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monomer
1 * 66000, SDS-PAGE, 1 * 54938, calculated
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x * 53000, His-tagged recombinant enzyme, SDS-PAGE
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x * 120000, SDS-PAGE and calculated
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x * 98000, SDS-PAGE and calculated
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x * 51200, isozyme HDAC3, SDS-PAGE, x * 77200, recombinant GST-tagged isozyme HDAC3, SDS-PAGE
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x * 90000, SDS-PAGE and calculated
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A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69 x * 41180, sequence calculation
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A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69 x * 22260, sequence calculation
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A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69 x * 26740, sequence calculation
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A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69 x * 38500, sequence calculation
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A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69 x * 45280, sequence calculation
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A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69 x * 45540, sequence calculation
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A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69 x * 48940, sequence calculation
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A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69 x * 52180, sequence calculation
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A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69 x * 52920, sequence calculation
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A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69 x * 53300, sequence calculation
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A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69 x * 55950, sequence calculation
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A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69 x * 55960, sequence calculation
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A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69 x * 56120, sequence calculation
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A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69 x * 56280, sequence calculation
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A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69 x * 59600, sequence calculation
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A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69 x * 72990, sequence calculation
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A0A0R0FIH2, A0A0R0H2W2, A0A0R0JU82, A0A0R0K0I2, I1JB12, I1JZJ1, I1K037, I1LFN1, I1LKU7, I1LTZ2, I1LWR2, I1MTD8, I1MUF8, I1MXC3, K7K0Q1, K7KKZ9, K7KL00, K7KR69 x * 73040, sequence calculation
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x * 105000, calculated, x * 119000, SDS-PAGE of FLAG-tagged protein
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x * 42188, calculated
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x * 42188, calculated
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dimer
2 * 55000, recombinant enzyme, SDS-PAGE
dimer
2 * 41000, crystal structure analysis
dimer
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2 * 41000, crystal structure analysis
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dimer
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2 * 41000, crystal structure analysis
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dimer
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2 * 41000, crystal structure analysis
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dimer
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2 * 41000, crystal structure analysis
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dimer
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2 * 41000, crystal structure analysis
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dimer
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2 * 41000, crystal structure analysis
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dimer
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2 * 41000, crystal structure analysis
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homodimer
2 * 24000, ARB2 domain, SDS-PAGE
homodimer
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2 * 24000, ARB2 domain, SDS-PAGE
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tetramer
4 * 41000, about, mass spectrometry
tetramer
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4 * 41000, about, mass spectrometry
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tetramer
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4 * 41000, about, mass spectrometry
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tetramer
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4 * 41000, about, mass spectrometry
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tetramer
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4 * 41000, about, mass spectrometry
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tetramer
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4 * 41000, about, mass spectrometry
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tetramer
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4 * 41000, about, mass spectrometry
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tetramer
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4 * 41000, about, mass spectrometry
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additional information
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enzyme interacts directly with transcription factor MEF-2
additional information
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isoform HD2 dissociates into HD1 when treated with 1.6 M NaCl or applied to a Q-Sepharose column. The active form of enzyme is a high-molecular-mass complex associated with proteins that are components of the nuclear matrix
additional information
domain architecture of HDACs in soybean, overview
additional information
domain architecture of HDACs in soybean, overview
additional information
domain architecture of HDACs in soybean, overview
additional information
domain architecture of HDACs in soybean, overview
additional information
domain architecture of HDACs in soybean, overview
additional information
domain architecture of HDACs in soybean, overview
additional information
domain architecture of HDACs in soybean, overview
additional information
domain architecture of HDACs in soybean, overview
additional information
domain architecture of HDACs in soybean, overview
additional information
domain architecture of HDACs in soybean, overview
additional information
domain architecture of HDACs in soybean, overview
additional information
domain architecture of HDACs in soybean, overview
additional information
domain architecture of HDACs in soybean, overview
additional information
domain architecture of HDACs in soybean, overview
additional information
domain architecture of HDACs in soybean, overview
additional information
domain architecture of HDACs in soybean, overview
additional information
domain architecture of HDACs in soybean, overview
additional information
domain architecture of HDACs in soybean, overview
additional information
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domain architecture of HDACs in soybean, overview
additional information
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class II histone deacetylases bind myocyte enhancer factor-2
additional information
