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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Transcription initiation factor TFIID subunit 11'''  also known as TAFII28, is a [[protein]] that in humans is encoded by the ''TAF11'' [[gene]].<ref name="pmid7729427">{{cite journal | vauthors = Mengus G, May M, Jacq X, Staub A, Tora L, Chambon P, Davidson I | title = Cloning and characterization of hTAFII18, hTAFII20 and hTAFII28: three subunits of the human transcription factor TFIID | journal = EMBO J. | volume = 14 | issue = 7 | pages = 1520–31  | date = May 1995 | pmid = 7729427 | pmc = 398239 | doi =  }}</ref><ref name="pmid8820923">{{cite journal | vauthors = Kuzuhara T, Horikoshi M | title = Isolation and characterization of a cDNA encoding a human TFIID subunit containing a variety of putative structural motifs including direct repeats | journal = Biol. Pharm. Bull. | volume = 19 | issue = 1 | pages = 122–6  | date = November 1996 | pmid = 8820923 | pmc =  | doi = 10.1248/bpb.19.122 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: TAF11 TAF11 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 28kDa| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6882| accessdate = }}</ref>
| update_page = yes
 
| require_manual_inspection = no
== Function ==
| update_protein_box = yes
 
| update_summary = yes
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 small subunit of TFIID that is present in all TFIID complexes and interacts with TBP. This subunit also interacts with another small subunit, TAF13, to form a heterodimer with a structure similar to the histone core structure.<ref name="entrez" />
| update_citations = yes
{{Infobox protein family
| Symbol = TAFII28
| Name = TAFII28
| image = PDB 1bh9 EBI.jpg
| width =
| caption = htafii18/htafii28 heterodimer crystal structure with bound pcmbs
| Pfam = PF04719
| Pfam_clan = CL0012
| InterPro = IPR006809
| SMART =
| PROSITE =
| MEROPS =
| SCOP = 1bh9
| TCDB =  
| OPM family =  
| OPM protein =  
| CAZy =  
| CDD =  
}}
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
In molecular biology, '''TAFII28''' refers to the [[TATA box]] binding protein associated factor. Together with the TATA-binding protein and other TAFs it forms the general [[Transcription (genetics)|transcription]] factor, TFIID. They together participate in the assembly of the [[transcription (biology)|transcription]] preinitiation [[Protein complex|complex]]. The [[conserved sequence|conserved]] region is found at the C terminus of most member [[protein]]s.
{{GNF_Protein_box
 
| image = PBB_Protein_TAF11_image.jpg
== Structure ==
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1bh8.
 
| PDB = {{PDB2|1bh8}}, {{PDB2|1bh9}}
The [[crystal structure]] of hTAFII28 with hTAFII18 shows that this region is involved in the [[Binding (molecular)|binding]] of these two [[protein subunit|subunits]]. The [[Conserved sequence|conserved]] region contains four [[alpha helix|alpha helices]] and three [[loop (biochemistry)|loops]] arranged as in [[histone]] H3.<ref name="pmid7729427" /><ref name="pmid9695952">{{cite journal | vauthors = Birck C, Poch O, Romier C, Ruff M, Mengus G, Lavigne AC, Davidson I, Moras D | title = Human TAF(II)28 and TAF(II)18 interact through a histone fold encoded by atypical evolutionary conserved motifs also found in the SPT3 family | journal = Cell | volume = 94 | issue = 2 | pages = 239–49 | date = July 1998 | pmid = 9695952 | doi = 10.1016/S0092-8674(00)81423-3 }}</ref>
| Name = TAF11 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 28kDa
 
