HDAC8
entrez
55869
canonical
uniprot
Q9BY41
canonical
ensembl
ENSG00000147099
resolver
ensp
ENSP00000362655
resolver
ensp
ENSP00000362657
resolver
ensp
ENSP00000362660
resolver
ensp
ENSP00000362674
resolver
ensp
ENSP00000362685
resolver
ensp
ENSP00000362691
resolver
ensp
ENSP00000414486
resolver
ensp
ENSP00000497188
resolver
ensp
ENSP00000497442
resolver
ensp
ENSP00000497568
resolver
ensp
ENSP00000497764
resolver
ensp
ENSP00000498144
resolver
ensp
ENSP00000551288
resolver
ensp
ENSP00000628794
resolver
ensp
ENSP00000628795
resolver
enst
ENST00000373583
resolver
enst
ENST00000647654
resolver
enst
ENST00000647886
resolver
enst
ENST00000648834
resolver
enst
ENST00000648939
resolver
enst
ENST00000650126
resolver
genesymbol
HDAC8
resolver
genesymbol_syn
HDACL1
resolver
hgnc
HGNC:13315
resolver
uniprot
A0A3B3IS68
resolver
uniprot
A0A3B3ISS7
resolver
uniprot
A0A3B3IT30
resolver
uniprot
A0A3B3IU01
resolver
uniprot
A6ND12
resolver
uniprot
A6ND61
resolver
uniprot
A6NET3
resolver
uniprot
A6NFW1
resolver
uniprot
A6NJR3
resolver
uniprot
A8MQ62
resolver
uniprot
B4DKN0
resolver
uniprot
B4DV22
resolver
uniprot
Q86VC8
resolver
uniprot
Q9NP76
resolver
uniprot
Q9NYH4
resolver
uniprot_entry
A0A3B3IS68_HUMAN
resolver
uniprot_entry
A0A3B3ISS7_HUMAN
resolver
uniprot_entry
A0A3B3IT30_HUMAN
resolver
uniprot_entry
A0A3B3IU01_HUMAN
resolver
uniprot_entry
A6NFW1_HUMAN
resolver
uniprot_entry
HDAC8_HUMAN
resolver
uniprot_sec
A6ND12
resolver
uniprot_sec
A6ND61
resolver
uniprot_sec
A6NET3
resolver
uniprot_sec
A6NJR3
resolver
uniprot_sec
A8MQ62
resolver
uniprot_sec
B4DKN0
resolver
uniprot_sec
B4DV22
resolver
uniprot_sec
Q86VC8
resolver
uniprot_sec
Q9NP76
resolver
uniprot_sec
Q9NYH4
resolver
activity_regulation
ACTIVITY REGULATION: Its activity is inhibited by trichostatin A (TSA), suberoylanilide hydroxamic acid (SAHA), 3-(1-methyl-4-phenylacetyl-1H-2-pyrrolyl)-N-hydroxy-2-propenamide (APHA), 4-dimethylamino-N-(6-hydroxycarbamoyethyl)benzamide-N-hydroxy-7-(4-dimethylaminobenzoyl)aminoheptanamide (MS-344), 5-(4-methyl-benzoylamino)-biphenyl-3,4'-dicarboxylic acid 3-dimethylamide 4'-hydroxyamide (CRA-A) and butyrate. {ECO:0000269|PubMed:15242608}.
