TAF4

TAF4 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 135kDa

PDB rendering based on 1h3o.
Identifiers
Symbols TAF4; FLJ41943; TAF2C; TAF2C1; TAF4A; TAFII130; TAFII135
External IDs OMIM: 601796 MGI: 2152346 HomoloGene: 55723 GeneCards: TAF4 Gene
RNA expression pattern
More reference expression data
Orthologs
Species Human Mouse
Entrez 6874 228980
Ensembl ENSG00000130699 ENSMUSG00000039117
UniProt O00268 n/a
RefSeq (mRNA) NM_003185 NM_001081092.1
RefSeq (protein) NP_003176 NP_001074561.1
Location (UCSC) Chr 20:
60.53 – 60.64 Mb		 Chr 2:
179.65 – 179.71 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]

Interactions

TAF4 has been shown to interact with TATA binding protein,[4][5] CBX5[6] and Transcription initiation protein SPT3 homolog.[7]

References

  1. ^ Tanese N, Saluja D, Vassallo MF, Chen JL, Admon A (Jan 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=19367. 
  2. ^ Mengus G, May M, Carre L, Chambon P, Davidson I (Jul 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". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6874. 
  4. ^ Pointud, Jean-Christophe; Mengus Gabrielle, Brancorsini Stefano, Monaco Lucia, Parvinen Martti, Sassone-Corsi Paolo, Davidson Irwin (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. (England) 116 (Pt 9): 1847–58. doi:10.1242/jcs.00391. ISSN 0021-9533. PMID 12665565. 
  5. ^ Bellorini, M; Lee D K, Dantonel J C, Zemzoumi K, Roeder R G, 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. (ENGLAND) 25 (11): 2174–81. doi:10.1093/nar/25.11.2174. ISSN 0305-1048. PMC 146709. PMID 9153318. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=146709. 
  6. ^ Vassallo, Milo F; Tanese Naoko (Apr. 2002). "Isoform-specific interaction of HP1 with human TAFII130". Proc. Natl. Acad. Sci. U.S.A. (United States) 99 (9): 5919–24. doi:10.1073/pnas.092025499. ISSN 0027-8424. PMC 122877. PMID 11959914. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=122877. 
  7. ^ Brand, M; Moggs J G, Oulad-Abdelghani M, Lejeune F, Dilworth F J, Stevenin J, Almouzni G, Tora L (Jun. 2001). "UV-damaged DNA-binding protein in the TFTC complex links DNA damage recognition to nucleosome acetylation". EMBO J. (England) 20 (12): 3187–96. doi:10.1093/emboj/20.12.3187. ISSN 0261-4189. PMC 150203. PMID 11406595. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=150203. 

Further reading