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Search results 101 to 200 out of 200 for Taf9

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Type Details Score
Publication
- | J:72247
       
First Author: DDB, FB, MGI, GOA, ZFIN curators
Year: 2001
Title: Gene Ontology annotation through association of InterPro records with GO terms
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Publication
- | J:78475
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Chromosome assignment of mouse genes using the Mouse Genome Sequencing Consortium (MGSC) assembly and the ENSEMBL Database
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Publication
11217851 | J:65060
First Author: Kawai J
Year: 2001
Journal: Nature
Title: Functional annotation of a full-length mouse cDNA collection.
Volume: 409
Issue: 6821
Pages: 685-90
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Publication
- | J:23000
       
First Author: MGD Nomenclature Committee
Year: 1995
Title: Nomenclature Committee Use
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Publication
- | J:342587
       
First Author: AgBase, BHF-UCL, Parkinson's UK-UCL, dictyBase, HGNC, Roslin Institute, FlyBase and UniProtKB curators
Year: 2011
Title: Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
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Publication
- | J:68900
     
First Author: The Jackson Laboratory Mouse Radiation Hybrid Database
Year: 2004
Journal: Database Release
Title: Mouse T31 Radiation Hybrid Data Load
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Publication
12466851 | J:80000
First Author: Okazaki Y
Year: 2002
Journal: Nature
Title: Analysis of the mouse transcriptome based on functional annotation of 60,770 full-length cDNAs.
Volume: 420
Issue: 6915
Pages: 563-73
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Publication
- | J:164563
       
First Author: The Gene Ontology Consortium
Year: 2010
Title: Automated transfer of experimentally-verified manual GO annotation data to mouse-human orthologs
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Publication
21267068 | J:153498
First Author: Diez-Roux G
Year: 2011
Journal: PLoS Biol
Title: A high-resolution anatomical atlas of the transcriptome in the mouse embryo.
Volume: 9
Issue: 1
Pages: e1000582
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Publication
- | J:75000
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Mouse Genome Informatics Computational Sequence to Gene Associations
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Publication
- | J:157972
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome U74 Array Platform (A, B, C v2).
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Publication
- | J:161428
       
First Author: Marc Feuermann, Huaiyu Mi, Pascale Gaudet, Dustin Ebert, Anushya Muruganujan, Paul Thomas
Year: 2010
Title: Annotation inferences using phylogenetic trees
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Publication
- | J:63103
     
First Author: Mouse Genome Database and National Center for Biotechnology Information
Year: 2000
Journal: Database Release
Title: Entrez Gene Load
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Publication
- | J:262123
     
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
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Publication
- | J:144086
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Gene 1.0 ST Array Platform
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Publication
- | J:155721
     
First Author: Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI)
Year: 2010
Journal: Database Download
Title: Consensus CDS project
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Publication
- | J:85324
     
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
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Publication
- | J:91388
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
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Publication
- | J:155221
     
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
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Publication
- | J:90438
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
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Publication
- | J:144087
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform
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Gene
294694 | Taf9-ps
Type: gene
Organism: rat
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Protein Domain
IPR046344 | TAF6_C_sf
Type: Homologous_superfamily
Description: This is the C-terminal domain of the TAF6 subunit of the general transcription factor TFIID. The crystal structure reveals the presence of five conserved HEAT repeats. This region is necessary for the complexing together of the subunits TAF5, TAF6 and TAF9 [, ].
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Protein Domain
IPR011442 | TAF6_C
Type: Domain
Description: This is the C-terminal domain of the TAF6 subunit of the general transcription factor TFIID. The crystal structure reveals the presence of five conserved HEAT repeats. This region is necessary for the complexing together of the subunits TAF5, TAF6 and TAF9 [, ].
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Publication
8598927 | -
First Author: Xie X
Year: 1996
Journal: Nature
Title: Structural similarity between TAFs and the heterotetrameric core of the histone octamer.
