Biology:TAF15
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TATA-binding protein-associated factor 2N is a protein that in humans is encoded by the TAF15 gene.[1][2][3]
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 subunit of TFIID present in a subset of TFIID complexes. Translocations involving chromosome 17 and chromosome 9, where the gene for the nuclear receptor CSMF is located, result in a gene fusion product that is an RNA binding protein associated with a subset of extraskeletal myxoid chondrosarcomas. Two transcripts encoding different isoforms have been identified.[3]
Interactions
TAF15 has been shown to interact with:
- POLR2C,[4]
- POLR2E,[4]
- POLR2G,[4]
- SAFB,[5]
- TAF11,[4]
- TAF13,[4]
- TAF5,[4]
- TAF7,[4] and
- TATA binding protein[6]
References
- ↑ "Cloning and mapping of a human RBP56 gene encoding a putative RNA binding protein similar to FUS/TLS and EWS proteins". Genomics 38 (1): 51–7. November 15, 1996. doi:10.1006/geno.1996.0591. PMID 8954779.
- ↑ "Genomic structure of the human RBP56/hTAFII68 and FUS/TLS genes". Gene 221 (2): 191–8. Dec 1998. doi:10.1016/S0378-1119(98)00463-6. PMID 9795213.
- ↑ 3.0 3.1 "Entrez Gene: TAF15 TAF15 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 68kDa". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8148.
- ↑ 4.0 4.1 4.2 4.3 4.4 4.5 4.6 "EWS, but not EWS-FLI-1, is associated with both TFIID and RNA polymerase II: interactions between two members of the TET family, EWS and hTAFII68, and subunits of TFIID and RNA polymerase II complexes". Mol. Cell. Biol. 18 (3): 1489–97. Mar 1998. doi:10.1128/mcb.18.3.1489. PMID 9488465.
- ↑ "Structure-function analysis of the estrogen receptor alpha corepressor scaffold attachment factor-B1: identification of a potent transcriptional repression domain". J. Biol. Chem. 279 (25): 26074–81. Jun 2004. doi:10.1074/jbc.M313726200. PMID 15066997.
- ↑ "Cloning and characterization of human TAF20/15. Multiple interactions suggest a central role in TFIID complex formation". J. Biol. Chem. 271 (30): 18194–202. Jul 1996. doi:10.1074/jbc.271.30.18194. PMID 8663456.
Further reading
- "Novel mechanism and factor for regulation by HIV-1 Tat". EMBO J. 14 (2): 321–8. 1995. doi:10.1002/j.1460-2075.1995.tb07006.x. PMID 7835343.
- "A novel LBP-1-mediated restriction of HIV-1 transcription at the level of elongation in vitro". J. Biol. Chem. 270 (5): 2274–83. 1995. doi:10.1074/jbc.270.5.2274. PMID 7836461.
- "Role of flanking E box motifs in human immunodeficiency virus type 1 TATA element function". J. Virol. 68 (11): 7188–99. 1994. doi:10.1128/JVI.68.11.7188-7199.1994. PMID 7933101.
- "Direct interaction of human TFIID with the HIV-1 transactivator tat". Nature 367 (6460): 295–9. 1994. doi:10.1038/367295a0. PMID 8121496. Bibcode: 1994Natur.367..295K.
- "Cloning and characterization of human TAF20/15. Multiple interactions suggest a central role in TFIID complex formation". J. Biol. Chem. 271 (30): 18194–202. 1996. doi:10.1074/jbc.271.30.18194. PMID 8663456.
- "Wild-type and transactivation-defective mutants of human immunodeficiency virus type 1 Tat protein bind human TATA-binding protein in vitro". J. Acquir. Immune Defic. Syndr. Hum. Retrovirol. 12 (2): 128–38. 1996. doi:10.1097/00042560-199606010-00005. PMID 8680883.
- "Mutations in the carboxy-terminal domain of TBP affect the synthesis of human immunodeficiency virus type 1 full-length and short transcripts similarly". J. Virol. 70 (8): 5025–34. 1996. doi:10.1128/JVI.70.8.5025-5034.1996. PMID 8764009.
- "Interaction of human immunodeficiency virus type 1 Tat with a unique site of TFIID inhibits negative cofactor Dr1 and stabilizes the TFIID-TFIIA complex". J. Virol. 70 (8): 5503–10. 1996. doi:10.1128/JVI.70.8.5503-5510.1996. PMID 8764062.
- "Tat-SF1: cofactor for stimulation of transcriptional elongation by HIV-1 Tat". Science 274 (5287): 605–10. 1996. doi:10.1126/science.274.5287.605. PMID 8849451. Bibcode: 1996Sci...274..605Z.
- "hTAF(II)68, a novel RNA/ssDNA-binding protein with homology to the pro-oncoproteins TLS/FUS and EWS is associated with both TFIID and RNA polymerase II". EMBO J. 15 (18): 5022–31. 1996. doi:10.1002/j.1460-2075.1996.tb00882.x. PMID 8890175.
- "Association of Tat with purified HIV-1 and HIV-2 transcription preinitiation complexes". J. Biol. Chem. 272 (11): 6951–8. 1997. doi:10.1074/jbc.272.11.6951. PMID 9054383.
- "EWS, but not EWS-FLI-1, is associated with both TFIID and RNA polymerase II: interactions between two members of the TET family, EWS and hTAFII68, and subunits of TFIID and RNA polymerase II complexes". Mol. Cell. Biol. 18 (3): 1489–97. 1998. doi:10.1128/mcb.18.3.1489. PMID 9488465.
- "The transcriptional repressor ZFM1 interacts with and modulates the ability of EWS to activate transcription". J. Biol. Chem. 273 (29): 18086–91. 1998. doi:10.1074/jbc.273.29.18086. PMID 9660765.
- "Recurrent rearrangement of the Ewing's sarcoma gene, EWSR1, or its homologue, TAF15, with the transcription factor CIZ/NMP4 in acute leukemia". Cancer Res. 62 (19): 5408–12. 2002. PMID 12359745.
- "Structure-function analysis of the estrogen receptor alpha corepressor scaffold attachment factor-B1: identification of a potent transcriptional repression domain". J. Biol. Chem. 279 (25): 26074–81. 2004. doi:10.1074/jbc.M313726200. PMID 15066997.
- "Stimulation of hTAFII68 (NTD)-mediated transactivation by v-Src". FEBS Lett. 564 (1–2): 188–98. 2004. doi:10.1016/S0014-5793(04)00314-X. PMID 15094065.
- "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization". Curr. Biol. 14 (16): 1436–50. 2004. doi:10.1016/j.cub.2004.07.051. PMID 15324660.
External links
- Overview of all the structural information available in the PDB for UniProt: Q92804 (TATA-binding protein-associated factor 2N) at the PDBe-KB.
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