enzyme contains an amino-terminal catalytic domain and a carboxyl pseudo-repeat that shares significant homology with its catalytic domain
additional information
enzyme has a bipartite modular structure consisting of a N-terminal putative deacetylase domain and a C-terminal leucine-rich domain. Isoform HDAC10 interacts with enzyme isoform HDAC3, but not with HDAC4 or HDAC6
additional information
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enzyme has a bipartite modular structure consisting of a N-terminal putative deacetylase domain and a C-terminal leucine-rich domain. Isoform HDAC10 interacts with enzyme isoform HDAC3, but not with HDAC4 or HDAC6
additional information
histone deacetylase activity of isoform HDAC7 maps to a C-terminal domain and is dependent on interaction with isoform HDAC3 in the nucleus. Cytoplasmic HDAC7 that is not bound to HDAC3 is inactive. Transcriptional corepressors SMRT and N-CoR may serve as critical mediators of interaction between HDAC7 and HDAC3
additional information
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histone deacetylase activity of isoform HDAC7 maps to a C-terminal domain and is dependent on interaction with isoform HDAC3 in the nucleus. Cytoplasmic HDAC7 that is not bound to HDAC3 is inactive. Transcriptional corepressors SMRT and N-CoR may serve as critical mediators of interaction between HDAC7 and HDAC3
additional information
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in undifferentiatied muscle cells, isoform HDAC1 associates with transcription factor MyoD resulting in silencing of MyoD-dependent transcription of endogenous p21 as well as muscle-specific genes
additional information
isoform HDAC11 interacts with isoform HDAC6
additional information
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isoform HDAC11 interacts with isoform HDAC6
additional information
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isoforms HDAC1 and HDAC2 are associated in vivo, complex is able to deacetylate all four core histones in vitro
additional information
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isoforms HDAC1, HDAC2, HDAC3 co-immunoprecipitate with the ATP-dependent chaperone protein Hsp70
additional information
similar histones substrate conversion is observed in the presence of octameric and monomeric enzyme
additional information
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similar histones substrate conversion is observed in the presence of octameric and monomeric enzyme
additional information
the exceptionally long L1 loop mediates the formation of a tetramer composed of two head-to-head dimers. The distinctive dimer interface significantly confines the entrance area of the active site, suggesting a crucial role for substrate recognition and selectivity
additional information
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the exceptionally long L1 loop mediates the formation of a tetramer composed of two head-to-head dimers. The distinctive dimer interface significantly confines the entrance area of the active site, suggesting a crucial role for substrate recognition and selectivity
additional information
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the exceptionally long L1 loop mediates the formation of a tetramer composed of two head-to-head dimers. The distinctive dimer interface significantly confines the entrance area of the active site, suggesting a crucial role for substrate recognition and selectivity
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additional information
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the exceptionally long L1 loop mediates the formation of a tetramer composed of two head-to-head dimers. The distinctive dimer interface significantly confines the entrance area of the active site, suggesting a crucial role for substrate recognition and selectivity
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additional information
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the exceptionally long L1 loop mediates the formation of a tetramer composed of two head-to-head dimers. The distinctive dimer interface significantly confines the entrance area of the active site, suggesting a crucial role for substrate recognition and selectivity
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additional information
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the exceptionally long L1 loop mediates the formation of a tetramer composed of two head-to-head dimers. The distinctive dimer interface significantly confines the entrance area of the active site, suggesting a crucial role for substrate recognition and selectivity
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additional information
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the exceptionally long L1 loop mediates the formation of a tetramer composed of two head-to-head dimers. The distinctive dimer interface significantly confines the entrance area of the active site, suggesting a crucial role for substrate recognition and selectivity
-
additional information
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the exceptionally long L1 loop mediates the formation of a tetramer composed of two head-to-head dimers. The distinctive dimer interface significantly confines the entrance area of the active site, suggesting a crucial role for substrate recognition and selectivity
-
additional information
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the exceptionally long L1 loop mediates the formation of a tetramer composed of two head-to-head dimers. The distinctive dimer interface significantly confines the entrance area of the active site, suggesting a crucial role for substrate recognition and selectivity
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additional information
the ARB2 domain of Hda1 exists as a homodimer. The ARB2 domain displays an alpha/beta sandwich architecture with an arm protruding outside. Two ARB2 domain molecules form a compact homodimer via the arm elements, and assemble as an inverse V shape, overall structure analysis, overview. Perturbation of the dimer interface abolishes the histone binding ability of the ARB2 domain. Hda1 consists of an N-terminal catalytic domain and a C-terminal non-catalytic domain (ARB2). The catalytic domain of Hda1 shows high sequence homology to the HDACs
additional information
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the ARB2 domain of Hda1 exists as a homodimer. The ARB2 domain displays an alpha/beta sandwich architecture with an arm protruding outside. Two ARB2 domain molecules form a compact homodimer via the arm elements, and assemble as an inverse V shape, overall structure analysis, overview. Perturbation of the dimer interface abolishes the histone binding ability of the ARB2 domain. Hda1 consists of an N-terminal catalytic domain and a C-terminal non-catalytic domain (ARB2). The catalytic domain of Hda1 shows high sequence homology to the HDACs
additional information
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the ARB2 domain of Hda1 exists as a homodimer. The ARB2 domain displays an alpha/beta sandwich architecture with an arm protruding outside. Two ARB2 domain molecules form a compact homodimer via the arm elements, and assemble as an inverse V shape, overall structure analysis, overview. Perturbation of the dimer interface abolishes the histone binding ability of the ARB2 domain. Hda1 consists of an N-terminal catalytic domain and a C-terminal non-catalytic domain (ARB2). The catalytic domain of Hda1 shows high sequence homology to the HDACs
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additional information
enzyme copurifies as a complex with a protein related to the retinoblastoma-associated protein, Rbap46
additional information
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enzyme copurifies as a complex with a protein related to the retinoblastoma-associated protein, Rbap46