TAF9: Difference between revisions

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Latest revision as of 18:17, 10 June 2018

TAF9 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 32kDa, also known as TAF9, is a protein that in humans is encoded by the TAF9 gene.^[1]^[2]

Function

Initiation of transcription by RNA polymerase II requires the activities of more than 70 polypeptides. The protein complex 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 (TAF9B) 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]

Structure

The 17-amino-acid-long trans-activating domains (TAD) of several transcription factors were reported to bind directly to TAF9: p53, VP16, HSF1, NF-IL6, NFAT1, NF-κB, and ALL1/MLL1.^[3] Inside of these 17 amino acids, a unique Nine-amino-acid transactivation domain (9aaTAD) was identified for each reported transcription factor.^[4] 9aaTAD is a novel domain common to a large superfamily of eukaryotic transcription factors represented by Gal4, Oaf1, Leu3, Rtg3, Pho4, Gln4, Gcn4 in yeast and by p53, NFAT, NF-κB and VP16 in mammals.^[5] TAF9 is supposed to be a universal transactivation cofactor for 9aaTAD transcription factors.^[4]

Interactions

TAF9 has been shown to interact with:

GCN5L2,^[6]
Myc,^[7]
SF3B3,^[6]
SUPT7L,^[6]
TADA3L,^[6]
TAF5,^[6]^[8]
TAF6L,^[6]
TAF10,^[6]
TAF12,^[6]
TAF5L,^[6]
TATA binding protein,^[6]^[9]
Transcription initiation protein SPT3 homolog,^[6] and
Transformation/transcription domain-associated protein.^[6]

References

↑ ^1.0 ^1.1 "Entrez Gene: TAF9 TAF9 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 32kDa".
↑ Evans SC, Foster CJ, El-Naggar AK, Lozano G (April 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.
↑ Uesugi M, Nyanguile O, Lu H, Levine AJ, Verdine GL (August 1997). "Induced alpha helix in the VP16 activation domain upon binding to a human TAF". Science. 277 (5330): 1310–3. doi:10.1126/science.277.5330.1310. PMID 9271577.Uesugi M, Verdine GL (December 1999). "The alpha-helical FXXPhiPhi motif in p53: TAF interaction and discrimination by MDM2". Proc. Natl. Acad. Sci. U.S.A. 96 (26): 14801–6. doi:10.1073/pnas.96.26.14801. PMC 24728. PMID 10611293.Choi Y, Asada S, Uesugi M (May 2000). "Divergent hTAFII31-binding motifs hidden in activation domains". J. Biol. Chem. 275 (21): 15912–6. doi:10.1074/jbc.275.21.15912. PMID 10821850.Venot C, Maratrat M, Sierra V, Conseiller E, Debussche L (April 1999). "Definition of a p53 transactivation function-deficient mutant and characterization of two independent p53 transactivation subdomains". Oncogene. 18 (14): 2405–10. doi:10.1038/sj.onc.1202539. PMID 10327062.Lin J, Chen J, Elenbaas B, Levine AJ (May 1994). "Several hydrophobic amino acids in the p53 amino-terminal domain are required for transcriptional activation, binding to mdm-2 and the adenovirus 5 E1B 55-kD protein". Genes Dev. 8 (10): 1235–46. doi:10.1101/gad.8.10.1235. PMID 7926727.
↑ ^4.0 ^4.1 Piskacek S, Gregor M, Nemethova M, Grabner M, Kovarik P, Piskacek M (June 2007). "Nine-amino-acid transactivation domain: establishment and prediction utilities". Genomics. 89 (6): 756–68. doi:10.1016/j.ygeno.2007.02.003. PMID 17467953.
↑ The prediction for 9aa TADs (for both acidic and hydrophilic transactivation domains) is available online from National EMBnet-Node Austria ("9aaTAD Prediction Webtool". EMBnet AUSTRIA. Archived from the original on 2007-07-01. Retrieved 2009-01-10.)
↑ ^6.00 ^6.01 ^6.02 ^6.03 ^6.04 ^6.05 ^6.06 ^6.07 ^6.08 ^6.09 ^6.10 ^6.11 Martinez E, Palhan VB, Tjernberg A, Lymar ES, Gamper AM, Kundu TK, Chait BT, Roeder RG (Oct 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.
↑ Liu X, Tesfai J, Evrard YA, Dent SY, Martinez E (May 2003). "c-Myc transformation domain recruits the human STAGA complex and requires TRRAP and GCN5 acetylase activity for transcription activation". J. Biol. Chem. 278 (22): 20405–12. doi:10.1074/jbc.M211795200. PMC 4031917. PMID 12660246.
↑ Tao Y, Guermah M, Martinez E, Oelgeschläger T, Hasegawa S, Takada R, Yamamoto T, Horikoshi M, Roeder RG (Mar 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.
↑ Bellorini M, Lee DK, Dantonel JC, Zemzoumi K, Roeder RG, Tora L, Mantovani R (Jun 1997). "CCAAT binding NF-Y-TBP interactions: NF-YB and NF-YC require short domains adjacent to their histone fold motifs for association with TBP basic residues". Nucleic Acids Res. 25 (11): 2174–81. doi:10.1093/nar/25.11.2174. PMC 146709. PMID 9153318.

