:G3O-30610-MON; -.
DR   Reactome; R-SCE-674695; RNA Polymerase II Pre-transcription Events.
DR   Reactome; R-SCE-6807505; RNA polymerase II transcribes snRNA genes.
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:P53040; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P53040; protein.
DR   GO; GO:0005829; C:cytosol; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
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: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:0016251; F:RNA polymerase II general transcription initiation factor activity; IEA:InterPro.
DR   GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IDA:SGD.
DR   GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
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:2000144; P:positive regulation of DNA-templated transcription, initiation; IMP:SGD.
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; 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; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..516
FT                   /note="Transcription initiation factor TFIID subunit 6"
FT                   /id="PRO_0000118878"
FT   DOMAIN          6..75
FT                   /note="Histone-fold"
FT   TURN            15..17
FT                   /evidence="ECO:0007829|PDB:6T9K"
FT   HELIX           18..24
FT                   /evidence="ECO:0007829|PDB:6T9K"
FT   HELIX           31..58
FT                   /evidence="ECO:0007829|PDB:6T9K"
FT   HELIX           66..69
FT                   /evidence="ECO:0007829|PDB:6T9K"
FT   HELIX           71..75
FT                   /evidence="ECO:0007829|PDB:6T9K"
FT   STRAND          103..105
FT                   /evidence="ECO:0007829|PDB:6T9K"
FT   STRAND          115..117
FT                   /evidence="ECO:0007829|PDB:6T9K"
FT   HELIX           118..121
FT                   /evidence="ECO:0007829|PDB:6T9K"
FT   STRAND          134..139
FT                   /evidence="ECO:0007829|PDB:6T9K"
FT   STRAND          141..144
FT                   /evidence="ECO:0007829|PDB:6T9K"
FT   TURN            156..160
FT                   /evidence="ECO:0007829|PDB:6T9K"
FT   TURN            163..165
FT                   /evidence="ECO:0007829|PDB:6T9K"
FT   TURN            191..196
FT                   /evidence="ECO:0007829|PDB:6T9K"
FT   STRAND          197..200
FT                   /evidence="ECO:0007829|PDB:6T9K"
FT   TURN            201..205
FT                   /evidence="ECO:0007829|PDB:6T9K"
FT   HELIX           221..231
FT                   /evidence="ECO:0007829|PDB:6T9K"
FT   HELIX           245..257
FT                   /evidence="ECO:0007829|PDB:6T9K"
FT   TURN            262..264
FT                   /evidence="ECO:0007829|PDB:6T9K"
FT   HELIX           265..277
FT                   /evidence="ECO:0007829|PDB:6T9K"
FT   HELIX           283..296
FT                   /evidence="ECO:0007829|PDB:6T9K"
FT   HELIX           306..308
FT                   /evidence="ECO:0007829|PDB:6T9K"
FT   TURN            309..311
FT                   /evidence="ECO:0007829|PDB:6T9K"
FT   HELIX           312..319
FT                   /evidence="ECO:0007829|PDB:6T9K"
FT   HELIX           333..360
FT                   /evidence="ECO:0007829|PDB:6T9K"
FT   TURN            363..367
FT                   /evidence="ECO:0007829|PDB:6T9K"
FT   HELIX           369..380
FT                   /evidence="ECO:0007829|PDB:6T9K"
FT   STRAND          383..385
FT                   /evidence="ECO:0007829|PDB:6T9K"
FT   HELIX           387..398
FT                   /evidence="ECO:0007829|PDB:6T9K"
FT   HELIX           403..406
FT                   /evidence="ECO:0007829|PDB:6T9K"
FT   HELIX           410..412
FT                   /evidence="ECO:0007829|PDB:6T9K"
FT   HELIX           413..419
FT                   /evidence="ECO:0007829|PDB:6T9K"
FT   STRAND          427..429
FT                   /evidence="ECO:0007829|PDB:6T9K"
FT   HELIX           430..432
FT                   /evidence="ECO:0007829|PDB:6T9K"
FT   HELIX           447..459
FT                   /evidence="ECO:0007829|PDB:6T9K"
FT   HELIX           461..463
FT                   /evidence="ECO:0007829|PDB:6T9K"
SQ   SEQUENCE   516 AA;  57902 MW;  14B590E02C16F289 CRC64;
     MSTQQQSYTI WSPQDTVKDV AESLGLENIN DDVLKALAMD VEYRILEIIE QAVKFKRHSK
     RDVLTTDDVS KALRVLNVEP LYGYYDGSEV NKAVSFSKVN TSGGQSVYYL DEEEVDFDRL
     INEPLPQVPR LPTFTTHWLA VEGVQPAIIQ NPNLNDIRVS QPPFIRGAIV TALNDNSLQT
     PVTSTTASAS VTDTGASQHL SNVKPGQNTE VKPLVKHVLS KELQIYFNKV ISTLTAKSQA
     DEAAQHMKQA ALTSLRTDSG LHQLVPYFIQ FIAEQITQNL SDLQLLTTIL EMIYSLLSNT
     SIFLDPYIHS LMPSILTLLL AKKLGGSPKD DSPQEIHEFL ERTNALRDFA ASLLDYVLKK
     FPQAYKSLKP RVTRTLLKTF LDINRVFGTY YGCLKGVSVL EGESIRFFLG NLNNWARLVF
     NESGITLDNI EEHLNDDSNP TRTKFTKEET QILVDTVISA LLVLKKDLPD LYEGKGEKVT
     DEDKEKLLER CGVTIGFHIL KRDDAKELIS AIFFGE
 
 
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