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Transcription initiation factor TFIID subunit 9 (RNA polymerase II TBP-associated factor subunit G) (STAF31/32) (Transcription initiation factor TFIID 31 kDa subunit) (TAFII-31) (TAFII31) (Transcription initiation factor TFIID 32 kDa subunit) (TAFII-32) (TAFII32)

 TAF9_HUMAN              Reviewed;         264 AA.
Q16594; D3DWA3; Q5U0D1; Q9BTS1;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 1.
25-OCT-2017, entry version 179.
RecName: Full=Transcription initiation factor TFIID subunit 9;
AltName: Full=RNA polymerase II TBP-associated factor subunit G;
AltName: Full=STAF31/32;
AltName: Full=Transcription initiation factor TFIID 31 kDa subunit;
Short=TAFII-31;
Short=TAFII31;
AltName: Full=Transcription initiation factor TFIID 32 kDa subunit;
Short=TAFII-32;
Short=TAFII32;
Name=TAF9; Synonyms=TAF2G, TAFII31;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH VP16 AND TFIIB.
PubMed=7761466; DOI=10.1073/pnas.92.11.5154;
Lu H., Levine A.J.;
"Human TAFII31 protein is a transcriptional coactivator of the p53
protein.";
Proc. Natl. Acad. Sci. U.S.A. 92:5154-5158(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH TAF6.
PubMed=7597030; DOI=10.1073/pnas.92.13.5788;
Klemm R.D., Goodrich J.A., Zhou S., Tjian R.;
"Molecular cloning and expression of the 32-kDa subunit of human TFIID
reveals interactions with VP16 and TFIIB that mediate transcriptional
activation.";
Proc. Natl. Acad. Sci. U.S.A. 92:5788-5792(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=7667268; DOI=10.1073/pnas.92.18.8195;
Hisatake K., Ohta T., Takada R., Guermah M., Horikoshi M.,
Nakatani Y., Roeder R.G.;
"Evolutionary conservation of human TATA-binding-polypeptide-
associated factors TAFII31 and TAFII80 and interactions of TAFII80
with other TAFs and with general transcription factors.";
Proc. Natl. Acad. Sci. U.S.A. 92:8195-8199(1995).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT MET-6.
NIEHS SNPs program;
Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
[6]
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.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta, 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).
[8]
PROTEIN SEQUENCE OF 25-55; 79-89; 176-200 AND 223-246, SUBUNIT,
SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=9674425; DOI=10.1016/S0092-8674(00)81219-2;
Ogryzko V.V., Kotani T., Zhang X., Schiltz R.L., Howard T.,
Yang X.-J., Howard B.H., Qin J., Nakatani Y.;
"Histone-like TAFs within the PCAF histone acetylase complex.";
Cell 94:35-44(1998).
[9]
SUBCELLULAR LOCATION, IDENTIFICATION IN THE STAGA COMPLEX WITH SUPT3H;
GCN5L2; KIAA0764; TAF5L; TAF6L; TRRAP; TADA3L; TAF10 AND TAF12, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=11564863; DOI=10.1128/MCB.21.20.6782-6795.2001;
Martinez E., Palhan V.B., Tjernberg A., Lymar E.S., Gamper A.M.,
Kundu T.K., Chait B.T., Roeder R.G.;
"Human STAGA complex is a chromatin-acetylating transcription
coactivator that interacts with pre-mRNA splicing and DNA damage-
binding factors in vivo.";
Mol. Cell. Biol. 21:6782-6795(2001).
[10]
IDENTIFICATION IN THE PCAF COMPLEX WITH TADA2L; TADA3L; TAF5L; SUPT3H;
TAF6L; TAF10; TAF12 AND TRRAP.
PubMed=9885574; DOI=10.1016/S1097-2765(00)80301-9;
Vassilev A., Yamauchi J., Kotani T., Prives C., Avantaggiati M.L.,
Qin J., Nakatani Y.;
"The 400 kDa subunit of the PCAF histone acetylase complex belongs to
the ATM superfamily.";
Mol. Cell 2:869-875(1998).
[11]
IDENTIFICATION IN THE MLL1/MLL COMPLEX.
