TAF6: Difference between revisions

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{{Infobox_gene}}
{{PBB_Controls
'''Transcription initiation factor TFIID subunit 6''' is a [[protein]] that in humans is encoded by the ''TAF6'' [[gene]].<ref name="pmid826207">{{cite journal | vauthors = Mathé G, Schwarzenberg L, Halle-Pannenko O, Simmler MC | title = Discussion paper: experimental and clinical immunopharmacology data applicable to cancer immunotherapy | journal = Ann N Y Acad Sci | volume = 277 | issue = 00 | pages = 467–84 | date = January 1977 | pmid = 826207 | pmc = | doi = 10.1111/j.1749-6632.1976.tb41721.x }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = TAF6 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 80kDa
| HGNCid = 11540
| Symbol = TAF6
| AltSymbols =; DKFZp781E21155; MGC:8964; TAF2E; TAFII70; TAFII80; TAFII85
| OMIM = 602955
| ECnumber = 
| Homologene = 7561
| MGIid = 109129
| GeneAtlas_image1 = PBB_GE_TAF6_203572_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003702 |text = RNA polymerase II transcription factor activity}} {{GNF_GO|id=GO:0004571 |text = mannosyl-oligosaccharide 1,2-alpha-mannosidase activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016251 |text = general RNA polymerase II transcription factor activity}} {{GNF_GO|id=GO:0016986 |text = transcription initiation factor activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005669 |text = transcription factor TFIID complex}} {{GNF_GO|id=GO:0005673 |text = transcription factor TFIIE complex}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006352 |text = transcription initiation}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0051090 |text = regulation of transcription factor activity}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 6878
    | Hs_Ensembl = ENSG00000106290
    | Hs_RefseqProtein = NP_005632
    | Hs_RefseqmRNA = NM_005641
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 7
    | Hs_GenLoc_start = 99542630
    | Hs_GenLoc_end = 99554915
    | Hs_Uniprot = P49848
    | Mm_EntrezGene = 21343
    | Mm_Ensembl = ENSMUSG00000036980
    | Mm_RefseqmRNA = NM_009315
    | Mm_RefseqProtein = NP_033341
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 5
    | Mm_GenLoc_start = 138408405
    | Mm_GenLoc_end = 138416974
    | Mm_Uniprot = Q62311
  }}
}}
'''TAF6 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 80kDa''', also known as '''TAF6''', is a human [[gene]].


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
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.<ref name="entrez">{{cite web | title = Entrez Gene: TAF6 TAF6 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 80kDa| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6878| accessdate = }}</ref>
{{PBB_Summary
| section_title =
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: TAF6 TAF6 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 80kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6878| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}