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. doi:10.1073/pnas.92.13.5788. PMC 41586. PMID 7597030.
Hisatake K, Ohta T, Takada R, Guermah M, Horikoshi M, Nakatani Y, Roeder RG (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. doi:10.1073/pnas.92.18.8195. PMC 41123. 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. doi:10.1073/pnas.92.11.5154. PMC 41867. 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. doi:10.1126/science.7809597. PMID 7809597.
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.
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.
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.
Adams MD, Soares MB, Kerlavage AR, Fields C, Venter JC (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, 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. 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. 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. doi:10.1126/science.274.5287.605. PMID 8849451.
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.
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.
Vassilev A, Yamauchi J, Kotani T, Prives C, Avantaggiati ML, Qin J, Nakatani Y (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.
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, Liu CS, Lin W (2000). "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics". Genome Res. 10 (5): 703–13. doi:10.1101/gr.10.5.703. PMC 310876. PMID 10810093.
Choi Y, Asada S, Uesugi M (2000). "Divergent hTAFII31-binding motifs hidden in activation domains". J. Biol. Chem. 275 (21): 15912–6. doi:10.1074/jbc.275.21.15912. PMID 10821850.

[entrez-1] 1.0 ^1.1 "Entrez Gene: TAF9 TAF9 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 32kDa".

[pmid10191103-2] Evans SC, Foster CJ, El-Naggar AK, Lozano G (April 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.

[TAF9_TAD-3] Uesugi M, Nyanguile O, Lu H, Levine AJ, Verdine GL (August 1997). "Induced alpha helix in the VP16 activation domain upon binding to a human TAF". Science. 277 (5330): 1310–3. doi:10.1126/science.277.5330.1310. PMID 9271577.Uesugi M, Verdine GL (December 1999). "The alpha-helical FXXPhiPhi motif in p53: TAF interaction and discrimination by MDM2". Proc. Natl. Acad. Sci. U.S.A. 96 (26): 14801–6. doi:10.1073/pnas.96.26.14801. PMC 24728. PMID 10611293.Choi Y, Asada S, Uesugi M (May 2000). "Divergent hTAFII31-binding motifs hidden in activation domains". J. Biol. Chem. 275 (21): 15912–6. doi:10.1074/jbc.275.21.15912. PMID 10821850.Venot C, Maratrat M, Sierra V, Conseiller E, Debussche L (April 1999). "Definition of a p53 transactivation function-deficient mutant and characterization of two independent p53 transactivation subdomains". Oncogene. 18 (14): 2405–10. doi:10.1038/sj.onc.1202539. PMID 10327062.Lin J, Chen J, Elenbaas B, Levine AJ (May 1994). "Several hydrophobic amino acids in the p53 amino-terminal domain are required for transcriptional activation, binding to mdm-2 and the adenovirus 5 E1B 55-kD protein". Genes Dev. 8 (10): 1235–46. doi:10.1101/gad.8.10.1235. PMID 7926727.

[pmid17467953-4] 4.0 ^4.1 Piskacek S, Gregor M, Nemethova M, Grabner M, Kovarik P, Piskacek M (June 2007). "Nine-amino-acid transactivation domain: establishment and prediction utilities". Genomics. 89 (6): 756–68. doi:10.1016/j.ygeno.2007.02.003. PMID 17467953.

[url9aaTAD_Prediction_Tool-5] The prediction for 9aa TADs (for both acidic and hydrophilic transactivation domains) is available online from National EMBnet-Node Austria ("9aaTAD Prediction Webtool". EMBnet AUSTRIA. Archived from the original on 2007-07-01. Retrieved 2009-01-10.)

[pmid11564863-6] 6.00 ^6.01 ^6.02 ^6.03 ^6.04 ^6.05 ^6.06 ^6.07 ^6.08 ^6.09 ^6.10 ^6.11 Martinez E, Palhan VB, Tjernberg A, Lymar ES, Gamper AM, Kundu TK, Chait BT, Roeder RG (Oct 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.