PubMed=15960975; DOI=10.1016/j.cell.2005.04.031;
Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J.,
Allis C.D., Chait B.T., Hess J.L., Roeder R.G.;
"Physical association and coordinate function of the H3 K4
methyltransferase MLL1 and the H4 K16 acetyltransferase MOF.";
Cell 121:873-885(2005).
[12]
IDENTIFICATION.
PubMed=16079131; DOI=10.1074/jbc.M501982200;
Santama N., Ogg S.C., Malekkou A., Zographos S.E., Weis K.,
Lamond A.I.;
"Characterization of hCINAP, a novel coilin-interacting protein
encoded by a transcript from the transcription factor TAFIID32
locus.";
J. Biol. Chem. 280:36429-36441(2005).
[13]
INTERACTION WITH TAF6 IN A COMPLEX WITH TAF6; TAF9; TAF12 AND TAF4B,
AND DNA-BINDING.
PubMed=15601843; DOI=10.1128/MCB.25.1.206-219.2005;
Shao H., Revach M., Moshonov S., Tzuman Y., Gazit K., Albeck S.,
Unger T., Dikstein R.;
"Core promoter binding by histone-like TAF complexes.";
Mol. Cell. Biol. 25:206-219(2005).
[14]
FUNCTION, SUBUNIT, INDUCTION, AND INTERACTION WITH TAF5 AND TAF6.
PubMed=15899866; DOI=10.1128/MCB.25.11.4638-4649.2005;
Frontini M., Soutoglou E., Argentini M., Bole-Feysot C., Jost B.,
Scheer E., Tora L.;
"TAF9b (formerly TAF9L) is a bona fide TAF that has unique and
overlapping roles with TAF9.";
Mol. Cell. Biol. 25:4638-4649(2005).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-161; THR-178 AND
SER-181, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149; SER-158 AND
THR-159, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-5, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149 AND THR-178, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149; SER-152; THR-178
AND SER-196, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
-!- FUNCTION: Essential for cell viability. TAF9 and TAF9B are
involved in transcriptional activation as well as repression of
distinct but overlapping sets of genes. May have a role in gene
regulation associated with apoptosis. TAFs are components of the
transcription factor IID (TFIID) complex, the TBP-free TAFII
complex (TFTC), the PCAF histone acetylase complex and the STAGA
transcription coactivator-HAT complex. TFIID or TFTC are essential
for the regulation of RNA polymerase II-mediated transcription.
{ECO:0000269|PubMed:15899866}.
-!- SUBUNIT: Component of TFIID, the TATA-binding protein-free TAF
complex (TFTC), the PCAF complex and the STAGA transcription
coactivator-HAT complex. The PCAF complex consists at least of
TADA2L/ADA2, SUPT3H/SPT3, TADA3L/ADA3, TAF5L/PAF65-beta,
TAF6L/PAF65-alpha, TAF10/TAFII30, TAF12/TAFII20, TAF9/TAFII31 and
TRRAP. The STAGA transcription coactivator-HAT complex consists at
least of SUPT3H, GCN5L2, SUPT7L, TAF5L, TAF6L, TADA3L, TAD1L,
TAF10, TAF12, TRRAP and TAF9. Binds N-terminal domain of p53/TP53
which is essential for transcription. Component of some MLL1/MLL
complex, at least composed of the core components KMT2A/MLL1,
ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative
components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX,
MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A,
RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Binds
TFIIB and the Herpes simplex virus activator VP16. Forms a
heterodimer with TAF6/TAFII80 in a complex with the
TAF4B/TAFII105-TAF12/TAFII20 heterodimer. Also interacts with
TAF5. Binds directly DNA. Increased DNA binding when complexed
with TAF6/TAFII80. {ECO:0000269|PubMed:11564863,
ECO:0000269|PubMed:15601843, ECO:0000269|PubMed:15899866,
ECO:0000269|PubMed:15960975, ECO:0000269|PubMed:7597030,
ECO:0000269|PubMed:7761466, ECO:0000269|PubMed:9674425,
ECO:0000269|PubMed:9885574}.