uniprot
proteins
amino_acid_sequence
MEEPEEPADSGQSLVPVYIYSPEYVSMCDSLAKIPKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDDDHPDSIEYGLGYDCPATEGIFDYAAAIGGATITAAQCLIDGMCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFERILYVDLDLHHGDGVEDAFSFTSKVMTVSLHKFSPGFFPGTGDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYILQWQLATLILGGGGYNLANTARCWTYLTGVILGKTLSSEIPDHEFFTAYGPDYVLEITPSCRPDRNEPHRIQQILNYIKGNLKHVV
uniprot
proteins
disease_involvement
DISEASE: Cornelia de Lange syndrome 5 (CDLS5) [MIM:300882]: A form of Cornelia de Lange syndrome, a clinically heterogeneous developmental disorder associated with malformations affecting multiple systems. It is characterized by facial dysmorphisms, abnormal hands and feet, growth delay, cognitive retardation, hirsutism, gastroesophageal dysfunction and cardiac, ophthalmologic and genitourinary anomalies. {ECO:0000269|PubMed:22885700, ECO:0000269|PubMed:22889856}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.5.1.-
uniprot
proteins
ec_number
3.5.1.98
uniprot
proteins
function
FUNCTION: Histone deacetylase that catalyzes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4) (PubMed:10748112, PubMed:10922473, PubMed:10926844, PubMed:14701748, PubMed:28497810). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events (PubMed:10748112, PubMed:10922473, PubMed:10926844, PubMed:14701748). Histone deacetylases act via the formation of large multiprotein complexes (PubMed:10748112, PubMed:10922473, PubMed:10926844, PubMed:14701748). Also involved in the deacetylation of cohesin complex protein SMC3 regulating release of cohesin complexes from chromatin (PubMed:22885700). May play a role in smooth muscle cell contractility (PubMed:15772115). In addition to protein deacetylase activity, also has protein-lysine deacylase activity: acts as a protein decrotonylase by mediating decrotonylation ((2E)-butenoyl) of histones (PubMed:28497810). {ECO:0000269|PubMed:10748112, ECO:0000269|PubMed:10922473, ECO:0000269|PubMed:10926844, ECO:0000269|PubMed:14701748, ECO:0000269|PubMed:15772115, ECO:0000269|PubMed:22885700, ECO:0000269|PubMed:28497810}.
uniprot
proteins
mass_dalton
41758
uniprot
proteins
mutagenesis
MUTAGEN 39; /note="S->A: Enhances the deacetylase activity."; /evidence="ECO:0000269|PubMed:14701748"; MUTAGEN 39; /note="S->E: Decreases the deacetylase activity."; /evidence="ECO:0000269|PubMed:14701748"; MUTAGEN 101; /note="D->A: Complete loss of catalytical activity. Complete loss of catalytical activity; when associated with F-306."; /evidence="ECO:0000269|PubMed:17721440, ECO:0000269|PubMed:19053282"; MUTAGEN 101; /note="D->E: Partial loss of catalytical activity."; /evidence="ECO:0000269|PubMed:17721440, ECO:0000269|PubMed:19053282"; MUTAGEN 101; /note="D->L: Complete loss of catalytical activity."; /evidence="ECO:0000269|PubMed:17721440, ECO:0000269|PubMed:19053282"; MUTAGEN 101; /note="D->N: Almost complete loss of catalytical activity."; /evidence="ECO:0000269|PubMed:17721440, ECO:0000269|PubMed:19053282"; MUTAGEN 142..143; /note="HH->AA: Strongly reduces histone deacetylase activity."; /evidence="ECO:0000269|PubMed:10926844"; MUTAGEN 143; /note="H->A: Loss of catalytic activity."; /evidence="ECO:0000269|PubMed:19053282"; MUTAGEN 306; /note="Y->F: Loss of catalytic activity. Complete loss of catalytic activity; when associated with A-101."; /evidence="ECO:0000269|PubMed:17721440
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by PKA on serine 39. Phosphorylation reduces deacetylase activity observed preferentially on histones H3 and H4. {ECO:0000269|PubMed:14701748, ECO:0000269|PubMed:15242608}.
uniprot
proteins
protein_family
HD type 1 subfamily
uniprot
proteins
protein_family
Histone deacetylase family
uniprot
proteins
pubmed
10748112
uniprot
proteins
pubmed
10756090
uniprot
proteins
pubmed
10922473
uniprot
proteins
pubmed
10926844
uniprot
proteins
pubmed
11533236
uniprot
proteins
pubmed
12509458
uniprot
proteins
pubmed
14701748
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15242608
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15772115
uniprot
proteins
pubmed
15772651
uniprot
proteins
pubmed
16538051
uniprot
proteins
pubmed
16809764
uniprot
proteins
pubmed
17721440
uniprot
proteins
pubmed
19053282
uniprot
proteins
pubmed
22885700
uniprot
proteins
pubmed
22889856
uniprot
proteins
pubmed
28497810
uniprot
proteins
pubmed
8889548
uniprot
proteins
sequence_length
377
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10748112, ECO:0000269|PubMed:14701748}. Chromosome {ECO:0000269|PubMed:10748112}. Cytoplasm {ECO:0000269|PubMed:15772115, ECO:0000269|PubMed:16538051}. Note=Excluded from the nucleoli (PubMed:10748112). Found in the cytoplasm of cells showing smooth muscle differentiation (PubMed:15772115, PubMed:16538051). {ECO:0000269|PubMed:10748112, ECO:0000269|PubMed:15772115, ECO:0000269|PubMed:16538051}.
uniprot
proteins