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MGP001427

UniProt Annotations

Entry Information
Gene Namehistone deacetylase 1
Protein EntryHDAC1_HUMAN
UniProt IDQ13547
SpeciesHuman
Comments
Comment typeDescription
Catalytic ActivityHydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone.
FunctionResponsible 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. Deacetylates SP proteins, SP1 and SP3, and regulates their function. Component of the BRG1-RB1-HDAC1 complex, which negatively regulates the CREST- mediated transcription in resting neurons. Upon calcium stimulation, HDAC1 is released from the complex and CREBBP is recruited, which facilitates transcriptional activation. Deacetylates TSHZ3 and regulates its transcriptional repressor activity. Deacetylates 'Lys-310' in RELA and thereby inhibits the transcriptional activity of NF-kappa-B. Deacetylates NR1D2 and abrogates the effect of KAT5-mediated relieving of NR1D2 transcription repression activity. 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. Involved in CIART-mediated transcriptional repression of the circadian transcriptional activator: CLOCK-ARNTL/BMAL1 heterodimer. Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex or CRY1 through histone deacetylation. {ECO:0000269|PubMed:12837748, ECO:0000269|PubMed:16478997, ECO:0000269|PubMed:17000776, ECO:0000269|PubMed:17704056, ECO:0000269|PubMed:17996965, ECO:0000269|PubMed:19081374, ECO:0000269|PubMed:19343227}.
InteractionQ9UKG1:APPL1; NbExp=2; IntAct=EBI-301834, EBI-741243; Q14865:ARID5B; NbExp=4; IntAct=EBI-301834, EBI-1210388; Q9C0K0:BCL11B; NbExp=3; IntAct=EBI-301834, EBI-6597578; Q9HCU9:BRMS1; NbExp=4; IntAct=EBI-301834, EBI-714781; Q6PH81:C16orf87; NbExp=3; IntAct=EBI-301834, EBI-6598617; Q14839:CHD4; NbExp=6; IntAct=EBI-301834, EBI-372916; P68400:CSNK2A1; NbExp=2; IntAct=EBI-301834, EBI-347804; Q9UER7:DAXX; NbExp=2; IntAct=EBI-301834, EBI-77321; Q92841-4:DDX17; NbExp=3; IntAct=EBI-301834, EBI-5280703; P17844:DDX5; NbExp=4; IntAct=EBI-301834, EBI-351962; Q7L2E3:DHX30; NbExp=3; IntAct=EBI-301834, EBI-1211456; Q9UJW3:DNMT3L; NbExp=3; IntAct=EBI-301834, EBI-740967; Q66K89:E4F1; NbExp=3; IntAct=EBI-301834, EBI-1227043; Q96KQ7:EHMT2; NbExp=3; IntAct=EBI-301834, EBI-744366; Q8N140:EID3; NbExp=2; IntAct=EBI-301834, EBI-744483; Q9NP50:FAM60A; NbExp=4; IntAct=EBI-301834, EBI-741906; Q99684:GFI1; NbExp=4; IntAct=EBI-301834, EBI-949368; P51610:HCFC1; NbExp=2; IntAct=EBI-301834, EBI-396176; Q92769:HDAC2; NbExp=10; IntAct=EBI-301834, EBI-301821; P62805:HIST2H4B; NbExp=2; IntAct=EBI-301834, EBI-302023; P43355:MAGEA1; NbExp=2; IntAct=EBI-301834, EBI-740978; Q9UIS9:MBD1; NbExp=2; IntAct=EBI-301834, EBI-867196; Q8N108:MIER1; NbExp=7; IntAct=EBI-301834, EBI-3504940; Q13330:MTA1; NbExp=4; IntAct=EBI-301834, EBI-714236; Q9Y618:NCOR2; NbExp=2; IntAct=EBI-301834, EBI-80830; P19838:NFKB1; NbExp=5; IntAct=EBI-301834, EBI-300010; P06748:NPM1; NbExp=2; IntAct=EBI-301834, EBI-78579; Q9Y5X4:NR2E3; NbExp=2; IntAct=EBI-301834, EBI-7216962; Q9NQX1:PRDM5; NbExp=3; IntAct=EBI-301834, EBI-4292031; Q96N64:PWWP2A; NbExp=4; IntAct=EBI-301834, EBI-6597774; P06400:RB1; NbExp=4; IntAct=EBI-301834, EBI-491274; Q09028:RBBP4; NbExp=6; IntAct=EBI-301834, EBI-620823; Q16576:RBBP7; NbExp=5; IntAct=EBI-301834, EBI-352227; Q04206:RELA; NbExp=5; IntAct=EBI-301834, EBI-73886; O00422:SAP18; NbExp=2; IntAct=EBI-301834, EBI-1044156; O43463:SUV39H1; NbExp=3; IntAct=EBI-301834, EBI-349968; P04637:TP53; NbExp=7; IntAct=EBI-301834, EBI-366083;
PtmPhosphorylation on Ser-421 and Ser-423 promotes enzymatic activity and interactions with NuRD and SIN3 complexes. Phosphorylated by CDK5. {ECO:0000269|PubMed:11602581, ECO:0000269|PubMed:17081983, ECO:0000269|PubMed:17487921, ECO:0000269|PubMed:18318008, ECO:0000269|PubMed:18691976, ECO:0000269|PubMed:19690332, ECO:0000269|PubMed:20068231, ECO:0000269|PubMed:21406692}.
