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Transcription initiation factor TFIID subunit 14 (Actin non-complementing mutant 1) (Chromosome stability protein 10) (SWI/SNF chromatin-remodeling complex subunit TAF14) (SWI/SNF complex 29 kDa subunit) (SWI/SNF complex subunit TAF14) (TBP-associated factor 14) (TBP-associated factor 30 kDa) (Transcription factor G 30 kDa subunit) (Transcription initiation factor TFIIF 30 kDa subunit)

 TAF14_YEAST             Reviewed;         244 AA.
P35189; D6W3N8; Q02460;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 1.
25-OCT-2017, entry version 156.
RecName: Full=Transcription initiation factor TFIID subunit 14;
AltName: Full=Actin non-complementing mutant 1;
AltName: Full=Chromosome stability protein 10;
AltName: Full=SWI/SNF chromatin-remodeling complex subunit TAF14;
AltName: Full=SWI/SNF complex 29 kDa subunit;
AltName: Full=SWI/SNF complex subunit TAF14;
AltName: Full=TBP-associated factor 14;
AltName: Full=TBP-associated factor 30 kDa;
AltName: Full=Transcription factor G 30 kDa subunit;
AltName: Full=Transcription initiation factor TFIIF 30 kDa subunit;
Name=TAF14; Synonyms=ANC1, CST10, SWP29, TAF30, TFG3;
OrderedLocusNames=YPL129W;
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 189-222.
STRAIN=ATCC 208279 / BJ926;
PubMed=7995524; DOI=10.1101/gad.8.23.2868;
Henry N.L., Campbell A.M., Feaver W.J., Poon D., Weil P.A.,
Kornberg R.D.;
"TFIIF-TAF-RNA polymerase II connection.";
Genes Dev. 8:2868-2878(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7949419; DOI=10.1091/mbc.5.6.617;
Welch M.D., Drubin D.G.;
"A nuclear protein with sequence similarity to proteins implicated in
human acute leukemias is important for cellular morphogenesis and
actin cytoskeletal function in Saccharomyces cerevisiae.";
Mol. Biol. Cell 5:617-632(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169875;
Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V.,
Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M.,
Chung E., Churcher C.M., Coster F., Davis K., Davis R.W.,
Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A.,
Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A.,
Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W.,
Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K.,
Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J.,
Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D.,
Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V.,
Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W.,
Zollner A., Vo D.H., Hani J.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
Nature 387:103-105(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] OF 10-244.
STRAIN=LN224;
PubMed=8423796; DOI=10.1128/MCB.13.2.1306;
Brigati C., Kurtz S., Balderes D., Vidali G., Shore D.M.;
"An essential yeast gene encoding a TTAGGG repeat-binding protein.";
Mol. Cell. Biol. 13:1306-1314(1993).
[6]
PROTEIN SEQUENCE OF 189-203, AND INTERACTION WITH SAS3.
PubMed=10817755;
John S., Howe L., Tafrov S.T., Grant P.A., Sternglanz R.,
Workman J.L.;
"The something about silencing protein, Sas3, is the catalytic subunit
of NuA3, a yTAF(II)30-containing HAT complex that interacts with the
Spt16 subunit of the yeast CP (Cdc68/Pob3)-FACT complex.";
Genes Dev. 14:1196-1208(2000).
[7]
CHARACTERIZATION.
PubMed=1331085;
Henry N.L., Sayre M.H., Kornberg R.D.;
"Purification and characterization of yeast RNA polymerase II general
initiation factor g.";
J. Biol. Chem. 267:23388-23392(1992).
[8]
FUNCTION, AND TAF14 IN TFIIF.
PubMed=9618449;
Hampsey M.;
"Molecular genetics of the RNA polymerase II general transcriptional
machinery.";
Microbiol. Mol. Biol. Rev. 62:465-503(1998).
[9]
FUNCTION, AND SUBUNIT.
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]
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).
[11]
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).
[12]
FUNCTION.
PubMed=12516863; DOI=10.1023/A:1021258713850;
Martinez E.;
"Multi-protein complexes in eukaryotic gene transcription.";
Plant Mol. Biol. 50:925-947(2002).
[13]
IDENTIFICATION IN THE INO80 COMPLEX.
