TAF12

From Wikipedia, the free encyclopedia

TAF12 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 20kDa

PDB rendering based on 1h3o.

Available structures: 1h3o

Identifiers

Symbol(s)

TAF12; TAF2J; TAFII20

External IDs

OMIM: 600773 MGI: 1913714 HomoloGene: 68477

Gene ontology
Molecular Function:	• protein binding • general RNA polymerase II transcription factor activity
Cellular Component:	• nucleus • transcription factor TFIID complex
Biological Process:	• transcription • transcription initiation • regulation of transcription, DNA-dependent

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_005644 (mRNA)
NP_005635 (protein)

XM_973809 (mRNA)
XP_978903 (protein)

Location

Chr 1: 28.8 - 28.84 Mb

Chr 4: 131.55 - 131.57 Mb

Pubmed search

[1]

[2]

TAF12 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 20kDa, also known as TAF12, is a human gene.^[1]

Control of transcription by RNA polymerase II involves the basal transcription machinery which is a collection of proteins. These proteins with RNA polymerase II, assemble into complexes which are modulated by transactivator proteins that bind to cis-regulatory elements located adjacent to the transcription start site. Some modulators interact directly with the basal complex, whereas others may act as bridging proteins linking transactivators to the basal transcription factors. Some of these associated factors are weakly attached while others are tightly associated with TBP in the TFIID complex. Among the latter are the TAF proteins. Different TAFs are predicted to mediate the function of distinct transcriptional activators for a variety of gene promoters and RNA polymerases. TAF12 interacts directly with TBP as well as with TAF2I.^[1]

[edit] References

^ ^a ^b Entrez Gene: TAF12 TAF12 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 20kDa.

[edit] Further reading

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Mengus G, May M, Jacq X, et al. (1995). "Cloning and characterization of hTAFII18, hTAFII20 and hTAFII28: three subunits of the human transcription factor TFIID.". EMBO J. 14 (7): 1520–31. PMID 7729427.
Zhou Q, Sharp PA (1995). "Novel mechanism and factor for regulation by HIV-1 Tat.". EMBO J. 14 (2): 321–8. 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. 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. PMID 7933101.
Kashanchi F, Piras G, Radonovich MF, et al. (1994). "Direct interaction of human TFIID with the HIV-1 transactivator tat.". Nature 367 (6460): 295–9. doi:10.1038/367295a0. PMID 8121496.
Hoffmann A, Chiang CM, Oelgeschläger T, et al. (1996). "A histone octamer-like structure within TFIID.". Nature 380 (6572): 356–9. doi:10.1038/380356a0. PMID 8598932.
Choi BI, Bando M, Hasegawa S, Horikoshi M (1996). "Isolation and characterization of a cDNA encoding a novel human transcription factor TFIID subunit containing similarities with histones H2B and H3.". Gene 169 (2): 263–7. PMID 8647459.
Hoffmann A, Roeder RG (1996). "Cloning and characterization of human TAF20/15. Multiple interactions suggest a central role in TFIID complex formation.". J. Biol. Chem. 271 (30): 18194–202. PMID 8663456.
Wang Z, Morris GF, Rice AP, et al. (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. 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. PMID 8764009.
Kashanchi F, Khleif SN, Duvall JF, et al. (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. PMID 8764062.
Zhou Q, Sharp PA (1996). "Tat-SF1: cofactor for stimulation of transcriptional elongation by HIV-1 Tat.". Science 274 (5287): 605–10. PMID 8849451.
Tao Y, Guermah M, Martinez E, et al. (1997). "Specific interactions and potential functions of human TAFII100.". J. Biol. Chem. 272 (10): 6714–21. 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. 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.
Ogryzko VV, Kotani T, Zhang X, et al. (1998). "Histone-like TAFs within the PCAF histone acetylase complex.". Cell 94 (1): 35–44. PMID 9674425.
Vassilev A, Yamauchi J, Kotani T, et al. (1999). "The 400 kDa subunit of the PCAF histone acetylase complex belongs to the ATM superfamily.". Mol. Cell 2 (6): 869–75. PMID 9885574.
Gangloff YG, Werten S, Romier C, et al. (2000). "The human TFIID components TAF(II)135 and TAF(II)20 and the yeast SAGA components ADA1 and TAF(II)68 heterodimerize to form histone-like pairs.". Mol. Cell. Biol. 20 (1): 340–51. PMID 10594036.
Brand M, Moggs JG, Oulad-Abdelghani M, et al. (2001). "UV-damaged DNA-binding protein in the TFTC complex links DNA damage recognition to nucleosome acetylation.". EMBO J. 20 (12): 3187–96. doi:10.1093/emboj/20.12.3187. PMID 11406595.