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Transcription initiation factor TFIID subunit 5 (Transcription initiation factor TFIID 100 kDa subunit) (TAF(II)100) (TAFII-100) (TAFII100)

 TAF5_HUMAN              Reviewed;         800 AA.
Q15542; A8K5B4; B2RMR0; B7ZKJ6; Q53EM4; Q5SYD5; Q86UZ7; Q9Y4K5;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
10-MAY-2005, sequence version 3.
05-DEC-2018, entry version 188.
RecName: Full=Transcription initiation factor TFIID subunit 5;
AltName: Full=Transcription initiation factor TFIID 100 kDa subunit;
Short=TAF(II)100;
Short=TAFII-100;
Short=TAFII100;
Name=TAF5; Synonyms=TAF2D;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), AND VARIANT ALA-130.
TISSUE=Cervix carcinoma;
PubMed=8758937;
Dubrovskaya V., Lavigne A.-C., Davidson I., Acker J., Staub A.,
Tora L.;
"Distinct domains of hTAFII100 are required for functional interaction
with transcription factor TFIIF beta (RAP30) and incorporation into
the TFIID complex.";
EMBO J. 15:3702-3712(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), PROTEIN SEQUENCE OF
109-117; 119-142; 151-174; 372-388; 611-621; 635-649 AND 737-742, AND
ALTERNATIVE SPLICING.
TISSUE=Cervix carcinoma;
PubMed=8942982; DOI=10.1073/pnas.93.24.13611;
Tanese N., Saluja D., Vassallo M.F., Chen J.-L., Admon A.;
"Molecular cloning and analysis of two subunits of the human TFIID
complex: hTAFII130 and hTAFII100.";
Proc. Natl. Acad. Sci. U.S.A. 93:13611-13616(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), AND VARIANT ALA-130.
TISSUE=Cervix carcinoma;
PubMed=9045704; DOI=10.1074/jbc.272.10.6714;
Tao Y., Guermah M., Martinez E., Oegelschlaeger T., Hasegawa S.,
Takada R., Yamamoto T., Horikoshi M., Roeder R.G.;
"Specific interactions and potential functions of human TAFII100.";
J. Biol. Chem. 272:6714-6721(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG), AND VARIANT
ALA-130.
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS LONG AND SHORT), AND
VARIANT ALA-130.
TISSUE=Prostate, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
INTERACTION WITH SV40 LARGE T ANTIGEN (MICROBIAL INFECTION).
PubMed=8647434; DOI=10.1101/gad.10.11.1369;
Damania B., Alwine J.C.;
"TAF-like function of SV40 large T antigen.";
Genes Dev. 10:1369-1381(1996).
[10]
IDENTIFICATION IN THE TFTC-HAT COMPLEX WITH TAF5L; TAF6L; TADA3L;
SUPT3H; TAF2; TAF4; TRRAP; GCN5L2 AND TAF10.
PubMed=10373431; DOI=10.1074/jbc.274.26.18285;
Brand M., Yamamoto K., Staub A., Tora L.;
"Identification of TATA-binding protein-free TAFII-containing complex
subunits suggests a role in nucleosome acetylation and signal
transduction.";
J. Biol. Chem. 274:18285-18289(1999).
[11]
IDENTIFICATION IN THE TFTC-HAT COMPLEX, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=12601814; DOI=10.1002/pmic.200390030;
Cavusoglu N., Brand M., Tora L., van Dorsselaer A.;
"Novel subunits of the TATA binding protein free TAFII-containing
transcription complex identified by matrix-assisted laser
desorption/ionization-time of flight mass spectrometry following one-
dimensional gel electrophoresis.";
Proteomics 3:217-223(2003).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[13]
X-RAY CRYSTALLOGRAPHY (2.17 ANGSTROMS) OF 188-343, AND SUBUNIT.
PubMed=17227857; DOI=10.1073/pnas.0610297104;
Bhattacharya S., Takada S., Jacobson R.H.;
"Structural analysis and dimerization potential of the human TAF5
subunit of TFIID.";
Proc. Natl. Acad. Sci. U.S.A. 104:1189-1194(2007).