Volume: 380
Issue: 6572
Pages: 316-22
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Publication
19308322 | -
First Author: Cler E
Year: 2009
Journal: Cell Mol Life Sci
Title: Recent advances in understanding the structure and function of general transcription factor TFIID.
Volume: 66
Issue: 13
Pages: 2123-34
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Publication
11295558 | -
First Author: Gangloff YG
Year: 2001
Journal: Trends Biochem Sci
Title: The histone fold is a key structural motif of transcription factor TFIID.
Volume: 26
Issue: 4
Pages: 250-7
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Publication
15899866 | -
First Author: Frontini M
Year: 2005
Journal: Mol Cell Biol
Title: TAF9b (formerly TAF9L) is a bona fide TAF that has unique and overlapping roles with TAF9.
Volume: 25
Issue: 11
Pages: 4638-49
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Protein Domain
IPR003162 | TFIID-31
Type: Family
Description: Human transcription initiation factor TFIID is composed of the TATA-binding polypeptide (TBP) and at least 13 TBP-associated factors (TAFs) that collectively or individually are involved in activator-dependent transcription [, , ]. This entry represents the N terminus of the 31kDa subunit (42kDa in Drosophila) of transcription initiation factor IID (TAFII31), also known astranscription initiation factor TFIID subunit 9 (TAF9). It has been shown that TAF9 interacts directly with different transcription factors such as p53, herpes simplex virus activator vp16 and the basal transcription factor TFIIB. Binding to p53 is an essential requirement for p53 mediated transcription activation.TAF9 is a component other TBP-free TAF complexes containing the GCN5-type histone acetyltransferase. Several TAFs interact via histone-fold (HFD) motifs; HFD is the interaction motif involved in heterodimerization of the core histones and their assembly into nucleosome octamers. The minimal HFD contains three α-helices linked by two loops and is found in core histones, TAFS and many other transcription factors. TFIID has a histone octamer-like substructure. TFIID has a histone octamer-like substructure. TAF9 is a shared subunit of both, histone acetyltransferase complex (SAGA) and TFIID complexes. TAF9 domain interacts with TAF6 to form a novel histone-like heterodimer that is structurally related to the histone H3 and H4 oligomer [, , , ].
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Publication
22696218 | -
First Author: Scheer E
Year: 2012
Journal: J Biol Chem
Title: TFIID TAF6-TAF9 complex formation involves the HEAT repeat-containing C-terminal domain of TAF6 and is modulated by TAF5 protein.
Volume: 287
Issue: 33
Pages: 27580-92
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Publication
29485702 | -
First Author: Dahiya R
Year: 2018
Journal: FEBS J
Title: Mutational analysis of TAF6 revealed the essential requirement of the histone-fold domain and the HEAT repeat domain for transcriptional activation.
Volume: 285
Issue: 8
Pages: 1491-1510
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Protein
Q6NZA9
Organism: Mus musculus/domesticus
Length: 249  
Fragment?: false
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Protein
Q8VI33
Organism: Mus musculus/domesticus
Length: 264  
Fragment?: false
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Protein
A2AP81
Organism: Mus musculus/domesticus
Length: 80  
Fragment?: true
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Protein
A2AP82
Organism: Mus musculus/domesticus
Length: 293  
Fragment?: false
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Protein
A0A087WNM2
Organism: Mus musculus/domesticus
Length: 181  
Fragment?: true
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Protein
A0A087WR08
Organism: Mus musculus/domesticus
Length: 155  
Fragment?: true
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Protein
A0A087WQ57
Organism: Mus musculus/domesticus
Length: 170  
Fragment?: true
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Publication
7667268 | -
First Author: Hisatake K
Year: 1995
Journal: Proc Natl Acad Sci U S A
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.
Volume: 92
Issue: 18
Pages: 8195-9
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Publication
14660634 | -
First Author: Daniel JA
Year: 2004
Journal: J Biol Chem
Title: Deubiquitination of histone H2B by a yeast acetyltransferase complex regulates transcription.
