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Wikipedia

TAF5

January 01, 1970

Transcription initiation factor TFIID subunit 5 is a protein that in humans is encoded by the TAF5 gene.[5][6][7]

TAF5
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesTAF5, TAF2D, TAFII100, TAF(II)100, TAFII-100, TATA-box binding protein associated factor 5
External IDsOMIM: 601787; MGI: 2442144; HomoloGene: 5064; GeneCards: TAF5; OMA:TAF5 - orthologs
Orthologs
SpeciesHumanMouse
Entrez

6877

226182

Ensembl

ENSG00000148835

ENSMUSG00000025049

UniProt

Q15542

Q8C092

RefSeq (mRNA)

NM_006951
NM_139052

NM_177342

RefSeq (protein)

NP_008882
NP_620640

NP_796316

Location (UCSC)Chr 10: 103.37 – 103.39 MbChr 19: 47.06 – 47.07 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Function edit

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 an integral subunit of TFIID associated with all transcriptionally competent forms of that complex. This subunit interacts strongly with two TFIID subunits that show similarity to histones H3 and H4, and it may participate in forming a nucleosome-like core in the TFIID complex.[7]

Interactions edit

TAF5 has been shown to interact with:

References edit

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000148835 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000025049 – 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. ^ Dubrovskaya V, Mattei MG, Tora L (February 1997). "Localization of the gene (TAF2D) encoding the 100-kDa subunit (hTAFII100) of the human TFIID complex to chromosome 10 band q24-q25.2". Genomics. 36 (3): 556–7. doi:10.1006/geno.1996.0509. PMID 8884287.
  6. ^ Tanese N, Saluja D, Vassallo MF, Chen JL, Admon A (January 1997). "Molecular cloning and analysis of two subunits of the human TFIID complex: hTAFII130 and hTAFII100". Proc Natl Acad Sci U S A. 93 (24): 13611–6. Bibcode:1996PNAS...9313611T. doi:10.1073/pnas.93.24.13611. PMC 19367. PMID 8942982.
  7. ^ a b "Entrez Gene: TAF5 TAF5 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 100kDa".
  8. ^ a b c Tao Y, Guermah M, Martinez E, Oelgeschläger T, Hasegawa S, Takada R, Yamamoto T, Horikoshi M, Roeder RG (March 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.
  9. ^ Hsieh YJ, Kundu TK, Wang Z, Kovelman R, Roeder RG (November 1999). "The TFIIIC90 subunit of TFIIIC interacts with multiple components of the RNA polymerase III machinery and contains a histone-specific acetyltransferase activity". Mol. Cell. Biol. 19 (11): 7697–704. doi:10.1128/mcb.19.11.7697. PMC 84812. PMID 10523658.
  10. ^ 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.
  11. ^ Bertolotti A, Melot T, Acker J, Vigneron M, Delattre O, Tora L (March 1998). "EWS, but not EWS-FLI-1, is associated with both TFIID and RNA polymerase II: interactions between two members of the TET family, EWS and hTAFII68, and subunits of TFIID and RNA polymerase II complexes". Mol. Cell. Biol. 18 (3): 1489–97. doi:10.1128/mcb.18.3.1489. PMC 108863. PMID 9488465.
  12. ^ Bellorini M, Lee DK, Dantonel JC, Zemzoumi K, Roeder RG, Tora L, Mantovani R (June 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.
  13. ^ Ruppert S, Wang EH, Tjian R (March 1993). "Cloning and expression of human TAFII250: a TBP-associated factor implicated in cell-cycle regulation". Nature. 362 (6416): 175–9. Bibcode:1993Natur.362..175R. doi:10.1038/362175a0. PMID 7680771. S2CID 4364676.

