Hdac1
entrez
433759
canonical
uniprot
O09106
canonical
ensembl
ENSMUSG00000028800
resolver
ensp
ENSMUSP00000099657
resolver
enst
ENSMUST00000102597
resolver
genesymbol
Hdac1
resolver
uniprot
P97476
resolver
uniprot
Q58E49
resolver
uniprot_entry
HDAC1_MOUSE
resolver
uniprot_entry
Q58E49_MOUSE
resolver
uniprot_sec
P97476
resolver
activity_regulation
ACTIVITY REGULATION: Inositol tetraphosphate (1D-myo-inositol 1,4,5,6-tetrakisphosphate) may act as an intermolecular glue between HDAC1 and N-Cor repressor complex components. {ECO:0000250|UniProtKB:O15379}.
uniprot
proteins
amino_acid_sequence
MAQTQGTKRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEEDPDKRISICSSDKRIACEEEFSDSDEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA
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:10615135, PubMed:15542849, PubMed:21960634, PubMed:30279482). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events (PubMed:10615135, PubMed:15542849, PubMed:21960634). Histone deacetylases act via the formation of large multiprotein complexes (PubMed:10615135, PubMed:21960634). Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin (By similarity). As part of the SIN3B complex is recruited downstream of the constitutively active genes transcriptional start sites through interaction with histones and mitigates histone acetylation and RNA polymerase II progression within transcribed regions contributing to the regulation of transcription (By similarity). Also functions as a deacetylase for non-histone targets, such as NR1D2, RELA, SP1, SP3, STAT3, ZNF76 and TSHZ3 (By similarity). Deacetylates SP proteins, SP1 and SP3, and regulates their function (By similarity). Component of the BRG1-RB1-HDAC1 complex, which negatively regulates the CREST-mediated transcription in resting neurons (By similarity). Upon calcium stimulation, HDAC1 is released from the complex and CREBBP is recruited, which facilitates transcriptional activation (By similarity). Deacetylates TSHZ3 and regulates its transcriptional repressor activity (By similarity). Deacetylates 'Lys-310' in RELA and thereby inhibits the transcriptional activity of NF-kappa-B (By similarity). Deacetylates NR1D2 and abrogates the effect of KAT5-mediated relieving of NR1D2 transcription repression activity (By similarity). Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development (PubMed:17707228). Involved in CIART-mediated transcriptional repression of the circadian transcriptional activator: CLOCK-BMAL1 heterodimer (PubMed:15226430, PubMed:24736997). Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex or CRY1 through histone deacetylation (PubMed:15226430). In addition to protein deacetylase activity, also has protein-lysine deacylase activity: acts as a protein decrotonylase and delactylase by mediating decrotonylation ((2E)-butenoyl) and delactylation (lactoyl) of histones, respectively (PubMed:30279482). {ECO:0000250|UniProtKB:Q13547, ECO:0000269|PubMed:10615135, ECO:0000269|PubMed:15226430, ECO:0000269|PubMed:15542849, ECO:0000269|PubMed:17707228, ECO:0000269|PubMed:21960634, ECO:0000269|PubMed:24736997, ECO:0000269|PubMed:30279482}.
uniprot
proteins
mass_dalton
55075
uniprot
proteins
post_translational_modification
PTM: Sumoylated on Lys-444 and Lys-476; which promotes enzymatic activity. Desumoylated by SENP1. {ECO:0000250|UniProtKB:Q13547}.; PTM: Phosphorylation on Ser-421 and Ser-423 promotes enzymatic activity and interactions with NuRD and SIN3 complexes. Phosphorylated by CDK5. {ECO:0000250|UniProtKB:Q13547}.; PTM: Ubiquitinated by CHFR and KCTD11, leading to its degradation by the proteasome. {ECO:0000250|UniProtKB:Q13547}.
uniprot
proteins
protein_family
HD type 1 subfamily
uniprot
proteins
protein_family
Histone deacetylase family
uniprot
proteins
pubmed
10615135
uniprot
proteins
pubmed
10984530
uniprot
proteins
pubmed
11022042
uniprot
proteins
pubmed
11115394
uniprot
proteins
pubmed
11533236
uniprot
proteins
pubmed
11788710
uniprot
proteins
pubmed
11909966
uniprot
proteins
pubmed
12198165
uniprot
proteins
pubmed
12398767
uniprot
proteins
pubmed
12616525
uniprot
proteins
pubmed
14645126
uniprot
proteins
pubmed
15060175
uniprot
proteins
pubmed
15140878
uniprot
proteins
pubmed
15226430
uniprot
proteins
pubmed
15542849
uniprot
proteins
pubmed
15711539
uniprot
proteins
pubmed
16085498
uniprot
proteins
pubmed
16107708
uniprot
proteins
pubmed
16166625
uniprot
proteins
pubmed
16537907
uniprot
proteins
pubmed
16611996
uniprot
proteins
pubmed
16805913
uniprot
proteins
pubmed
17707228
uniprot
proteins
pubmed
18849567
uniprot
proteins
pubmed
19144721
uniprot
proteins
pubmed
19483677
uniprot
proteins
pubmed
19501046
uniprot
proteins
pubmed
20124407
uniprot
proteins
pubmed
20154723
uniprot
proteins
pubmed
20478393
uniprot
proteins
pubmed
20675388
uniprot
proteins
pubmed
21177534
uniprot
proteins
pubmed
21454521
uniprot
proteins
pubmed
21937600
uniprot
proteins
pubmed
21960634
uniprot
proteins
pubmed
22242125
uniprot
proteins
pubmed
24227653
uniprot
proteins
pubmed
24413057
uniprot
proteins
pubmed
24736997
uniprot
proteins
pubmed
27806305
uniprot
proteins
pubmed
28554894
uniprot
proteins
pubmed
30228260
uniprot
proteins
pubmed
30279482
uniprot
proteins
pubmed
33831416
uniprot
proteins
pubmed
34075040
uniprot
proteins
pubmed
34180153
uniprot
proteins
pubmed
35341968
uniprot
proteins
pubmed
9271381
uniprot
proteins
pubmed
9702189
uniprot
proteins
sequence_length
482
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11115394, ECO:0000269|PubMed:21454521}.
uniprot
proteins