Volume: 279
Issue: 3
Pages: 1867-71
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Publication
24307402 | -
First Author: Kamata K
Year: 2014
Journal: J Biochem
Title: The N-terminus and Tudor domains of Sgf29 are important for its heterochromatin boundary formation function.
Volume: 155
Issue: 3
Pages: 159-71
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Protein Domain
IPR037802 | SGF29
Type: Family
Description: SAGA-associated factor 29 (SGF29) is a chromatin reader and a component of the transcription regulatory histone acetylation (HAT) complexes SAGA and SLIK [, ]. In the SAGA complex, SGF29 binds histone H3 that has been methylated at Lys-4 (H3K4me), and preferably binds the trimethylated form (H3K4me3) []. SGF29 also acts as a boundary, preventing the spread of heterochromatin into neighbouring genes [].The transcription regulatory histone acetylation complex Spt-Ada-Gcn5 acetyltransferase (SAGA) is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. SAGA preferentially acetylates histones H3 and H2B and deubiquitinates histone H2B []. SAGA is known as PCAF in vertebrates and PCAF acetylates nucleosomal histone H3 []. The SAGA complex consists of at least TRA1, CHD1, SPT7, TAF5, ADA3, SGF73, SPT20/ADA5, SPT8, TAF12, TAF6, HFI1/ADA1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10, TAF9, SGF11 and SUS1, and some of these components are present as two copies. The complex is built up from distinct modules, each of which has a separate function and crosslinks with either other proteins or other modules in the complex [].SLIK (SAGA-like) is a multi-subunit histone acetyltransferase complex that preferentially acetylates histones H3 and H2B and deubiquitinates histone H2B. It is an embellishment of the SAGA complex. The yeast SLIK complex consists of at least TRA1, CHD1, SPT7, CC TAF5, ADA3, SPT20, RTG2, TAF12, TAF6, HFI1, UBP8 (a deubiquitinase), GCN5, ADA2, SPT3, SGF29, TAF10 and TAF9 [, ].
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Protein Domain
IPR037826 | TAF5L
Type: Family
Description: TAF5-like RNA polymerase II p300/CBP-associated factor-associated factor 65kDa subunit 5L (TAF5L) is a component of the a component of the PCAF complex, the human version of the yeast SAGA complex []. TAF5L is also a component of the STAGA transcription coactivator-HAT complex [].The transcription regulatory histone acetylation complex Spt-Ada-Gcn5 acetyltransferase (SAGA) is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. SAGA preferentially acetylates histones H3 and H2B and deubiquitinates histone H2B []. SAGA is known as PCAF in vertebrates and PCAF acetylates nucleosomal histone H3 []. The SAGA complex consists of at least TRA1, CHD1, SPT7, TAF5, ADA3, SGF73, SPT20/ADA5, SPT8, TAF12, TAF6, HFI1/ADA1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10, TAF9, SGF11 and SUS1, and some of these components are present as two copies. The complex is built up from distinct modules, each of which has a separate function and crosslinks with either other proteins or other modules in the complex [].The STAGA transcription coactivator-HAT complex is a chromatin-acetylating transcription coactivator that interacts with pre-mRNA splicing and DNA damage-binding factors. The STAGA complex is composed of at least SUPT3H, KAT2A, SUPT7L, TAF5L, TAF6L, TADA3L, TAD1L, TAF10, TAF12, TRRAP and TAF9 [].
