TAF9

From Wikipedia, the free encyclopedia


TAF9 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 32kDa
PDB rendering based on 1rkb.
Available structures: 1rkb
Identifiers
Symbol(s) TAF9; AD-004; AK6; CGI-137; CINAP; CIP; MGC1603; MGC3647; MGC5067; MGC:1603; MGC:3647; MGC:5067; TAF2G; TAFII31; TAFII32; TAFIID32
External IDs OMIM: 600822 MGI: 1888697 HomoloGene: 39986
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 6880 108143
Ensembl ENSG00000085231 n/a
Uniprot Q9Y3D8 n/a
Refseq NM_001015891 (mRNA)
NP_001015891 (protein)		 NM_001015889 (mRNA)
NP_001015889 (protein)
Location Chr c5_H2: 69.11 - 69.13 Mb n/a
Pubmed search [1] [2]

TAF9 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 32kDa, also known as TAF9, is a human gene.[1]

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 one of the smaller subunits of TFIID that binds to the basal transcription factor GTF2B as well as to several transcriptional activators such as p53 and VP16. A similar but distinct gene (TAF9L) has been found on the X chromosome and a pseudogene has been identified on chromosome 19. Alternative splicing results in multiple transcript variants encoding different isoforms.[1]

[edit] References

  1. ^ a b Entrez Gene: TAF9 TAF9 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 32kDa.

[edit] Further reading

  • Klemm RD, Goodrich JA, Zhou S, Tjian R (1995). "Molecular cloning and expression of the 32-kDa subunit of human TFIID reveals interactions with VP16 and TFIIB that mediate transcriptional activation.". Proc. Natl. Acad. Sci. U.S.A. 92 (13): 5788–92. PMID 7597030. 
  • Hisatake K, Ohta T, Takada R, et al. (1995). "Evolutionary conservation of human TATA-binding-polypeptide-associated factors TAFII31 and TAFII80 and interactions of TAFII80 with other TAFs and with general transcription factors.". Proc. Natl. Acad. Sci. U.S.A. 92 (18): 8195–9. PMID 7667268. 
  • Lu H, Levine AJ (1995). "Human TAFII31 protein is a transcriptional coactivator of the p53 protein.". Proc. Natl. Acad. Sci. U.S.A. 92 (11): 5154–8. PMID 7761466. 
  • Thut CJ, Chen JL, Klemm R, Tjian R (1995). "p53 transcriptional activation mediated by coactivators TAFII40 and TAFII60.". Science 267 (5194): 100–4. PMID 7809597. 
  • 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. 
  • Adams MD, Soares MB, Kerlavage AR, et al. (1993). "Rapid cDNA sequencing (expressed sequence tags) from a directionally cloned human infant brain cDNA library.". Nat. Genet. 4 (4): 373–80. doi:10.1038/ng0893-373. PMID 8401585. 
  • 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. 
  • 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. 
  • Evans SC, Foster CJ, El-Naggar AK, Lozano G (1999). "Mapping and mutational analysis of the human TAF2G gene encoding a p53 cofactor.". Genomics 57 (1): 182–3. doi:10.1006/geno.1999.5745. PMID 10191103. 
  • Lai CH, Chou CY, Ch'ang LY, et al. (2000). "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics.". Genome Res. 10 (5): 703–13. PMID 10810093. 
  • Choi Y, Asada S, Uesugi M (2000). "Divergent hTAFII31-binding motifs hidden in activation domains.". J. Biol. Chem. 275 (21): 15912–6. PMID 10821850. 
 This protein-related article is a stub. You can help Wikipedia by expanding it.