TAF6

Protein-coding gene in the species Homo sapiens
TAF6
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

5FUR

Identifiers
AliasesTAF6, MGC:8964, TAF(II)70, TAF(II)80, TAF2E, TAFII-70, TAFII-80, TAFII70, TAFII80, TAFII85, TATA-box binding protein associated factor 6, ALYUS
External IDsOMIM: 602955; MGI: 109129; HomoloGene: 7561; GeneCards: TAF6; OMA:TAF6 - orthologs
Gene location (Human)
Chromosome 7 (human)
Chr.Chromosome 7 (human)[1]
Chromosome 7 (human)
Genomic location for TAF6
Genomic location for TAF6
Band7q22.1Start100,106,876 bp[1]
End100,119,841 bp[1]
Gene location (Mouse)
Chromosome 5 (mouse)
Chr.Chromosome 5 (mouse)[2]
Chromosome 5 (mouse)
Genomic location for TAF6
Genomic location for TAF6
Band5|5 G2Start138,176,879 bp[2]
End138,185,713 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • stromal cell of endometrium

  • right hemisphere of cerebellum

  • right frontal lobe

  • body of uterus

  • pituitary gland

  • anterior pituitary

  • canal of the cervix

  • right ovary

  • cingulate gyrus

  • anterior cingulate cortex
Top expressed in
  • genital tubercle

  • tail of embryo

  • ventricular zone

  • yolk sac

  • muscle of thigh

  • neural layer of retina

  • right kidney

  • neural tube

  • internal carotid artery

  • spermatid
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • DNA-binding transcription factor activity
  • DNA binding
  • protein binding
  • protein heterodimerization activity
  • aryl hydrocarbon receptor binding
Cellular component
  • MLL1 complex
  • transcription factor TFTC complex
  • cytosol
  • nucleus
  • nucleoplasm
  • SAGA complex
  • transcription factor TFIID complex
  • SLIK (SAGA-like) complex
  • protein-containing complex
Biological process
  • negative regulation of cell cycle
  • transcription initiation from RNA polymerase II promoter
  • transcription by RNA polymerase II
  • regulation of DNA-binding transcription factor activity
  • transcription, DNA-templated
  • DNA-templated transcription, initiation
  • negative regulation of cell population proliferation
  • regulation of transcription, DNA-templated
  • snRNA transcription by RNA polymerase II
  • regulation of signal transduction by p53 class mediator
  • chromatin organization
  • RNA polymerase II preinitiation complex assembly
  • regulation of transcription by RNA polymerase II
  • apoptotic process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

6878

21343

Ensembl

ENSG00000106290

ENSMUSG00000036980

UniProt

P49848

Q62311

RefSeq (mRNA)
NM_001190415
NM_005641
NM_139122
NM_139123
NM_139315

NM_001364998
NM_001364999
NM_001365000
NM_001365001
NM_001365002
NM_001365003
NM_001365004

NM_009315
NM_001356600
NM_001356601
NM_001356602

RefSeq (protein)
NP_001177344
NP_005632
NP_647476
NP_001351927
NP_001351928

NP_001351929
NP_001351930
NP_001351931
NP_001351932
NP_001351933

NP_033341
NP_001343529
NP_001343530
NP_001343531

Location (UCSC)Chr 7: 100.11 – 100.12 MbChr 5: 138.18 – 138.19 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Transcription initiation factor TFIID subunit 6 is a protein that in humans is encoded by the TAF6 gene.[5]

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 one of the smaller subunits of TFIID that binds weakly to TBP but strongly to TAF1, the largest subunit of TFIID. Four isoforms have been identified but complete transcripts have been determined for only three isoforms. One of the isoforms has been shown to preclude binding of one of the other TFIID subunits, thereby reducing transcription and initiating signals that trigger apoptosis.[6]

Interactions

TAF6 has been shown to interact with:

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000106290 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000036980 – 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. ^ Mathé G, Schwarzenberg L, Halle-Pannenko O, Simmler MC (January 1977). "Discussion paper: experimental and clinical immunopharmacology data applicable to cancer immunotherapy". Ann N Y Acad Sci. 277: 467–84. doi:10.1111/j.1749-6632.1976.tb41721.x. PMID 826207. S2CID 33523496.
  6. ^ "Entrez Gene: TAF6 TAF6 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 80kDa".
  7. ^ 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.
  8. ^ 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. ^ Pointud JC, Mengus G, Brancorsini S, Monaco L, Parvinen M, Sassone-Corsi P, Davidson I (May 2003). "The intracellular localisation of TAF7L, a paralogue of transcription factor TFIID subunit TAF7, is developmentally regulated during male germ-cell differentiation". J. Cell Sci. 116 (Pt 9): 1847–58. doi:10.1242/jcs.00391. PMID 12665565. S2CID 24519687.
  10. ^ 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.
  11. ^ 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