[pmid12660246-7] Liu X, Tesfai J, Evrard YA, Dent SY, Martinez E (May 2003). "c-Myc transformation domain recruits the human STAGA complex and requires TRRAP and GCN5 acetylase activity for transcription activation". J. Biol. Chem. 278 (22): 20405–12. doi:10.1074/jbc.M211795200. PMC 4031917. PMID 12660246.

[pmid9045704-8] Tao Y, Guermah M, Martinez E, Oelgeschläger T, Hasegawa S, Takada R, Yamamoto T, Horikoshi M, Roeder RG (Mar 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.

[pmid9153318-9] Bellorini M, Lee DK, Dantonel JC, Zemzoumi K, Roeder RG, Tora L, Mantovani R (Jun 1997). "CCAAT binding NF-Y-TBP interactions: NF-YB and NF-YC require short domains adjacent to their histone fold motifs for association with TBP basic residues". Nucleic Acids Res. 25 (11): 2174–81. doi:10.1093/nar/25.11.2174. PMC 146709. PMID 9153318.

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@@ Line 1: / Line 1: @@
-<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
+{{Infobox_gene}}
-{{PBB_Controls
+'''TAF9 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 32kDa''', also known as '''TAF9''', is a [[protein]] that in humans is encoded by the ''TAF9'' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TAF9 TAF9 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 32kDa| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6880| accessdate = }}</ref><ref name="pmid10191103">{{cite journal | vauthors = Evans SC, Foster CJ, El-Naggar AK, Lozano G | title = Mapping and mutational analysis of the human TAF2G gene encoding a p53 cofactor | journal = Genomics | volume = 57 | issue = 1 | pages = 182–3 | date = April 1999 | pmid = 10191103 | doi = 10.1006/geno.1999.5745 | url =  }}</ref>
-| update_page = yes
-| require_manual_inspection = no
-| update_protein_box = yes
-| update_summary = yes
-| update_citations = yes
-}}
-<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
+== Function ==
-{{GNF_Protein_box
+Initiation of transcription by [[RNA polymerase II]] requires the activities of more than 70 polypeptides. The protein complex that coordinates these activities is transcription factor IID ([[Transcription Factor II D|TFIID]]), which binds to the core [[promotor (biology)|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 ([[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 factor]]s (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 [[Herpes simplex virus protein vmw65|VP16]]. A similar but distinct gene ([[TAF9B]]) 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.<ref name="entrez"/>
- | image = PBB_Protein_TAF9_image.jpg
- | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1rkb.
- | PDB = {{PDB2|1rkb}}
- | Name = TAF9 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 32kDa
- | HGNCid = 11542
- | Symbol = TAF9
- | AltSymbols =; AD-004; AK6; CGI-137; CINAP; CIP; MGC1603; MGC3647; MGC5067; MGC:1603; MGC:3647; MGC:5067; TAF2G; TAFII31; TAFII32; TAFIID32
- | OMIM = 600822
- | ECnumber =
- | Homologene = 39986
- | MGIid = 1888697
- | GeneAtlas_image1 = PBB_GE_TAF9_203893_at_tn.png
- | GeneAtlas_image2 = PBB_GE_TAF9_202168_at_tn.png
- | Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0003713 |text = transcription coactivator activity}} {{GNF_GO|id=GO:0004017 |text = adenylate kinase activity}} {{GNF_GO|id=GO:0004765 |text = shikimate kinase activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0008022 |text = protein C-terminus binding}} {{GNF_GO|id=GO:0016251 |text = general RNA polymerase II transcription factor activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0019201 |text = nucleotide kinase activity}}
- | Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005669 |text = transcription factor TFIID complex}}
- | Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006352 |text = transcription initiation}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006366 |text = transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0008652 |text = amino acid biosynthetic process}}
