Hdac7
entrez
56233
canonical
uniprot
Q8C2B3
canonical
ensembl
ENSMUSG00000022475
resolver
ensp
ENSMUSP00000078766
resolver
ensp
ENSMUSP00000085744
resolver
ensp
ENSMUSP00000112109
resolver
ensp
ENSMUSP00000112110
resolver
ensp
ENSMUSP00000112446
resolver
ensp
ENSMUSP00000112459
resolver
ensp
ENSMUSP00000112641
resolver
ensp
ENSMUSP00000113380
resolver
ensp
ENSMUSP00000199197
resolver
ensp
ENSMUSP00000199198
resolver
enst
ENSMUST00000119670
resolver
enst
ENSMUST00000120683
resolver
enst
ENSMUST00000121514
resolver
genesymbol
Hdac7
resolver
genesymbol_syn
Hdac7a
resolver
uniprot
E9PX62
resolver
uniprot
E9PXW1
resolver
uniprot
E9PXW8
resolver
uniprot
Q8C2C9
resolver
uniprot
Q8C8X4
resolver
uniprot
Q8CB80
resolver
uniprot
Q8CDA3
resolver
uniprot
Q9JL72
resolver
uniprot_entry
E9PX62_MOUSE
resolver
uniprot_entry
E9PXW1_MOUSE
resolver
uniprot_entry
E9PXW8_MOUSE
resolver
uniprot_entry
HDAC7_MOUSE
resolver
uniprot_sec
Q8C2C9
resolver
uniprot_sec
Q8C8X4
resolver
uniprot_sec
Q8CB80
resolver
uniprot_sec
Q8CDA3
resolver
uniprot_sec
Q9JL72
resolver
activity_regulation
ACTIVITY REGULATION: Its activity is inhibited by Trichostatin A (TSA), a known histone deacetylase inhibitor. {ECO:0000269|PubMed:10640276}.
uniprot
proteins
amino_acid_sequence
MHSPGAGCPALQPDTPGSQPQPMDLRVGQRPTVEPPPEPALLTLQHPQRLHRHLFLAGLHQQQRSAEPMRLSMDPPMPELQGGQQEQELRQLLNKDKSKRSAVASSVVKQKLAEVILKKQQAALERTVHPSSPSIPYRTLEPLDTEGAARSVLSSFLPPVPSLPTEPPEHFPLRKTVSEPNLKLRYKPKKSLERRKNPLLRKESAPPSLRRRPAETLGDSSPSSSSTPASGCSSPNDSEHGPNPALGSEADGDRRTHSTLGPRGPVLGNPHAPLFLHHGLEPEAGGTLPSRLQPILLLDPSVSHAPLWTVPGLGPLPFHFAQPLLTTERLSGSGLHRPLNRTRSEPLPPSATASPLLAPLQPRQDRLKPHVQLIKPAISPPQRPAKPSEKPRLRQIPSAEDLETDGGGVGPMANDGLEHRESGRGPPEGRGSISLQQHQQVPPWEQQHLAGRLSQGSPGDSVLIPLAQVGHRPLSRTQSSPAAPVSLLSPEPTCQTQVLNSSETPATGLVYDSVMLKHQCSCGDNSKHPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVLLYGTNPLSRLKLDNGKLTGLLAQRTFVMLPCGGVGVDTDTIWNELHSSNAARWAAGSVTDLAFKVASRELKNGFAVVRPPGHHADHSTAMGFCFFNSVAIACRQLQQHGKASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHDDGNFFPGSGAVDEVGTGSGEGFNVNVAWAGGLDPPMGDPEYLAAFRIVVMPIAREFAPDLVLVSAGFDAAEGHPAPLGGYHVSAKCFGYMTQQLMNLAGGAVVLALEGGHDLTAICDASEACVAALLGNKVDPLSEESWKQKPNLSAIRSLEAVVRVHRKYWGCMQRLASCPDSWLPRVPGADAEVEAVTALASLSVGILAEDRPSERLVEEEEPMNL
uniprot
proteins
ec_number
3.5.1.-
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) (PubMed:10640276, PubMed:10984530, PubMed:11279209). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events (PubMed:10640276, PubMed:10984530, PubMed:11279209). Histone deacetylases act via the formation of large multiprotein complexes (PubMed:10640276, PubMed:10984530, PubMed:11279209). Involved in muscle maturation by repressing transcription of myocyte enhancer factors such as MEF2A, MEF2B and MEF2C (PubMed:11279209). During muscle differentiation, it shuttles into the cytoplasm, allowing the expression of myocyte enhancer factors (PubMed:11279209). Positively regulates the transcriptional repressor activity of FOXP3 (By similarity). Serves as a corepressor of RARA, causing its deacetylation and inhibition of RARE DNA element binding (By similarity). In association with RARA, plays a role in the repression of microRNA-10a and thereby in the inflammatory response (By similarity). Also acetylates non-histone proteins, such as ALKBH5 (By similarity). {ECO:0000250|UniProtKB:Q8WUI4, ECO:0000269|PubMed:10640276, ECO:0000269|PubMed:10984530, ECO:0000269|PubMed:11279209}.