==Further reading==
TAF6 has been shown to [[Protein-protein interaction|interact]] with:
* [[TAF5]]<ref name = pmid10523658>{{cite journal | vauthors = Hsieh YJ, Kundu TK, Wang Z, Kovelman R, Roeder RG | title = The TFIIIC90 subunit of TFIIIC interacts with multiple components of the RNA polymerase III machinery and contains a histone-specific acetyltransferase activity | journal = Mol. Cell. Biol. | volume = 19 | issue = 11 | pages = 7697–704 | date = November 1999 | pmid = 10523658 | pmc = 84812 | doi =  10.1128/mcb.19.11.7697}}</ref><ref name = pmid9045704>{{cite journal | vauthors = Tao Y, Guermah M, Martinez E, Oelgeschläger T, Hasegawa S, Takada R, Yamamoto T, Horikoshi M, Roeder RG | title = Specific interactions and potential functions of human TAFII100 | journal = J. Biol. Chem. | volume = 272 | issue = 10 | pages = 6714–21 | date = March 1997 | pmid = 9045704 | doi =  10.1074/jbc.272.10.6714}}</ref>  and
* [[TATA binding protein]].<ref name = pmid12665565>{{cite journal | vauthors = Pointud JC, Mengus G, Brancorsini S, Monaco L, Parvinen M, Sassone-Corsi P, Davidson I | title = The intracellular localisation of TAF7L, a paralogue of transcription factor TFIID subunit TAF7, is developmentally regulated during male germ-cell differentiation | journal = J. Cell Sci. | volume = 116 | issue = Pt 9 | pages = 1847–58 | date = May 2003 | pmid = 12665565 | doi =  10.1242/jcs.00391}}</ref><ref name = pmid9153318>{{cite journal | vauthors = Bellorini M, Lee DK, Dantonel JC, Zemzoumi K, Roeder RG, Tora L, Mantovani R | title = 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 | journal = Nucleic Acids Res. | volume = 25 | issue = 11 | pages = 2174–81 | date = June 1997 | pmid = 9153318 | pmc = 146709 | doi =  10.1093/nar/25.11.2174}}</ref><ref name = pmid7680771>{{cite journal | vauthors = Ruppert S, Wang EH, Tjian R | title = Cloning and expression of human TAFII250: a TBP-associated factor implicated in cell-cycle regulation | journal = Nature | volume = 362 | issue = 6416 | pages = 175–9 | date = March 1993 | pmid = 7680771 | doi = 10.1038/362175a0 }}</ref>
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Klemm RD, Goodrich JA, Zhou S, Tjian R | title = Molecular cloning and expression of the 32-kDa subunit of human TFIID reveals interactions with VP16 and TFIIB that mediate transcriptional activation. | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 92 | issue = 13 | pages = 5788–92 | year = 1995 | pmid = 7597030 | pmc = 41586 | doi = 10.1073/pnas.92.13.5788 }}
| citations =
* {{cite journal | vauthors = Chen HI, Sudol M | title = The WW domain of Yes-associated protein binds a proline-rich ligand that differs from the consensus established for Src homology 3-binding modules. | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 92 | issue = 17 | pages = 7819–23 | year = 1995 | pmid = 7644498 | pmc = 41237 | doi = 10.1073/pnas.92.17.7819 }}
*{{cite journal | author=Klemm RD, Goodrich JA, Zhou S, Tjian R |title=Molecular cloning and expression of the 32-kDa subunit of human TFIID reveals interactions with VP16 and TFIIB that mediate transcriptional activation. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 13 |pages= 5788-92 |year= 1995 |pmid= 7597030 |doi= }}
* {{cite journal | vauthors = Hisatake K, Ohta T, Takada R, Guermah M, Horikoshi M, Nakatani Y, Roeder RG | title = Evolutionary conservation of human TATA-binding-polypeptide-associated factors TAFII31 and TAFII80 and interactions of TAFII80 with other TAFs and with general transcription factors. | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 92 | issue = 18 | pages = 8195–9 | year = 1995 | pmid = 7667268 | pmc = 41123 | doi = 10.1073/pnas.92.18.8195 }}