- | Orthologs = {{GNF_Ortholog_box
-    | Hs_EntrezGene = 6880
-    | Hs_Ensembl = ENSG00000085231
-    | Hs_RefseqProtein = NP_001015891
-    | Hs_RefseqmRNA = NM_001015891
-    | Hs_GenLoc_db =
-    | Hs_GenLoc_chr = c5_H2
-    | Hs_GenLoc_start = 69107684
-    | Hs_GenLoc_end = 69125972
-    | Hs_Uniprot = Q9Y3D8
-    | Mm_EntrezGene = 108143
-    | Mm_Ensembl =
-    | Mm_RefseqmRNA = NM_001015889
-    | Mm_RefseqProtein = NP_001015889
-    | Mm_GenLoc_db =
-    | Mm_GenLoc_chr =
-    | Mm_GenLoc_start =
-    | Mm_GenLoc_end =
-    | Mm_Uniprot =
-  }}
-}}
-'''TAF9 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 32kDa''', also known as '''TAF9''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TAF9 TAF9 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 32kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6880| accessdate = }}</ref>
-<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
+== Structure ==
-{{PBB_Summary
+The 17-amino-acid-long trans-activating domains (TAD) of several transcription factors were reported to bind directly to TAF9: p53, VP16, [[HSF1]], [[NF-IL6]], [[NFAT1]], [[NF-κB]], and ALL1/MLL1.<ref name = "TAF9_TAD">{{cite journal | vauthors = Uesugi M, Nyanguile O, Lu H, Levine AJ, [[Gregory L. Verdine|Verdine GL]] | title = Induced alpha helix in the VP16 activation domain upon binding to a human TAF | journal = Science | volume = 277 | issue = 5330 | pages = 1310–3 | date = August 1997 | pmid = 9271577 | doi = 10.1126/science.277.5330.1310 | url =  }}{{cite journal | vauthors = Uesugi M, Verdine GL | title = The alpha-helical FXXPhiPhi motif in p53: TAF interaction and discrimination by MDM2 | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 96 | issue = 26 | pages = 14801–6 | date = December 1999 | pmid = 10611293 | pmc = 24728 | doi = 10.1073/pnas.96.26.14801 | url =  }}{{cite journal | vauthors = Choi Y, Asada S, Uesugi M | title = Divergent hTAFII31-binding motifs hidden in activation domains | journal = J. Biol. Chem. | volume = 275 | issue = 21 | pages = 15912–6 | date = May 2000 | pmid = 10821850 | doi = 10.1074/jbc.275.21.15912 | url =  }}{{cite journal | vauthors = Venot C, Maratrat M, Sierra V, Conseiller E, Debussche L | title = Definition of a p53 transactivation function-deficient mutant and characterization of two independent p53 transactivation subdomains | journal = Oncogene | volume = 18 | issue = 14 | pages = 2405–10 | date = April 1999 | pmid = 10327062 | doi = 10.1038/sj.onc.1202539 | url =  }}{{cite journal | vauthors = Lin J, Chen J, Elenbaas B, Levine AJ | title = Several hydrophobic amino acids in the p53 amino-terminal domain are required for transcriptional activation, binding to mdm-2 and the adenovirus 5 E1B 55-kD protein | journal = Genes Dev. | volume = 8 | issue = 10 | pages = 1235–46 | date = May 1994 | pmid = 7926727 | doi = 10.1101/gad.8.10.1235 | url =  }}</ref> Inside of these 17 amino acids, a unique Nine-amino-acid transactivation domain (9aaTAD) was identified for each reported transcription factor.<ref name="pmid17467953">{{cite journal | vauthors = Piskacek S, Gregor M, Nemethova M, Grabner M, Kovarik P, Piskacek M | title = Nine-amino-acid transactivation domain: establishment and prediction utilities | journal = Genomics | volume = 89 | issue = 6 | pages = 756–68 | date = June 2007 | pmid = 17467953 | doi = 10.1016/j.ygeno.2007.02.003 | url =  }}</ref> 9aaTAD is a novel domain common to a large superfamily of eukaryotic transcription factors represented by [[Gal4]], Oaf1, Leu3, Rtg3, [[Pho4]], Gln4, Gcn4 in yeast and by p53, NFAT, NF-κB and VP16 in mammals.<ref name="url9aaTAD Prediction Tool">The prediction for 9aa TADs (for both acidic and hydrophilic transactivation domains) is available online from National EMBnet-Node Austria ({{cite web| url =https://emb1.bcc.univie.ac.at/toolbox/9aatad/webtool.htm| title =9aaTAD Prediction Webtool| authorlink =| work =| publisher =EMBnet AUSTRIA| pages =| archiveurl =https://web.archive.org/web/20070701165648/https://emb1.bcc.univie.ac.at/toolbox/9aatad/webtool.htm| archivedate =2007-07-01| quote =| accessdate =2009-01-10| deadurl =yes| df =}})</ref> TAF9 is supposed to be a universal transactivation cofactor for 9aaTAD transcription factors.<ref name="pmid17467953"/>