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Protein Domain
IPR037798 | UBP8
Type: Family
Description: This entry includes the ubiquitin carboxyl-terminal hydrolases 8 (UBP8; from Saccharomyces cerevisiae; MEROPS identifier C19.087). UBP8 is a component of the transcription regulatory histone acetylation (HAT) complexes SAGA and SLIK []. In SAGA and SLIK, UBP8 deubiquitinates histone H2B and this regulates transcription []. UBP8 has a zinc-binding domain with which it associates with the SAGA complex via the Sgf11 protein [].The transcription regulatory histone acetylation complex Spt-Ada-Gcn5 acetyltransferase (SAGA) is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. SAGA preferentially acetylates histones H3 and H2B and deubiquitinates histone H2B []. SAGA is known as PCAF in vertebrates and PCAF acetylates nucleosomal histone H3 []. The SAGA complex consists of at least TRA1, CHD1, SPT7, TAF5, ADA3, SGF73, SPT20/ADA5, SPT8, TAF12, TAF6, HFI1/ADA1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10, TAF9, SGF11 and SUS1, and some of these components are present as two copies. The complex is built up from distinct modules, each of which has a separate function and crosslinks with either other proteins or other modules in the complex [].SLIK (SAGA-like) is a multi-subunit histone acetyltransferase complex that preferentially acetylates histones H3 and H2B and deubiquitinates histone H2B. It is an embellishment of the SAGA complex. The yeast SLIK complex consists of at least TRA1, CHD1, SPT7, CC TAF5, ADA3, SPT20, RTG2, TAF12, TAF6, HFI1, UBP8 (a deubiquitinase), GCN5, ADA2, SPT3, SGF29, TAF10 and TAF9 [, ].
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Publication
10026213 | -
First Author: Grant PA
Year: 1999
Journal: J Biol Chem
Title: Expanded lysine acetylation specificity of Gcn5 in native complexes.
Volume: 274
Issue: 9
Pages: 5895-900
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Publication
15657441 | -
First Author: Ingvarsdottir K
Year: 2005
Journal: Mol Cell Biol
Title: H2B ubiquitin protease Ubp8 and Sgf11 constitute a discrete functional module within the Saccharomyces cerevisiae SAGA complex.
Volume: 25
Issue: 3
Pages: 1162-72
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Protein Domain
IPR037794 | TAF12
Type: Family
Description: Transcription initiation factor TFIID subunit 12 (TAF12) is a component of the DNA-binding general transcription factor complex TFIID []and the transcription regulatory histone acetylation (HAT) complexes SAGA [], SALSA []and SLIK [].The DNA-binding general transcription factor complex TFIID is central to the initiation of DNA-dependent RNA polymerase II transcription. TFIID is the only general transcription initiation factor that bind to the TATA box. The binding of TFIID to the TATA-box is the first step in the formation of a complex able to initiate transcription []. TFIID consists of the TATA binding protein (TBP) and 14 TBP-associated factors (TAFs). One copy of each TAF1, TAF2, TAF3, TAF7, TAF8, TAF11, TAF13, two copies of each TAF4, TAF5, TAF6, TAF9, TAF10, TAF12, and three copies of TAF14 [].The transcription regulatory histone acetylation complex Spt-Ada-Gcn5 acetyltransferase (SAGA) is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. SAGA preferentially acetylates histones H3 and H2B and deubiquitinates histone H2B []. SAGA is known as PCAF in vertebrates and PCAF acetylates nucleosomal histone H3 []. The SAGA complex consists of at least TRA1, CHD1, SPT7, TAF5, ADA3, SGF73, SPT20/ADA5, SPT8, TAF12, TAF6, HFI1/ADA1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10, TAF9, SGF11 and SUS1, and some of these components are present as two copies. The complex is built up from distinct modules, each of which has a separate function and crosslinks with either other proteins or other modules in the complex [].SLIK (SAGA-like) is a multi-subunit histone acetyltransferase complex that preferentially acetylates histones H3 and H2B and deubiquitinates histone H2B. It is an embellishment of the SAGA complex. The yeast SLIK complex consists of at least TRA1, CHD1, SPT7, CC TAF5, ADA3, SPT20, RTG2, TAF12, TAF6, HFI1, UBP8 (a deubiquitinase), GCN5, ADA2, SPT3, SGF29, TAF10 and TAF9 [, ].The yeast SALSA complex is an altered form of the SAGA complex and consists of at least TRA1, SPT7 (C-terminal truncated form), TAF5, ADA3, SPT20, TAF12, TAF6, HFI1, GCN5, ADA2 and SPT3 [].
