TAF5L

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TAF5-like RNA polymerase II, p300/CBP-associated factor (PCAF)-associated factor, 65kDa
Identifiers
Symbols TAF5L ; PAF65B
External IDs Template:MGI HomoloGene8676
RNA expression pattern
File:PBB GE TAF5L 213654 at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

TAF5-like RNA polymerase II, p300/CBP-associated factor (PCAF)-associated factor, 65kDa, also known as TAF5L, is a human gene.[1]

The product of this gene belongs to the WD-repeat TAF5 family of proteins. This gene encodes a protein that is a component of the PCAF histone acetylase complex. The PCAF histone acetylase complex, which is composed of more than 20 polypeptides some of which are TAFs, is required for myogenic transcription and differentiation. TAFs may participate in basal transcription, serve as coactivators, function in promoter recognition or modify general transcription factors to facilitate complex assembly and transcription initiation. The encoded protein is structurally similar to one of the histone-like TAFs, TAF5. Alternatively spliced transcript variants encoding different isoforms have been identified for this gene.[1]

References

  1. 1.0 1.1 "Entrez Gene: TAF5L TAF5-like RNA polymerase II, p300/CBP-associated factor (PCAF)-associated factor, 65kDa".

Further reading

  • Struhl K, Moqtaderi Z (1998). "The TAFs in the HAT". Cell. 94 (1): 1–4. PMID 9674419.
  • Ogryzko VV, Kotani T, Zhang X; et al. (1998). "Histone-like TAFs within the PCAF histone acetylase complex". Cell. 94 (1): 35–44. PMID 9674425.
  • Brand M, Yamamoto K, Staub A, Tora L (1999). "Identification of TATA-binding protein-free TAFII-containing complex subunits suggests a role in nucleosome acetylation and signal transduction". J. Biol. Chem. 274 (26): 18285–9. PMID 10373431.
  • Stanchi F, Bertocco E, Toppo S; et al. (2001). "Characterization of 16 novel human genes showing high similarity to yeast sequences". Yeast. 18 (1): 69–80. doi:10.1002/1097-0061(200101)18:1<69::AID-YEA647>3.0.CO;2-H. PMID 11124703.
  • Brand M, Moggs JG, Oulad-Abdelghani M; et al. (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. PMID 11406595.
  • Martinez E, Palhan VB, Tjernberg A; et al. (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. PMID 11564863.
  • Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
  • Cavusoglu N, Brand M, Tora L, Van Dorsselaer A (2003). "Novel subunits of the TATA binding protein free TAFII-containing transcription complex identified by matrix-assisted laser desorption/ionization-time of flight mass spectrometry following one-dimensional gel electrophoresis". Proteomics. 3 (2): 217–23. doi:10.1002/pmic.200390030. PMID 12601814.
  • Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
  • Zhang K, Faiola F, Martinez E (2005). "Six lysine residues on c-Myc are direct substrates for acetylation by p300". Biochem. Biophys. Res. Commun. 336 (1): 274–80. doi:10.1016/j.bbrc.2005.08.075. PMID 16126174.
  • Chistiakov DA, Chernisheva A, Savost'anov KV; et al. (2005). "The TAF5L gene on chromosome 1q42 is associated with type 1 diabetes in Russian affected patients". Autoimmunity. 38 (4): 283–93. PMID 16206511.
  • Kuninger D, Wright A, Rotwein P (2006). "Muscle cell survival mediated by the transcriptional coactivators p300 and PCAF displays different requirements for acetyltransferase activity". Am. J. Physiol., Cell Physiol. 291 (4): C699–709. doi:10.1152/ajpcell.00056.2006. PMID 16672693.
  • Okumura K, Mendoza M, Bachoo RM; et al. (2006). "PCAF modulates PTEN activity". J. Biol. Chem. 281 (36): 26562–8. doi:10.1074/jbc.M605391200. PMID 16829519.
  • Ravnskjaer K, Kester H, Liu Y; et al. (2007). "Cooperative interactions between CBP and TORC2 confer selectivity to CREB target gene expression". EMBO J. 26 (12): 2880–9. doi:10.1038/sj.emboj.7601715. PMID 17476304.

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