-!- INTERACTION:
Q14919:DRAP1; NbExp=8; IntAct=EBI-712521, EBI-712941;
Q92831:KAT2B; NbExp=3; IntAct=EBI-712521, EBI-477430;
P46099:Klf1 (xeno); NbExp=3; IntAct=EBI-712521, EBI-15761537;
P52294:KPNA1; NbExp=4; IntAct=EBI-712521, EBI-358383;
O60684:KPNA6; NbExp=5; IntAct=EBI-712521, EBI-359923;
Q9Y6J9:TAF6L; NbExp=8; IntAct=EBI-712521, EBI-743984;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11564863,
ECO:0000269|PubMed:9674425}.
-!- INDUCTION: 6 to 8-fold by apoptotic signals.
{ECO:0000269|PubMed:15899866}.
-!- SIMILARITY: Belongs to the TAF9 family. {ECO:0000305}.
-!- CAUTION: AK6 and TAF9 were initially considered as products of the
same gene since they share two exons. However, they are translated
from different initiation codons and reading frames and encode
unrelated proteins. This arrangement is conserved in some
mammalian species. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/taf9/";
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EMBL; U25112; AAA91318.1; -; mRNA.
EMBL; U21858; AAC50153.1; -; mRNA.
EMBL; U30504; AAA84389.1; -; mRNA.
EMBL; BT019652; AAV38458.1; -; mRNA.
EMBL; AY189986; AAN84793.1; -; Genomic_DNA.
EMBL; CH471137; EAW51295.1; -; Genomic_DNA.
EMBL; CH471137; EAW51296.1; -; Genomic_DNA.
EMBL; BC003400; AAH03400.1; -; mRNA.
EMBL; BC033320; AAH33320.1; -; mRNA.
CCDS; CCDS4002.1; -.
PIR; I39141; I39141.
RefSeq; NP_001015892.1; NM_001015892.1.
RefSeq; NP_003178.1; NM_003187.4.
UniGene; Hs.653163; -.
ProteinModelPortal; Q16594; -.
SMR; Q16594; -.
BioGrid; 112743; 90.
CORUM; Q16594; -.
DIP; DIP-435N; -.
IntAct; Q16594; 55.
MINT; MINT-2860193; -.
STRING; 9606.ENSP00000217893; -.
iPTMnet; Q16594; -.
PhosphoSitePlus; Q16594; -.
BioMuta; SLC26A3; -.
DMDM; 2498981; -.
EPD; Q16594; -.
MaxQB; Q16594; -.
PaxDb; Q16594; -.
PeptideAtlas; Q16594; -.
PRIDE; Q16594; -.
DNASU; 6880; -.
Ensembl; ENST00000217893; ENSP00000217893; ENSG00000273841.
Ensembl; ENST00000328663; ENSP00000370193; ENSG00000273841.
Ensembl; ENST00000506736; ENSP00000421873; ENSG00000273841.
Ensembl; ENST00000615404; ENSP00000478935; ENSG00000276463.
Ensembl; ENST00000616867; ENSP00000477750; ENSG00000276463.
Ensembl; ENST00000617893; ENSP00000477611; ENSG00000276463.
GeneID; 6880; -.
KEGG; hsa:6880; -.
UCSC; uc003jwc.2; human.
CTD; 6880; -.
DisGeNET; 6880; -.
EuPathDB; HostDB:ENSG00000273841.4; -.
GeneCards; TAF9; -.
HGNC; HGNC:11542; TAF9.
HPA; HPA028930; -.
HPA; HPA053429; -.
HPA; HPA058961; -.
MIM; 600822; gene.
neXtProt; NX_Q16594; -.
OpenTargets; ENSG00000273841; -.
PharmGKB; PA36317; -.
eggNOG; KOG3334; Eukaryota.
eggNOG; COG5094; LUCA.
GeneTree; ENSGT00390000001626; -.
HOGENOM; HOG000231730; -.
HOVERGEN; HBG002304; -.
InParanoid; Q16594; -.
KO; K14535; -.
OMA; IQCRMDQ; -.
OrthoDB; EOG091G0RPE; -.
PhylomeDB; Q16594; -.
TreeFam; TF351417; -.
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-3214847; HATs acetylate histones.
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.
GeneWiki; TAF9; -.
GenomeRNAi; 6880; -.
PRO; PR:Q16594; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000273841; -.
CleanEx; HS_TAF9; -.
ExpressionAtlas; Q16594; baseline and differential.
Genevisible; Q16594; HS.
GO; GO:0071339; C:MLL1 complex; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0000125; C:PCAF complex; IDA:UniProtKB.
