TAF12

Transcription initiation factor TFIID subunit 12 is a protein that in humans is encoded by the TAF12 gene.[5][6]

TAF12
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1H3O
Identifiers
Aliases	TAF12, TAF2J, TAFII20, TATA-box binding protein associated factor 12
External IDs	OMIM: 600773 MGI: 1913714 HomoloGene: 68477 GeneCards: TAF12
Gene location (Human) Chr. Chromosome 1 (human)[1] Band 1p35.3 Start 28,589,323 bp[1] End 28,643,085 bp[1]
Gene location (Mouse) Chr. Chromosome 4 (mouse)[2] Band 4|4 D2.3 Start 132,274,375 bp[2] End 132,295,766 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • DNA binding • GO:0001131, GO:0001151, GO:0001130, GO:0001204 DNA-binding transcription factor activity • GO:0001105 transcription coactivator activity • transcription factor binding • GO:0001948 protein binding • protein heterodimerization activity • RNA polymerase II activating transcription factor binding • TBP-class protein binding • histone acetyltransferase activity Cellular component • transcription factor TFTC complex • STAGA complex • transcription factor TFIID complex • nucleoplasm • PCAF complex • cell nucleus • SAGA complex • SLIK (SAGA-like) complex Biological process • regulation of transcription, DNA-templated • positive regulation of sequence-specific DNA binding transcription factor activity • transcription from RNA polymerase II promoter • transcription, DNA-templated • DNA-templated transcription, initiation • transcription initiation from RNA polymerase II promoter • regulation of signal transduction by p53 class mediator • RNA polymerase II transcriptional preinitiation complex assembly • histone H3 acetylation • positive regulation of nucleic acid-templated transcription Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	6883	66464
Ensembl	ENSG00000120656	ENSMUSG00000028899
UniProt	Q16514	Q8VE65
RefSeq (mRNA)	NM_001135218 NM_005644	NM_025579
RefSeq (protein)	NP_001128690 NP_005635	NP_079855
Location (UCSC)	Chr 1: 28.59 – 28.64 Mb	Chr 4: 132.27 – 132.3 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

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 that 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, whereas 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.[6]

Interactions

TAF12 has been shown to interact with TAF9[7] and Transcription initiation protein SPT3 homolog.[7]

References

1. GRCh38: Ensembl release 89: ENSG00000120656 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000028899 - 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. 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. "Entrez Gene: TAF12 TAF12 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 20kDa".
7. Martinez E, Palhan VB, Tjernberg A, Lymar ES, Gamper AM, Kundu TK, Chait BT, Roeder RG (October 2001). "Human STAGA complex is a chromatin-acetylating transcription coactivator that interacts with pre-mRNA splicing and DNA damage-binding factors in vivo". Mol. Cell. Biol. 21 (20): 6782–95. doi:10.1128/MCB.21.20.6782-6795.2001. PMC 99856. PMID 11564863.

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. 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. Bibcode:1994Natur.367..295K. doi:10.1038/367295a0. PMID 8121496. S2CID 4362048.
• Hoffmann A, Chiang CM, Oelgeschläger T, Xie X, Burley SK, Nakatani Y, Roeder RG (1996). "A histone octamer-like structure within TFIID". Nature. 380 (6572): 356–9. Bibcode:1996Natur.380..356H. doi:10.1038/380356a0. PMID 8598932. S2CID 4263436.
• 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, 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. S2CID 13266489.
• Tao Y, Guermah M, Martinez E, Oelgeschläger T, Hasegawa S, Takada R, Yamamoto T, Horikoshi M, Roeder RG (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. Bibcode:1997Natur.389..399D. doi:10.1038/38763. PMID 9311784. S2CID 4413324.
• Ogryzko VV, Kotani T, Zhang X, Schiltz RL, Howard T, Yang XJ, Howard BH, Qin J, Nakatani Y (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. S2CID 18942972.
• Vassilev A, Yamauchi J, Kotani T, Prives C, Avantaggiati ML, Qin J, Nakatani Y (1998). "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, Carré L, Poch O, Moras D, Davidson I (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.
• Brand M, Moggs JG, Oulad-Abdelghani M, Lejeune F, Dilworth FJ, Stevenin J, Almouzni G, Tora L (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.

External links

• Overview of all the structural information available in the PDB for UniProt: Q16514 (Transcription initiation factor TFIID subunit 12) at the PDBe-KB.