-!- FUNCTION: TAFs are components of the transcription factor IID
(TFIID) complex, PCAF histone acetylase complex and TBP-free TAFII
complex (TFTC). TAFs components-TIIFD are essential for mediating
regulation of RNA polymerase transcription. TAF5/TAFII100
interacts strongly with the histone H4-related TAF6/TAFII80 and
the histone H3-related TAF9/TAFII31, as well as a stable complex
comprised of both TAF5/TAFII80 and TAF6/TAFII31. Apparently weaker
interactions of TAF5/TAFII100 with TBP, TAF1/TAFII250,
TAF11/TAFII28, and TAF12/TAFII20, but not TAF7/TAFII55, also have
been observed.
-!- SUBUNIT: Homodimer. TFIID and PCAF are composed of TATA binding
protein (TBP) and a number of TBP-associated factors (TAFs). TBP
is not part of TFTC. Component of the TFTC-HAT complex, at least
composed of TAF5L, TAF6L, TADA3L, SUPT3H/SPT3, TAF2/TAFII150,
TAF4/TAFII135, TAF5/TAFII100, GCN5L2/GCN5, TAF10 and TRRAP.
{ECO:0000269|PubMed:10373431, ECO:0000269|PubMed:12601814,
ECO:0000269|PubMed:17227857}.
-!- SUBUNIT: (Microbial infection) Interacts with SV40 Large T
antigen. {ECO:0000269|PubMed:8647434}.
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-1560145, EBI-1560145;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Long;
IsoId=Q15542-1; Sequence=Displayed;
Name=Short;
IsoId=Q15542-2; Sequence=VSP_006787;
-!- DOMAIN: Distinct domains of TAF5/TAFII100 are required for
functional interaction with transcription factor TFIIFB (RAP30)
and incorporation into the TFIID complex.
-!- SIMILARITY: Belongs to the WD repeat TAF5 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC50902.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAD97335.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; X95525; CAA64777.1; -; mRNA.
EMBL; U75309; AAC50902.1; ALT_INIT; mRNA.
EMBL; U80191; AAC51215.1; -; mRNA.
EMBL; AK223615; BAD97335.1; ALT_INIT; mRNA.
EMBL; AK291229; BAF83918.1; -; mRNA.
EMBL; AL591408; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471066; EAW49645.1; -; Genomic_DNA.
EMBL; CH471066; EAW49646.1; -; Genomic_DNA.
EMBL; BC052268; AAH52268.2; -; mRNA.
EMBL; BC136340; AAI36341.1; -; mRNA.
EMBL; BC136348; AAI36349.1; -; mRNA.
CCDS; CCDS7547.1; -. [Q15542-1]
RefSeq; NP_008882.2; NM_006951.4. [Q15542-1]
RefSeq; NP_620640.1; NM_139052.2. [Q15542-2]
UniGene; Hs.96103; -.
PDB; 2NXP; X-ray; 2.17 A; A/B/C/D/E/F/G/H=188-343.
PDBsum; 2NXP; -.
ProteinModelPortal; Q15542; -.
SMR; Q15542; -.
BioGrid; 112740; 45.
ComplexPortal; CPX-903; TFTC histone acetylation complex.
ComplexPortal; CPX-915; General transcription factor complex TFIID.
ComplexPortal; CPX-930; General transcription factor complex TFIID, TAF4B variant.
CORUM; Q15542; -.
DIP; DIP-28150N; -.
IntAct; Q15542; 23.
MINT; Q15542; -.
STRING; 9606.ENSP00000358854; -.
iPTMnet; Q15542; -.
PhosphoSitePlus; Q15542; -.
BioMuta; TAF5; -.
DMDM; 78103206; -.
EPD; Q15542; -.
MaxQB; Q15542; -.
PaxDb; Q15542; -.
PeptideAtlas; Q15542; -.
PRIDE; Q15542; -.
ProteomicsDB; 60623; -.
ProteomicsDB; 60624; -. [Q15542-2]
TopDownProteomics; Q15542-2; -. [Q15542-2]
Ensembl; ENST00000369839; ENSP00000358854; ENSG00000148835. [Q15542-1]
GeneID; 6877; -.
KEGG; hsa:6877; -.
UCSC; uc001kwv.5; human. [Q15542-1]
CTD; 6877; -.