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Protein Domain
IPR037796 | TAF6
Type: Family
Description: Transcription initiation factor TFIID subunit 6 (TAF6) is a component of the DNA-binding general transcription factor complex TFIID []and the regulatory transcription regulatory histone acetylation (HAT) complexes SAGA [], SALSA []and SLIK [].The DNA-binding general transcription factor complex TFIID is central to the initiation of DNA-dependent RNA polymerase II transcription. TFIID is the only general transcription initiation factor that bind to the TATA box. The binding of TFIID to the TATA-box is the first step in the formation of a complex able to initiate transcription []. TFIID consists of the TATA binding protein (TBP) and 14 TBP-associated factors (TAFs). One copy of each TAF1, TAF2, TAF3, TAF7, TAF8, TAF11, TAF13, two copies of each TAF4, TAF5, TAF6, TAF9, TAF10, TAF12, and three copies of TAF14 [].The transcription regulatory histone acetylation complex Spt-Ada-Gcn5 acetyltransferase (SAGA) is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. SAGA preferentially acetylates histones H3 and H2B and deubiquitinates histone H2B []. SAGA is known as PCAF in vertebrates and PCAF acetylates nucleosomal histone H3 []. The SAGA complex consists of at least TRA1, CHD1, SPT7, TAF5, ADA3, SGF73, SPT20/ADA5, SPT8, TAF12, TAF6, HFI1/ADA1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10, TAF9, SGF11 and SUS1, and some of these components are present as two copies. The complex is built up from distinct modules, each of which has a separate function and crosslinks with either other proteins or other modules in the complex [].SLIK (SAGA-like) is a multi-subunit histone acetyltransferase complex that preferentially acetylates histones H3 and H2B and deubiquitinates histone H2B. It is an embellishment of the SAGA complex. The yeast SLIK complex consists of at least TRA1, CHD1, SPT7, CC TAF5, ADA3, SPT20, RTG2, TAF12, TAF6, HFI1, UBP8 (a deubiquitinase), GCN5, ADA2, SPT3, SGF29, TAF10 and TAF9 [, ].The yeast SALSA complex is an altered form of the SAGA complex and consists of at least TRA1, SPT7 (C-terminal truncated form), TAF5, ADA3, SPT20, TAF12, TAF6, HFI1, GCN5, ADA2 and SPT3 [].
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Protein
Q8R2K4
Organism: Mus musculus/domesticus
Length: 616  
Fragment?: false
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Protein
Q62311
Organism: Mus musculus/domesticus
Length: 678  
Fragment?: false
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Protein
H3BK01
Organism: Mus musculus/domesticus
Length: 623  
Fragment?: false
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Protein
D3Z0T0
Organism: Mus musculus/domesticus
Length: 636  
Fragment?: false
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Protein
H3BJR2
Organism: Mus musculus/domesticus
Length: 598  
Fragment?: false
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Protein
A0A087WQC4
Organism: Mus musculus/domesticus
Length: 597  
Fragment?: false
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Protein
K3W4L1
Organism: Mus musculus/domesticus
Length: 622  
Fragment?: false
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Publication
11963920 | -
First Author: Tora L
Year: 2002
Journal: Genes Dev
Title: A unified nomenclature for TATA box binding protein (TBP)-associated factors (TAFs) involved in RNA polymerase II transcription.
Volume: 16
Issue: 6
Pages: 673-5
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Publication
10664584 | -
First Author: Green MR
Year: 2000
Journal: Trends Biochem Sci
Title: TBP-associated factors (TAFIIs): multiple, selective transcriptional mediators in common complexes.
Volume: 25
Issue: 2
Pages: 59-63
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Publication
15647753 | -
First Author: Pray-Grant MG
Year: 2005
Journal: Nature
Title: Chd1 chromodomain links histone H3 methylation with SAGA- and SLIK-dependent acetylation.