*{{cite journal | author=Chen HI, Sudol M |title=The WW domain of Yes-associated protein binds a proline-rich ligand that differs from the consensus established for Src homology 3-binding modules. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 17 |pages= 7819-23 |year= 1995 |pmid= 7644498 |doi= }}
* {{cite journal | vauthors = Zhou Q, Sharp PA | title = Novel mechanism and factor for regulation by HIV-1 Tat. | journal = EMBO J. | volume = 14 | issue = 2 | pages = 321–8 | year = 1995 | pmid = 7835343 | pmc = 398086 | doi =  }}
*{{cite journal | author=Hisatake K, Ohta T, Takada R, ''et al.'' |title=Evolutionary conservation of human TATA-binding-polypeptide-associated factors TAFII31 and TAFII80 and interactions of TAFII80 with other TAFs and with general transcription factors. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 18 |pages= 8195-9 |year= 1995 |pmid= 7667268 |doi= }}
* {{cite journal | vauthors = Parada CA, Yoon JB, Roeder RG | title = A novel LBP-1-mediated restriction of HIV-1 transcription at the level of elongation in vitro. | journal = J. Biol. Chem. | volume = 270 | issue = 5 | pages = 2274–83 | year = 1995 | pmid = 7836461 | doi = 10.1074/jbc.270.5.2274 }}
*{{cite journal | author=Zhou Q, Sharp PA |title=Novel mechanism and factor for regulation by HIV-1 Tat. |journal=EMBO J. |volume=14 |issue= 2 |pages= 321-8 |year= 1995 |pmid= 7835343 |doi=  }}
* {{cite journal | vauthors = Ou SH, Garcia-Martínez LF, Paulssen EJ, Gaynor RB | title = Role of flanking E box motifs in human immunodeficiency virus type 1 TATA element function. | journal = J. Virol. | volume = 68 | issue = 11 | pages = 7188–99 | year = 1994 | pmid = 7933101 | pmc = 237158 | doi =  }}
*{{cite journal | author=Parada CA, Yoon JB, Roeder RG |title=A novel LBP-1-mediated restriction of HIV-1 transcription at the level of elongation in vitro. |journal=J. Biol. Chem. |volume=270 |issue= 5 |pages= 2274-83 |year= 1995 |pmid= 7836461 |doi= }}
* {{cite journal | vauthors = Kashanchi F, Piras G, Radonovich MF, Duvall JF, Fattaey A, Chiang CM, Roeder RG, Brady JN | title = Direct interaction of human TFIID with the HIV-1 transactivator tat. | journal = Nature | volume = 367 | issue = 6460 | pages = 295–9 | year = 1994 | pmid = 8121496 | doi = 10.1038/367295a0 }}
*{{cite journal | author=Ou SH, Garcia-Martínez LF, Paulssen EJ, Gaynor RB |title=Role of flanking E box motifs in human immunodeficiency virus type 1 TATA element function. |journal=J. Virol. |volume=68 |issue= 11 |pages= 7188-99 |year= 1994 |pmid= 7933101 |doi=  }}
* {{cite journal | vauthors = Wang Z, Morris GF, Rice AP, Xiong W, Morris CB | title = Wild-type and transactivation-defective mutants of human immunodeficiency virus type 1 Tat protein bind human TATA-binding protein in vitro. | journal = J. Acquir. Immune Defic. Syndr. Hum. Retrovirol. | volume = 12 | issue = 2 | pages = 128–38 | year = 1996 | pmid = 8680883 | doi = 10.1097/00042560-199606010-00005 }}
*{{cite journal | author=Kashanchi F, Piras G, Radonovich MF, ''et al.'' |title=Direct interaction of human TFIID with the HIV-1 transactivator tat. |journal=Nature |volume=367 |issue= 6460 |pages= 295-9 |year= 1994 |pmid= 8121496 |doi= 10.1038/367295a0 }}
* {{cite journal | vauthors = Pendergrast PS, Morrison D, Tansey WP, Hernandez N | title = Mutations in the carboxy-terminal domain of TBP affect the synthesis of human immunodeficiency virus type 1 full-length and short transcripts similarly. | journal = J. Virol. | volume = 70 | issue = 8 | pages = 5025–34 | year = 1996 | pmid = 8764009 | pmc = 190456 | doi =  }}
*{{cite journal | author=Weinzierl RO, Ruppert S, Dynlacht BD, ''et al.'' |title=Cloning and expression of Drosophila TAFII60 and human TAFII70 reveal conserved interactions with other subunits of TFIID. |journal=EMBO J. |volume=12 |issue= 13 |pages= 5303-9 |year= 1994 |pmid= 8262073 |doi= }}