EuPathDB; HostDB:ENSG00000148835.10; -.
GeneCards; TAF5; -.
HGNC; HGNC:11539; TAF5.
HPA; HPA006195; -.
HPA; HPA006474; -.
MIM; 601787; gene.
neXtProt; NX_Q15542; -.
OpenTargets; ENSG00000148835; -.
PharmGKB; PA36314; -.
eggNOG; KOG0263; Eukaryota.
eggNOG; ENOG410XPM5; LUCA.
GeneTree; ENSGT00940000153342; -.
HOVERGEN; HBG050226; -.
InParanoid; Q15542; -.
KO; K03130; -.
OMA; DCVQFHP; -.
OrthoDB; EOG091G03SP; -.
PhylomeDB; Q15542; -.
TreeFam; TF300669; -.
Reactome; R-HSA-167161; HIV Transcription Initiation.
Reactome; R-HSA-167162; RNA Polymerase II HIV Promoter Escape.
Reactome; R-HSA-167172; Transcription of the HIV genome.
Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
Reactome; R-HSA-73776; RNA Polymerase II Promoter Escape.
Reactome; R-HSA-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
Reactome; R-HSA-75953; RNA Polymerase II Transcription Initiation.
Reactome; R-HSA-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
SignaLink; Q15542; -.
ChiTaRS; TAF5; human.
EvolutionaryTrace; Q15542; -.
GeneWiki; TAF5; -.
GenomeRNAi; 6877; -.
PRO; PR:Q15542; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000148835; Expressed in 202 organ(s), highest expression level in female gonad.
CleanEx; HS_TAF5; -.
Genevisible; Q15542; HS.
GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
GO; GO:0000790; C:nuclear chromatin; IDA:ParkinsonsUK-UCL.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005669; C:transcription factor TFIID complex; IDA:UniProtKB.
GO; GO:0033276; C:transcription factor TFTC complex; IDA:UniProtKB.
GO; GO:0003700; F:DNA-binding transcription factor activity; IMP:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046983; F:protein dimerization activity; IDA:UniProtKB.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
GO; GO:0006325; P:chromatin organization; IC:UniProtKB.
GO; GO:0006352; P:DNA-templated transcription, initiation; IDA:UniProtKB.
GO; GO:0016573; P:histone acetylation; IEA:GOC.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
GO; GO:0042795; P:snRNA transcription by RNA polymerase II; TAS:Reactome.
GO; GO:0006366; P:transcription by RNA polymerase II; TAS:Reactome.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
CDD; cd08044; TAF5_NTD2; 1.
Gene3D; 1.25.40.500; -; 1.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR020472; G-protein_beta_WD-40_rep.
InterPro; IPR006594; LisH.
InterPro; IPR037783; Taf5.
InterPro; IPR007582; TFIID_NTD2.
InterPro; IPR037264; TFIID_NTD2_sf.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR019775; WD40_repeat_CS.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
PANTHER; PTHR19879:SF4; PTHR19879:SF4; 1.
Pfam; PF04494; TFIID_NTD2; 1.
Pfam; PF00400; WD40; 6.
PRINTS; PR00320; GPROTEINBRPT.
SMART; SM00320; WD40; 6.
SUPFAM; SSF160897; SSF160897; 1.
SUPFAM; SSF50978; SSF50978; 1.
PROSITE; PS50896; LISH; 1.
PROSITE; PS00678; WD_REPEATS_1; 3.
PROSITE; PS50082; WD_REPEATS_2; 6.
PROSITE; PS50294; WD_REPEATS_REGION; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Direct protein sequencing; Host-virus interaction; Nucleus;
Polymorphism; Reference proteome; Repeat; Transcription;
Transcription regulation; WD repeat.
CHAIN 1 800 Transcription initiation factor TFIID
subunit 5.
/FTId=PRO_0000051257.
DOMAIN 92 124 LisH. {ECO:0000255|PROSITE-
ProRule:PRU00126}.
REPEAT 468 507 WD 1.
REPEAT 541 580 WD 2.
REPEAT 583 624 WD 3.
REPEAT 625 666 WD 4.
REPEAT 667 706 WD 5.
REPEAT 709 748 WD 6.
COMPBIAS 46 49 Poly-Gly.