Volume: 433
Issue: 7024
Pages: 434-8
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Publication
25216679 | -
First Author: Han Y
Year: 2014
Journal: EMBO J
Title: Architecture of the Saccharomyces cerevisiae SAGA transcription coactivator complex.
Volume: 33
Issue: 21
Pages: 2534-46
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Publication
12446794 | -
First Author: Pray-Grant MG
Year: 2002
Journal: Mol Cell Biol
Title: The novel SLIK histone acetyltransferase complex functions in the yeast retrograde response pathway.
Volume: 22
Issue: 24
Pages: 8774-86
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Publication
9674426 | -
First Author: Grant PA
Year: 1998
Journal: Cell
Title: A subset of TAF(II)s are integral components of the SAGA complex required for nucleosome acetylation and transcriptional stimulation.
Volume: 94
Issue: 1
Pages: 45-53
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Publication
17301242 | J:219098
First Author: Wiper-Bergeron N
Year: 2007
Journal: Proc Natl Acad Sci U S A
Title: Glucocorticoid-stimulated preadipocyte differentiation is mediated through acetylation of C/EBPbeta by GCN5.
Volume: 104
Issue: 8
Pages: 2703-8
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Protein
Q9DA08
Organism: Mus musculus/domesticus
Length: 293  
Fragment?: false
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Protein
E9Q1F7
Organism: Mus musculus/domesticus
Length: 211  
Fragment?: true
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Protein
A0A0U1RNS1
Organism: Mus musculus/domesticus
Length: 160  
Fragment?: true
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Protein
F6ZCH1
Organism: Mus musculus/domesticus
Length: 66  
Fragment?: true
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Protein
F6SIC5
Organism: Mus musculus/domesticus
Length: 118  
Fragment?: true
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Publication
21685874 | -
First Author: Bian C
Year: 2011
Journal: EMBO J
Title: Sgf29 binds histone H3K4me2/3 and is required for SAGA complex recruitment and histone H3 acetylation.
Volume: 30
Issue: 14
Pages: 2829-42
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Publication
12186975 | -
First Author: Sterner DE
Year: 2002
Journal: Proc Natl Acad Sci U S A
Title: SALSA, a variant of yeast SAGA, contains truncated Spt7, which correlates with activated transcription.
Volume: 99
Issue: 18
Pages: 11622-7
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Publication
11279037 | -
First Author: Mitsuzawa H
Year: 2001
Journal: J Biol Chem
Title: Two WD repeat-containing TATA-binding protein-associated factors in fission yeast that suppress defects in the anaphase-promoting complex.
Volume: 276
Issue: 20
Pages: 17117-24
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Publication
9224714 | -
First Author: Grant PA
Year: 1997
Journal: Genes Dev
Title: Yeast Gcn5 functions in two multisubunit complexes to acetylate nucleosomal histones: characterization of an Ada complex and the SAGA (Spt/Ada) complex.
