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Search results 601 to 627 out of 627 for Acly

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Type Details Score
Publication
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
Protein Domain
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 [].
Publication  
First Author: Jing Z
Year: 2023
Journal: Front Cell Dev Biol
Title: Epigenetic and transcriptomic alterations in the ClC-3-deficient mice consuming a normal diet.
Volume: 11
Pages: 1196684
Publication
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
Publication
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
Publication
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
Protein
Organism: Mus musculus/domesticus
Length: 116  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 660  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 473  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 813  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 830  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 829  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 830  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 833  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 813  
Fragment?: false
Publication
First Author: Kim W
Year: 2006
Journal: J Bacteriol
Title: Both subunits of ATP-citrate lyase from Chlorobium tepidum contribute to catalytic activity.
Volume: 188
Issue: 18
Pages: 6544-52
Publication
First Author: Bauer DE
Year: 2005
Journal: Oncogene
Title: ATP citrate lyase is an important component of cell growth and transformation.
Volume: 24
Issue: 41
Pages: 6314-22
Publication
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
Protein
Organism: Mus musculus/domesticus
Length: 1091  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1091  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1034  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 1101  
Fragment?: false
Publication
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
Publication
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
Publication
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
Publication
First Author: Ogryzko VV
Year: 1998
Journal: Cell
Title: Histone-like TAFs within the PCAF histone acetylase complex.
Volume: 94
Issue: 1
Pages: 35-44
Publication
First Author: Gerhard DS
Year: 2004
Journal: Genome Res
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Volume: 14
Issue: 10B
Pages: 2121-7