COMPBIAS 399 407 Poly-Lys.
VAR_SEQ 556 610 Missing (in isoform Short).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_006787.
VARIANT 130 130 S -> A (in dbSNP:rs10883859).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:8758937,
ECO:0000269|PubMed:9045704,
ECO:0000269|Ref.5}.
/FTId=VAR_018462.
CONFLICT 126 126 A -> T (in Ref. 1; CAA64777 and 5;
BAD97335). {ECO:0000305}.
CONFLICT 300 300 F -> L (in Ref. 1; CAA64777).
{ECO:0000305}.
CONFLICT 455 455 P -> S (in Ref. 1; CAA64777).
{ECO:0000305}.
CONFLICT 469 469 A -> V (in Ref. 1; CAA64777).
{ECO:0000305}.
CONFLICT 778 778 Missing (in Ref. 1; CAA64777).
{ECO:0000305}.
CONFLICT 787 787 R -> L (in Ref. 8; AAH52268).
{ECO:0000305}.
HELIX 198 202 {ECO:0000244|PDB:2NXP}.
HELIX 203 205 {ECO:0000244|PDB:2NXP}.
HELIX 214 226 {ECO:0000244|PDB:2NXP}.
HELIX 230 236 {ECO:0000244|PDB:2NXP}.
HELIX 237 239 {ECO:0000244|PDB:2NXP}.
HELIX 240 253 {ECO:0000244|PDB:2NXP}.
HELIX 257 267 {ECO:0000244|PDB:2NXP}.
HELIX 268 270 {ECO:0000244|PDB:2NXP}.
HELIX 273 275 {ECO:0000244|PDB:2NXP}.
HELIX 276 283 {ECO:0000244|PDB:2NXP}.
HELIX 288 291 {ECO:0000244|PDB:2NXP}.
HELIX 295 300 {ECO:0000244|PDB:2NXP}.
HELIX 302 304 {ECO:0000244|PDB:2NXP}.
STRAND 305 310 {ECO:0000244|PDB:2NXP}.
HELIX 311 321 {ECO:0000244|PDB:2NXP}.
HELIX 328 335 {ECO:0000244|PDB:2NXP}.
STRAND 338 342 {ECO:0000244|PDB:2NXP}.
SEQUENCE 800 AA; 86830 MW; 87A178BFB7071992 CRC64;
MAALAEEQTE VAVKLEPEGP PTLLPPQAGD GAGEGSGGTT NNGPNGGGGN VAASSSTGGD
GGTPKPTVAV SAAAPAGAAP VPAAAPDAGA PHDRQTLLAV LQFLRQSKLR EAEEALRREA
GLLEEAVAGS GAPGEVDSAG AEVTSALLSR VTASAPGPAA PDPPGTGASG ATVVSGSASG
PAAPGKVGSV AVEDQPDVSA VLSAYNQQGD PTMYEEYYSG LKHFIECSLD CHRAELSQLF
YPLFVHMYLE LVYNQHENEA KSFFEKFHGD QECYYQDDLR VLSSLTKKEH MKGNETMLDF
RTSKFVLRIS RDSYQLLKRH LQEKQNNQIW NIVQEHLYID IFDGMPRSKQ QIDAMVGSLA
GEAKREANKS KVFFGLLKEP EIEVPLDDED EEGENEEGKP KKKKPKKDSI GSKSKKQDPN
APPQNRIPLP ELKDSDKLDK IMNMKETTKR VRLGPDCLPS ICFYTFLNAY QGLTAVDVTD
DSSLIAGGFA DSTVRVWSVT PKKLRSVKQA SDLSLIDKES DDVLERIMDE KTASELKILY
GHSGPVYGAS FSPDRNYLLS SSEDGTVRLW SLQTFTCLVG YKGHNYPVWD TQFSPYGYYF
VSGGHDRVAR LWATDHYQPL RIFAGHLADV NCTRFHPNSN YVATGSADRT VRLWDVLNGN
CVRIFTGHKG PIHSLTFSPN GRFLATGATD GRVLLWDIGH GLMVGELKGH TDTVCSLRFS
RDGEILASGS MDNTVRLWDA IKAFEDLETD DFTTATGHIN LPENSQELLL GTYMTKSTPV
VHLHFTRRNL VLAAGAYSPQ


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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
EIAAB41301 Mouse,Mus musculus,TAF(II)100,Taf5,TAFII100,TAFII-100,Transcription initiation factor TFIID 100 kDa subunit,Transcription initiation factor TFIID subunit 5
EIAAB41272 Homo sapiens,Human,PRO2134,TAF(II)28,TAF11,TAF2I,TAFII28,TAFII-28,TFIID subunit p30-beta,Transcription initiation factor TFIID 28 kDa subunit,Transcription initiation factor TFIID subunit 11
EIAAB41273 Rat,Rattus norvegicus,TAF(II)28,Taf11,TAFII28,TAFII-28,TFIID subunit p30-beta,Transcription initiation factor TFIID 28 kDa subunit,Transcription initiation factor TFIID subunit 11
