Hdac4
entrez
208727
canonical
uniprot
Q6NZM9
canonical
ensembl
ENSMUSG00000026313
resolver
ensp
ENSMUSP00000095249
resolver
ensp
ENSMUSP00000281295
resolver
genesymbol
Hdac4
resolver
uniprot
Q3TRZ9
resolver
uniprot
Q3U2J3
resolver
uniprot
Q3V3Y4
resolver
uniprot_entry
HDAC4_MOUSE
resolver
uniprot_sec
Q3TRZ9
resolver
uniprot_sec
Q3U2J3
resolver
uniprot_sec
Q3V3Y4
resolver
amino_acid_sequence
MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPTAVPMDLRLDHQFSLPLEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSASYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVATALKKRPLDVTDSACSSAPGSGPSSPNSSSGNVSTENGIAPTVPSAPAETSLAHRLVTREGSVAPLPLYTSPSLPNITLGLPATGPAAGAAGQQDAERLALPALQQRILFPGTHLTPYLSTSPLERDGAAAHNPLLQHMVLLEQPPTQTPLVTGLGALPLHSQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLHLSKIISKPSEPPRQPESHPEETEEELREHQALLDEPYLDRLPGQKEPSLAGVQVKQEPIESEEEEAEATRETEPGQRPATEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGSHRPLSRAQSSPASATFPMSVQEPPTKPRFTTGLVYDTLMLKHQCTCGNTNSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSSLTSVFVRLPCGGVGVDSDTIWNEVHSSGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLNVSKILIVDWDVHHGNGTQQAFYNDPNVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLEPPMGDAEYLAAFRTVVMPIANEFAPDVVLVSSGFDAVEGHPTPLGGYNLSAKCFGYLTKQLMGLAGGRLVLALEGGHDLTAICDASEACVSALLGNELEPLPEKVLHQRPNANAVHSMEKVMDIHSKYWRCLQRLSSTVGHSLIEAQKCEKEEAETVTAMASLSVGVKPAEKRSEEEPMEEEPPL
uniprot
proteins
ec_number
3.5.1.98
uniprot
proteins
function
FUNCTION: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). 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 via its interaction with the myocyte enhancer factors such as MEF2A, MEF2C and MEF2D. Deacetylates HSPA1A and HSPA1A at 'Lys-77' leading to their preferential binding to co-chaperone STUB1. {ECO:0000250|UniProtKB:P56524}.
uniprot
proteins
mass_dalton
118562
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by CaMK4 at Ser-245, Ser-465 and Ser-629. Phosphorylation at other residues by CaMK2D is required for the interaction with 14-3-3. Phosphorylation at Ser-349, within the PxLPxI/L motif, impairs the binding of ANKRA2 but generates a high-affinity docking site for 14-3-3 (By similarity). {ECO:0000250|UniProtKB:P56524}.; PTM: Sumoylation on Lys-556 is promoted by the E3 SUMO-protein ligase RANBP2, and prevented by phosphorylation by CaMK4. {ECO:0000269|PubMed:17468767, ECO:0000269|PubMed:17923476}.
uniprot
proteins
protein_family
HD type 2 subfamily
uniprot
proteins
protein_family
Histone deacetylase family
uniprot
proteins
pubmed
10984530
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15601857
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17468767
uniprot
proteins
pubmed
17923476
uniprot
proteins
pubmed
17949687
uniprot
proteins
pubmed
19131326
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21590736
uniprot
proteins
pubmed
22318228
uniprot
proteins
pubmed
22730529
uniprot
proteins
sequence_length
1076
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22318228}. Cytoplasm {ECO:0000269|PubMed:22318228}. Note=Shuttles between the nucleus and the cytoplasm. Upon muscle cells differentiation, it accumulates in the nuclei of myotubes, suggesting a positive role of nuclear HDAC4 in muscle differentiation. The export to cytoplasm depends on the interaction with a 14-3-3 chaperone protein and is due to its phosphorylation at Ser-245, Ser-465 and Ser-629 by CaMK4 and SIK1. The nuclear localization probably depends on sumoylation (By similarity). Interaction with SIK3 leads to HDAC4 retention in the cytoplasm (PubMed:22318228). {ECO:0000250, ECO:0000269|PubMed:22318228}.
uniprot
proteins