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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Transcription initiation factor TFIID subunit 12''' is a [[protein]] that in humans is encoded by the ''TAF12'' [[gene]].<ref name="pmid7729427">{{cite journal | vauthors = Mengus G, May M, Jacq X, Staub A, Tora L, Chambon P, Davidson I | title = Cloning and characterization of hTAFII18, hTAFII20 and hTAFII28: three subunits of the human transcription factor TFIID | journal = EMBO J. | volume = 14 | issue = 7 | pages = 1520–31  | date = May 1995 | pmid = 7729427 | pmc = 398239 | doi =  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: TAF12 TAF12 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 20kDa| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6883| accessdate = }}</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
| image = PBB_Protein_TAF12_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1h3o.
| PDB = {{PDB2|1h3o}}
| Name = TAF12 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 20kDa
| HGNCid = 11545
| Symbol = TAF12
| AltSymbols =; TAF2J; TAFII20
| OMIM = 600773
| ECnumber = 
| Homologene = 68477
| MGIid = 1913714
| GeneAtlas_image1 = PBB_GE_TAF12_209463_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016251 |text = general RNA polymerase II transcription factor 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}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 6883
    | Hs_Ensembl = ENSG00000120656
    | Hs_RefseqProtein = NP_005635
    | Hs_RefseqmRNA = NM_005644
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 28801949
    | Hs_GenLoc_end = 28842165
    | Hs_Uniprot = Q16514
    | Mm_EntrezGene = 66464
    | Mm_Ensembl = ENSMUSG00000028899
    | Mm_RefseqmRNA = XM_973809
    | Mm_RefseqProtein = XP_978903
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 4
    | Mm_GenLoc_start = 131546489
    | Mm_GenLoc_end = 131565403
    | Mm_Uniprot = Q3UT56
  }}
}}
'''TAF12 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 20kDa''', also known as '''TAF12''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TAF12 TAF12 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 20kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6883| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
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.<ref name="entrez"/>
{{PBB_Summary
| section_title =
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: TAF12 TAF12 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 20kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6883| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal  | author=Schweisguth DC, Hammerstedt RH |title=Evaluation of plasma membrane stability by detergent-induced rupture of osmotically swollen sperm. |journal=J. Biochem. Biophys. Methods |volume=24 |issue= 1-2 |pages= 81-94 |year= 1992 |pmid= 1560184 |doi=  }}
*{{cite journal  | author=Mengus G, May M, Jacq X, ''et al.'' |title=Cloning and characterization of hTAFII18, hTAFII20 and hTAFII28: three subunits of the human transcription factor TFIID. |journal=EMBO J. |volume=14 |issue= 7 |pages= 1520-31 |year= 1995 |pmid= 7729427 |doi=  }}
*{{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=  }}
*{{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=  }}
*{{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=  }}
*{{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 }}
*{{cite journal  | author=Hoffmann A, Chiang CM, Oelgeschläger T, ''et al.'' |title=A histone octamer-like structure within TFIID. |journal=Nature |volume=380 |issue= 6572 |pages= 356-9 |year= 1996 |pmid= 8598932 |doi= 10.1038/380356a0 }}
*{{cite journal  | author=Choi BI, Bando M, Hasegawa S, Horikoshi M |title=Isolation and characterization of a cDNA encoding a novel human transcription factor TFIID subunit containing similarities with histones H2B and H3. |journal=Gene |volume=169 |issue= 2 |pages= 263-7 |year= 1996 |pmid= 8647459 |doi=  }}
*{{cite journal  | author=Hoffmann A, Roeder RG |title=Cloning and characterization of human TAF20/15. Multiple interactions suggest a central role in TFIID complex formation. |journal=J. Biol. Chem. |volume=271 |issue= 30 |pages= 18194-202 |year= 1996 |pmid= 8663456 |doi=  }}
*{{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=  }}
*{{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=  }}
*{{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=  }}
*{{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=  }}
*{{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=Dantonel JC, Murthy KG, Manley JL, Tora L |title=Transcription factor TFIID recruits factor CPSF for formation of 3' end of mRNA. |journal=Nature |volume=389 |issue= 6649 |pages= 399-402 |year= 1997 |pmid= 9311784 |doi= 10.1038/38763 }}
*{{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=  }}
*{{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=  }}
*{{cite journal  | author=Gangloff YG, Werten S, Romier C, ''et al.'' |title=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. |journal=Mol. Cell. Biol. |volume=20 |issue= 1 |pages= 340-51 |year= 2000 |pmid= 10594036 |doi=  }}
*{{cite journal  | author=Brand M, Moggs JG, Oulad-Abdelghani M, ''et al.'' |title=UV-damaged DNA-binding protein in the TFTC complex links DNA damage recognition to nucleosome acetylation. |journal=EMBO J. |volume=20 |issue= 12 |pages= 3187-96 |year= 2001 |pmid= 11406595 |doi= 10.1093/emboj/20.12.3187 }}
}}
{{refend}}


