3.5.1.98: histone deacetylase
This is an abbreviated version!
For detailed information about histone deacetylase, go to the full flat file.
Word Map on EC 3.5.1.98
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3.5.1.98
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hdacs
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chromatin
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deacetylases
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trichostatin
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deacetylation
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hydroxamic
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valproic
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saha
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acetyltransferase
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leukemia
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butyrate
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hyperacetylation
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methyltransferase
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vorinostat
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repressor
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lymphoma
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microtubule
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cyclin
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sirtuins
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nucleosome
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t-cells
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transactivation
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caspase
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bcl-2
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metastasis
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myeloid
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proteasome
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hypermethylation
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tumorigenesis
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cardiac
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sirt1
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neurodegenerative
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hematological
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prostate
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demethylation
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antiproliferative
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corepressors
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sirnas
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cpg
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non-histone
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5-aza-2'-deoxycytidine
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valproate
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medicine
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polycomb
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bortezomib
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dnmt3a
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heterochromatin
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creb-binding
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epigenome
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drug development
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coactivator
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relapsed
- 3.5.1.98
- hdacs
- chromatin
- deacetylases
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trichostatin
-
deacetylation
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hydroxamic
-
valproic
- saha
- acetyltransferase
- leukemia
- butyrate
-
hyperacetylation
- methyltransferase
- vorinostat
- repressor
- lymphoma
- microtubule
- cyclin
- sirtuins
- nucleosome
- t-cells
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transactivation
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caspase
- bcl-2
- metastasis
- myeloid
- proteasome
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hypermethylation
- tumorigenesis
- cardiac
- sirt1
- neurodegenerative
- hematological
- prostate
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demethylation
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antiproliferative
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corepressors
- sirnas
- cpg
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non-histone
- 5-aza-2'-deoxycytidine
- valproate
- medicine
-
polycomb
- bortezomib
- dnmt3a
- heterochromatin
-
creb-binding
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epigenome
- drug development
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coactivator
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relapsed
Reaction
hydrolysis of an N6-acetyl-lysine residue of a histone to yield a deacetylated histone =
Synonyms
acetyl-lysine deacetylase, AhHDA1, AtHD1, class I acetyl-lysine deacetylase, class I HDAC, class I histone deacetylase, class II Hda1 HDAC, class II histone deacetylase, class IIa HDAC, class IIa histone deacetylase, Clr6, cytoplasmic deacetylase, deacetylase-like amidohydrolase, dRPD3, FB188 HDAH, Glyma.01 g245100, Glyma.04 g000200, Glyma.04 g187000, Glyma.04 g187100, Glyma.05 g012900, Glyma.05 g021400, Glyma.05 g040600, Glyma.05 g192600, Glyma.06 g000100, Glyma.06 g178700, Glyma.11 g000300, Glyma.11 g187800, Glyma.12 g086700, Glyma.12 g188200, Glyma.17 g078000, Glyma.17 g085700, Glyma.17 g120900, Glyma.17 g229600, GmHDA1, GmHDA10, GmHDA11, GmHDA12, GmHDA13, GmHDA14, GmHDA15, GmHDA16, GmHDA17, GmHDA18, GmHDA2, GmHDA3, GmHDA4, GmHDA5, GmHDA6, GmHDA7, GmHDA8, GmHDA9, GmHDAC, HD1B, HD2, HD8, HDA, HDA-1, HDA-2, HDA-3, HDA-4, hda1, HDA15, HDA19, HDA9, HdaA, HDAC, HDAC 11, HDAC 3, HDAC1, HDAC10, HDAC2, HDAC2-1, HDAC2-2, HDAC3, HDAC4, HDAC5, HDAC6, HDAC6p114, HDAC6p131, HDAC7, HDAC8, HDAC9, HDAH, HDLP, HDT1, HDT2, histone deacetylase, histone deacetylase 1, histone deacetylase 10, histone deacetylase 11, histone deacetylase 2, histone deacetylase 3, histone deacetylase 4, histone deacetylase 6, histone deacetylase 7, histone deacetylase 8, histone deacetylase-1, histone deacetylase-7, histone deacetylase-like amidohydrolase, histone deacetylase-like protein, histone deacetylase1, Hos2, HosB, PA3774, pfHDAC-1, RPD3, Set3 complex, Set3C, tubulin deacetylase, zinc-dependent histone deacetylase, Zn(II)-dependent deacetylase, Zn-HDAC
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3.5.1.98 histone deacetylaseAdvanced search results
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results (Natural Substrates Products
Natural Substrates Products on EC 3.5.1.98 - histone deacetylase
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NATURAL SUBSTRATE 
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
alpha-tubulin + H2O
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splicing variant HDAC6p114 is intact in its deacetylase activity against a-tubulin
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N-acetyl-lysine-heat shock protein 90 + H2O
acetate + heat shock protein 90
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N-acetyl-lysine-MyoD + H2O
acetate + MyoD
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transcription factor MyoD, its activity is co-dependent on isoform HDAC1 and transcriptional co-activator P/CAF
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N-acetyl-lysine-histone H4 + H2O
acetate + histone H4
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rate of deacetylation is not uniform. H4 K5 is deacetylated first, followed by K8, K12 and K16. The specificity of deacetylation and the histone-binding preference of transcriptional co-repressors N-CoR/SMRT match each other
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?