-| section_title =
-| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: TAF9 TAF9 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 32kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6880| accessdate = }}</ref>
-}}
-==References==
+== Interactions ==
-{{reflist|2}}
-==Further reading==
+TAF9 has been shown to [[Protein-protein interaction|interact]] with:
-{{refbegin | 2}}
+* [[GCN5L2]],<ref name = pmid11564863>{{cite journal | vauthors = Martinez E, Palhan VB, Tjernberg A, Lymar ES, Gamper AM, Kundu TK, Chait BT, Roeder RG | title = Human STAGA complex is a chromatin-acetylating transcription coactivator that interacts with pre-mRNA splicing and DNA damage-binding factors in vivo | journal = Mol. Cell. Biol. | volume = 21 | issue = 20 | pages = 6782–95 | date = Oct 2001 | pmid = 11564863 | pmc = 99856 | doi = 10.1128/MCB.21.20.6782-6795.2001 }}</ref>
-{{PBB_Further_reading
+* [[Myc]],<ref name = pmid12660246>{{cite journal | vauthors = Liu X, Tesfai J, Evrard YA, Dent SY, Martinez E | title = c-Myc transformation domain recruits the human STAGA complex and requires TRRAP and GCN5 acetylase activity for transcription activation | journal = J. Biol. Chem. | volume = 278 | issue = 22 | pages = 20405–12 | date = May 2003 | pmid = 12660246 | pmc = 4031917 | doi = 10.1074/jbc.M211795200 }}</ref>
-| citations =
+* [[SF3B3]],<ref name = pmid11564863/>
-*{{cite journal  | author=Klemm RD, Goodrich JA, Zhou S, Tjian R |title=Molecular cloning and expression of the 32-kDa subunit of human TFIID reveals interactions with VP16 and TFIIB that mediate transcriptional activation. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 13 |pages= 5788-92 |year= 1995 |pmid= 7597030 |doi=  }}
+* [[SUPT7L]],<ref name = pmid11564863/>
-*{{cite journal  | author=Hisatake K, Ohta T, Takada R, ''et al.'' |title=Evolutionary conservation of human TATA-binding-polypeptide-associated factors TAFII31 and TAFII80 and interactions of TAFII80 with other TAFs and with general transcription factors. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 18 |pages= 8195-9 |year= 1995 |pmid= 7667268 |doi=  }}
+* [[TADA3L]],<ref name = pmid11564863/>
-*{{cite journal  | author=Lu H, Levine AJ |title=Human TAFII31 protein is a transcriptional coactivator of the p53 protein. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 11 |pages= 5154-8 |year= 1995 |pmid= 7761466 |doi=  }}
+* [[TAF5]],<ref name = pmid11564863/><ref name = pmid9045704>{{cite journal | vauthors = Tao Y, Guermah M, Martinez E, Oelgeschläger T, Hasegawa S, Takada R, Yamamoto T, Horikoshi M, Roeder RG | title = Specific interactions and potential functions of human TAFII100 | journal = J. Biol. Chem. | volume = 272 | issue = 10 | pages = 6714–21 | date = Mar 1997 | pmid = 9045704 | doi =  10.1074/jbc.272.10.6714}}</ref>
-*{{cite journal  | author=Thut CJ, Chen JL, Klemm R, Tjian R |title=p53 transcriptional activation mediated by coactivators TAFII40 and TAFII60. |journal=Science |volume=267 |issue= 5194 |pages= 100-4 |year= 1995 |pmid= 7809597 |doi=  }}
+* [[TAF6L]],<ref name = pmid11564863/>
-*{{cite journal  | author=Zhou Q, Sharp PA |title=Novel mechanism and factor for regulation by HIV-1 Tat. |journal=EMBO J. |volume=14 |issue= 2 |pages= 321-8 |year= 1995 |pmid= 7835343 |doi=  }}
+* [[TAF10]],<ref name = pmid11564863/>