Further reading edit

  • 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.
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
  • 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.
  • Dubrovskaya V, Lavigne AC, Davidson I, Acker J, Staub A, Tora L (1996). "Distinct domains of hTAFII100 are required for functional interaction with transcription factor TFIIF beta (RAP30) and incorporation into the TFIID complex". EMBO J. 15 (14): 3702–12. doi:10.1002/j.1460-2075.1996.tb00740.x. PMC 452026. PMID 8758937.
  • 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.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
  • Bertolotti A, Melot T, Acker J, Vigneron M, Delattre O, Tora L (1998). "EWS, but not EWS-FLI-1, is associated with both TFIID and RNA polymerase II: interactions between two members of the TET family, EWS and hTAFII68, and subunits of TFIID and RNA polymerase II complexes". Mol. Cell. Biol. 18 (3): 1489–97. doi:10.1128/mcb.18.3.1489. PMC 108863. PMID 9488465.
  • Brand M, Yamamoto K, Staub A, Tora L (1999). "Identification of TATA-binding protein-free TAFII-containing complex subunits suggests a role in nucleosome acetylation and signal transduction". J. Biol. Chem. 274 (26): 18285–9. doi:10.1074/jbc.274.26.18285. PMID 10373431.
  • 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.
  • Martinez E, Palhan VB, Tjernberg A, Lymar ES, Gamper AM, Kundu TK, Chait BT, Roeder RG (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.

External links edit

  • Overview of all the structural information available in the PDB for UniProt: Q15542 (Transcription initiation factor TFIID subunit 5) at the PDBe-KB.