PubMed=12887900; DOI=10.1016/S1097-2765(03)00264-8;
Shen X., Ranallo R., Choi E., Wu C.;
"Involvement of actin-related proteins in ATP-dependent chromatin
remodeling.";
Mol. Cell 12:147-155(2003).
[14]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-181, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22106047; DOI=10.1002/pmic.201100166;
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
"Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
Proteomics 12:236-240(2012).
[15]
3D-STRUCTURE MODELING OF THE SWI/SNF COMPLEX, AND ELECTRON MICROSCOPY
OF THE SWI/SNF COMPLEX.
PubMed=12524530; DOI=10.1038/nsb888;
Smith C.L., Horowitz-Scherer R., Flanagan J.F., Woodcock C.L.,
Peterson C.L.;
"Structural analysis of the yeast SWI/SNF chromatin remodeling
complex.";
Nat. Struct. Biol. 10:141-145(2003).
[16]
FUNCTION, AND SWI/SNF STOICHIOMETRY.
PubMed=12672490; DOI=10.1016/S0959-437X(03)00022-4;
Martens J.A., Winston F.;
"Recent advances in understanding chromatin remodeling by SWI/SNF
complexes.";
Curr. Opin. Genet. Dev. 13:136-142(2003).
[17]
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).
[18]
FUNCTION OF THE NUA3 COMPLEX, IDENTIFICATION IN THE NUA3 COMPLEX, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17157260; DOI=10.1016/j.molcel.2006.10.026;
Taverna S.D., Ilin S., Rogers R.S., Tanny J.C., Lavender H., Li H.,
Baker L., Boyle J., Blair L.P., Chait B.T., Patel D.J.,
Aitchison J.D., Tackett A.J., Allis C.D.;
"Yng1 PHD finger binding to H3 trimethylated at K4 promotes NuA3 HAT
activity at K14 of H3 and transcription at a subset of targeted
ORFs.";
Mol. Cell 24:785-796(2006).
[19]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-137.
PubMed=26341557; DOI=10.1101/gad.269977.115;
Shanle E.K., Andrews F.H., Meriesh H., McDaniel S.L., Dronamraju R.,
DiFiore J.V., Jha D., Wozniak G.G., Bridgers J.B., Kerschner J.L.,
Krajewski K., Martin G.M., Morrison A.J., Kutateladze T.G.,
Strahl B.D.;
"Association of Taf14 with acetylated histone H3 directs gene
transcription and the DNA damage response.";
Genes Dev. 29:1795-1800(2015).
[20]
X-RAY CRYSTALLOGRAPHY (2.22 ANGSTROMS) OF 1-137, FUNCTION, DOMAIN, AND
MUTAGENESIS OF VAL-24 AND GLY-80.
PubMed=27089029; DOI=10.1038/nchembio.2065;
Andrews F.H., Shinsky S.A., Shanle E.K., Bridgers J.B., Gest A.,
Tsun I.K., Krajewski K., Shi X., Strahl B.D., Kutateladze T.G.;
"The Taf14 YEATS domain is a reader of histone crotonylation.";
Nat. Chem. Biol. 12:396-398(2016).
-!- FUNCTION: Functions as a component of the DNA-binding general
transcription factor complex TFIID, the RNA polymerase II
associated general transcription factor complex TFIIF, and the
chromatin-remodeling complex SWI/SNF (PubMed:10788514,
PubMed:12138208, PubMed:12516863, PubMed:9618449). Binding of
TFIID to a promoter (with or without TATA element) is the initial
step in preinitiation complex (PIC) formation (PubMed:10788514,
PubMed:12138208, PubMed:12516863, PubMed:9618449). 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
(PubMed:10788514, PubMed:12138208, PubMed:12516863,
PubMed:9618449). TFIIF is essential for the initiation of
transcription by RNA polymerase II (PubMed:10788514,
PubMed:12138208, PubMed:12516863, PubMed:9618449). TFIIF functions
include the recruitment of RNA polymerase II to the promoter bound
DNA-TBP-TFIIB complex, decreasing the affinity of RNA polymerase
II for non-specific DNA, allowing for the subsequent recruitment
of TFIIE and TFIIH, and facilitating RNA polymerase II elongation
(PubMed:10788514, PubMed:12138208, PubMed:12516863,
PubMed:9618449). TAF14 acts as a chromatin reader that
specifically recognizes and binds histones that are acylated
(PubMed:26341557, PubMed:27089029). Recognizes and binds histone
H3 acetylated or crotonylated at 'Lys-9' (H3K9ac and H3K9cr,
respectively) (PubMed:26341557, PubMed:27089029). Component of the
SWI/SNF complex, an ATP-dependent chromatin-remodeling complex, is
required for the positive and negative regulation of gene
expression of a large number of genes (PubMed:12672490). It
changes chromatin structure by altering DNA-histone contacts
within a nucleosome, leading eventually to a change in nucleosome
position, thus facilitating or repressing binding of gene-specific
transcription factors (PubMed:12672490). Component of the histone
acetyltransferase NuA3 complex, that acetylates Lys-14 of histone
H3. Recruitment of NuA3 to nucleosomes requires methylated histone
H3 (PubMed:17157260). In conjunction with the FACT complex, NuA3
may be involved in transcriptional regulation (PubMed:17157260).
