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Transcription initiation factor TFIID subunit 6 (TBP-associated factor 6) (TBP-associated factor 60 kDa) (TAFII-60) (TAFII60)

 TAF6_YEAST              Reviewed;         516 AA.
P53040; D6VU35;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
25-OCT-2017, entry version 161.
RecName: Full=Transcription initiation factor TFIID subunit 6;
AltName: Full=TBP-associated factor 6;
AltName: Full=TBP-associated factor 60 kDa;
Short=TAFII-60;
Short=TAFII60;
Name=TAF6; Synonyms=TAF60; OrderedLocusNames=YGL112C; ORFNames=G2985;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 72-92;
99-132 AND 222-229.
STRAIN=ATCC 76621 / YPH252;
PubMed=7667272; DOI=10.1073/pnas.92.18.8224;
Poon D., Bai Y., Campbell A.M., Bjorklund S., Kim Y.-J., Zhou S.,
Kornberg R.D., Weil P.A.;
"Identification and characterization of a TFIID-like multiprotein
complex from Saccharomyces cerevisiae.";
Proc. Natl. Acad. Sci. U.S.A. 92:8224-8228(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9046090;
DOI=10.1002/(SICI)1097-0061(199701)13:1<85::AID-YEA53>3.0.CO;2-E;
Paoluzi S., Minenkova O., Castagnoli L.;
"The genes encoding the transcription factor yTAFII60, the G4p1
protein and a putative glucose transporter are contained in a 12.3 kb
DNA fragment on the left arm of Saccharomyces cerevisiae chromosome
VII.";
Yeast 13:85-91(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169869;
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M.,
Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J.,
Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E.,
Clemente M.L., Coblenz A., Coglievina M., Coissac E., Defoor E.,
Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B.,
Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L.,
Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M.,
Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M.,
Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B.,
Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W.,
Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A.,
Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S.,
Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L.,
Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S.,
Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J.,
Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M.,
Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B.,
Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J.,
Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M.,
van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M.,
Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H.,
Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M.,
Zollner A., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
Nature 387:81-84(1997).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[6]
FUNCTION, AND TAF-TAF INTERACTION THROUGH HISTONE-FOLD DOMAIN.
PubMed=9695952; DOI=10.1016/S0092-8674(00)81423-3;
Birck C., Poch O., Romier C., Ruff M., Mengus G., Lavigne A.C.,
Davidson I., Moras D.;
"Human TAF(II)28 and TAF(II)18 interact through a histone fold encoded
by atypical evolutionary conserved motifs also found in the SPT3
family.";
Cell 94:239-249(1998).
[7]
FUNCTION, IDENTIFICATION IN THE SAGA COMPLEX, AND IDENTIFICATION BY
MASS SPECTROMETRY.
PubMed=9674426; DOI=10.1016/S0092-8674(00)81220-9;
Grant P.A., Schieltz D., Pray-Grant M.G., Steger D.J., Reese J.C.,
Yates J.R. III, Workman J.L.;
"A subset of TAF(II)s are integral components of the SAGA complex
required for nucleosome acetylation and transcriptional stimulation.";
Cell 94:45-53(1998).
[8]
FUNCTION IN HISTONE ACETYLATION AT THE SAGA COMPLEX.
PubMed=10026213; DOI=10.1074/jbc.274.9.5895;
Grant P.A., Eberharter A., John S., Cook R.G., Turner B.M.,
Workman J.L.;
"Expanded lysine acetylation specificity of Gcn5 in native
complexes.";
J. Biol. Chem. 274:5895-5900(1999).
[9]
FUNCTION, AND IDENTIFICATION IN THE TFIID COMPLEX.
PubMed=10788514; DOI=10.1074/jbc.275.18.13895;
Sanders S.L., Weil P.A.;
"Identification of two novel TAF subunits of the yeast Saccharomyces
cerevisiae TFIID complex.";
J. Biol. Chem. 275:13895-13900(2000).
[10]
FUNCTION, AND INTERACTION IN TFIID AND SAGA.
PubMed=11238921; DOI=10.1128/MCB.21.5.1841-1853.2001;
Gangloff Y.G., Sanders S.L., Romier C., Kirschner D.B., Weil P.A.,
Tora L., Davidson I.;
"Histone folds mediate selective heterodimerization of yeast TAF(II)25
with TFIID components yTAF(II)47 and yTAF(II)65 and with SAGA
component ySPT7.";
Mol. Cell. Biol. 21:1841-1853(2001).
[11]
FUNCTION, AND HISTONE-FOLD DOMAIN CHARACTERIZATION.
PubMed=11295558; DOI=10.1016/S0968-0004(00)01741-2;
Gangloff Y.G., Romier C., Thuault S., Werten S., Davidson I.;
"The histone fold is a key structural motif of transcription factor
TFIID.";
Trends Biochem. Sci. 26:250-257(2001).