-*{{cite journal  | author=Parada CA, Yoon JB, Roeder RG |title=A novel LBP-1-mediated restriction of HIV-1 transcription at the level of elongation in vitro. |journal=J. Biol. Chem. |volume=270 |issue= 5 |pages= 2274-83 |year= 1995 |pmid= 7836461 |doi=  }}
+* [[TAF12]],<ref name = pmid11564863/>
-*{{cite journal  | author=Ou SH, Garcia-Martínez LF, Paulssen EJ, Gaynor RB |title=Role of flanking E box motifs in human immunodeficiency virus type 1 TATA element function. |journal=J. Virol. |volume=68 |issue= 11 |pages= 7188-99 |year= 1994 |pmid= 7933101 |doi=  }}
+* [[TAF5L]],<ref name = pmid11564863/>
-*{{cite journal  | author=Kashanchi F, Piras G, Radonovich MF, ''et al.'' |title=Direct interaction of human TFIID with the HIV-1 transactivator tat. |journal=Nature |volume=367 |issue= 6460 |pages= 295-9 |year= 1994 |pmid= 8121496 |doi= 10.1038/367295a0 }}
+* [[TATA binding protein]],<ref name = pmid11564863/><ref name = pmid9153318>{{cite journal | vauthors = Bellorini M, Lee DK, Dantonel JC, Zemzoumi K, Roeder RG, Tora L, Mantovani R | title = CCAAT binding NF-Y-TBP interactions: NF-YB and NF-YC require short domains adjacent to their histone fold motifs for association with TBP basic residues | journal = Nucleic Acids Res. | volume = 25 | issue = 11 | pages = 2174–81 | date = Jun 1997 | pmid = 9153318 | pmc = 146709 | doi =  10.1093/nar/25.11.2174}}</ref>
-*{{cite journal  | author=Adams MD, Soares MB, Kerlavage AR, ''et al.'' |title=Rapid cDNA sequencing (expressed sequence tags) from a directionally cloned human infant brain cDNA library. |journal=Nat. Genet. |volume=4 |issue= 4 |pages= 373-80 |year= 1993 |pmid= 8401585 |doi= 10.1038/ng0893-373 }}
+* [[Transcription initiation protein SPT3 homolog]],<ref name = pmid11564863/>  and
-*{{cite journal  | author=Wang Z, Morris GF, Rice AP, ''et al.'' |title=Wild-type and transactivation-defective mutants of human immunodeficiency virus type 1 Tat protein bind human TATA-binding protein in vitro. |journal=J. Acquir. Immune Defic. Syndr. Hum. Retrovirol. |volume=12 |issue= 2 |pages= 128-38 |year= 1996 |pmid= 8680883 |doi=  }}
+* [[Transformation/transcription domain-associated protein]].<ref name = pmid11564863/>
-*{{cite journal  | author=Pendergrast PS, Morrison D, Tansey WP, Hernandez N |title=Mutations in the carboxy-terminal domain of TBP affect the synthesis of human immunodeficiency virus type 1 full-length and short transcripts similarly. |journal=J. Virol. |volume=70 |issue= 8 |pages= 5025-34 |year= 1996 |pmid= 8764009 |doi=  }}
+{{Clear}}
-*{{cite journal  | author=Kashanchi F, Khleif SN, Duvall JF, ''et al.'' |title=Interaction of human immunodeficiency virus type 1 Tat with a unique site of TFIID inhibits negative cofactor Dr1 and stabilizes the TFIID-TFIIA complex. |journal=J. Virol. |volume=70 |issue= 8 |pages= 5503-10 |year= 1996 |pmid= 8764062 |doi=  }}
-*{{cite journal  | author=Zhou Q, Sharp PA |title=Tat-SF1: cofactor for stimulation of transcriptional elongation by HIV-1 Tat. |journal=Science |volume=274 |issue= 5287 |pages= 605-10 |year= 1996 |pmid= 8849451 |doi=  }}
+== References ==
-*{{cite journal  | author=Tao Y, Guermah M, Martinez E, ''et al.'' |title=Specific interactions and potential functions of human TAFII100. |journal=J. Biol. Chem. |volume=272 |issue= 10 |pages= 6714-21 |year= 1997 |pmid= 9045704 |doi=  }}
+{{reflist|35em}}
-*{{cite journal  | author=García-Martínez LF, Ivanov D, Gaynor RB |title=Association of Tat with purified HIV-1 and HIV-2 transcription preinitiation complexes. |journal=J. Biol. Chem. |volume=272 |issue= 11 |pages= 6951-8 |year= 1997 |pmid= 9054383 |doi=  }}
-*{{cite journal  | author=Ogryzko VV, Kotani T, Zhang X, ''et al.'' |title=Histone-like TAFs within the PCAF histone acetylase complex. |journal=Cell |volume=94 |issue= 1 |pages= 35-44 |year= 1998 |pmid= 9674425 |doi=  }}
+== Further reading ==