{ECO:0000269|PubMed:10788514, ECO:0000269|PubMed:12138208,
ECO:0000269|PubMed:12516863, ECO:0000269|PubMed:12672490,
ECO:0000269|PubMed:17157260, ECO:0000269|PubMed:26341557,
ECO:0000269|PubMed:27089029, ECO:0000269|PubMed:9618449}.
-!- SUBUNIT: 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.
TFIIF is composed of three different subunits: TFG1/RAP74,
TFG2/RAP30 and TAF14. Component of the SWI/SNF global
transcription activator complex. The 1.14 MDa SWI/SNF complex is
composed of 11 different subunits: one copy each of SWI1,
SNF2/SWI2, SNF5, SNF12/SWP73, ARP7/SWP61, ARP9/SWP59; two copies
each of SWI3, SNF6, SNF11, SWP82; and three copies of TAF14/SWP29.
Component of the chromatin-remodeling INO80 complex, at least
composed of ARP4, ARP5, ARP8, RVB1, RVB2, TAF14, NHP10, IES1,
IES3, IES4, IES6, ACT1, IES2, IES5 and INO80. Component of the
NuA3 complex, composed of at least NTO1, SAS3, TAF14, YNG1 and
EAF6. {ECO:0000269|PubMed:10788514, ECO:0000269|PubMed:12887900,
ECO:0000269|PubMed:17157260}.
-!- INTERACTION:
P34218:SAS3; NbExp=3; IntAct=EBI-18920, EBI-16484;
P18480:SNF5; NbExp=2; IntAct=EBI-18920, EBI-17546;
P18888:SNF6; NbExp=4; IntAct=EBI-18920, EBI-17550;
Q08465:YNG1; NbExp=3; IntAct=EBI-18920, EBI-31890;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- DOMAIN: The YEATS domain specifically recognizes and binds
acylated histones (acetylated and crotonylated).
{ECO:0000269|PubMed:26341557, ECO:0000269|PubMed:27089029}.
-!- MISCELLANEOUS: TAF14 is the only non-essential TAF.
-!- MISCELLANEOUS: Present with 3100 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- MISCELLANEOUS: There is no homolog of TAF14 present in the TFIIF
complexes of higher eukaryotes.
-!- SIMILARITY: Belongs to the TAF14 family. {ECO:0000305}.
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EMBL; U13017; AAA61644.1; -; Genomic_DNA.
EMBL; Z26040; CAA81125.1; -; Genomic_DNA.
EMBL; U43703; AAB68235.1; -; Genomic_DNA.
EMBL; X69394; CAA49192.1; -; Genomic_DNA.
EMBL; BK006949; DAA11304.1; -; Genomic_DNA.
PIR; S38568; S38568.
RefSeq; NP_015196.1; NM_001183943.1.
PDB; 2L7E; NMR; -; A=1-123.
PDB; 3QRL; X-ray; 1.70 A; A=1-137.
PDB; 5D7E; X-ray; 1.90 A; A=1-137.
PDB; 5IOK; X-ray; 2.22 A; A=1-137.
PDB; 5SVA; EM; 15.30 A; n=1-244.
PDBsum; 2L7E; -.
PDBsum; 3QRL; -.
PDBsum; 5D7E; -.
PDBsum; 5IOK; -.
