TAF15

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TAF15 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 68kDa
Identifiers
Symbols TAF15 ; Npl3; RBP56; TAF2N; TAFII68; hTAFII68
External IDs Template:OMIM5 Template:MGI HomoloGene69430
RNA expression pattern
File:PBB GE TAF15 202840 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

TAF15 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 68kDa, also known as TAF15, is a human gene.[1]

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.[1]

References

  1. 1.0 1.1 "Entrez Gene: TAF15 TAF15 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 68kDa".

Further reading

  • Zhou Q, Sharp PA (1995). "Novel mechanism and factor for regulation by HIV-1 Tat". EMBO J. 14 (2): 321–8. PMID 7835343.
  • Parada CA, Yoon JB, Roeder RG (1995). "A novel LBP-1-mediated restriction of HIV-1 transcription at the level of elongation in vitro". J. Biol. Chem. 270 (5): 2274–83. PMID 7836461.
  • Ou SH, Garcia-Martínez LF, Paulssen EJ, Gaynor RB (1994). "Role of flanking E box motifs in human immunodeficiency virus type 1 TATA element function". J. Virol. 68 (11): 7188–99. PMID 7933101.
  • Kashanchi F, Piras G, Radonovich MF; et al. (1994). "Direct interaction of human TFIID with the HIV-1 transactivator tat". Nature. 367 (6460): 295–9. doi:10.1038/367295a0. PMID 8121496.
  • Hoffmann A, Roeder RG (1996). "Cloning and characterization of human TAF20/15. Multiple interactions suggest a central role in TFIID complex formation". J. Biol. Chem. 271 (30): 18194–202. PMID 8663456.
  • Wang Z, Morris GF, Rice AP; et al. (1996). "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. PMID 8680883.
  • Pendergrast PS, Morrison D, Tansey WP, Hernandez N (1996). "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. PMID 8764009.
  • Kashanchi F, Khleif SN, Duvall JF; et al. (1996). "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. PMID 8764062.
  • Zhou Q, Sharp PA (1996). "Tat-SF1: cofactor for stimulation of transcriptional elongation by HIV-1 Tat". Science. 274 (5287): 605–10. PMID 8849451.
  • Bertolotti A, Lutz Y, Heard DJ; et al. (1996). "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. PMID 8890175.
  • Morohoshi F, Arai K, Takahashi EI; et al. (1997). "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. doi:10.1006/geno.1996.0591. PMID 8954779.
  • García-Martínez LF, Ivanov D, Gaynor RB (1997). "Association of Tat with purified HIV-1 and HIV-2 transcription preinitiation complexes". J. Biol. Chem. 272 (11): 6951–8. PMID 9054383.
  • Bertolotti A, Melot T, Acker J; et al. (1998). "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. PMID 9488465.
  • Zhang D, Paley AJ, Childs G (1998). "The transcriptional repressor ZFM1 interacts with and modulates the ability of EWS to activate transcription". J. Biol. Chem. 273 (29): 18086–91. PMID 9660765.
  • Morohoshi F, Ootsuka Y, Arai K; et al. (1998). "Genomic structure of the human RBP56/hTAFII68 and FUS/TLS genes". Gene. 221 (2): 191–8. PMID 9795213.
  • Martini A, La Starza R, Janssen H; et al. (2002). "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. PMID 12359745.
  • 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.
  • Townson SM, Kang K, Lee AV, Oesterreich S (2004). "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. doi:10.1074/jbc.M313726200. PMID 15066997.
  • Lee HJ, Kim S, Pelletier J, Kim J (2004). "Stimulation of hTAFII68 (NTD)-mediated transactivation by v-Src". FEBS Lett. 564 (1–2): 188–98. doi:10.1016/S0014-5793(04)00314-X. PMID 15094065.
  • Jin J, Smith FD, Stark C; et al. (2004). "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. doi:10.1016/j.cub.2004.07.051. PMID 15324660.

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