January 01, 1970
taf5, transcription, initiation, factor, tfiid, subunit, protein, that, humans, encoded, gene, available, structurespdbortholog, search, pdbe, rcsblist, codes2nxpidentifiersaliases, taf2d, tafii100, tafii, tata, binding, protein, associated, factor, 5external,. Transcription initiation factor TFIID subunit 5 is a protein that in humans is encoded by the TAF5 gene 5 6 7 TAF5Available structuresPDBOrtholog search PDBe RCSBList of PDB id codes2NXPIdentifiersAliasesTAF5 TAF2D TAFII100 TAF II 100 TAFII 100 TATA box binding protein associated factor 5External IDsOMIM 601787 MGI 2442144 HomoloGene 5064 GeneCards TAF5 OMA TAF5 orthologsGene location Human Chr Chromosome 10 human 1 Band10q24 33Start103 367 966 bp 1 End103 389 065 bp 1 Gene location Mouse Chr Chromosome 19 mouse 2 Band19 19 C3Start47 056 185 bp 2 End47 071 918 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed insecondary oocyteamniotic fluidembryoganglionic eminenceBrodmann area 23middle temporal gyrustibiatesticletrabecular bonebone marrowTop expressed insecondary oocytemedial ganglionic eminencehandprimitive streakPaneth cellspermatidcumulus cellspermatocytemedullary collecting ducttrigeminal ganglionMore reference expression dataBioGPSMore reference expression dataGene ontologyMolecular functionprotein dimerization activity DNA binding transcription factor activity histone acetyltransferase activity protein binding identical protein binding RNA polymerase II general transcription initiation factor activityCellular componentnucleolus actin cytoskeleton nucleus transcription factor TFTC complex transcription factor TFIID complex nucleoplasmBiological processtranscription DNA templated DNA templated transcription initiation regulation of transcription DNA templated transcription by RNA polymerase II transcription initiation from RNA polymerase II promoter snRNA transcription by RNA polymerase II regulation of signal transduction by p53 class mediator histone acetylation viral process chromatin organizationSources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez6877226182EnsemblENSG00000148835ENSMUSG00000025049UniProtQ15542Q8C092RefSeq mRNA NM 006951NM 139052NM 177342RefSeq protein NP 008882NP 620640NP 796316Location UCSC Chr 10 103 37 103 39 MbChr 19 47 06 47 07 MbPubMed search 3 4 WikidataView Edit HumanView Edit Mouse Contents 1 Function 2 Interactions 3 References 4 Further reading 5 External linksFunction editInitiation 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 an integral subunit of TFIID associated with all transcriptionally competent forms of that complex This subunit interacts strongly with two TFIID subunits that show similarity to histones H3 and H4 and it may participate in forming a nucleosome like core in the TFIID complex 7 Interactions editTAF5 has been shown to interact with TAF6 8 9 TAF9 8 10 and TAF15 11 TATA binding protein 8 12 13 References edit a b c GRCh38 Ensembl release 89 ENSG00000148835 Ensembl May 2017 a b c GRCm38 Ensembl release 89 ENSMUSG00000025049 Ensembl May 2017 Human PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Mouse PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Dubrovskaya V Mattei MG Tora L February 1997 Localization of the gene TAF2D encoding the 100 kDa subunit hTAFII100 of the human TFIID complex to chromosome 10 band q24 q25 2 Genomics 36 3 556 7 doi 10 1006 geno 1996 0509 PMID 8884287 Tanese N Saluja D Vassallo MF Chen JL Admon A January 1997 Molecular cloning and analysis of two subunits of the human TFIID complex hTAFII130 and hTAFII100 Proc Natl Acad Sci U S A 93 24 13611 6 Bibcode 1996PNAS 9313611T doi 10 1073 pnas 93 24 13611 PMC 19367 PMID 8942982 a b Entrez Gene TAF5 TAF5 RNA polymerase II TATA box binding protein TBP associated factor 100kDa a b c Tao Y Guermah M Martinez E Oelgeschlager T Hasegawa S Takada R Yamamoto T Horikoshi M Roeder RG March 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 Hsieh YJ Kundu TK Wang Z Kovelman R Roeder RG November 1999 The TFIIIC90 subunit of TFIIIC interacts with multiple components of the RNA polymerase III machinery and contains a histone specific acetyltransferase activity Mol Cell Biol 19 11 7697 704 doi 10 1128 mcb 19 11 7697 PMC 84812 PMID 10523658 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 Bertolotti A Melot T Acker J Vigneron M Delattre O Tora L March 1998 EWS but not EWS FLI 1 is associated with both TFIID and RNA polymerase II interactions between two members of the TET family EWS and hTAFII68 and subunits of TFIID and RNA polymerase II complexes Mol Cell Biol 18 3 1489 97 doi 10 1128 mcb 18 3 1489 PMC 108863 PMID 9488465 Bellorini M Lee DK Dantonel JC Zemzoumi K Roeder RG Tora L Mantovani R June 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 Ruppert S Wang EH Tjian R March 1993 Cloning and expression of human TAFII250 a TBP associated factor implicated in cell cycle regulation Nature 362 6416 175 9 Bibcode 1993Natur 362 175R doi 10 1038 362175a0 PMID 7680771 S2CID 4364676 Further reading editZhou 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 Martinez 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 Maruyama K Sugano S 1994 Oligo capping a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides Gene 138 1 2 171 4 doi 10 1016 0378 1119 94 90802 8 PMID 8125298 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 Dubrovskaya V Lavigne AC Davidson I Acker J Staub A Tora L 1996 Distinct domains of hTAFII100 are required for functional interaction with transcription factor TFIIF beta RAP30 and incorporation into the TFIID complex EMBO J 15 14 3702 12 doi 10 1002 j 1460 2075 1996 tb00740 x PMC 452026 PMID 8758937 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 Oelgeschlager 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 Garcia Martinez 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 Suzuki Y Yoshitomo Nakagawa K Maruyama K Suyama A Sugano S 1997 Construction and characterization of a full length enriched and a 5 end enriched cDNA library Gene 200 1 2 149 56 doi 10 1016 S0378 1119 97 00411 3 PMID 9373149 Bertolotti A Melot T Acker J Vigneron M Delattre O Tora L 1998 EWS but not EWS FLI 1 is associated with both TFIID and RNA polymerase II interactions between two members of the TET family EWS and hTAFII68 and subunits of TFIID and RNA polymerase II complexes Mol Cell Biol 18 3 1489 97 doi 10 1128 mcb 18 3 1489 PMC 108863 PMID 9488465 Brand M Yamamoto K Staub A Tora L 1999 Identification of TATA binding protein free TAFII containing complex subunits suggests a role in nucleosome acetylation and signal transduction J Biol Chem 274 26 18285 9 doi 10 1074 jbc 274 26 18285 PMID 10373431 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 Martinez E Palhan VB Tjernberg A Lymar ES Gamper AM Kundu TK Chait BT Roeder RG 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 External links editOverview of all the structural information available in the PDB for UniProt Q15542 Transcription initiation factor TFIID subunit 5 at the PDBe KB Retrieved from https en wikipedia org w index php title TAF5 amp oldid 1191538313, wikipedia, wiki, book, books, library,

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