HDAC1
entrez
3065
canonical
uniprot
Q13547
canonical
ensembl
ENSG00000116478
resolver
ensp
ENSP00000362649
resolver
enst
ENST00000373548
resolver
genesymbol
HDAC1
resolver
genesymbol_syn
RPD3L1
resolver
hgnc
HGNC:4852
resolver
uniprot
D3DPP9
resolver
uniprot
Q6IT96
resolver
uniprot
Q92534
resolver
uniprot_entry
HDAC1_HUMAN
resolver
uniprot_entry
Q6IT96_HUMAN
resolver
uniprot_sec
D3DPP9
resolver
uniprot_sec
Q92534
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
MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA
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:16762839, PubMed:17704056, PubMed:28497810). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events (PubMed:16762839, PubMed:17704056). Histone deacetylases act via the formation of large multiprotein complexes (PubMed:16762839, PubMed:17704056). Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin (PubMed:16428440, PubMed:28977666). 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 (PubMed:21041482). Also functions as a deacetylase for non-histone targets, such as NR1D2, RELA, SP1, SP3, STAT3, ZNF76 and TSHZ3 (PubMed:12837748, PubMed:16285960, PubMed:16337145, PubMed:16478997, PubMed:17996965, PubMed:19343227). Deacetylates SP proteins, SP1 and SP3, and regulates their function (PubMed:12837748, PubMed:16478997). Component of the BRG1-RB1-HDAC1 complex, which negatively regulates the CREST-mediated transcription in resting neurons (PubMed:19081374). Upon calcium stimulation, HDAC1 is released from the complex and CREBBP is recruited, which facilitates transcriptional activation (PubMed:19081374). Deacetylates TSHZ3 and regulates its transcriptional repressor activity (PubMed:19343227). Deacetylates 'Lys-310' in RELA and thereby inhibits the transcriptional activity of NF-kappa-B (PubMed:17000776). Deacetylates NR1D2 and abrogates the effect of KAT5-mediated relieving of NR1D2 transcription repression activity (PubMed:17996965). 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 (By similarity). Involved in CIART-mediated transcriptional repression of the circadian transcriptional activator: CLOCK-BMAL1 heterodimer (By similarity). Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex or CRY1 through histone deacetylation (By similarity). 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:28497810, PubMed:35044827). {ECO:0000250|UniProtKB:O09106, ECO:0000269|PubMed:12837748, ECO:0000269|PubMed:16285960, ECO:0000269|PubMed:16337145, ECO:0000269|PubMed:16428440, ECO:0000269|PubMed:16478997, ECO:0000269|PubMed:16762839, ECO:0000269|PubMed:17000776, ECO:0000269|PubMed:17704056, ECO:0000269|PubMed:17996965, ECO:0000269|PubMed:19081374, ECO:0000269|PubMed:19343227, ECO:0000269|PubMed:21041482, ECO:0000269|PubMed:28497810, ECO:0000269|PubMed:28977666, ECO:0000269|PubMed:35044827}.
uniprot
proteins
mass_dalton
55103
uniprot
proteins
mutagenesis
MUTAGEN 136..138; /note="AGG->VRPP: Impaired protein deacetylase activity without affecting the protein decrotonylase activity."; /evidence="ECO:0000269|PubMed:28497810"; MUTAGEN 141; /note="H->A: Abolishes histone deacetylase and decrotonylase activities."; /evidence="ECO:0000269|PubMed:19182791, ECO:0000269|PubMed:28497810"; MUTAGEN 287; /note="F->Y: Abolishes interaction with CHFR; when associated with I-297."; /evidence="ECO:0000269|PubMed:19182791"; MUTAGEN 297; /note="M->I: Abolishes interaction with CHFR; when associated with Y-287."; /evidence="ECO:0000269|PubMed:19182791"; MUTAGEN 391..482; /note="Missing: Strongly decreases deacetylase activity, and disrupts interaction with NuRD and SIN3 complexes."; MUTAGEN 421; /note="S->A: Strongly decreases deacetylase activity, and disrupts interaction with NuRD and SIN3 complexes."; /evidence="ECO:0000269|PubMed:11602581"; MUTAGEN 421; /note="S->D,E: Slightly decreases deacetylase activity."; /evidence="ECO:0000269|PubMed:11602581"; MUTAGEN 423; /note="S->A: Strongly decreases deacetylase activity, and disrupts interaction with NuRD and SIN3 complexes."; /evidence="ECO:0000269|PubMed:11602581"; MUTAGEN 423; /note="S->D,E: Decreases deacetylase activity."; /evidence="ECO:0000269|PubMed:11602581"; MUTAGEN 424..426; /note="EEE->AEA: Abolished histone deacetylase and decrotonylase activities."; /evidence="ECO:0000269|PubMed:28497810"; MUTAGEN 424; /note="E->A: Slightly decreases deacetylase activity, no effect on interaction with NuRD and SIN3 complexes."; /evidence="ECO:0000269|PubMed:11602581"; MUTAGEN 425; /note="E->A: No effect on deacetylase activity, no effect on interaction with NuRD and SIN3 complexes."; /evidence="ECO:0000269|PubMed:11602581"; MUTAGEN 426; /note="E->A: Decreases deacetylase activity, and disrupts interaction with NuRD and SIN3 complexes."; /evidence="ECO:0000269|PubMed:11602581
uniprot
proteins
post_translational_modification
PTM: Sumoylated on Lys-444 and Lys-476; which promotes enzymatic activity. Desumoylated by SENP1. {ECO:0000269|PubMed:11960997, ECO:0000269|PubMed:12032081, ECO:0000269|PubMed:15199155}.; PTM: Phosphorylation on Ser-421 and Ser-423 promotes enzymatic activity and interactions with NuRD and SIN3 complexes. Phosphorylated by CDK5. {ECO:0000269|PubMed:11602581}.; PTM: Ubiquitinated by CHFR, leading to its degradation by the proteasome. Ubiquitinated by KCTD11, leading to proteasomal degradation. {ECO:0000269|PubMed:19182791, ECO:0000269|PubMed:20081843}.