EIAAB41271 Mouse,Mus musculus,TAF(II)28,Taf11,TAFII28,TAFII-28,TFIID subunit p30-beta,Transcription initiation factor TFIID 28 kDa subunit,Transcription initiation factor TFIID subunit 11
EIAAB41305 Mouse,Mus musculus,p80,TAF(II)70,TAF(II)80,Taf2e,Taf6,TAFII70,TAFII-70,TAFII80,TAFII-80,Transcription initiation factor TFIID 70 kDa subunit,Transcription initiation factor TFIID 80 kDa subunit,Transc
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
EIAAB41306 p80,Rat,Rattus norvegicus,TAF(II)70,TAF(II)80,Taf2e,Taf6,TAFII70,TAFII80,TAFII-80,Transcription initiation factor TFIID 70 kDa subunit,Transcription initiation factor TFIID 80 kDa subunit,Transcriptio
EIAAB41312 Mouse,Mus musculus,RNA polymerase II TBP-associated factor subunit F,TAF(II)55,Taf2f,Taf7,TAFII55,TAFII-55,Transcription initiation factor TFIID 55 kDa subunit,Transcription initiation factor TFIID su
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
EIAAB41274 Bos taurus,Bovine,TAF12,TAFII20_TAFII15,TAFII-20_TAFII-15,Transcription initiation factor TFIID 20_15 kDa subunits,Transcription initiation factor TFIID subunit 12
15-288-21282 Transcription initiation factor TFIID subunit 9 - Transcription initiation factor TFIID 31 kDa subunit; TAFII-31; TAFII-32; TAFII32; STAF31_32 Polyclonal 0.1 mg
15-288-21282 Transcription initiation factor TFIID subunit 9 - Transcription initiation factor TFIID 31 kDa subunit; TAFII-31; TAFII-32; TAFII32; STAF31_32 Polyclonal 0.05 mg
18-003-42548 Transcription initiation factor TFIID subunit 9 - Transcription initiation factor TFIID 31 kDa subunit; TAFII-31; TAFII-32; TAFII32; STAF31_32 Polyclonal 0.05 mg Aff Pur
EIAAB41275 Homo sapiens,Human,TAF12,TAF15,TAF2J,TAFII20,TAFII20_TAFII15,TAFII-20_TAFII-15,Transcription initiation factor TFIID 20_15 kDa subunits,Transcription initiation factor TFIID subunit 12
EIAAB41279 Bos taurus,Bovine,TAF(II)18,TAF13,TAFII18,TAFII-18,Transcription initiation factor TFIID 18 kDa subunit,Transcription initiation factor TFIID subunit 13
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
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
EIAAB41276 Mouse,Mus musculus,Taf12,TAFII20,TAFII-20,Transcription initiation factor TFIID 20 kDa subunits,Transcription initiation factor TFIID subunit 12
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
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
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
EIAAB41300 Homo sapiens,Human,TAF(II)105,TAF2C2,TAF4B,TAFII105,TAFII105,TAFII-105,Transcription initiation factor TFIID 105 kDa subunit,Transcription initiation factor TFIID subunit 4B
EIAAB41278 Homo sapiens,Human,TAF(II)18,TAF13,TAF2K,TAFII18,TAFII18,TAFII-18,Transcription initiation factor TFIID 18 kDa subunit,Transcription initiation factor TFIID subunit 13


 

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