HDAC5
entrez
10014
canonical
uniprot
Q9UQL6
canonical
ensembl
ENSG00000108840
resolver
ensp
ENSP00000225983
resolver
ensp
ENSP00000468004
resolver
ensp
ENSP00000507606
resolver
ensp
ENSP00000534959
resolver
ensp
ENSP00000534960
resolver
ensp
ENSP00000534961
resolver
ensp
ENSP00000534973
resolver
ensp
ENSP00000534975
resolver
ensp
ENSP00000534981
resolver
ensp
ENSP00000727398
resolver
genesymbol
HDAC5
resolver
genesymbol_syn
KIAA0600
resolver
hgnc
HGNC:14068
resolver
uniprot
C9JFV9
resolver
uniprot
O60340
resolver
uniprot
O60528
resolver
uniprot
Q96DY4
resolver
uniprot_entry
HDAC5_HUMAN
resolver
uniprot_sec
C9JFV9
resolver
uniprot_sec
O60340
resolver
uniprot_sec
O60528
resolver
uniprot_sec
Q96DY4
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by trichostatin A. {ECO:0000269|PubMed:10220385}.
uniprot
proteins
amino_acid_sequence
MNSPNESDGMSGREPSLEILPRTSLHSIPVTVEVKPVLPRAMPSSMGGGGGGSPSPVELRGALVGSVDPTLREQQLQQELLALKQQQQLQKQLLFAEFQKQHDHLTRQHEVQLQKHLKQQQEMLAAKQQQEMLAAKRQQELEQQRQREQQRQEELEKQRLEQQLLILRNKEKSKESAIASTEVKLRLQEFLLSKSKEPTPGGLNHSLPQHPKCWGAHHASLDQSSPPQSGPPGTPPSYKLPLPGPYDSRDDFPLRKTASEPNLKVRSRLKQKVAERRSSPLLRRKDGTVISTFKKRAVEITGAGPGASSVCNSAPGSGPSSPNSSHSTIAENGFTGSVPNIPTEMLPQHRALPLDSSPNQFSLYTSPSLPNISLGLQATVTVTNSHLTASPKLSTQQEAERQALQSLRQGGTLTGKFMSTSSIPGCLLGVALEGDGSPHGHASLLQHVLLLEQARQQSTLIAVPLHGQSPLVTGERVATSMRTVGKLPRHRPLSRTQSSPLPQSPQALQQLVMQQQHQQFLEKQKQQQLQLGKILTKTGELPRQPTTHPEETEEELTEQQEVLLGEGALTMPREGSTESESTQEDLEEEDEEDDGEEEEDCIQVKDEEGESGAEEGPDLEEPGAGYKKLFSDAQPLQPLQVYQAPLSLATVPHQALGRTQSSPAAPGGMKSPPDQPVKHLFTTGVVYDTFMLKHQCMCGNTHVHPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHTLLYGTSPLNRQKLDSKKLLGPISQKMYAVLPCGGIGVDSDTVWNEMHSSSAVRMAVGCLLELAFKVAAGELKNGFAIIRPPGHHAEESTAMGFCFFNSVAITAKLLQQKLNVGKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYDNGNFFPGSGAPEEVGGGPGVGYNVNVAWTGGVDPPIGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGHLSPLGGYSVTARCFGHLTRQLMTLAGGRVVLALEGGHDLTAICDASEACVSALLSVELQPLDEAVLQQKPNINAVATLEKVIEIQSKHWSCVQKFAAGLGRSLREAQAGETEEAETVSAMALLSVGAEQAQAAAAREHSPRPAEEPMEQEPAL
uniprot
proteins
ec_number
3.5.1.98
uniprot
proteins
function
FUNCTION: In vitro, it deacetylates lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4) (PubMed:10220385). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Involved in muscle maturation by repressing transcription of myocyte enhancer MEF2C. During muscle differentiation, it shuttles into the cytoplasm, allowing the expression of myocyte enhancer factors. Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer. Serves as a corepressor of RARA and causes its deacetylation (PubMed:28167758). In association with RARA, plays a role in the repression of microRNA-10a and thereby in the inflammatory response (PubMed:28167758). {ECO:0000269|PubMed:10220385, ECO:0000269|PubMed:24413532, ECO:0000269|PubMed:28167758}.
