TAF5L

TAF5-like RNA polymerase II, p300/CBP-associated factor (PCAF)-associated factor, 65kDa
Identifiers
Symbols	TAF5L; PAF65B
External IDs	MGI: 1919039 HomoloGene: 8676 GeneCards: TAF5L Gene
Gene Ontology Molecular function • sequence-specific DNA binding transcription factor activity • transcription coactivator activity • histone acetyltransferase activity Cellular component • nucleus • STAGA complex • transcription factor TFTC complex Biological process • regulation of transcription, DNA-dependent • transcription from RNA polymerase II promoter • histone H3 acetylation Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	27097	102162
Ensembl	ENSG00000135801	ENSMUSG00000038697
UniProt	O75529	Q3U3C7
RefSeq (mRNA)	NM_001025247.1	NM_133966.2
RefSeq (protein)	NP_001020418.1	NP_598727.1
Location (UCSC)	Chr 1: 229.73 – 229.76 Mb	Chr 8: 126.52 – 126.55 Mb
PubMed search	[1]	[2]

TAF5-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 5L is an enzyme that in humans is encoded by the TAF5L gene.

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.

Interactions

TAF5L has been shown to interact with TAF9 and Transcription initiation protein SPT3 homolog.

Further reading

• Struhl K, Moqtaderi Z (1998). "The TAFs in the HAT.". Cell 94 (1): 1–4. doi:10.1016/S0092-8674(00)81213-1. PMID 9674419. 
• 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. doi:10.1074/jbc.274.26.18285. PMID 10373431. 
• 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. PMC 150203. PMID 11406595. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=150203. 
• 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. PMC 99856. PMID 11564863. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=99856. 
• 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. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• 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. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928. 
• 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. doi:10.1080/08916930500128594. 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. PMC 1894761. PMID 17476304. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1894761.