-*{{cite journal  | author=Vassilev A, Yamauchi J, Kotani T, ''et al.'' |title=The 400 kDa subunit of the PCAF histone acetylase complex belongs to the ATM superfamily. |journal=Mol. Cell |volume=2 |issue= 6 |pages= 869-75 |year= 1999 |pmid= 9885574 |doi=  }}
+{{refbegin |35em}}
-*{{cite journal  | author=Evans SC, Foster CJ, El-Naggar AK, Lozano G |title=Mapping and mutational analysis of the human TAF2G gene encoding a p53 cofactor. |journal=Genomics |volume=57 |issue= 1 |pages= 182-3 |year= 1999 |pmid= 10191103 |doi= 10.1006/geno.1999.5745 }}
+* {{cite journal | vauthors = Klemm RD, Goodrich JA, Zhou S, Tjian R | title = Molecular cloning and expression of the 32-kDa subunit of human TFIID reveals interactions with VP16 and TFIIB that mediate transcriptional activation. | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 92 | issue = 13 | pages = 5788–92 | year = 1995 | pmid = 7597030 | pmc = 41586 | doi = 10.1073/pnas.92.13.5788 }}
-*{{cite journal  | author=Lai CH, Chou CY, Ch'ang LY, ''et al.'' |title=Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics. |journal=Genome Res. |volume=10 |issue= 5 |pages= 703-13 |year= 2000 |pmid= 10810093 |doi=  }}
+* {{cite journal | vauthors = Hisatake K, Ohta T, Takada R, Guermah M, Horikoshi M, Nakatani Y, Roeder RG | title = Evolutionary conservation of human TATA-binding-polypeptide-associated factors TAFII31 and TAFII80 and interactions of TAFII80 with other TAFs and with general transcription factors. | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 92 | issue = 18 | pages = 8195–9 | year = 1995 | pmid = 7667268 | pmc = 41123 | doi = 10.1073/pnas.92.18.8195 }}
-*{{cite journal  | author=Choi Y, Asada S, Uesugi M |title=Divergent hTAFII31-binding motifs hidden in activation domains. |journal=J. Biol. Chem. |volume=275 |issue= 21 |pages= 15912-6 |year= 2000 |pmid= 10821850 |doi=  }}
+* {{cite journal | vauthors = Lu H, Levine AJ | title = Human TAFII31 protein is a transcriptional coactivator of the p53 protein. | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 92 | issue = 11 | pages = 5154–8 | year = 1995 | pmid = 7761466 | pmc = 41867 | doi = 10.1073/pnas.92.11.5154 }}
-}}
+* {{cite journal | vauthors = Thut CJ, Chen JL, Klemm R, Tjian R | title = p53 transcriptional activation mediated by coactivators TAFII40 and TAFII60. | journal = Science | volume = 267 | issue = 5194 | pages = 100–4 | year = 1995 | pmid = 7809597 | doi = 10.1126/science.7809597 }}
+* {{cite journal | vauthors = Zhou Q, Sharp PA | title = Novel mechanism and factor for regulation by HIV-1 Tat. | journal = EMBO J. | volume = 14 | issue = 2 | pages = 321–8 | year = 1995 | pmid = 7835343 | pmc = 398086 | doi =  }}
+* {{cite journal | vauthors = Parada CA, Yoon JB, Roeder RG | title = A novel LBP-1-mediated restriction of HIV-1 transcription at the level of elongation in vitro. | journal = J. Biol. Chem. | volume = 270 | issue = 5 | pages = 2274–83 | year = 1995 | pmid = 7836461 | doi = 10.1074/jbc.270.5.2274 }}
+* {{cite journal | vauthors = Ou SH, Garcia-Martínez LF, Paulssen EJ, Gaynor RB | title = Role of flanking E box motifs in human immunodeficiency virus type 1 TATA element function. | journal = J. Virol. | volume = 68 | issue = 11 | pages = 7188–99 | year = 1994 | pmid = 7933101 | pmc = 237158 | doi =  }}
+* {{cite journal | vauthors = Kashanchi F, Piras G, Radonovich MF, Duvall JF, Fattaey A, Chiang CM, Roeder RG, Brady JN | title = Direct interaction of human TFIID with the HIV-1 transactivator tat. | journal = Nature | volume = 367 | issue = 6460 | pages = 295–9 | year = 1994 | pmid = 8121496 | doi = 10.1038/367295a0 }}
+* {{cite journal | vauthors = Adams MD, Soares MB, Kerlavage AR, Fields C, Venter JC | title = Rapid cDNA sequencing (expressed sequence tags) from a directionally cloned human infant brain cDNA library. | journal = Nat. Genet. | volume = 4 | issue = 4 | pages = 373–80 | year = 1993 | pmid = 8401585 | doi = 10.1038/ng0893-373 }}