| HGNCid = 11544
== Interactions ==
| Symbol = TAF11
 
| AltSymbols =; MGC:15243; PRO2134; TAF2I; TAFII28
TAF11 has been shown to [[Protein-protein interaction|interact]] with:
| OMIM = 600772
{{div col|colwidth=20em}}
  | ECnumber =
* [[GTF2F1]],<ref name = pmid9159119>{{cite journal | date = May 1997 | vauthors = Scully R, Anderson SF, Chao DM, Wei W, Ye L, Young RA, Livingston DM, Parvin JD | title = BRCA1 is a component of the RNA polymerase II holoenzyme | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 94 | issue = 11 | pages = 5605–10 | pmid = 9159119 | pmc = 20825 | doi = 10.1073/pnas.94.11.5605}}</ref>
| Homologene = 55918
* [[POLR2A]]<ref name = pmid9159119/> and
| MGIid = 1916026
* [[TAF13]],<ref name = pmid7729427 /><ref name = pmid9695952 />
| GeneAtlas_image1 = PBB_GE_TAF11_209358_at_tn.png
* [[TAF15]],<ref name = pmid9488465>{{cite journal | date = March 1998 | vauthors = Bertolotti A, Melot T, Acker J, Vigneron M, Delattre O, Tora L | title = 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 | journal = Mol. Cell. Biol. | volume = 18 | issue = 3 | pages = 1489–97 | pmid = 9488465 | pmc = 108863 | doi = 10.1128/mcb.18.3.1489}}</ref>
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016251 |text = general RNA polymerase II transcription factor activity}}
* [[TATA binding protein]],<ref name = pmid7729427/><ref name = pmid9153318>{{cite journal | date = June 1997 | 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 | pmid = 9153318 | pmc = 146709 | doi = 10.1093/nar/25.11.2174}}</ref><ref name = pmid8670810>{{cite journal | date = June 1996 | vauthors = May M, Mengus G, Lavigne AC, Chambon P, Davidson I | title = Human TAF(II28) promotes transcriptional stimulation by activation function 2 of the retinoid X receptors | journal = EMBO J. | volume = 15 | issue = 12 | pages = 3093–104 | pmid = 8670810 | pmc = 450252 | doi = }}</ref> and
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005669 |text = transcription factor TFIID complex}}  
* [[Transcription Factor II B]].<ref name = pmid9159119/>
| Process = {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}}
{{Div col end}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 6882
    | Hs_Ensembl = ENSG00000064995
    | Hs_RefseqProtein = NP_005634
    | Hs_RefseqmRNA = NM_005643
    | Hs_GenLoc_db =
    | Hs_GenLoc_chr = 6
    | Hs_GenLoc_start = 34953533
    | Hs_GenLoc_end = 34963844
    | Hs_Uniprot = Q15544
    | Mm_EntrezGene = 68776
    | Mm_Ensembl = ENSMUSG00000024218
    | Mm_RefseqmRNA = NM_026836
    | Mm_RefseqProtein = NP_081112
    | Mm_GenLoc_db =
    | Mm_GenLoc_chr = 17
    | Mm_GenLoc_start = 27628717
    | Mm_GenLoc_end = 27635313
    | Mm_Uniprot = Q99JX1
  }}
}}
'''TAF11 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 28kDa''', also known as '''TAF11''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TAF11 TAF11 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 28kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6882| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== References ==
{{PBB_Summary
{{reflist}}
| 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 a small subunit of TFIID that is present in all TFIID complexes and interacts with TBP. This subunit also interacts with another small subunit, TAF13, to form a heterodimer with a structure similar to the histone core structure.<ref name="entrez">{{cite web | title = Entrez Gene: TAF11 TAF11 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 28kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6882| accessdate = }}</ref>
}}