GO; GO:0070761; C:pre-snoRNP complex; IDA:BHF-UCL.
GO; GO:0000124; C:SAGA complex; IBA:GO_Central.
GO; GO:0030914; C:STAGA complex; IDA:UniProtKB.
GO; GO:0005669; C:transcription factor TFIID complex; IDA:UniProtKB.
GO; GO:0033276; C:transcription factor TFTC complex; IDA:UniProtKB.
GO; GO:0033613; F:activating transcription factor binding; IPI:BHF-UCL.
GO; GO:0051117; F:ATPase binding; IPI:UniProtKB.
GO; GO:0070742; F:C2H2 zinc finger domain binding; IPI:BHF-UCL.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0002039; F:p53 binding; IPI:BHF-UCL.
GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:BHF-UCL.
GO; GO:0000492; P:box C/D snoRNP assembly; IDA:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IC:BHF-UCL.
GO; GO:0043966; P:histone H3 acetylation; IDA:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:BHF-UCL.
GO; GO:1902166; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IC:BHF-UCL.
GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:BHF-UCL.
GO; GO:0030307; P:positive regulation of cell growth; IMP:UniProtKB.
GO; GO:0060760; P:positive regulation of response to cytokine stimulus; IMP:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0050821; P:protein stabilization; IDA:BHF-UCL.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
GO; GO:0070555; P:response to interleukin-1; IMP:BHF-UCL.
GO; GO:0051123; P:RNA polymerase II transcriptional preinitiation complex assembly; IEA:GOC.
GO; GO:0042795; P:snRNA transcription from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
CDD; cd07979; TAF9; 1.
InterPro; IPR009072; Histone-fold.
InterPro; IPR003162; TFIID-31.
Pfam; PF02291; TFIID-31kDa; 1.
SUPFAM; SSF47113; SSF47113; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Direct protein sequencing;
DNA-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Transcription; Transcription regulation.
CHAIN 1 264 Transcription initiation factor TFIID
subunit 9.
/FTId=PRO_0000118888.
DNA_BIND 120 137
COMPBIAS 250 262 Poly-Asp.
MOD_RES 5 5 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 149 149 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 152 152 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 155 155 Phosphoserine.
{ECO:0000250|UniProtKB:Q8VI33}.
MOD_RES 158 158 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 159 159 Phosphothreonine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 161 161 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 164 164 Phosphothreonine.
{ECO:0000250|UniProtKB:Q8VI33}.
MOD_RES 178 178 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 181 181 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 196 196 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VARIANT 6 6 T -> M (in dbSNP:rs4252233).
{ECO:0000269|Ref.5}.
/FTId=VAR_016279.
VARIANT 210 210 Q -> H (in dbSNP:rs11542580).
/FTId=VAR_052260.
CONFLICT 46 46 Y -> V (in Ref. 8; AA sequence).
{ECO:0000305}.
CONFLICT 225 225 L -> F (in Ref. 7; AAH03400).
{ECO:0000305}.
SEQUENCE 264 AA; 28974 MW; 1925AEC65D6C84C7 CRC64;
MESGKTASPK SMPKDAQMMA QILKDMGITE YEPRVINQML EFAFRYVTTI LDDAKIYSSH
AKKATVDADD VRLAIQCRAD QSFTSPPPRD FLLDIARQRN QTPLPLIKPY SGPRLPPDRY
CLTAPNYRLK SLQKKASTSA GRITVPRLSV GSVTSRPSTP TLGTPTPQTM SVSTKVGTPM
SLTGQRFTVQ MPTSQSPAVK ASIPATSAVQ NVLINPSLIG SKNILITTNM MSSQNTANES
SNALKRKRED DDDDDDDDDD YDNL


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EIAAB41320 Rat,Rattus norvegicus,RNA polymerase II TBP-associated factor subunit G,Taf2g,Taf9,TAFII31,Tafii31,TAFII-31,TAFII32,TAFII-32,Transcription initiation factor TFIID 31 kDa subunit,Transcription initiati
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
EIAAB41276 Mouse,Mus musculus,Taf12,TAFII20,TAFII-20,Transcription initiation factor TFIID 20 kDa subunits,Transcription initiation factor TFIID subunit 12


 

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