PDBsum; 5SVA; -.
ProteinModelPortal; P35189; -.
SMR; P35189; -.
BioGrid; 36052; 285.
DIP; DIP-1147N; -.
IntAct; P35189; 53.
MINT; MINT-646854; -.
STRING; 4932.YPL129W; -.
iPTMnet; P35189; -.
MaxQB; P35189; -.
PRIDE; P35189; -.
EnsemblFungi; YPL129W; YPL129W; YPL129W.
GeneID; 855974; -.
KEGG; sce:YPL129W; -.
EuPathDB; FungiDB:YPL129W; -.
SGD; S000006050; TAF14.
GeneTree; ENSGT00530000068270; -.
HOGENOM; HOG000176324; -.
InParanoid; P35189; -.
KO; K03140; -.
OMA; SIDLYTM; -.
OrthoDB; EOG092C5Z86; -.
BioCyc; YEAST:G3O-34028-MONOMER; -.
EvolutionaryTrace; P35189; -.
PRO; PR:P35189; -.
Proteomes; UP000002311; Chromosome XVI.
GO; GO:0031011; C:Ino80 complex; IDA:SGD.
GO; GO:0016592; C:mediator complex; IPI:SGD.
GO; GO:0033100; C:NuA3 histone acetyltransferase complex; IDA:SGD.
GO; GO:1990467; C:NuA3a histone acetyltransferase complex; IDA:SGD.
GO; GO:1990468; C:NuA3b histone acetyltransferase complex; IDA:SGD.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0016514; C:SWI/SNF complex; IDA:SGD.
GO; GO:0005669; C:transcription factor TFIID complex; IDA:SGD.
GO; GO:0005674; C:transcription factor TFIIF complex; IDA:SGD.
GO; GO:0000991; F:transcription factor activity, core RNA polymerase II binding; IDA:SGD.
GO; GO:0006338; P:chromatin remodeling; IC:SGD.
GO; GO:0016573; P:histone acetylation; IDA:SGD.
GO; GO:0042766; P:nucleosome mobilization; IDA:SGD.
GO; GO:0001111; P:promoter clearance from RNA polymerase II promoter; IC:SGD.
GO; GO:0051123; P:RNA polymerase II transcriptional preinitiation complex assembly; IC:SGD.
GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IC:SGD.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; IDA:SGD.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:SGD.
GO; GO:0001174; P:transcriptional start site selection at RNA polymerase II promoter; IC:SGD.
InterPro; IPR027353; NET_dom.
InterPro; IPR016665; Sas5/TAF14.
InterPro; IPR005033; YEATS.
PANTHER; PTHR23195; PTHR23195; 1.
PANTHER; PTHR23195:SF2; PTHR23195:SF2; 1.
Pfam; PF17035; BET; 1.
Pfam; PF03366; YEATS; 1.
PIRSF; PIRSF016551; SAS5/TFIID_14; 1.
PROSITE; PS51037; YEATS; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Isopeptide bond; Nucleus; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 244 Transcription initiation factor TFIID
subunit 14.
/FTId=PRO_0000211241.
DOMAIN 8 115 YEATS. {ECO:0000255|PROSITE-
ProRule:PRU00376}.
REGION 59 61 Acylated histone binding.
{ECO:0000244|PDB:5D7E,
ECO:0000269|PubMed:26341557}.
REGION 81 83 Acylated histone binding.
{ECO:0000244|PDB:5D7E,
ECO:0000269|PubMed:26341557}.
BINDING 104 104 Acylated histone. {ECO:0000244|PDB:5D7E,
ECO:0000269|PubMed:26341557}.
CROSSLNK 181 181 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
MUTAGEN 24 24 V->A: Does not affect binding to acylated
histone H3.
{ECO:0000269|PubMed:27089029}.
MUTAGEN 80 80 G->A: Abolished binding to acylated
histone H3.
{ECO:0000269|PubMed:27089029}.
MUTAGEN 81 81 W->A: Abolished binding to acetylated
histone H3.
{ECO:0000269|PubMed:26341557}.
CONFLICT 116 116 H -> Q (in Ref. 5; CAA49192).
{ECO:0000305}.
STRAND 3 17 {ECO:0000244|PDB:3QRL}.