Volume: 11
Issue: 13
Pages: 1640-50
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Protein Domain
IPR037800 | GCN5
Type: Family
Description: This entry includes histone acetyltransferases GCN5, KAT2A and KAT2B (all of which are included in ). GCN5 acetylates histones H2B, H3 and H4, providing a specific tag for epigenetic transcription activation. GCN5 is a component of the transcription regulatory histone acetylation (HAT) complexes SAGA [], SLIK [], SALSA []and ADA []. Mammals have two paralogues: KAT2A (also known as GCN5) and KAT2B. KAT2A acetylates core histones to provide a specific tag for epigenetic transcription activation, but not nucleosome core particles. It also acetylates proteins such as CEBPB []. KAT2A is a component of the ATAC complex, which has acetyltransferase activity on histones H3 and H4 []. KAT2B (also known as P300/calcium-binding protein (CBP)-associated factor or PCAF) can acetylate the core histones H3 and H4 as well as nucleosome core particles and non-histone proteins such as ACLY [].The transcription regulatory histone acetylation complex Spt-Ada-Gcn5 acetyltransferase (SAGA) is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. SAGA preferentially acetylates histones H3 and H2B and deubiquitinates histone H2B []. SAGA is known as PCAF in vertebrates and PCAF acetylates nucleosomal histone H3 []. The SAGA complex consists of at least TRA1, CHD1, SPT7, TAF5, ADA3, SGF73, SPT20/ADA5, SPT8, TAF12, TAF6, HFI1/ADA1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10, TAF9, SGF11 and SUS1, and some of these components are present as two copies. The complex is built up from distinct modules, each of which has a separate function and crosslinks with either other proteins or other modules in the complex [].SLIK (SAGA-like) is a multi-subunit histone acetyltransferase complex that preferentially acetylates histones H3 and H2B and deubiquitinates histone H2B. It is an embellishment of the SAGA complex. The yeast SLIK complex consists of at least TRA1, CHD1, SPT7, CC TAF5, ADA3, SPT20, RTG2, TAF12, TAF6, HFI1, UBP8 (a deubiquitinase), GCN5, ADA2, SPT3, SGF29, TAF10 and TAF9 [, ].The yeast SALSA complex is an altered form of the SAGA complex and consists of at least TRA1, SPT7 (C-terminal truncated form), TAF5, ADA3, SPT20, TAF12, TAF6, HFI1, GCN5, ADA2 and SPT3 [].The ADA complex is a transcription regulatory histone acetylation (HAT) complex. ADA preferentially acetylates nucleosomal histones H3 (at 'Lys-14' and 'Lys-18') and H2B. The complex consists of at least ADA2, ADA3, AHC1, and GCN5. AHC1 is required for the overall structural integrity of the ADA complex [].
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Protein Domain
IPR037783 | Taf5
Type: Family
Description: Transcription initiation factor TFIID subunit 5 is a component of the DNA-binding general transcription factor complex TFIID []and the transcription regulatory histone acetylation (HAT) complexes SAGA [], SALSA []and SLIK []. In Schizosaccharomyces pombe, there is an additional subunit known as Taf73 []which is also a member of this fmaily.The DNA-binding general transcription factor complex TFIID is central to the initiation of DNA-dependent RNA polymerase II transcription. TFIID is the only general transcription initiation factor that bind to the TATA box. The binding of TFIID to the TATA-box is the first step in the formation of a complex able to initiate transcription []. TFIID consists of the TATA binding protein (TBP) and 14 TBP-associated factors (TAFs). One copyof each TAF1, TAF2, TAF3, TAF7, TAF8, TAF11, TAF13, two copies of each TAF4, TAF5, TAF6, TAF9, TAF10, TAF12, and three copies of TAF14 [].The transcription regulatory histone acetylation complex Spt-Ada-Gcn5 acetyltransferase (SAGA) is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. SAGA preferentially acetylates histones H3 and H2B and deubiquitinates histone H2B []. SAGA is known as PCAF in vertebrates and PCAF acetylates nucleosomal histone H3 []. The SAGA complex consists of at least TRA1, CHD1, SPT7, TAF5, ADA3, SGF73, SPT20/ADA5, SPT8, TAF12, TAF6, HFI1/ADA1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10, TAF9, SGF11 and SUS1, and some of these components are present as two copies. The complex is built up from distinct modules, each of which has a separate function and crosslinks with either other proteins or other modules in the complex [].SLIK (SAGA-like) is a multi-subunit histone acetyltransferase complex that preferentially acetylates histones H3 and H2B and deubiquitinates histone H2B. It is an embellishment of the SAGA complex. The yeast SLIK complex consists of at least TRA1, CHD1, SPT7, CC TAF5, ADA3, SPT20, RTG2, TAF12, TAF6, HFI1, UBP8 (a deubiquitinase), GCN5, ADA2, SPT3, SGF29, TAF10 and TAF9 [, ].The yeast SALSA complex is an altered form of the SAGA complex and consists of at least TRA1, SPT7 (C-terminal truncated form), TAF5, ADA3, SPT20, TAF12, TAF6, HFI1, GCN5, ADA2 and SPT3 [].