* {{cite journal | vauthors = Kashanchi F, Khleif SN, Duvall JF, Sadaie MR, Radonovich MF, Cho M, Martin MA, Chen SY, Weinmann R, Brady JN | title = Interaction of human immunodeficiency virus type 1 Tat with a unique site of TFIID inhibits negative cofactor Dr1 and stabilizes the TFIID-TFIIA complex. | journal = J. Virol. | volume = 70 | issue = 8 | pages = 5503–10 | year = 1996 | pmid = 8764062 | pmc = 190508 | doi =  }}
*{{cite journal | author=Wang Z, Morris GF, Rice AP, ''et al.'' |title=Wild-type and transactivation-defective mutants of human immunodeficiency virus type 1 Tat protein bind human TATA-binding protein in vitro. |journal=J. Acquir. Immune Defic. Syndr. Hum. Retrovirol. |volume=12 |issue= 2 |pages= 128-38 |year= 1996 |pmid= 8680883 |doi=  }}
* {{cite journal | vauthors = Zhou Q, Sharp PA | title = Tat-SF1: cofactor for stimulation of transcriptional elongation by HIV-1 Tat. | journal = Science | volume = 274 | issue = 5287 | pages = 605–10 | year = 1996 | pmid = 8849451 | doi = 10.1126/science.274.5287.605 }}
*{{cite journal | author=Pendergrast PS, Morrison D, Tansey WP, Hernandez N |title=Mutations in the carboxy-terminal domain of TBP affect the synthesis of human immunodeficiency virus type 1 full-length and short transcripts similarly. |journal=J. Virol. |volume=70 |issue= 8 |pages= 5025-34 |year= 1996 |pmid= 8764009 |doi=  }}
* {{cite journal | vauthors = Tao Y, Guermah M, Martinez E, Oelgeschläger T, Hasegawa S, Takada R, Yamamoto T, Horikoshi M, Roeder RG | title = Specific interactions and potential functions of human TAFII100. | journal = J. Biol. Chem. | volume = 272 | issue = 10 | pages = 6714–21 | year = 1997 | pmid = 9045704 | doi = 10.1074/jbc.272.10.6714 }}
*{{cite journal | author=Kashanchi F, Khleif SN, Duvall JF, ''et al.'' |title=Interaction of human immunodeficiency virus type 1 Tat with a unique site of TFIID inhibits negative cofactor Dr1 and stabilizes the TFIID-TFIIA complex. |journal=J. Virol. |volume=70 |issue= 8 |pages= 5503-10 |year= 1996 |pmid= 8764062 |doi= }}
* {{cite journal | vauthors = García-Martínez LF, Ivanov D, Gaynor RB | title = Association of Tat with purified HIV-1 and HIV-2 transcription preinitiation complexes. | journal = J. Biol. Chem. | volume = 272 | issue = 11 | pages = 6951–8 | year = 1997 | pmid = 9054383 | doi = 10.1074/jbc.272.11.6951 }}
*{{cite journal | author=Zhou Q, Sharp PA |title=Tat-SF1: cofactor for stimulation of transcriptional elongation by HIV-1 Tat. |journal=Science |volume=274 |issue= 5287 |pages= 605-10 |year= 1996 |pmid= 8849451 |doi= }}
* {{cite journal | vauthors = Mahanta SK, Scholl T, Yang FC, Strominger JL | title = Transactivation by CIITA, the type II bare lymphocyte syndrome-associated factor, requires participation of multiple regions of the TATA box binding protein. | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 94 | issue = 12 | pages = 6324–9 | year = 1997 | pmid = 9177216 | pmc = 21048 | doi = 10.1073/pnas.94.12.6324 }}
*{{cite journal | author=Tao Y, Guermah M, Martinez E, ''et al.'' |title=Specific interactions and potential functions of human TAFII100. |journal=J. Biol. Chem. |volume=272 |issue= 10 |pages= 6714-21 |year= 1997 |pmid= 9045704 |doi= }}
* {{cite journal | vauthors = Guermah M, Malik S, Roeder RG | title = Involvement of TFIID and USA components in transcriptional activation of the human immunodeficiency virus promoter by NF-kappaB and Sp1. | journal = Mol. Cell. Biol. | volume = 18 | issue = 6 | pages = 3234–44 | year = 1998 | pmid = 9584164 | pmc = 108905 | doi =  10.1128/mcb.18.6.3234}}
*{{cite journal | author=García-Martínez LF, Ivanov D, Gaynor RB |title=Association of Tat with purified HIV-1 and HIV-2 transcription preinitiation complexes. |journal=J. Biol. Chem. |volume=272 |issue= 11 |pages= 6951-8 |year= 1997 |pmid= 9054383 |doi= }}
