TAF13

Transcription initiation factor TFIID subunit 13 is a protein that in humans is encoded by the TAF13 gene.[4][5]

TAF13
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1BH8, 1BH9
Identifiers
Aliases	TAF13, TAF(II)18, TAF2K, TAFII-18, TAFII18, TATA-box binding protein associated factor 13, MRT60
External IDs	OMIM: 600774 MGI: 1913500 HomoloGene: 4126 GeneCards: TAF13
Gene location (Human) Chr. Chromosome 1 (human)[1] Band 1p13.3 Start 109,062,486 bp[1] End 109,076,003 bp[1]
RNA expression pattern More reference expression data
Gene ontology Molecular function • GO:0001131, GO:0001151, GO:0001130, GO:0001204 DNA-binding transcription factor activity • protein C-terminus binding • GO:0001948 protein binding • protein heterodimerization activity • DNA binding • GO:0001104 transcription cofactor activity Cellular component • nucleolus • transcription factor TFIID complex • cell nucleus • nucleoplasm Biological process • transcription initiation from RNA polymerase II promoter • regulation of transcription, DNA-templated • transcription from RNA polymerase II promoter • transcription, DNA-templated • DNA-templated transcription, initiation • snRNA transcription from RNA polymerase II promoter • regulation of signal transduction by p53 class mediator • regulation of transcription from RNA polymerase II promoter Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	6884	99730
Ensembl	ENSG00000197780	n/a
UniProt	Q15543	P61216
RefSeq (mRNA)	NM_005645	NM_025444
RefSeq (protein)	NP_005636	NP_079720
Location (UCSC)	Chr 1: 109.06 – 109.08 Mb	n/a
PubMed search	[2]	[3]
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 associated with a subset of TFIID complexes. This subunit interacts with TBP and with two other small subunits of TFIID, TAF10 and TAF11. There is a pseudogene located on chromosome 6.[5]

Interactions

TAF13 has been shown to interact with TAF15,[6] TAF11,[4][7] TAF10[4] and TATA binding protein.[4]

References

1. GRCh38: Ensembl release 89: ENSG00000197780 - Ensembl, May 2017
2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
3. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. 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.
5. "Entrez Gene: TAF13 TAF13 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 18kDa".
6. Bertolotti A, Melot T, Acker J, Vigneron M, Delattre O, Tora L (Mar 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. Birck C, Poch O, Romier C, Ruff M, Mengus G, Lavigne AC, Davidson I, Moras D (Jul 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.

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.
• 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.
• 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.
• 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.
• 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.
• 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.
• Imabayashi H, Mori T, Gojo S, Kiyono T, Sugiyama T, Irie R, Isogai T, Hata J, Toyama Y, Umezawa A (2003). "Redifferentiation of dedifferentiated chondrocytes and chondrogenesis of human bone marrow stromal cells via chondrosphere formation with expression profiling by large-scale cDNA analysis". Exp. Cell Res. 288 (1): 35–50. doi:10.1016/S0014-4827(03)00130-7. PMID 12878157.

External links

• Overview of all the structural information available in the PDB for UniProt: Q15543 (Transcription initiation factor TFIID subunit 13) at the PDBe-KB.