  • Klemm RD, Goodrich JA, Zhou S, Tjian R (1995). "Molecular cloning and expression of the 32-kDa subunit of human TFIID reveals interactions with VP16 and TFIIB that mediate transcriptional activation". Proc. Natl. Acad. Sci. U.S.A. 92 (13): 5788–92. Bibcode:1995PNAS...92.5788K. doi:10.1073/pnas.92.13.5788. PMC 41586. PMID 7597030.
  • Chen HI, Sudol M (1995). "The WW domain of Yes-associated protein binds a proline-rich ligand that differs from the consensus established for Src homology 3-binding modules". Proc. Natl. Acad. Sci. U.S.A. 92 (17): 7819–23. Bibcode:1995PNAS...92.7819C. doi:10.1073/pnas.92.17.7819. PMC 41237. PMID 7644498.
  • Hisatake K, Ohta T, Takada R, Guermah M, Horikoshi M, Nakatani Y, Roeder RG (1995). "Evolutionary conservation of human TATA-binding-polypeptide-associated factors TAFII31 and TAFII80 and interactions of TAFII80 with other TAFs and with general transcription factors". Proc. Natl. Acad. Sci. U.S.A. 92 (18): 8195–9. Bibcode:1995PNAS...92.8195H. doi:10.1073/pnas.92.18.8195. PMC 41123. PMID 7667268.
  • Zhou Q, Sharp PA (1995). "Novel mechanism and factor for regulation by HIV-1 Tat". EMBO J. 14 (2): 321–8. doi:10.1002/j.1460-2075.1995.tb07006.x. 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. doi:10.1128/JVI.68.11.7188-7199.1994. 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. Bibcode:1994Natur.367..295K. doi:10.1038/367295a0. PMID 8121496. S2CID 4362048.
  • 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. doi:10.1128/JVI.70.8.5025-5034.1996. 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. doi:10.1128/JVI.70.8.5503-5510.1996. 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. Bibcode:1996Sci...274..605Z. doi:10.1126/science.274.5287.605. PMID 8849451. S2CID 13266489.
  • Tao Y, Guermah M, Martinez E, Oelgeschläger T, Hasegawa S, Takada R, Yamamoto T, Horikoshi M, Roeder RG (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.
  • 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.
  • Mahanta SK, Scholl T, Yang FC, Strominger JL (1997). "Transactivation by CIITA, the type II bare lymphocyte syndrome-associated factor, requires participation of multiple regions of the TATA box binding protein". Proc. Natl. Acad. Sci. U.S.A. 94 (12): 6324–9. Bibcode:1997PNAS...94.6324M. doi:10.1073/pnas.94.12.6324. PMC 21048. PMID 9177216.
  • Guermah M, Malik S, Roeder RG (1998). "Involvement of TFIID and USA components in transcriptional activation of the human immunodeficiency virus promoter by NF-kappaB and Sp1". Mol. Cell. Biol. 18 (6): 3234–44. doi:10.1128/mcb.18.6.3234. PMC 108905. PMID 9584164.
  • Brand M, Moggs JG, Oulad-Abdelghani M, Lejeune F, Dilworth FJ, Stevenin J, Almouzni G, Tora L (2001). "UV-damaged DNA-binding protein in the TFTC complex links DNA damage recognition to nucleosome acetylation". EMBO J. 20 (12): 3187–96. doi:10.1093/emboj/20.12.3187. PMC 150203. PMID 11406595.
  • Martinez E, Palhan VB, Tjernberg A, Lymar ES, Gamper AM, Kundu TK, Chait BT, Roeder RG (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.
  • Bell B, Scheer E, Tora L (2001). "Identification of hTAF(II)80 delta links apoptotic signaling pathways to transcription factor TFIID function". Mol. Cell. 8 (3): 591–600. doi:10.1016/S1097-2765(01)00325-2. PMID 11583621.

External links

  • Overview of all the structural information available in the PDB for UniProt: P49848 (Transcription initiation factor TFIID subunit 6) at the PDBe-KB.
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