==References==
== Further reading ==
{{reflist|2}}
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{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 =  }}
| citations =
* {{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=Mengus G, May M, Jacq X, ''et al.'' |title=Cloning and characterization of hTAFII18, hTAFII20 and hTAFII28: three subunits of the human transcription factor TFIID. |journal=EMBO J. |volume=14 |issue= 7 |pages= 1520-31 |year= 1995 |pmid= 7729427 |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=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 = 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=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 = May M, Mengus G, Lavigne AC, Chambon P, Davidson I | title = Human TAF(II28) promotes transcriptional stimulation by activation function 2 of the retinoid X receptors | journal = EMBO J. | volume = 15 | issue = 12 | pages = 3093–104 | year = 1996 | pmid = 8670810 | pmc = 450252 | doi = }}
*{{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=May M, Mengus G, Lavigne AC, ''et al.'' |title=Human TAF(II28) promotes transcriptional stimulation by activation function 2 of the retinoid X receptors. |journal=EMBO J. |volume=15 |issue= 12 |pages= 3093-104 |year= 1996 |pmid= 8670810 |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=Kuzuhara T, Horikoshi M |title=Isolation and characterization of a cDNA encoding a human TFIID subunit containing a variety of putative structural motifs including direct repeats. |journal=Biol. Pharm. Bull. |volume=19 |issue= 1 |pages= 122-6 |year= 1996 |pmid= 8820923 |doi= }}
* {{cite journal | vauthors = Scully R, Anderson SF, Chao DM, Wei W, Ye L, Young RA, Livingston DM, Parvin JD | title = BRCA1 is a component of the RNA polymerase II holoenzyme | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 94 | issue = 11 | pages = 5605–10 | year = 1997 | pmid = 9159119 | pmc = 20825 | doi = 10.1073/pnas.94.11.5605 }}
*{{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 = Dantonel JC, Murthy KG, Manley JL, Tora L | title = Transcription factor TFIID recruits factor CPSF for formation of 3' end of mRNA | journal = Nature | volume = 389 | issue = 6649 | pages = 399–402 | year = 1997 | pmid = 9311784 | doi = 10.1038/38763 }}
*{{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 = Bertolotti A, Melot T, Acker J, Vigneron M, Delattre O, Tora L | title = 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 | journal = Mol. Cell. Biol. | volume = 18 | issue = 3 | pages = 1489–97 | year = 1998 | pmid = 9488465 | pmc = 108863 | doi =  10.1128/mcb.18.3.1489}}
*{{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 = 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=Scully R, Anderson SF, Chao DM, ''et al.'' |title=BRCA1 is a component of the RNA polymerase II holoenzyme. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 11 |pages= 5605-10 |year= 1997 |pmid= 9159119 |doi=  }}
* {{cite journal | vauthors = Fraser RA, Heard DJ, Adam S, Lavigne AC, Le Douarin B, Tora L, Losson R, Rochette-Egly C, Chambon P | title = The putative cofactor TIF1alpha is a protein kinase that is hyperphosphorylated upon interaction with liganded nuclear receptors | journal = J. Biol. Chem. | volume = 273 | issue = 26 | pages = 16199–204 | year = 1998 | pmid = 9632676 | doi = 10.1074/jbc.273.26.16199 }}
*{{cite journal | author=Dantonel JC, Murthy KG, Manley JL, Tora L |title=Transcription factor TFIID recruits factor CPSF for formation of 3' end of mRNA. |journal=Nature |volume=389 |issue= 6649 |pages= 399-402 |year= 1997 |pmid= 9311784 |doi= 10.1038/38763 }}
* {{cite journal | vauthors = Birck C, Poch O, Romier C, Ruff M, Mengus G, Lavigne AC, Davidson I, Moras D | title = Human TAF(II)28 and TAF(II)18 interact through a histone fold encoded by atypical evolutionary conserved motifs also found in the SPT3 family | journal = Cell | volume = 94 | issue = 2 | pages = 239–49 | year = 1998 | pmid = 9695952 | doi = 10.1016/S0092-8674(00)81423-3 }}
*{{cite journal | author=Bertolotti A, Melot T, Acker J, ''et al.'' |title=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. |journal=Mol. Cell. Biol. |volume=18 |issue= 3 |pages= 1489-97 |year= 1998 |pmid= 9488465 |doi= }}
*{{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  | author=Fraser RA, Heard DJ, Adam S, ''et al.'' |title=The putative cofactor TIF1alpha is a protein kinase that is hyperphosphorylated upon interaction with liganded nuclear receptors. |journal=J. Biol. Chem. |volume=273 |issue= 26 |pages= 16199-204 |year= 1998 |pmid= 9632676 |doi=  }}
*{{cite journal  | author=Birck C, Poch O, Romier C, ''et al.'' |title=Human TAF(II)28 and TAF(II)18 interact through a histone fold encoded by atypical evolutionary conserved motifs also found in the SPT3 family. |journal=Cell |volume=94 |issue= 2 |pages= 239-49 |year= 1998 |pmid= 9695952 |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}}
{{PDB Gallery|geneid=6882}}
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Latest revision as of 20:45, 17 March 2018

