TAF6L

TAF6-like RNA polymerase II, p300/CBP-associated factor (PCAF)-associated factor, 65kDa
Identifiers
Symbols	TAF6L ; PAF65A
External IDs	OMIM: 602946 MGI: 2444957 HomoloGene: 4728 GeneCards: TAF6L Gene
Gene ontology Molecular function • DNA binding • transcription coactivator activity • histone acetyltransferase activity • protein binding • protein heterodimerization activity Cellular component • histone deacetylase complex • STAGA complex • extracellular exosome Biological process • chromatin organization • chromatin remodeling • DNA-templated transcription, initiation • regulation of transcription from RNA polymerase II promoter • histone H3 acetylation • regulation of sequence-specific DNA binding transcription factor activity Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	10629	225895
Ensembl	ENSG00000162227	ENSMUSG00000003680
UniProt	Q9Y6J9	Q8R2K4
RefSeq (mRNA)	NM_006473	NM_001177798
RefSeq (protein)	NP_006464	NP_001171269
Location (UCSC)	Chr 11: 62.77 – 62.79 Mb	Chr 19: 8.77 – 8.79 Mb
PubMed search

TAF6-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 6L is an enzyme that in humans is encoded by the TAF6L gene.^[1][2]

Function

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 a protein that is a component of the PCAF histone acetylase complex and structurally similar to one of the histone-like TAFs, TAF6. 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.^[2]

Interactions

TAF6L has been shown to interact with TAF9^[3] and Transcription initiation protein SPT3 homolog.^[3]

References

1. Ogryzko VV, Kotani T, Zhang X, Schiltz RL, Howard T, Yang XJ, Howard BH, Qin J, Nakatani Y (August 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.
2. "Entrez Gene: TAF6L TAF6-like RNA polymerase II, p300/CBP-associated factor (PCAF)-associated factor, 65kDa".
3. Martinez E, Palhan VB, Tjernberg A, Lymar ES, Gamper AM, Kundu TK, Chait BT, Roeder RG (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. 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, 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.
• Pitkänen J, Rebane A, Rowell J, Murumägi A, Ströbel P, Möll K, Saare M, Heikkilä J, Doucas V, Marx A, Peterson P (2005). "Cooperative activation of transcription by autoimmune regulator AIRE and CBP". Biochem. Biophys. Res. Commun. 333 (3): 944–53. doi:10.1016/j.bbrc.2005.05.187. PMID 15964547.
• Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
• Lim J, Hao T, Shaw C, Patel AJ, Szabó G, Rual JF, Fisk CJ, Li N, Smolyar A, Hill DE, Barabási AL, Vidal M, Zoghbi HY (2006). "A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration". Cell 125 (4): 801–14. doi:10.1016/j.cell.2006.03.032. PMID 16713569.