TAF11

Transcription initiation factor TFIID subunit 11 also known as TAFII28, is a protein that in humans is encoded by the TAF11 gene.[5][6][7]

TAF11
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1BH8, 1BH9
Identifiers
Aliases	TAF11, MGC:15243, TAF2I, TAFII28, PRO2134, TATA-box binding protein associated factor 11
External IDs	OMIM: 600772 MGI: 1916026 HomoloGene: 55918 GeneCards: TAF11
Gene location (Human) Chr. Chromosome 6 (human)[1] Band 6p21.31 Start 34,877,462 bp[1] End 34,888,071 bp[1]
Gene location (Mouse) Chr. Chromosome 17 (mouse)[2] Band 17|17 A3.3 Start 27,901,122 bp[2] End 27,909,844 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • protein heterodimerization activity • GO:0001105 transcription coactivator activity • GO:0001948 protein binding • vitamin D receptor binding • protein N-terminus binding • thyroid hormone receptor binding • DNA binding • transcription factor binding Cellular component • Golgi apparatus • transcription factor TFIID complex • cell nucleus • nucleoplasm Biological process • RNA polymerase II transcriptional preinitiation complex assembly • transcription initiation from RNA polymerase II promoter • regulation of transcription, DNA-templated • transcription from RNA polymerase II promoter • positive regulation by host of viral transcription • transcription, DNA-templated • snRNA transcription from RNA polymerase II promoter • regulation of signal transduction by p53 class mediator • positive regulation of nucleic acid-templated transcription Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	6882	68776
Ensembl	ENSG00000064995	ENSMUSG00000024218
UniProt	Q15544	Q99JX1
RefSeq (mRNA)	NM_001270488 NM_005643	NM_026836 NM_001379368
RefSeq (protein)	NP_001257417 NP_005634	NP_081112 NP_001366297
Location (UCSC)	Chr 6: 34.88 – 34.89 Mb	Chr 17: 27.9 – 27.91 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/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 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.[7]

TAFII28
htafii18/htafii28 heterodimer crystal structure with bound pcmbs
Identifiers
Symbol	TAFII28
Pfam	PF04719
Pfam clan	CL0012
InterPro	IPR006809
SCOP2	1bh9 / SCOPe / SUPFAM
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

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.[5][8]

Interactions

TAF11 has been shown to interact with:

• GTF2F1,[9]
• POLR2A[9] and
• TAF13,[5][8]
• TAF15,[10]
• TATA binding protein,[5][11][12] and
• Transcription Factor II B.[9]

References

1. GRCh38: Ensembl release 89: ENSG00000064995 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000024218 - 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. 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. doi:10.1002/j.1460-2075.1995.tb07138.x. PMC 398239. PMID 7729427.
6. 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.
7. "Entrez Gene: TAF11 TAF11 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 28kDa".
8. 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. S2CID 6274415.
9. 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.
10. 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.
11. 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.
12. 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. doi:10.1002/j.1460-2075.1996.tb00672.x. PMC 450252. PMID 8670810.

Further reading

• 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. doi:10.1038/367295a0. PMID 8121496. S2CID 4362048.
• May M, Mengus G, Lavigne AC, Chambon P, Davidson I (1996). "Human TAF(II28) promotes transcriptional stimulation by activation function 2 of the retinoid X receptors". EMBO J. 15 (12): 3093–104. doi:10.1002/j.1460-2075.1996.tb00672.x. PMC 450252. PMID 8670810.
• 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.
• Scully R, Anderson SF, Chao DM, Wei W, Ye L, Young RA, Livingston DM, Parvin JD (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.
• Dantonel JC, Murthy KG, Manley JL, Tora L (1997). "Transcription factor TFIID recruits factor CPSF for formation of 3' end of mRNA". Nature. 389 (6649): 399–402. doi:10.1038/38763. PMID 9311784. S2CID 4413324.
• Bertolotti A, Melot T, Acker J, Vigneron M, Delattre O, Tora L (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.
• 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.
• Fraser RA, Heard DJ, Adam S, Lavigne AC, Le Douarin B, Tora L, Losson R, Rochette-Egly C, Chambon P (1998). "The putative cofactor TIF1alpha is a protein kinase that is hyperphosphorylated upon interaction with liganded nuclear receptors". J. Biol. Chem. 273 (26): 16199–204. doi:10.1074/jbc.273.26.16199. PMID 9632676.
• Birck C, Poch O, Romier C, Ruff M, Mengus G, Lavigne AC, Davidson I, Moras D (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. S2CID 6274415.