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TAF5

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TAF5
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesTAF5, TAF2D, TAFII100, TAF(II)100, TAFII-100, TATA-box binding protein associated factor 5
External IDsOMIM: 601787; MGI: 2442144; HomoloGene: 5064; GeneCards: TAF5; OMA:TAF5 - orthologs
Orthologs
SpeciesHumanMouse
Entrez

6877

226182

Ensembl

ENSG00000148835

ENSMUSG00000025049

UniProt

Q15542

Q8C092

RefSeq (mRNA)

NM_006951
NM_139052

NM_177342

RefSeq (protein)

NP_008882
NP_620640

NP_796316

Location (UCSC)Chr 10: 103.37 – 103.39 MbChr 19: 47.06 – 47.07 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Transcription initiation factor TFIID subunit 5 is a protein that in humans is encoded by the TAF5 gene.[5][6][7]

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 an integral subunit of TFIID associated with all transcriptionally competent forms of that complex. This subunit interacts strongly with two TFIID subunits that show similarity to histones H3 and H4, and it may participate in forming a nucleosome-like core in the TFIID complex.[7]

Interactions

TAF5 has been shown to interact with:

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000148835 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000025049 – 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. ^ Dubrovskaya V, Mattei MG, Tora L (February 1997). "Localization of the gene (TAF2D) encoding the 100-kDa subunit (hTAFII100) of the human TFIID complex to chromosome 10 band q24-q25.2". Genomics. 36 (3): 556–7. doi:10.1006/geno.1996.0509. PMID 8884287.
  6. ^ Tanese N, Saluja D, Vassallo MF, Chen JL, Admon A (January 1997). "Molecular cloning and analysis of two subunits of the human TFIID complex: hTAFII130 and hTAFII100". Proc Natl Acad Sci U S A. 93 (24): 13611–6. doi:10.1073/pnas.93.24.13611. PMC 19367. PMID 8942982.
  7. ^ a b "Entrez Gene: TAF5 TAF5 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 100kDa".
  8. ^ a b c Tao Y, Guermah M, Martinez E, Oelgeschläger T, Hasegawa S, Takada R, Yamamoto T, Horikoshi M, Roeder RG (March 1997). "Specific interactions and potential functions of human TAFII100". J. Biol. Chem. 272 (10): 6714–21. doi:10.1074/jbc.272.10.6714. PMID 9045704.
  9. ^ Hsieh YJ, Kundu TK, Wang Z, Kovelman R, Roeder RG (November 1999). "The TFIIIC90 subunit of TFIIIC interacts with multiple components of the RNA polymerase III machinery and contains a histone-specific acetyltransferase activity". Mol. Cell. Biol. 19 (11): 7697–704. doi:10.1128/mcb.19.11.7697. PMC 84812. PMID 10523658.
  10. ^ 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.
  11. ^ Bertolotti A, Melot T, Acker J, Vigneron M, Delattre O, Tora L (March 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.
  12. ^ Bellorini M, Lee DK, Dantonel JC, Zemzoumi K, Roeder RG, Tora L, Mantovani R (June 1997). "CCAAT binding NF-Y-TBP interactions: NF-YB and NF-YC require short domains adjacent to their histone fold motifs for association with TBP basic residues". Nucleic Acids Res. 25 (11): 2174–81. doi:10.1093/nar/25.11.2174. PMC 146709. PMID 9153318.
  13. ^ Ruppert S, Wang EH, Tjian R (March 1993). "Cloning and expression of human TAFII250: a TBP-associated factor implicated in cell-cycle regulation". Nature. 362 (6416): 175–9. Bibcode:1993Natur.362..175R. doi:10.1038/362175a0. PMID 7680771. S2CID 4364676.

Further reading

  • Overview of all the structural information available in the PDB for UniProt: Q15542 (Transcription initiation factor TFIID subunit 5) at the PDBe-KB.
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