[12]
FUNCTION, AND TAF OCTAMER FORMATION.
PubMed=11473260; DOI=10.1038/90408;
Selleck W., Howley R., Fang Q., Podolny V., Fried M.G., Buratowski S.,
Tan S.;
"A histone fold TAF octamer within the yeast TFIID transcriptional
coactivator.";
Nat. Struct. Biol. 8:695-700(2001).
[13]
FUNCTION, AND IDENTIFICATION IN THE SAGA COMPLEX.
PubMed=12052880; DOI=10.1128/MCB.22.13.4723-4738.2002;
Sanders S.L., Jennings J., Canutescu A., Link A.J., Weil P.A.;
"Proteomics of the eukaryotic transcription machinery: identification
of proteins associated with components of yeast TFIID by
multidimensional mass spectrometry.";
Mol. Cell. Biol. 22:4723-4738(2002).
[14]
IDENTIFICATION IN THE SALSA COMPLEX.
PubMed=12186975; DOI=10.1073/pnas.182021199;
Sterner D.E., Belotserkovskaya R., Berger S.L.;
"SALSA, a variant of yeast SAGA, contains truncated Spt7, which
correlates with activated transcription.";
Proc. Natl. Acad. Sci. U.S.A. 99:11622-11627(2002).
[15]
FUNCTION, AND TFIID STOICHIOMETRY.
PubMed=12138208; DOI=10.1128/MCB.22.16.6000-6013.2002;
Sanders S.L., Garbett K.A., Weil P.A.;
"Molecular characterization of Saccharomyces cerevisiae TFIID.";
Mol. Cell. Biol. 22:6000-6013(2002).
[16]
IDENTIFICATION IN THE SLIK COMPLEX.
PubMed=12446794; DOI=10.1128/MCB.22.24.8774-8786.2002;
Pray-Grant M.G., Schieltz D., McMahon S.J., Wood J.M., Kennedy E.L.,
Cook R.G., Workman J.L., Yates J.R. III, Grant P.A.;
"The novel SLIK histone acetyltransferase complex functions in the
yeast retrograde response pathway.";
Mol. Cell. Biol. 22:8774-8786(2002).
[17]
FUNCTION.
PubMed=12516863; DOI=10.1023/A:1021258713850;
Martinez E.;
"Multi-protein complexes in eukaryotic gene transcription.";
Plant Mol. Biol. 50:925-947(2002).
[18]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[19]
IDENTIFICATION IN THE SLIK COMPLEX.
PubMed=15647753; DOI=10.1038/nature03242;
Pray-Grant M.G., Daniel J.A., Schieltz D., Yates J.R. III, Grant P.A.;
"Chd1 chromodomain links histone H3 methylation with SAGA- and SLIK-
dependent acetylation.";
Nature 433:434-438(2005).
[20]
3D-STRUCTURE, AND ELECTRON MICROSCOPY OF TFIID.
PubMed=12093743; DOI=10.1093/emboj/cdf342;
Leurent C., Sanders S.L., Ruhlmann C., Mallouh V., Weil P.A.,
Kirschner D.B., Tora L., Schultz P.;
"Mapping histone fold TAFs within yeast TFIID.";
EMBO J. 21:3424-3433(2002).
[21]
3D-STRUCTURE MODELING OF THE SAGA COMPLEX.
PubMed=15260971; DOI=10.1016/j.molcel.2004.06.005;
Wu P.Y., Ruhlmann C., Winston F., Schultz P.;
"Molecular architecture of the S. cerevisiae SAGA complex.";
Mol. Cell 15:199-208(2004).
-!- FUNCTION: Functions as a component of the DNA-binding general
transcription factor complex TFIID and the regulatory
transcription regulatory histone acetylation (HAT) complexes SAGA,
SALSA and SLIK. Binding of TFIID to a promoter (with or without
TATA element) is the initial step in preinitiation complex (PIC)
formation. TFIID plays a key role in the regulation of gene
expression by RNA polymerase II through different activities such
as transcription activator interaction, core promoter recognition
and selectivity, TFIIA and TFIIB interaction, chromatin
modification (histone acetylation by TAF1), facilitation of DNA
opening and initiation of transcription. SAGA is involved in RNA
polymerase II-dependent transcriptional regulation of
approximately 10% of yeast genes. At the promoters, SAGA is
required for recruitment of the basal transcription machinery. It
influences RNA polymerase II transcriptional activity through
different activities such as TBP interaction (SPT3, SPT8 and
SPT20) and promoter selectivity, interaction with transcription
activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification
through histone acetylation (GCN5) and deubiquitination (UBP8).