{{protein-stub}}
TAF12 has been shown to [[Protein-protein interaction|interact]] with [[TAF9]]<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 = October 2001 | pmid = 11564863 | pmc = 99856 | doi = 10.1128/MCB.21.20.6782-6795.2001 }}</ref> and [[Transcription initiation protein SPT3 homolog]].<ref name=pmid11564863/>
{{WikiDoc Sources}}
 
== References ==
{{Reflist}}
 
== Further reading ==
{{Refbegin | 2}}
* {{cite journal | vauthors = Schweisguth DC, Hammerstedt RH | title = Evaluation of plasma membrane stability by detergent-induced rupture of osmotically swollen sperm | journal = J. Biochem. Biophys. Methods | volume = 24 | issue = 1-2 | pages = 81–94 | year = 1992 | pmid = 1560184 | doi = 10.1016/0165-022X(92)90049-G }}
* {{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 = Hoffmann A, Chiang CM, Oelgeschläger T, Xie X, Burley SK, Nakatani Y, Roeder RG | title = A histone octamer-like structure within TFIID | journal = Nature | volume = 380 | issue = 6572 | pages = 356–9 | year = 1996 | pmid = 8598932 | doi = 10.1038/380356a0 }}
* {{cite journal | vauthors = Choi BI, Bando M, Hasegawa S, Horikoshi M | title = Isolation and characterization of a cDNA encoding a novel human transcription factor TFIID subunit containing similarities with histones H2B and H3 | journal = Gene | volume = 169 | issue = 2 | pages = 263–7 | year = 1996 | pmid = 8647459 | doi = 10.1016/0378-1119(95)00838-1 }}
* {{cite journal | vauthors = Hoffmann A, Roeder RG | title = Cloning and characterization of human TAF20/15. Multiple interactions suggest a central role in TFIID complex formation | journal = J. Biol. Chem. | volume = 271 | issue = 30 | pages = 18194–202 | year = 1996 | pmid = 8663456 | doi = 10.1074/jbc.271.30.18194 }}
* {{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 = Dantonel JC, Murthy KG, Manley JL, Tora L | title = Transcription factor TFIID recruits factor CPSF for formation of 3' end of mRNA | journal = Nature | volume = 389 | issue = 6649 | pages = 399–402 | year = 1997 | pmid = 9311784 | doi = 10.1038/38763 }}
* {{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 = 1998 | pmid = 9885574 | doi = 10.1016/S1097-2765(00)80301-9 }}
* {{cite journal | vauthors = Gangloff YG, Werten S, Romier C, Carré L, Poch O, Moras D, Davidson I | title = 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 | journal = Mol. Cell. Biol. | volume = 20 | issue = 1 | pages = 340–51 | year = 2000 | pmid = 10594036 | pmc = 85089 | doi = 10.1128/MCB.20.1.340-351.2000 }}
* {{cite journal | vauthors = Brand M, Moggs JG, Oulad-Abdelghani M, Lejeune F, Dilworth FJ, Stevenin J, Almouzni G, Tora L | title = UV-damaged DNA-binding protein in the TFTC complex links DNA damage recognition to nucleosome acetylation | journal = EMBO J. | volume = 20 | issue = 12 | pages = 3187–96 | year = 2001 | pmid = 11406595 | pmc = 150203 | doi = 10.1093/emboj/20.12.3187 }}
{{Refend}}
 
{{PDB Gallery|geneid=6883}}
 
 
{{Gene-1-stub}}

Latest revision as of 01:52, 27 October 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Transcription initiation factor TFIID subunit 12 is a protein that in humans is encoded by the TAF12 gene.[1][2]

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.[2]

Interactions

TAF12 has been shown to interact with TAF9[3] and Transcription initiation protein SPT3 homolog.[3]

References

  1. ↑ 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. PMC 398239. PMID 7729427.
  2. ↑ 2.0 2.1 "Entrez Gene: TAF12 TAF12 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 20kDa".
  3. ↑ 3.0 3.1 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


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