N-acetyl-lysine-histone H4 + H2O
acetate + histone H4
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?
additional information
?
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conserved mechanism of histone deacetylase repression of some secondary metabolite gene clusters
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?
additional information
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deacetylation of histone H4 by Set3C is independent of H3K4 methylation at the PFK1 locus. Set3 interacts with Hos2
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?
additional information
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isoform HDAC4 is an essential regulator of myofibroblastic differentiation
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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
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additional information
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HDAC6 deacetylases tubulins, best noted substrate is beta-tubulin
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additional information
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HDACs catalyse the removal of acetyl groups from e-N-acetylated lysine residues of various protein substrates
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additional information
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HDACs catalyze the deacetylation of lysine residues in the N-terminal tails of core histones, in addition non-histone proteins may also serve as substrates
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?
additional information
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HDACs catalyze the deacetylation of lysine residues in the N-terminal tails of core histones, in addition non-histone proteins may also serve as substrates
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additional information
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histone deacetylase proteins catalyze the removal of acetyl groups from acetylated lysines on histone substrates
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additional information
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histone deacetylases catalyse the removal of the N-acetyl lysine residues from the histone tails, they also deacetylate a growing number of non-histone proteins
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additional information
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histone deacetylases catalyze the removal of acetyl groups from histones, leading to chromatin condensation and transcriptional repression
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additional information
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the acetylation status of lysine residues in nucleosomal proteins is tightly controlled by two counteracting enzyme families, the histone acetyl transferases and the histone deacetylases, HDACs
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additional information
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HDAC7 physically binds to PLZF and modulates its transcriptional activity. PLZF belongs to the BTB-ZF family of transcription factors
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additional information
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HDAC7 physically binds to PLZF and modulates its transcriptional activity. PLZF belongs to the BTB-ZF family of transcription factors
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additional information
?
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histone deacetylases regulate the expression of HoxA9, which acts as a master switch to regulate the expression of prototypical endothelial-committed genes such as endothelial nitric oxide synthase, VE-cadherin, VEGF-R2, and mediates the shear stress-induced maturation of endothelial cells
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additional information
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HDAC7 physically binds to PLZF and modulates its transcriptional activity. PLZF belongs to the BTB-ZF family of transcription factors
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additional information
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HDAC7 physically binds to PLZF and modulates its transcriptional activity. PLZF belongs to the BTB-ZF family of transcription factors
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additional information
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catalytic reactive mechanism with catalytic Zn2+, detailed overview. Structure comparison of PA3774 with several HDACs and HDLP. 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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catalytic reactive mechanism with catalytic Zn2+, detailed overview. Structure comparison of PA3774 with several HDACs and HDLP. 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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catalytic reactive mechanism with catalytic Zn2+, detailed overview. Structure comparison of PA3774 with several HDACs and HDLP. 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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catalytic reactive mechanism with catalytic Zn2+, detailed overview. Structure comparison of PA3774 with several HDACs and HDLP. 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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catalytic reactive mechanism with catalytic Zn2+, detailed overview. Structure comparison of PA3774 with several HDACs and HDLP. 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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catalytic reactive mechanism with catalytic Zn2+, detailed overview. Structure comparison of PA3774 with several HDACs and HDLP. 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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-
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additional information
?
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catalytic reactive mechanism with catalytic Zn2+, detailed overview. Structure comparison of PA3774 with several HDACs and HDLP. 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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-
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additional information
?
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catalytic reactive mechanism with catalytic Zn2+, detailed overview. Structure comparison of PA3774 with several HDACs and HDLP. 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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catalytic reactive mechanism with catalytic Zn2+, detailed overview. Structure comparison of PA3774 with several HDACs and HDLP. 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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acetylation of histone core proteins is regulated by HDAC, H3K9-K14 deacetylation is mediated, at least in part, by HDAC 11
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