SAGA acetylates nucleosomal histone H3 to some extent (to form
H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via
upstream activating sequences (UASs). SALSA, an altered form of
SAGA, may be involved in positive transcriptional regulation. SLIK
is proposed to have partly overlapping functions with SAGA. It
preferentially acetylates methylated histone H3, at least after
activation at the GAL1-10 locus. {ECO:0000269|PubMed:10026213,
ECO:0000269|PubMed:10788514, ECO:0000269|PubMed:11238921,
ECO:0000269|PubMed:11295558, ECO:0000269|PubMed:11473260,
ECO:0000269|PubMed:12052880, ECO:0000269|PubMed:12138208,
ECO:0000269|PubMed:12516863, ECO:0000269|PubMed:9674426,
ECO:0000269|PubMed:9695952}.
-!- SUBUNIT: In TFIID, TAF6 heterodimerizes with TAF9, forming
ultimately an octamer consisting of a TAF6/TAF9 heterotetramer
core flanked by TAF4/TAF12 dimers on either side, similar to the
histone H2A/H2B/H3/H4 octamer. The 1.2 MDa TFIID complex is
composed of TATA binding protein (TBP) and the 14 TBP-associated
factors. One copy of each TAF1, TAF2, TAF3, TAF7, TAF8, TAF11,
TAF13, two copies of each TAF4, TAF5, TAF6, TAF9, TAF10, TAF12,
and three copies of TAF14. Component of the 1.8 MDa SAGA complex,
which consists of at least TRA1, CHD1, SPT7, TAF5, ADA3, SGF73,
SPT20/ADA5, SPT8, TAF12, TAF6, HFI1/ADA1, UBP8, GCN5, ADA2, SPT3,
SGF29, TAF10, TAF9, SGF11 and SUS1. TAF5, TAF6, TAF9, TAF19, TAF12
and ADA1 seem to be present in 2 copies. SAGA is built of 5
distinct domains with specialized functions. Domain I (containing
TRA1) probably represents the activator interaction surface.
Domain II (containing TAF5 and TAF6, and probably TAF9 and TAF10),
domain III (containing GCN5, TAF10, SPT7, TAF5 and ADA1, and
probably ADA2, ADA3 and TAF12), and domain IV (containing
HFI1/ADA1 and TAF6, and probably TAF9) are believed to play
primarily an architectural role. Domain III also harbors the HAT
activity. Domain V (containing SPT3 and SPT20, and probably SPT8)
represents the TBP-interacting module, which may be associated
transiently with SAGA. Component of the SALSA complex, which
consists of at least TRA1, SPT7 (C-terminal truncated form), TAF5,
ADA3, SPT20, TAF12, TAF6, HFI1, GCN5, ADA2 and SPT3. Component of
the SLIK complex, which consists of at least TRA1, CHD1, SPT7,
TAF5, ADA3, SPT20, RTG2, TAF12, TAF6, HFI1, UBP8, GCN5, ADA2,
SPT3, SGF29, TAF10 and TAF9. {ECO:0000269|PubMed:10788514,
ECO:0000269|PubMed:12052880, ECO:0000269|PubMed:12186975,
ECO:0000269|PubMed:12446794, ECO:0000269|PubMed:15647753,
ECO:0000269|PubMed:9674426}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-18876, EBI-18876;
P35817:BDF1; NbExp=2; IntAct=EBI-18876, EBI-3493;
Q12060:HFI1; NbExp=9; IntAct=EBI-18876, EBI-8287;
P46677:TAF1; NbExp=6; IntAct=EBI-18876, EBI-18855;
Q12030:TAF10; NbExp=8; IntAct=EBI-18876, EBI-18889;
P38129:TAF5; NbExp=12; IntAct=EBI-18876, EBI-18868;
Q05027:TAF9; NbExp=11; IntAct=EBI-18876, EBI-27500;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- MISCELLANEOUS: Present with 6506 (+/-1290) molecules/cell in log
phase SD medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the TAF6 family. {ECO:0000305}.
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EMBL; X97644; CAA66240.1; -; Genomic_DNA.
EMBL; L40145; AAA83389.1; -; Genomic_DNA.
EMBL; Z72634; CAA96819.1; -; Genomic_DNA.
EMBL; AY723809; AAU09726.1; -; Genomic_DNA.
EMBL; BK006941; DAA07996.1; -; Genomic_DNA.
PIR; S64120; S64120.
RefSeq; NP_011403.1; NM_001180977.1.
ProteinModelPortal; P53040; -.
BioGrid; 33139; 407.
DIP; DIP-981N; -.
IntAct; P53040; 122.
MINT; MINT-405577; -.
STRING; 4932.YGL112C; -.
MaxQB; P53040; -.
PRIDE; P53040; -.
EnsemblFungi; YGL112C; YGL112C; YGL112C.
GeneID; 852766; -.
KEGG; sce:YGL112C; -.
EuPathDB; FungiDB:YGL112C; -.
SGD; S000003080; TAF6.
