Jump to content

TAF11

From Wikipedia, the free encyclopedia

This is an old revision of this page, as edited by Rjwilmsi (talk | contribs) at 17:08, 3 July 2020 (→Further reading: Journal cites:, added 3 DOIs, added 1 Bibcode). The present address (URL) is a permanent link to this revision, which may differ significantly from the current revision.

TAF11
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesTAF11, MGC:15243, TAF2I, TAFII28, PRO2134, TATA-box binding protein associated factor 11
External IDsOMIM: 600772; MGI: 1916026; HomoloGene: 55918; GeneCards: TAF11; OMA:TAF11 - orthologs
Orthologs
SpeciesHumanMouse
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 MbChr 17: 28.12 – 28.13 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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]

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
SymbolTAFII28
PfamPF04719
Pfam clanCL0012
InterProIPR006809
SCOP21bh9 / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure 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:

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000064995 – Ensembl, May 2017
  2. ^ a b c 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. ^ a b c d 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. ^ a b "Entrez Gene: TAF11 TAF11 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 28kDa".
  8. ^ a b 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.
  9. ^ a b c 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

Retrieved from "https://en.wikipedia.org/w/index.php?title=TAF11&oldid=965828683"