uniprot
proteins
mass_dalton
101287
uniprot
proteins
mutagenesis
MUTAGEN 178; /note="S->A: Strong reduction of CaMK1-dependent nuclear export. Reduces interaction with YWHAE."; /evidence="ECO:0000269|PubMed:11585834"; MUTAGEN 344; /note="S->A: Strong reduction of CaMK1-dependent nuclear export. Reduces interaction with YWHAE."; /evidence="ECO:0000269|PubMed:11585834"; MUTAGEN 479; /note="S->A: Strong reduction of CaMK1-dependent nuclear export. Reduces interaction with YWHAE."; /evidence="ECO:0000269|PubMed:11585834"; MUTAGEN 657; /note="H->A: Abolishes deacetylase activity, but not the interaction with HDAC2 and HDAC3."; /evidence="ECO:0000269|PubMed:10984530, ECO:0000269|PubMed:11279209"; MUTAGEN 692; /note="D->A: Disrupts the dot-like nuclear pattern."; /evidence="ECO:0000269|PubMed:10984530"; MUTAGEN 694; /note="D->A: Disrupts the dot-like nuclear pattern. Abolishes deacetylase activity, but not the interaction with HDAC2 and HDAC3."; /evidence="ECO:0000269|PubMed:10984530"; MUTAGEN 717; /note="H->A: Abolishes deacetylase activity, but not the interaction with HDAC2 and HDAC3."; /evidence="ECO:0000269|PubMed:10984530
uniprot
proteins
post_translational_modification
PTM: May be phosphorylated by CaMK1. Phosphorylated by the PKC kinases PKN1 and PKN2, impairing nuclear import. Phosphorylation at Ser-178 by MARK2, MARK3 and PRKD1 promotes interaction with 14-3-3 proteins and export from the nucleus. Phosphorylation at Ser-178 is a prerequisite for phosphorylation at Ser-204 (By similarity). {ECO:0000250|UniProtKB:Q8WUI4}.
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
11279209
uniprot
proteins
pubmed
11509672
uniprot
proteins
pubmed
11585834
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
18509061
uniprot
proteins
pubmed
19131326
uniprot
proteins
pubmed
19696312
uniprot
proteins
pubmed
20675388
uniprot
proteins
pubmed
21183079
uniprot
proteins
sequence_length
938
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10640276, ECO:0000269|PubMed:11279209, ECO:0000269|PubMed:11585834}. Cytoplasm {ECO:0000269|PubMed:11279209, ECO:0000269|PubMed:11585834}. Note=In the nucleus, it associates with distinct subnuclear dot-like structures (PubMed:10640276). Shuttles between the nucleus and the cytoplasm (PubMed:11279209, PubMed:11585834). In muscle cells, it shuttles into the cytoplasm during myocyte differentiation (PubMed:11279209). The export to cytoplasm depends on the interaction with the 14-3-3 protein YWHAE and is due to its phosphorylation (PubMed:11585834). {ECO:0000269|PubMed:10640276, ECO:0000269|PubMed:11279209, ECO:0000269|PubMed:11585834}.
uniprot
proteins