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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n/a

Ensembl

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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 11 also known as TAFII28, is a protein that in humans is encoded by the TAF11 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 small subunit of TFIID that is present in all TFIID complexes and interacts with TBP. This subunit also interacts with another small subunit, TAF13, to form a heterodimer with a structure similar to the histone core structure.[3]

TAFII28
File:PDB 1bh9 EBI.jpg
htafii18/htafii28 heterodimer crystal structure with bound pcmbs
Identifiers
SymbolTAFII28
PfamPF04719
Pfam clanCL0012
InterProIPR006809
SCOP1bh9
SUPERFAMILY1bh9

In molecular biology, TAFII28 refers to the TATA box binding protein associated factor. Together with the TATA-binding protein and other TAFs it forms the general transcription factor, TFIID. They together participate in the assembly of the transcription preinitiation complex. The conserved region is found at the C terminus of most member proteins.

Structure

The crystal structure of hTAFII28 with hTAFII18 shows that this region is involved in the binding of these two subunits. The conserved region contains four alpha helices and three loops arranged as in histone H3.[1][4]

Interactions

TAF11 has been shown to interact with:

References

  1. ↑ 1.0 1.1 1.2 1.3 Mengus G, May M, Jacq X, Staub A, Tora L, Chambon P, Davidson I (May 1995). "Cloning and characterization of hTAFII18, hTAFII20 and hTAFII28: three subunits of the human transcription factor TFIID". EMBO J. 14 (7): 1520–31. PMC 398239. PMID 7729427.
  2. ↑ Kuzuhara T, Horikoshi M (November 1996). "Isolation and characterization of a cDNA encoding a human TFIID subunit containing a variety of putative structural motifs including direct repeats". Biol. Pharm. Bull. 19 (1): 122–6. doi:10.1248/bpb.19.122. PMID 8820923.
  3. ↑ 3.0 3.1 "Entrez Gene: TAF11 TAF11 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 28kDa".
  4. ↑ 4.0 4.1 Birck C, Poch O, Romier C, Ruff M, Mengus G, Lavigne AC, Davidson I, Moras D (July 1998). "Human TAF(II)28 and TAF(II)18 interact through a histone fold encoded by atypical evolutionary conserved motifs also found in the SPT3 family". Cell. 94 (2): 239–49. doi:10.1016/S0092-8674(00)81423-3. PMID 9695952.
  5. ↑ 5.0 5.1 5.2 Scully R, Anderson SF, Chao DM, Wei W, Ye L, Young RA, Livingston DM, Parvin JD (May 1997). "BRCA1 is a component of the RNA polymerase II holoenzyme". Proc. Natl. Acad. Sci. U.S.A. 94 (11): 5605–10. doi:10.1073/pnas.94.11.5605. PMC 20825. PMID 9159119.
  6. ↑ 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.
  7. ↑ 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.
  8. ↑ May M, Mengus G, Lavigne AC, Chambon P, Davidson I (June 1996). "Human TAF(II28) promotes transcriptional stimulation by activation function 2 of the retinoid X receptors". EMBO J. 15 (12): 3093–104. PMC 450252. PMID 8670810.

Further reading

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