GeneTree; ENSGT00640000091486; -.
HOGENOM; HOG000159894; -.
InParanoid; P53040; -.
KO; K03131; -.
OMA; DVEYRIH; -.
OrthoDB; EOG092C0TYK; -.
BioCyc; YEAST:G3O-30610-MONOMER; -.
Reactome; R-SCE-674695; RNA Polymerase II Pre-transcription Events.
Reactome; R-SCE-73776; RNA Polymerase II Promoter Escape.
Reactome; R-SCE-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
Reactome; R-SCE-75953; RNA Polymerase II Transcription Initiation.
Reactome; R-SCE-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
PRO; PR:P53040; -.
Proteomes; UP000002311; Chromosome VII.
GO; GO:0005829; C:cytosol; IDA:SGD.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0000124; C:SAGA complex; IDA:SGD.
GO; GO:0046695; C:SLIK (SAGA-like) complex; IDA:SGD.
GO; GO:0005669; C:transcription factor TFIID complex; IDA:SGD.
GO; GO:0003682; F:chromatin binding; IDA:SGD.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0032947; F:protein complex scaffold activity; IMP:SGD.
GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
GO; GO:0001102; F:RNA polymerase II activating transcription factor binding; IDA:SGD.
GO; GO:0006325; P:chromatin organization; IDA:SGD.
GO; GO:0016573; P:histone acetylation; IDA:SGD.
GO; GO:0051090; P:regulation of sequence-specific DNA binding transcription factor activity; IEA:InterPro.
GO; GO:0051123; P:RNA polymerase II transcriptional preinitiation complex assembly; IMP:SGD.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; IDA:SGD.
Gene3D; 1.25.10.10; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR009072; Histone-fold.
InterPro; IPR011442; TAF6_C.
InterPro; IPR004823; TAF_TATA-bd.
Pfam; PF02969; TAF; 1.
Pfam; PF07571; TAF6_C; 1.
SMART; SM00803; TAF; 1.
SUPFAM; SSF47113; SSF47113; 1.
SUPFAM; SSF48371; SSF48371; 1.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Nucleus;
Reference proteome; Transcription; Transcription regulation.
CHAIN 1 516 Transcription initiation factor TFIID
subunit 6.
/FTId=PRO_0000118878.
DOMAIN 6 75 Histone-fold.
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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18-003-43231 Transcription initiation factor TFIID subunit 6 - Transcription initiation factor TFIID 70 kDa subunit; TAF(II)70; TAFII-70; TAFII-80; TAFII80 Polyclonal 0.1 mg Protein A
EIAAB41276 Mouse,Mus musculus,Taf12,TAFII20,TAFII-20,Transcription initiation factor TFIID 20 kDa subunits,Transcription initiation factor TFIID subunit 12
EIAAB41277 Mouse,Mus musculus,TAF(II)18,Taf13,Taf2k,TAFII18,TAFII-18,Transcription initiation factor TFIID 18 kDa subunit,Transcription initiation factor TFIID subunit 13
18-003-43310 Transcription initiation factor TFIID subunit 11 - Transcription initiation factor TFIID 28 kDa subunit; TAF(II)28; TAFII-28; TAFII28; TFIID subunit p30-beta Polyclonal 0.05 mg Aff Pur
EIAAB41301 Mouse,Mus musculus,TAF(II)100,Taf5,TAFII100,TAFII-100,Transcription initiation factor TFIID 100 kDa subunit,Transcription initiation factor TFIID subunit 5
EIAAB41279 Bos taurus,Bovine,TAF(II)18,TAF13,TAFII18,TAFII-18,Transcription initiation factor TFIID 18 kDa subunit,Transcription initiation factor TFIID subunit 13
EIAAB41294 Chicken,Gallus gallus,RCJMB04_23j21,TAF(II)150,TAF2,TAFII150,TAFII-150,TBP-associated factor 150 kDa,Transcription initiation factor TFIID 150 kDa subunit,Transcription initiation factor TFIID subunit
EIAAB41270 Homo sapiens,Human,STAF28,TAF(II)30,TAF10,TAF2A,TAF2H,TAFII30,TAFII30,TAFII-30,Transcription initiation factor TFIID 30 kDa subunit,Transcription initiation factor TFIID subunit 10
18-003-43065 Transcription initiation factor TFIID subunit 10 - Transcription initiation factor TFIID 30 kDa subunit; TAF(II)30; TAFII-30; TAFII30; STAF28 Polyclonal 0.05 mg Aff Pur
EIAAB41321 Homo sapiens,Human,RNA polymerase II TBP-associated factor subunit G,STAF31_32,TAF2G,TAF9,TAFII31,TAFII31,TAFII-31,TAFII32,TAFII-32,Transcription initiation factor TFIID 31 kDa subunit,Transcription i


 

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