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Protein
A0A1D5RMJ9
Organism: Mus musculus/domesticus
Length: 192  
Fragment?: true
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Publication
10788514 | -
First Author: Sanders SL
Year: 2000
Journal: J Biol Chem
Title: Identification of two novel TAF subunits of the yeast Saccharomyces cerevisiae TFIID complex.
Volume: 275
Issue: 18
Pages: 13895-900
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Publication
8946909 | -
First Author: Orphanides G
Year: 1996
Journal: Genes Dev
Title: The general transcription factors of RNA polymerase II.
Volume: 10
Issue: 21
Pages: 2657-83
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Protein
A0A0U1RNH1
Organism: Mus musculus/domesticus
Length: 152  
Fragment?: false
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Protein
A0A0U1RPT9
Organism: Mus musculus/domesticus
Length: 163  
Fragment?: false
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Publication
23932781 | -
First Author: Lin R
Year: 2013
Journal: Mol Cell
Title: Acetylation stabilizes ATP-citrate lyase to promote lipid biosynthesis and tumor growth.
Volume: 51
Issue: 4
Pages: 506-518
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Publication
9885573 | -
First Author: Grant PA
Year: 1998
Journal: Mol Cell
Title: The ATM-related cofactor Tra1 is a component of the purified SAGA complex.
Volume: 2
Issue: 6
Pages: 863-7
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Protein
Q91WQ5
Organism: Mus musculus/domesticus
Length: 589  
Fragment?: false
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Protein
Q3U3C7
Organism: Mus musculus/domesticus
Length: 560  
Fragment?: true
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Publication
19103755 | J:145720
First Author: Guelman S
Year: 2009
Journal: Mol Cell Biol
Title: The double-histone-acetyltransferase complex ATAC is essential for mammalian development.
Volume: 29
Issue: 5
Pages: 1176-88
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Protein
Q8VE65
Organism: Mus musculus/domesticus
Length: 161  
Fragment?: false
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Protein
D3Z5H6
Organism: Mus musculus/domesticus
Length: 214  
Fragment?: true
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Protein
D3Z4X5
Organism: Mus musculus/domesticus
Length: 55  
Fragment?: true
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Protein
E9QNT5
Organism: Mus musculus/domesticus
Length: 213  
Fragment?: false
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Protein
Q3UT56
Organism: Mus musculus/domesticus
Length: 162  
Fragment?: false
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Protein
Q99KW4
Organism: Mus musculus/domesticus
Length: 116  
Fragment?: true
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Protein
Q3UVE8
Organism: Mus musculus/domesticus
Length: 660  
Fragment?: true
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Protein
S4R1R2
Organism: Mus musculus/domesticus
Length: 114  
Fragment?: false
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Protein
Q3U2D4
Organism: Mus musculus/domesticus
Length: 473  
Fragment?: false
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Protein
Q9JHD1
Organism: Mus musculus/domesticus
Length: 813  
Fragment?: false
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Protein
Q9JHD2
Organism: Mus musculus/domesticus
Length: 830  
Fragment?: false
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Protein
Q8C092
Organism: Mus musculus/domesticus
Length: 801  
Fragment?: false
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Protein
Q6P3Z8
Organism: Mus musculus/domesticus
Length: 829  
Fragment?: false
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Protein
Q3UD69
Organism: Mus musculus/domesticus
Length: 830  
Fragment?: false
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Protein
Q3UM02
Organism: Mus musculus/domesticus
Length: 833  
Fragment?: false
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Protein
B2RR30
Organism: Mus musculus/domesticus
Length: 813  
Fragment?: false
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Protein
F8VPY2
Organism: Mus musculus/domesticus
Length: 801  
Fragment?: false
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MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

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