+* {{cite journal | vauthors = Wang Z, Morris GF, Rice AP, Xiong W, Morris CB | title = Wild-type and transactivation-defective mutants of human immunodeficiency virus type 1 Tat protein bind human TATA-binding protein in vitro. | journal = J. Acquir. Immune Defic. Syndr. Hum. Retrovirol. | volume = 12 | issue = 2 | pages = 128–38 | year = 1996 | pmid = 8680883 | doi = 10.1097/00042560-199606010-00005 }}
+* {{cite journal | vauthors = Pendergrast PS, Morrison D, Tansey WP, Hernandez N | title = Mutations in the carboxy-terminal domain of TBP affect the synthesis of human immunodeficiency virus type 1 full-length and short transcripts similarly. | journal = J. Virol. | volume = 70 | issue = 8 | pages = 5025–34 | year = 1996 | pmid = 8764009 | pmc = 190456 | doi =  }}
+* {{cite journal | vauthors = Kashanchi F, Khleif SN, Duvall JF, Sadaie MR, Radonovich MF, Cho M, Martin MA, Chen SY, Weinmann R, Brady JN | title = Interaction of human immunodeficiency virus type 1 Tat with a unique site of TFIID inhibits negative cofactor Dr1 and stabilizes the TFIID-TFIIA complex. | journal = J. Virol. | volume = 70 | issue = 8 | pages = 5503–10 | year = 1996 | pmid = 8764062 | pmc = 190508 | doi =  }}
+* {{cite journal | vauthors = Zhou Q, Sharp PA | title = Tat-SF1: cofactor for stimulation of transcriptional elongation by HIV-1 Tat. | journal = Science | volume = 274 | issue = 5287 | pages = 605–10 | year = 1996 | pmid = 8849451 | doi = 10.1126/science.274.5287.605 }}
+* {{cite journal | vauthors = Tao Y, Guermah M, Martinez E, Oelgeschläger T, Hasegawa S, Takada R, Yamamoto T, Horikoshi M, Roeder RG | title = Specific interactions and potential functions of human TAFII100. | journal = J. Biol. Chem. | volume = 272 | issue = 10 | pages = 6714–21 | year = 1997 | pmid = 9045704 | doi = 10.1074/jbc.272.10.6714 }}
+* {{cite journal | vauthors = García-Martínez LF, Ivanov D, Gaynor RB | title = Association of Tat with purified HIV-1 and HIV-2 transcription preinitiation complexes. | journal = J. Biol. Chem. | volume = 272 | issue = 11 | pages = 6951–8 | year = 1997 | pmid = 9054383 | doi = 10.1074/jbc.272.11.6951 }}
+* {{cite journal | vauthors = Ogryzko VV, Kotani T, Zhang X, Schiltz RL, Howard T, Yang XJ, Howard BH, Qin J, Nakatani Y | title = Histone-like TAFs within the PCAF histone acetylase complex. | journal = Cell | volume = 94 | issue = 1 | pages = 35–44 | year = 1998 | pmid = 9674425 | doi = 10.1016/S0092-8674(00)81219-2 }}
+* {{cite journal | vauthors = Vassilev A, Yamauchi J, Kotani T, Prives C, Avantaggiati ML, Qin J, Nakatani Y | title = The 400 kDa subunit of the PCAF histone acetylase complex belongs to the ATM superfamily. | journal = Mol. Cell | volume = 2 | issue = 6 | pages = 869–75 | year = 1999 | pmid = 9885574 | doi = 10.1016/S1097-2765(00)80301-9 }}
+* {{cite journal | vauthors = Evans SC, Foster CJ, El-Naggar AK, Lozano G | title = Mapping and mutational analysis of the human TAF2G gene encoding a p53 cofactor. | journal = Genomics | volume = 57 | issue = 1 | pages = 182–3 | year = 1999 | pmid = 10191103 | doi = 10.1006/geno.1999.5745 }}
+* {{cite journal | vauthors = Lai CH, Chou CY, Ch'ang LY, Liu CS, Lin W | title = Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics. | journal = Genome Res. | volume = 10 | issue = 5 | pages = 703–13 | year = 2000 | pmid = 10810093 | pmc = 310876 | doi = 10.1101/gr.10.5.703 }}
+* {{cite journal | vauthors = Choi Y, Asada S, Uesugi M | title = Divergent hTAFII31-binding motifs hidden in activation domains. | journal = J. Biol. Chem. | volume = 275 | issue = 21 | pages = 15912–6 | year = 2000 | pmid = 10821850 | doi = 10.1074/jbc.275.21.15912 }}
 {{refend}}
+{{PDB Gallery|geneid=6880}}
-{{protein-stub}}
-{{WikiDoc Sources}}

TAF9: Difference between revisions

Latest revision as of 18:17, 10 June 2018

Contents

Function

Structure

Interactions

References

Further reading

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