TAF15

TAF15 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 68kDa
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 2MMY​
Identifiers
Symbols	TAF15 ; Npl3; RBP56; TAF2N; TAFII68
External IDs	OMIM: 601574 MGI: 1917689 HomoloGene: 131088 GeneCards: TAF15 Gene
Gene ontology Molecular function • nucleotide binding • DNA binding • protein binding • zinc ion binding • poly(A) RNA binding Cellular component • nucleus • nucleoplasm • nucleolus • cytoplasm Biological process • positive regulation of transcription, DNA-templated Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	8148	70439
Ensembl	ENSG00000270647	ENSMUSG00000020680
UniProt	Q92804	E9Q6D4
RefSeq (mRNA)	NM_003487	NM_027427
RefSeq (protein)	NP_003478	NP_081703
Location (UCSC)	Chr 17: 35.71 – 35.86 Mb	Chr 11: 83.47 – 83.51 Mb
PubMed search

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

1. Morohoshi F, Arai K, Takahashi EI, Tanigami A, Ohki M (Mar 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. Check date values in: |year= / |date= mismatch (help)
2. Morohoshi F, Ootsuka Y, Arai K, Ichikawa H, Mitani S, Munakata N, Ohki M (Dec 1998). "Genomic structure of the human RBP56/hTAFII68 and FUS/TLS genes". Gene 221 (2): 191–8. doi:10.1016/S0378-1119(98)00463-6. PMID 9795213.
3. "Entrez Gene: TAF15 TAF15 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 68kDa".
4. Bertolotti A, Melot T, Acker J, Vigneron M, Delattre O, Tora L (Mar 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. PMC 108863. PMID 9488465.
5. Townson SM, Kang K, Lee AV, Oesterreich S (Jun 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.
6. Hoffmann A, Roeder RG (Jul 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. doi:10.1074/jbc.271.30.18194. PMID 8663456.

Further reading

• Zhou Q, Sharp PA (1995). "Novel mechanism and factor for regulation by HIV-1 Tat". EMBO J. 14 (2): 321–8. PMC 398086. 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. doi:10.1074/jbc.270.5.2274. 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. PMC 237158. PMID 7933101.
• Kashanchi F, Piras G, Radonovich MF, Duvall JF, Fattaey A, Chiang CM, Roeder RG, Brady JN (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. doi:10.1074/jbc.271.30.18194. PMID 8663456.
• Wang Z, Morris GF, Rice AP, Xiong W, Morris CB (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. doi:10.1097/00042560-199606010-00005. 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. PMC 190456. PMID 8764009.
• Kashanchi F, Khleif SN, Duvall JF, Sadaie MR, Radonovich MF, Cho M, Martin MA, Chen SY, Weinmann R, Brady JN (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. PMC 190508. PMID 8764062.
• Zhou Q, Sharp PA (1996). "Tat-SF1: cofactor for stimulation of transcriptional elongation by HIV-1 Tat". Science 274 (5287): 605–10. doi:10.1126/science.274.5287.605. PMID 8849451.
• Bertolotti A, Lutz Y, Heard DJ, Chambon P, Tora L (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. PMC 452240. PMID 8890175.
• 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. doi:10.1074/jbc.272.11.6951. PMID 9054383.
• Bertolotti A, Melot T, Acker J, Vigneron M, Delattre O, Tora L (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. PMC 108863. 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. doi:10.1074/jbc.273.29.18086. PMID 9660765.
• Martini A, La Starza R, Janssen H, Bilhou-Nabera C, Corveleyn A, Somers R, Aventin A, Foà R, Hagemeijer A, Mecucci C, Marynen P (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.
• 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, Wells CD, Fawcett JP, Kulkarni S, Metalnikov P, O'Donnell P, Taylor P, Taylor L, Zougman A, Woodgett JR, Langeberg LK, Scott JD, Pawson T (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.