TAF5L

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.[5][6][7]

TAF5L
Identifiers
Aliases	TAF5L, PAF65B, TATA-box binding protein associated factor 5 like
External IDs	MGI: 1919039 HomoloGene: 8676 GeneCards: TAF5L
Gene location (Human) Chr. Chromosome 1 (human)[1] Band 1q42.13 Start 229,593,111 bp[1] End 229,626,047 bp[1]
Gene location (Mouse) Chr. Chromosome 8 (mouse)[2] Band 8|8 E2 Start 123,996,318 bp[2] End 124,021,397 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • GO:0001131, GO:0001151, GO:0001130, GO:0001204 DNA-binding transcription factor activity • GO:0001105 transcription coactivator activity • GO:0001948 protein binding • histone acetyltransferase activity Cellular component • nuclear speck • cell nucleus • cytoplasmic ribonucleoprotein granule • STAGA complex • transcription factor TFTC complex Biological process • regulation of transcription, DNA-templated • transcription from RNA polymerase II promoter • histone H3 acetylation • transcription, DNA-templated • positive regulation of nucleic acid-templated transcription Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	27097	102162
Ensembl	ENSG00000135801	ENSMUSG00000038697
UniProt	O75529	Q91WQ5
RefSeq (mRNA)	NM_001025247 NM_014409	NM_133966 NM_001357315
RefSeq (protein)	NP_001020418 NP_055224	NP_598727 NP_001344244
Location (UCSC)	Chr 1: 229.59 – 229.63 Mb	Chr 8: 124 – 124.02 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

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.[7]

Interactions

TAF5L has been shown to interact with TAF9[8] and Transcription initiation protein SPT3 homolog.[8]

References

1. GRCh38: Ensembl release 89: ENSG00000135801 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000038697 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Ogryzko VV, Kotani T, Zhang X, Schiltz RL, Howard T, Yang XJ, Howard BH, Qin J, Nakatani Y (Aug 1998). "Histone-like TAFs within the PCAF histone acetylase complex". Cell. 94 (1): 35–44. doi:10.1016/S0092-8674(00)81219-2. PMID 9674425.
6. Stanchi F, Bertocco E, Toppo S, Dioguardi R, Simionati B, Cannata N, Zimbello R, Lanfranchi G, Valle G (Jan 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.
7. "Entrez Gene: TAF5L TAF5-like RNA polymerase II, p300/CBP-associated factor (PCAF)-associated factor, 65kDa".
8. Martinez E, Palhan VB, Tjernberg A, Lymar ES, Gamper AM, Kundu TK, Chait BT, Roeder RG (Oct 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.

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, Lejeune F, Dilworth FJ, Stevenin J, Almouzni G, Tora L (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.
• Martinez E, Palhan VB, Tjernberg A, Lymar ES, Gamper AM, Kundu TK, Chait BT, Roeder RG (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.
• 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.
• 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, Turakulov RI, Kuraeva TL, Dedov II, Nosikov VV (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, DePinho RA, Cavenee WK, Furnari FB (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, Zhang X, Lee D, Yates JR, Montminy M (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.