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TAF5 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 100kDa
Protein TAF5 PDB 2nxp.png
PDB rendering based on 2nxp.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols TAF5 ; TAF2D; TAFII100
External IDs OMIM601787 MGI2442144 HomoloGene5064 GeneCards: TAF5 Gene
RNA expression pattern
PBB GE TAF5 210053 at tn.png
More reference expression data
Species Human Mouse
Entrez 6877 226182
Ensembl ENSG00000148835 ENSMUSG00000025049
UniProt Q15542 Q8C092
RefSeq (mRNA) NM_006951 NM_177342
RefSeq (protein) NP_008882 NP_796316
Location (UCSC) Chr 10:
105.13 – 105.15 Mb
Chr 19:
47.07 – 47.08 Mb
PubMed search [1] [2]

Transcription initiation factor TFIID subunit 5 is a protein that in humans is encoded by the TAF5 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 an integral subunit of TFIID associated with all transcriptionally competent forms of that complex. This subunit interacts strongly with two TFIID subunits that show similarity to histones H3 and H4, and it may participate in forming a nucleosome-like core in the TFIID complex.[3]


TAF5 has been shown to interact with TAF9,[4][5] TAF15,[6] TAF6[4][7] and TATA binding protein.[4][8][9]


  1. ^ Dubrovskaya V, Mattei MG, Tora L (February 1997). "Localization of the gene (TAF2D) encoding the 100-kDa subunit (hTAFII100) of the human TFIID complex to chromosome 10 band q24-q25.2". Genomics 36 (3): 556–7. doi:10.1006/geno.1996.0509. PMID 8884287. 
  2. ^ 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. 
  3. ^ a b "Entrez Gene: TAF5 TAF5 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 100kDa". 
  4. ^ a b c Tao, Y; Guermah M; Martinez E; Oelgeschläger T; Hasegawa S; Takada R; Yamamoto T; Horikoshi M; Roeder R G (March 1997). "Specific interactions and potential functions of human TAFII100". J. Biol. Chem. (UNITED STATES) 272 (10): 6714–21. doi:10.1074/jbc.272.10.6714. ISSN 0021-9258. PMID 9045704. 
  5. ^ Martinez, E; Palhan V B; Tjernberg A; Lymar E S; Gamper A M; Kundu T K; Chait B T; Roeder R G (October 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. (United States) 21 (20): 6782–95. doi:10.1128/MCB.21.20.6782-6795.2001. ISSN 0270-7306. PMC 99856. PMID 11564863. 
  6. ^ Bertolotti, A; Melot T; Acker J; Vigneron M; Delattre O; Tora L (March 1998). "EWS, but not EWS-FLI-1, is associated with both TFIID and RNA polymerase II: interactions between two members of the TET family, EWS and hTAFII68, and subunits of TFIID and RNA polymerase II complexes". Mol. Cell. Biol. (UNITED STATES) 18 (3): 1489–97. ISSN 0270-7306. PMC 108863. PMID 9488465. 
  7. ^ Hsieh, Y J; Kundu T K; Wang Z; Kovelman R; Roeder R G (November 1999). "The TFIIIC90 subunit of TFIIIC interacts with multiple components of the RNA polymerase III machinery and contains a histone-specific acetyltransferase activity". Mol. Cell. Biol. (UNITED STATES) 19 (11): 7697–704. ISSN 0270-7306. PMC 84812. PMID 10523658. 
  8. ^ Bellorini, M; Lee D K; Dantonel J C; Zemzoumi K; Roeder R G; Tora L; Mantovani R (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. (ENGLAND) 25 (11): 2174–81. doi:10.1093/nar/25.11.2174. ISSN 0305-1048. PMC 146709. PMID 9153318. 
  9. ^ Ruppert, S; Wang E H; Tjian R (March 1993). "Cloning and expression of human TAFII250: a TBP-associated factor implicated in cell-cycle regulation". Nature (ENGLAND) 362 (6416): 175–9. doi:10.1038/362175a0. ISSN 0028-0836. PMID 7680771. 

Further reading[edit]