STRAND 30 39 {ECO:0000244|PDB:3QRL}.
STRAND 40 43 {ECO:0000244|PDB:2L7E}.
STRAND 45 47 {ECO:0000244|PDB:5D7E}.
STRAND 51 57 {ECO:0000244|PDB:3QRL}.
STRAND 62 64 {ECO:0000244|PDB:3QRL}.
STRAND 66 69 {ECO:0000244|PDB:3QRL}.
STRAND 76 82 {ECO:0000244|PDB:3QRL}.
STRAND 86 92 {ECO:0000244|PDB:3QRL}.
HELIX 93 95 {ECO:0000244|PDB:3QRL}.
STRAND 97 103 {ECO:0000244|PDB:3QRL}.
STRAND 107 122 {ECO:0000244|PDB:3QRL}.
HELIX 125 131 {ECO:0000244|PDB:3QRL}.
TURN 132 134 {ECO:0000244|PDB:3QRL}.
SEQUENCE 244 AA; 27440 MW; 60EA5EC2474B1B9C CRC64;
MVATVKRTIR IKTQQHILPE VPPVENFPVR QWSIEIVLLD DEGKEIPATI FDKVIYHLHP
TFANPNRTFT DPPFRIEEQG WGGFPLDISV FLLEKAGERK IPHDLNFLQE SYEVEHVIQI
PLNKPLLTEE LAKSGSTEET TANTGTIGKR RTTTNTTAEP KAKRAKTGSA STVKGSVDLE
KLAFGLTKLN EDDLVGVVQM VTDNKTPEMN VTNNVEEGEF IIDLYSLPEG LLKSLWDYVK
KNTE


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18-003-42223 Transcription initiation factor TFIID subunit 1 - EC 2.7.11.1; Transcription initiation factor TFIID 250 kDa subunit; TAF(II)250; TAFII-250; TAFII250; TBP-associated factor 250 kDa; p250; Cell cycle g 0.05 mg Aff Pur
EIAAB41293 Mouse,Mus musculus,TAF(II)150,Taf2,TAFII150,TAFII-150,TBP-associated factor 150 kDa,Transcription initiation factor TFIID 150 kDa subunit,Transcription initiation factor TFIID subunit 2
EIAAB41292 Homo sapiens,Human,TAF(II)210,TAF1L,TBP-associated factor 1-like,TBP-associated factor 210 kDa,Transcription initiation factor TFIID 210 kDa subunit,Transcription initiation factor TFIID subunit 1-lik
EIAAB41302 Homo sapiens,Human,TAF(II)100,TAF2D,TAF5,TAFII100,TAFII-100,Transcription initiation factor TFIID 100 kDa subunit,Transcription initiation factor TFIID subunit 5
EIAAB40078 Chromatin-specific transcription elongation factor 80 kDa subunit,Facilitates chromatin transcription complex 80 kDa subunit,Facilitates chromatin transcription complex subunit SSRP1,FACT 80 kDa subun
EIAAB42031 General transcription factor IIA subunit 1,GTF2A1,Homo sapiens,Human,TF2A1,TFIIA-42,TFIIAL,Transcription initiation factor IIA subunit 1,Transcription initiation factor TFIIA 42 kDa subunit
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
EIAAB41322 Mouse,Mus musculus,RNA polymerase II TBP-associated factor subunit G,Taf2g,Taf9,TAFII31,TAFII-31,TAFII32,TAFII-32,Transcription initiation factor TFIID 31 kDa subunit,Transcription initiation factor T
EIAAB41310 Homo sapiens,Human,RNA polymerase II TBP-associated factor subunit F,TAF(II)55,TAF2F,TAF7,TAFII55,TAFII55,TAFII-55,Transcription initiation factor TFIID 55 kDa subunit,Transcription initiation factor
EIAAB41103 ATP-dependent helicase GTF2F2,General transcription factor IIF subunit 2,Gtf2f2,Rap30,Rat,Rattus norvegicus,TFIIF-beta,Transcription initiation factor IIF subunit beta,Transcription initiation factor
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
18-003-43035 TFIIH basal transcription factor complex p44 subunit - Basic transcription factor 2 44 kDa subunit; BTF2-p44; General transcription factor IIH polypeptide 2 Polyclonal 0.1 mg Protein A


 

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