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Protein TAF9 PDB 1rkb.png
Aliases TAF9, MGC:5067, STAF31/32, TAF2G, TAFII-31, TAFII-32, TAFII31, TAFII32, TAFIID32, TATA-box binding protein associated factor 9
External IDs MGI: 1888697 HomoloGene: 39986 GeneCards: TAF9
RNA expression pattern
PBB GE TAF9 202168 at fs.png

PBB GE TAF9 203893 at fs.png
More reference expression data
Species Human Mouse
RefSeq (mRNA)



RefSeq (protein)



Location (UCSC) Chr 5: 69.35 – 69.37 Mb Chr 13: 100.65 – 100.66 Mb
PubMed search [1] [2]
View/Edit Human View/Edit Mouse

TAF9 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 32kDa, also known as TAF9, is a protein that in humans is encoded by the TAF9 gene.[3][4]


Initiation of transcription by RNA polymerase II requires the activities of more than 70 polypeptides. The protein complex that coordinates these activities is transcription factor IID (TFIID), which binds to the core promoter to position the polymerase properly, serves as the scaffold for assembly of the remainder of the transcription complex, and acts as a channel for regulatory signals. TFIID is composed of the TATA-binding protein (TBP) and a group of evolutionarily conserved proteins known as TBP-associated factors or TAFs. TAFs may participate in basal transcription, serve as coactivators, function in promoter recognition or modify general transcription factors (GTFs) to facilitate complex assembly and transcription initiation. This gene encodes one of the smaller subunits of TFIID that binds to the basal transcription factor GTF2B as well as to several transcriptional activators such as p53 and VP16. A similar but distinct gene (TAF9B) has been found on the X chromosome and a pseudogene has been identified on chromosome 19. Alternative splicing results in multiple transcript variants encoding different isoforms.[3]


The 17-amino-acid-long trans-activating domains (TAD) of several transcription factors were reported to bind directly to TAF9: p53, VP16, HSF1, NF-IL6, NFAT1, NF-κB, and ALL1/MLL1.[5] Inside of these 17 amino acids, a unique Nine-amino-acid transactivation domain (9aaTAD) was identified for each reported transcription factor.[6] 9aaTAD is a novel domain common to a large superfamily of eukaryotic transcription factors represented by Gal4, Oaf1, Leu3, Rtg3, Pho4, Gln4, Gcn4 in yeast and by p53, NFAT, NF-κB and VP16 in mammals.[7] TAF9 is supposed to be a universal transactivation cofactor for 9aaTAD transcription factors.[6]


TAF9 has been shown to interact with:


  1. ^ "Human PubMed Reference:". 
  2. ^ "Mouse PubMed Reference:". 
  3. ^ a b "Entrez Gene: TAF9 TAF9 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 32kDa". 
  4. ^ Evans SC, Foster CJ, El-Naggar AK, Lozano G (April 1999). "Mapping and mutational analysis of the human TAF2G gene encoding a p53 cofactor". Genomics. 57 (1): 182–3. doi:10.1006/geno.1999.5745. PMID 10191103. 
  5. ^ Uesugi M, Nyanguile O, Lu H, Levine AJ, Verdine GL (August 1997). "Induced alpha helix in the VP16 activation domain upon binding to a human TAF". Science. 277 (5330): 1310–3. doi:10.1126/science.277.5330.1310. PMID 9271577. Uesugi M, Verdine GL (December 1999). "The alpha-helical FXXPhiPhi motif in p53: TAF interaction and discrimination by MDM2". Proc. Natl. Acad. Sci. U.S.A. 96 (26): 14801–6. doi:10.1073/pnas.96.26.14801. PMC 24728Freely accessible. PMID 10611293. Choi Y, Asada S, Uesugi M (May 2000). "Divergent hTAFII31-binding motifs hidden in activation domains". J. Biol. Chem. 275 (21): 15912–6. doi:10.1074/jbc.275.21.15912. PMID 10821850. Venot C, Maratrat M, Sierra V, Conseiller E, Debussche L (April 1999). "Definition of a p53 transactivation function-deficient mutant and characterization of two independent p53 transactivation subdomains". Oncogene. 18 (14): 2405–10. doi:10.1038/sj.onc.1202539. PMID 10327062. Lin J, Chen J, Elenbaas B, Levine AJ (May 1994). "Several hydrophobic amino acids in the p53 amino-terminal domain are required for transcriptional activation, binding to mdm-2 and the adenovirus 5 E1B 55-kD protein". Genes Dev. 8 (10): 1235–46. doi:10.1101/gad.8.10.1235. PMID 7926727. 
  6. ^ a b Piskacek S, Gregor M, Nemethova M, Grabner M, Kovarik P, Piskacek M (June 2007). "Nine-amino-acid transactivation domain: establishment and prediction utilities". Genomics. 89 (6): 756–68. doi:10.1016/j.ygeno.2007.02.003. PMID 17467953. 
  7. ^ The prediction for 9aa TADs (for both acidic and hydrophilic transactivation domains) is available online from National EMBnet-Node Austria ("9aaTAD Prediction Webtool". EMBnet AUSTRIA. Retrieved 2009-01-10. )
  8. ^ a b c d e f g h i j k l Martinez E, Palhan VB, Tjernberg A, Lymar ES, Gamper AM, Kundu TK, Chait BT, Roeder RG (Oct 2001). "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 (20): 6782–95. doi:10.1128/MCB.21.20.6782-6795.2001. PMC 99856Freely accessible. PMID 11564863. 
  9. ^ Liu X, Tesfai J, Evrard YA, Dent SY, Martinez E (May 2003). "c-Myc transformation domain recruits the human STAGA complex and requires TRRAP and GCN5 acetylase activity for transcription activation". J. Biol. Chem. 278 (22): 20405–12. doi:10.1074/jbc.M211795200. PMC 4031917Freely accessible. PMID 12660246. 
  10. ^ Tao Y, Guermah M, Martinez E, Oelgeschläger T, Hasegawa S, Takada R, Yamamoto T, Horikoshi M, Roeder RG (Mar 1997). "Specific interactions and potential functions of human TAFII100". J. Biol. Chem. 272 (10): 6714–21. doi:10.1074/jbc.272.10.6714. PMID 9045704. 
  11. ^ Bellorini M, Lee DK, Dantonel JC, Zemzoumi K, Roeder RG, Tora L, Mantovani R (Jun 1997). "CCAAT binding NF-Y-TBP interactions: NF-YB and NF-YC require short domains adjacent to their histone fold motifs for association with TBP basic residues". Nucleic Acids Res. 25 (11): 2174–81. doi:10.1093/nar/25.11.2174. PMC 146709Freely accessible. PMID 9153318. 

Further reading[edit]