uniprot
proteins
protein_family
HD type 1 subfamily
uniprot
proteins
protein_family
Histone deacetylase family
uniprot
proteins
pubmed
10487760
uniprot
proteins
pubmed
10655483
uniprot
proteins
pubmed
10669754
uniprot
proteins
pubmed
10846170
uniprot
proteins
pubmed
10898795
uniprot
proteins
pubmed
10904264
uniprot
proteins
pubmed
11006275
uniprot
proteins
pubmed
11102443
uniprot
proteins
pubmed
11331609
uniprot
proteins
pubmed
11427533
uniprot
proteins
pubmed
11533236
uniprot
proteins
pubmed
11602581
uniprot
proteins
pubmed
11960997
uniprot
proteins
pubmed
12032081
uniprot
proteins
pubmed
12482978
uniprot
proteins
pubmed
12493763
uniprot
proteins
pubmed
12670868
uniprot
proteins
pubmed
12724404
uniprot
proteins
pubmed
12730668
uniprot
proteins
pubmed
12837748
uniprot
proteins
pubmed
14633989
uniprot
proteins
pubmed
15199155
uniprot
proteins
pubmed
15273251
uniprot
proteins
pubmed
15361834
uniprot
proteins
pubmed
15451426
uniprot
proteins
pubmed
15454082
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15701600
uniprot
proteins
pubmed
15927959
uniprot
proteins
pubmed
16166625
uniprot
proteins
pubmed
16285960
uniprot
proteins
pubmed
16337145
uniprot
proteins
pubmed
16428440
uniprot
proteins
pubmed
16478997
uniprot
proteins
pubmed
16569215
uniprot
proteins
pubmed
16762839
uniprot
proteins
pubmed
16820529
uniprot
proteins
pubmed
17000776
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17341466
uniprot
proteins
pubmed
17369852
uniprot
proteins
pubmed
17373667
uniprot
proteins
pubmed
17487921
uniprot
proteins
pubmed
17548428
uniprot
proteins
pubmed
17704056
uniprot
proteins
pubmed
17872950
uniprot
proteins
pubmed
17963697
uniprot
proteins
pubmed
17996965
uniprot
proteins
pubmed
18093978
uniprot
proteins
pubmed
18279852
uniprot
proteins
pubmed
18318008
uniprot
proteins
pubmed
18438403
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19049980
uniprot
proteins
pubmed
19061646
uniprot
proteins
pubmed
19081374
uniprot
proteins
pubmed
19182791
uniprot
proteins
pubmed
19343227
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19433865
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
19729656
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20081843
uniprot
proteins
pubmed
20523938
uniprot
proteins
pubmed
21030595
uniprot
proteins
pubmed
21041482
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21549307
uniprot
proteins
pubmed
21829689
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25218447
uniprot
proteins
pubmed
25514493
uniprot
proteins
pubmed
25593309
uniprot
proteins
pubmed
25653165
uniprot
proteins
pubmed
25755297
uniprot
proteins
pubmed
25772364
uniprot
proteins
pubmed
26030138
uniprot
proteins
pubmed
27616479
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
28497810
uniprot
proteins
pubmed
28977666
uniprot
proteins
pubmed
29656858
uniprot
proteins
pubmed
30110327
uniprot
proteins
pubmed
30487602
uniprot
proteins
pubmed
33283408
uniprot
proteins
pubmed
35044827
uniprot
proteins
pubmed
36064715
uniprot
proteins
pubmed
37179361
uniprot
proteins
pubmed
8602529
uniprot
proteins
pubmed
8646880
uniprot
proteins
sequence_length
482
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10846170, ECO:0000269|PubMed:20523938, ECO:0000269|PubMed:28977666, ECO:0000269|PubMed:33283408}.
uniprot
proteins