TAF15

TATA-binding protein-associated factor 2N is a protein that in humans is encoded by the TAF15 gene.[5][6][7]

TAF15
Available structures
PDBHuman UniProt search: PDBe RCSB
Identifiers
AliasesTAF15, Npl3, RBP56, TAF2N, TAFII68, TATA-box binding protein associated factor 15
External IDsOMIM: 601574 MGI: 1917689 HomoloGene: 131088 GeneCards: TAF15
Gene location (Human)
Chr.Chromosome 17 (human)[1]
Band17q12Start35,713,791 bp[1]
End35,864,615 bp[1]
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

8148

70439

Ensembl

ENSG00000270647
ENSG00000276833

ENSMUSG00000020680

UniProt

Q92804

n/a

RefSeq (mRNA)

NM_003487
NM_139215

NM_027427

RefSeq (protein)

NP_003478
NP_631961

n/a

Location (UCSC)Chr 17: 35.71 – 35.86 MbChr 11: 83.47 – 83.51 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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.[7]

Interactions

TAF15 has been shown to interact with:

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References

  1. ENSG00000276833 GRCh38: Ensembl release 89: ENSG00000270647, ENSG00000276833 - Ensembl, May 2017
  2. GRCm38: Ensembl release 89: ENSMUSG00000020680 - 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. Morohoshi F, Arai K, Takahashi EI, Tanigami A, Ohki M (November 15, 1996). "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.
  6. 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.
  7. "Entrez Gene: TAF15 TAF15 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 68kDa".
  8. 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. doi:10.1128/mcb.18.3.1489. PMC 108863. PMID 9488465.
  9. 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.
  10. 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

  • 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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