* {{cite journal | vauthors = Brand M, Moggs JG, Oulad-Abdelghani M, Lejeune F, Dilworth FJ, Stevenin J, Almouzni G, Tora L | title = UV-damaged DNA-binding protein in the TFTC complex links DNA damage recognition to nucleosome acetylation. | journal = EMBO J. | volume = 20 | issue = 12 | pages = 3187–96 | year = 2001 | pmid = 11406595 | pmc = 150203 | doi = 10.1093/emboj/20.12.3187 }}
*{{cite journal | author=Mahanta SK, Scholl T, Yang FC, Strominger JL |title=Transactivation by CIITA, the type II bare lymphocyte syndrome-associated factor, requires participation of multiple regions of the TATA box binding protein. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 12 |pages= 6324-9 |year= 1997 |pmid= 9177216 |doi=  }}
* {{cite journal | vauthors = Martinez E, Palhan VB, Tjernberg A, Lymar ES, Gamper AM, Kundu TK, Chait BT, Roeder RG | title = Human STAGA complex is a chromatin-acetylating transcription coactivator that interacts with pre-mRNA splicing and DNA damage-binding factors in vivo. | journal = Mol. Cell. Biol. | volume = 21 | issue = 20 | pages = 6782–95 | year = 2001 | pmid = 11564863 | pmc = 99856 | doi = 10.1128/MCB.21.20.6782-6795.2001 }}
*{{cite journal | author=Guermah M, Malik S, Roeder RG |title=Involvement of TFIID and USA components in transcriptional activation of the human immunodeficiency virus promoter by NF-kappaB and Sp1. |journal=Mol. Cell. Biol. |volume=18 |issue= 6 |pages= 3234-44 |year= 1998 |pmid= 9584164 |doi= }}
* {{cite journal | vauthors = Bell B, Scheer E, Tora L | title = Identification of hTAF(II)80 delta links apoptotic signaling pathways to transcription factor TFIID function. | journal = Mol. Cell | volume = 8 | issue = 3 | pages = 591–600 | year = 2001 | pmid = 11583621 | doi = 10.1016/S1097-2765(01)00325-2 }}
*{{cite journal  | author=Brand M, Moggs JG, Oulad-Abdelghani M, ''et al.'' |title=UV-damaged DNA-binding protein in the TFTC complex links DNA damage recognition to nucleosome acetylation. |journal=EMBO J. |volume=20 |issue= 12 |pages= 3187-96 |year= 2001 |pmid= 11406595 |doi= 10.1093/emboj/20.12.3187 }}
*{{cite journal | author=Martinez E, Palhan VB, Tjernberg A, ''et al.'' |title=Human STAGA complex is a chromatin-acetylating transcription coactivator that interacts with pre-mRNA splicing and DNA damage-binding factors in vivo. |journal=Mol. Cell. Biol. |volume=21 |issue= 20 |pages= 6782-95 |year= 2001 |pmid= 11564863 |doi= 10.1128/MCB.21.20.6782-6795.2001 }}
*{{cite journal  | author=Bell B, Scheer E, Tora L |title=Identification of hTAF(II)80 delta links apoptotic signaling pathways to transcription factor TFIID function. |journal=Mol. Cell |volume=8 |issue= 3 |pages= 591-600 |year= 2001 |pmid= 11583621 |doi=  }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
 
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Latest revision as of 20:59, 8 November 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

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Ensembl

n/a

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UniProt

n/a

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Transcription initiation factor TFIID subunit 6 is a protein that in humans is encoded by the TAF6 gene.[1]

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.[2]

Interactions

TAF6 has been shown to interact with:

References

  1. ↑ 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 (00): 467–84. doi:10.1111/j.1749-6632.1976.tb41721.x. PMID 826207.
  2. ↑ "Entrez Gene: TAF6 TAF6 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 80kDa".
  3. ↑ 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.
  4. ↑ 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.
  5. ↑ 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.
  6. ↑ 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.
  7. ↑ 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. doi:10.1038/362175a0. PMID 7680771.

Further reading


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