Q9Z2V6
uniprot
Q9Z2V6
canonical
activity_regulation
ACTIVITY REGULATION: Inhibited by trichostatin A. {ECO:0000269|PubMed:9891014}.
uniprot
proteins
amino_acid_sequence
MNSPNESDGMSGREPSLGILPRTPLHSIPVAVEVKPVLPGAMPSSMGGGGGGSPSPVELRGALAGPMDPALREQQLQQELLVLKQQQQLQKQLLFAEFQKQHDHLTRQHEVQLQKHLKQQQEMLAAKRQQELEQQRQREQQRQEELEKQRLEQQLLILRNKEKSKESAIASTEVKLRLQEFLLSKSKEPTPGGLNHSLPQHPKCWGAHHASLDQSSPPQSGPPGTPPSYKLPLLGPYDSRDDFPLRKTASEPNLKVRSRLKQKVAERRSSPLLRRKDGTVISTFKKRAVEITGTGPGVSSVCNSAPGSGPSSPNSSHSTIAENGFTGSVPNIPTEMIPQHRALPLDSSPNQFSLYTSPSLPNISLGLQATVTVTNSHLTASPKLSTQQEAERQALQSLRQGGTLTGKFMSTSSIPGCLLGVALEGDTSPHGHASLLQHVCSWTGRQQSTLIAVPLHGQSPLVTGERVATSMRTVGKLPRHRPLSRTQSSPLPQSPQALQQLVMQQQHQQFLEKQKQQQMQLGKILTKTGELSRQPTTHPEETEEELTEQQEALLGEGALTIPREGSTESESTQEDLEEEEEEEEEEEEDCIQVKDEDGESGPDEGPDLEESSAGYKKLFADAQQLQPLQVYQAPLSLATVPHQALGRTQSSPAAPGSMKSPTDQPTVVKHLFTTGVVYDTFMLKHQCMCGNTHVHPEHAGRIQSIWSRLQETGLLGKCERIRGRKATLDEIQTVHSEYHTLLYGTSPLNRQKLDSKKLLGPISQKMYAMLPCGGIGVDSDTVWNEMHSSSAVRMAVGCLVELAFKVAAGELKNGFAIIRPPGHHAEESTAMGFCFFNSVAITAKLLQQKLSVGKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYDNGNFFPGSGAPEEVGGGPGVGYNVNVAWTGGVDPPIGDVEYLTAFRTVVMPIAQEFSPDVVLVSAGFDAVEGHLSPLGGYSVTARCFGHLTRQLMTLAGGRVVLALEGGHDLTAICDASEACVSALLSVELQPLDEAVLQQKPSVNAVATLEKVIEIQSKHWSCVQRFAAGLGCSLREAQTGEKEEAETVSAMALLSVGAEQAQAVATQEHSPRPAEEPMEQEPAL
uniprot
proteins
ec_number
3.5.1.98
uniprot
proteins
function
FUNCTION: In vitro, it deacetylates core histones (PubMed:10984530, PubMed:9891014). Deacetylates lysine residues on the N-terminal part of the histones H2A, H2B, H3 and H4 (By similarity). 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 (By similarity). Serves as a corepressor of RARA and causes its deacetylation (By similarity). In association with RARA, plays a role in the repression of microRNA-10a and thereby in the inflammatory response (By similarity). {ECO:0000250|UniProtKB:Q9UQL6, ECO:0000269|PubMed:10984530, ECO:0000269|PubMed:9891014}.
uniprot
proteins
mass_dalton
120942
uniprot
proteins
mutagenesis
MUTAGEN 250; /note="S->A: Abolishes phosphorylation by SIK1 and fails to promote beta-catenin expression; when associated with A-488."; /evidence="ECO:0000269|PubMed:17468767, ECO:0000269|PubMed:21454484"; MUTAGEN 488; /note="S->A: Abolishes phosphorylation by SIK1 and fails to promote beta-catenin expression; when associated with A-250."; /evidence="ECO:0000269|PubMed:17468767, ECO:0000269|PubMed:21454484"; MUTAGEN 824; /note="H->A: Abolishes deacetylase activity."; /evidence="ECO:0000269|PubMed:10984530"; MUTAGEN 884; /note="H->F: Abolishes deacetylase activity. Disrupts the dot-like nuclear pattern."; /evidence="ECO:0000269|PubMed:10984530
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by AMPK, CaMK1, SIK1 and PRKD1 at Ser-250 and Ser-488. The phosphorylation is required for the export to the cytoplasm and inhibition. Phosphorylated by the PKC kinases PKN1 and PKN2, impairing nuclear import (By similarity). Phosphorylated by GRK5, leading to nuclear export of HDAC5 and allowing MEF2-mediated transcription. {ECO:0000250, ECO:0000269|PubMed:17468767, ECO:0000269|PubMed:18711143, ECO:0000269|PubMed:21454484}.; PTM: Ubiquitinated. Polyubiquitination however does not lead to its degradation (By similarity). {ECO:0000250}.
uniprot
proteins
protein_family
HD type 2 subfamily
uniprot
proteins
protein_family
Histone deacetylase family
uniprot
proteins
pubmed
10640276
uniprot
proteins
pubmed
10984530
uniprot
proteins
pubmed
11022042
uniprot
proteins
pubmed
15060175
uniprot
proteins
pubmed
15140878
uniprot
proteins
pubmed
15601857
uniprot
proteins
pubmed
17468767
uniprot
proteins
pubmed
17949687
uniprot
proteins
pubmed
18711143
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21454484
uniprot
proteins
pubmed
22730529
uniprot
proteins
pubmed
9891014
uniprot
proteins
sequence_length
1113
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-250 and Ser-488 by AMPK, CaMK1 and SIK1.
uniprot
proteins