TAF12

TAF12 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 20kDa
PDB rendering based on 1h3o.
Available structures PDB 1h3o
Identifiers
Symbols	TAF12; TAF2J; TAFII20
External IDs	OMIM: 600773 MGI: 1913714 HomoloGene: 68477 GeneCards: TAF12 Gene
Gene Ontology Molecular function • DNA binding • sequence-specific DNA binding transcription factor activity • transcription coactivator activity • histone acetyltransferase activity • protein binding Cellular component • PCAF complex • nucleus • nucleoplasm • nucleoplasm • transcription factor TFIID complex • STAGA complex • STAGA complex • transcription factor TFTC complex Biological process • transcription from RNA polymerase II promoter • transcription initiation from RNA polymerase II promoter • transcription initiation from RNA polymerase II promoter • transcription initiation from RNA polymerase II promoter • transcription elongation from RNA polymerase II promoter • gene expression • viral reproduction • histone H3 acetylation Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	6883	66464
Ensembl	ENSG00000120656	ENSMUSG00000028899
UniProt	Q16514	Q3UT56
RefSeq (mRNA)	NM_001135218.1	NM_025579.3
RefSeq (protein)	NP_001128690.1	NP_079855.2
Location (UCSC)	Chr 1: 28.92 – 28.97 Mb	Chr 4: 131.83 – 131.85 Mb
PubMed search	[1]	[2]

Transcription initiation factor TFIID subunit 12 is a protein that in humans is encoded by the TAF12 gene.

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.

Interactions

TAF12 has been shown to interact with TAF9 and Transcription initiation protein SPT3 homolog.

Further reading

• Schweisguth DC, Hammerstedt RH (1992). "Evaluation of plasma membrane stability by detergent-induced rupture of osmotically swollen sperm.". J. Biochem. Biophys. Methods 24 (1–2): 81–94. doi:10.1016/0165-022X(92)90049-G. PMID 1560184. 
• Zhou Q, Sharp PA (1995). "Novel mechanism and factor for regulation by HIV-1 Tat". EMBO J. 14 (2): 321–8. PMC 398086. PMID 7835343. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=398086. 
• 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. PMC 237158. PMID 7933101. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=237158. 
• 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. doi:10.1016/0378-1119(95)00838-1. 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. doi:10.1074/jbc.271.30.18194. 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. 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. PMC 190456. PMID 8764009. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=190456. 
• 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. PMC 190508. PMID 8764062. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=190508. 
• Zhou Q, Sharp PA (1996). "Tat-SF1: cofactor for stimulation of transcriptional elongation by HIV-1 Tat". Science 274 (5287): 605–10. doi:10.1126/science.274.5287.605. 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. 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. 
• 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. doi:10.1016/S0092-8674(00)81219-2. 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. doi:10.1016/S1097-2765(00)80301-9. 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. doi:10.1128/MCB.20.1.340-351.2000. PMC 85089. PMID 10594036. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=85089. 
• 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. PMC 150203. PMID 11406595. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=150203.