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TAF4 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 135kDa
Protein TAF4 PDB 1h3o.png
PDB rendering based on 1h3o.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols TAF4 ; TAF2C; TAF2C1; TAF4A; TAFII130; TAFII135
External IDs OMIM601796 MGI2152346 HomoloGene55723 GeneCards: TAF4 Gene
RNA expression pattern
PBB GE TAF4 213090 s at tn.png
PBB GE TAF4 208545 x at tn.png
More reference expression data
Species Human Mouse
Entrez 6874 228980
Ensembl ENSG00000130699 ENSMUSG00000039117
UniProt O00268 A2AC70
RefSeq (mRNA) NM_003185 NM_001081092
RefSeq (protein) NP_003176 NP_001074561
Location (UCSC) Chr 20:
60.53 – 60.64 Mb
Chr 2:
179.91 – 179.98 Mb
PubMed search [1] [2]

Transcription initiation factor TFIID subunit 4 is a protein that in humans is encoded by the TAF4 gene.[1][2][3]


Initiation of transcription by RNA polymerase II requires the activities of more than 70 polypeptides. The protein 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 larger subunits of TFIID that has been shown to potentiate transcriptional activation by retinoic acid, thyroid hormone and vitamin D3 receptors. In addition, this subunit interacts with the transcription factor CREB, which has a glutamine-rich activation domain, and binds to other proteins containing glutamine-rich regions. Aberrant binding to this subunit by proteins with expanded polyglutamine regions has been suggested as one of the pathogenetic mechanisms underlying a group of neurodegenerative disorders referred to as polyglutamine diseases.[3]


TAF4 has been shown to interact with:

Protein domain[edit]

PDB 1h3o EBI.jpg
crystal structure of the human taf4-taf12 (tafii135-tafii20) complex
Symbol TAF4
Pfam PF05236
InterPro IPR007900
SCOP 1h3o

Yeast TFIID comprises the TATA binding protein and 14 TBP-associated factors (TAFIIs), nine of which contain histone-fold domains (INTERPRO). The C-terminal region of the TFIID-specific yeast TAF4 (yTAF4) containing the HFD shares strong sequence similarity with Drosophila (d)TAF4 and human TAF4. A structure/function analysis of yTAF4 demonstrates that the HFD, a short conserved C-terminal domain (CCTD), and the region separating them are all required for yTAF4 function. This region of similarity is found in Transcription initiation factor TFIID component TAF4.[8]


  1. ^ Tanese N, Saluja D, Vassallo MF, Chen JL, Admon A (January 1997). "Molecular cloning and analysis of two subunits of the human TFIID complex: hTAFII130 and hTAFII100". Proc. Natl. Acad. Sci. U.S.A. 93 (24): 13611–6. doi:10.1073/pnas.93.24.13611. PMC 19367. PMID 8942982.  Check date values in: |year= / |date= mismatch (help)
  2. ^ Mengus G, May M, Carré L, Chambon P, Davidson I (July 1997). "Human TAF(II)135 potentiates transcriptional activation by the AF-2s of the retinoic acid, vitamin D3, and thyroid hormone receptors in mammalian cells". Genes Dev. 11 (11): 1381–95. doi:10.1101/gad.11.11.1381. PMID 9192867. 
  3. ^ a b "Entrez Gene: TAF4 TAF4 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 135kDa". 
  4. ^ Vassallo MF, Tanese N (April 2002). "Isoform-specific interaction of HP1 with human TAFII130". Proc. Natl. Acad. Sci. U.S.A. 99 (9): 5919–24. doi:10.1073/pnas.092025499. PMC 122877. PMID 11959914. 
  5. ^ Pointud JC, Mengus G, Brancorsini S, Monaco L, Parvinen M, Sassone-Corsi P et al. (May 2003). "The intracellular localisation of TAF7L, a paralogue of transcription factor TFIID subunit TAF7, is developmentally regulated during male germ-cell differentiation". J. Cell. Sci. 116 (Pt 9): 1847–58. doi:10.1242/jcs.00391. PMID 12665565. 
  6. ^ Bellorini M, Lee DK, Dantonel JC, Zemzoumi K, Roeder RG, Tora L et al. (June 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 146709. PMID 9153318. 
  7. ^ Brand M, Moggs JG, Oulad-Abdelghani M, Lejeune F, Dilworth FJ, Stevenin J et al. (June 2001). "UV-damaged DNA-binding protein in the TFTC complex links DNA damage recognition to nucleosome acetylation". EMBO J. 20 (12): 3187–96. doi:10.1093/emboj/20.12.3187. PMC 150203. PMID 11406595. 
  8. ^ Thuault S, Gangloff YG, Kirchner J, Sanders S, Werten S, Romier C et al. (November 2002). "Functional analysis of the TFIID-specific yeast TAF4 (yTAF(II)48) reveals an unexpected organization of its histone-fold domain". J. Biol. Chem. 277 (47): 45510–7. doi:10.1074/jbc.M206556200. PMID 12237303. 

Further reading[edit]