uniprot
proteins
mass_dalton
121978
uniprot
proteins
mutagenesis
MUTAGEN 259; /note="S->A: Reduces AMPK- and caMK-dependent phosphorylation and the subsequent nuclear export. Abolishes nuclear export; when associated with A-498. Does not affect phosphorylation by PKN1 and PKN2."; /evidence="ECO:0000269|PubMed:11081517, ECO:0000269|PubMed:18184930, ECO:0000269|PubMed:20188095"; MUTAGEN 279; /note="S->A: No effect."; /evidence="ECO:0000269|PubMed:11081517"; MUTAGEN 291; /note="S->A: Does not affect phosphorylation by PKC."; /evidence="ECO:0000269|PubMed:20188095"; MUTAGEN 292; /note="T->A: Abolishes phosphorylation by PKC."; /evidence="ECO:0000269|PubMed:20188095"; MUTAGEN 498; /note="S->A: Reduces AMPK- and CaMK-dependent phosphorylation and the subsequent nuclear export. Abolishes nuclear export; when associated with A-259."; /evidence="ECO:0000269|PubMed:11081517, ECO:0000269|PubMed:18184930"; MUTAGEN 661; /note="S->A: No effect."; /evidence="ECO:0000269|PubMed:11081517"; MUTAGEN 713; /note="S->A: No effect."; /evidence="ECO:0000269|PubMed:11081517"; MUTAGEN 1086; /note="V->A: Reduces CaMK-dependent nuclear export."; /evidence="ECO:0000269|PubMed:11509672"; MUTAGEN 1092; /note="L->A: Reduces CaMK-dependent nuclear export."; /evidence="ECO:0000269|PubMed:11509672
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by AMPK, CaMK1, SIK1 and PRKD1 at Ser-259 and Ser-498. The phosphorylation is required for the export to the cytoplasm and inhibition. Phosphorylated by the PKC kinases PKN1 and PKN2, impairing nuclear import. Phosphorylated by GRK5, leading to nuclear export of HDAC5 and allowing MEF2-mediated transcription (By similarity). {ECO:0000250}.; PTM: Ubiquitinated. Polyubiquitination however does not lead to its degradation. {ECO:0000269|PubMed:12354939}.
uniprot
proteins
protein_family
HD type 2 subfamily
uniprot
proteins
protein_family
Histone deacetylase family
uniprot
proteins
pubmed
10220385
uniprot
proteins
pubmed
10898795
uniprot
proteins
pubmed
11018260
uniprot
proteins
pubmed
11081517
uniprot
proteins
pubmed
11114197
uniprot
proteins
pubmed
11509672
uniprot
proteins
pubmed
12168954
uniprot
proteins
pubmed
12354939
uniprot
proteins
pubmed
12504096
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16625196
uniprot
proteins
pubmed
17373667
uniprot
proteins
pubmed
17872950
uniprot
proteins
pubmed
18184930
uniprot
proteins
pubmed
18332134
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19666599
uniprot
proteins
pubmed
20188095
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22649097
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24413532
uniprot
proteins
pubmed
25752541
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
28167758
uniprot
proteins
pubmed
9610721
uniprot
proteins
pubmed
9628581
uniprot
proteins
sequence_length
1122
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Shuttles between the nucleus and the cytoplasm. In muscle cells, it shuttles into the cytoplasm during myocyte differentiation. The export to cytoplasm depends on the interaction with a 14-3-3 chaperone protein and is due to its phosphorylation at Ser-259 and Ser-498 by AMPK, CaMK1 and SIK1.
uniprot
proteins