PtmSumoylated 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}.
PtmUbiquitinated by CHFR, leading to its degradation by the proteasome. Ubiquitinated by KCTD11, leading to proteasomal degradation. {ECO:0000269|PubMed:19182791, ECO:0000269|PubMed:20081843}.
SimilarityBelongs to the histone deacetylase family. HD type 1 subfamily. {ECO:0000305}.
Subcellular LocationNucleus.
SubunitPart of the core histone deacetylase (HDAC) complex composed of HDAC1, HDAC2, RBBP4 and RBBP7. The core complex associates with MTA2, MBD2, MBD3, MTA1L1, CHD3 and CHD4 to form the nucleosome remodeling and histone deacetylation (NuRD) complex, or with SIN3, SAP18 and SAP30 to form the SIN3 HDAC complex. Component of a BHC histone deacetylase complex that contains HDAC1, HDAC2, HMG20B/BRAF35, KDM1A, RCOR1/CoREST and PHF21A/BHC80. The BHC complex may also contain ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I. Component of a mSin3A corepressor complex that contains SIN3A, SAP130, SUDS3/SAP45, ARID4B/SAP180, HDAC1 and HDAC2. Found in a trimeric complex with APBB1 and TSHZ3; the interaction between HDAC1 and APBB1 is mediated by TSHZ3. Component of a RCOR/GFI/KDM1A/HDAC complex. Part of a complex composed of TRIM28, HDAC1, HDAC2 and EHMT2. Part of a complex containing at least CDYL, MIER1, MIER2, HDAC1 and HDAC2. The large PER complex involved in the histone deacetylation is composed of at least HDAC1, PER2, SFPQ and SIN3A. Associates with the 9-1-1 complex; interacts with HUS1. Found in a complex with DNMT3A and HDAC7. Interacts with the non-histone region of H2AFY. Interacts with TRIM28; the interaction recruits HDAC1 to E2F1 and inhibits its acetylation. Interacts with SP1; the interaction deacetylates SP1 and regulates its transcriptional activity. Interacts with SP3; the interaction deacetylates SP3 and regulates its transcriptional activity. In vitro, C(18) ceramides increase this interaction and the subsequent SP3 deacetylation and SP3-mediated repression of the TERT promoter. Interacts with TSHZ3 (via N- terminus); the interaction is direct. Interacts with APEX1; the interaction is not dependent on the acetylated status of APEX1. Interacts with C10orf90/FATS (via its N-terminal); the interaction prevents binding of HDAC1 to CDKN1A/p21 and facilitates the acetylation and stabilization of CDKN1A/p21. Interacts with CDKN1A/p21. Interacts with CDK5 complexed to CDK5R1 (p25). Interacts directly with GFI1 and GFI1B. Interacts with NR1D2 (via C-terminus). Interacts with TSC22D3 isoform 1; this interaction affects HDAC1 activity on MYOG promoter and thus inhibits MYOD1 transcriptional activity. Interacts with BAZ2A/TIP5, BANP, BCL6, BCOR, BHLHE40/DEC1, BRMS1, BRMS1L, CBFA2T3, CHFR, CIART, CRY1, DAXX, DDIT3/CHOP, DDX5, DNMT1, E4F1, EP300, HCFC1, HDAC9, INSM1, NFE4, NR4A2/NURR1, MIER1, KDM4A, KDM5B, KLF1, MINT, NRIP1, PCAF, PHB2, PRDM6, PRDM16, RB1, RERE, SAMSN1, SAP30L, SETDB1, SMAD3, SMARCA4/BRG1, SMYD2, SUV39H1, TGIF, TGIF2, TRAF6, UHRF1, UHRF2, ZMYND15, ZNF431 and ZNF541. Interacts with KDM5A (By similarity). {ECO:0000250|UniProtKB:O09106, ECO:0000269|PubMed:10487760, ECO:0000269|PubMed:10655483, ECO:0000269|PubMed:10669754, ECO:0000269|PubMed:10846170, ECO:0000269|PubMed:10898795, ECO:0000269|PubMed:11006275, ECO:0000269|PubMed:11102443, ECO:0000269|PubMed:11331609, ECO:0000269|PubMed:11427533, ECO:0000269|PubMed:11533236, ECO:0000269|PubMed:12482978, ECO:0000269|PubMed:12493763, ECO:0000269|PubMed:12670868, ECO:0000269|PubMed:12724404, ECO:0000269|PubMed:12730668, ECO:0000269|PubMed:12837748, ECO:0000269|PubMed:14633989, ECO:0000269|PubMed:15273251, ECO:0000269|PubMed:15361834, ECO:0000269|PubMed:15451426, ECO:0000269|PubMed:15454082, ECO:0000269|PubMed:15927959, ECO:0000269|PubMed:16166625, ECO:0000269|PubMed:16478997, ECO:0000269|PubMed:16569215, ECO:0000269|PubMed:16820529, ECO:0000269|PubMed:17000776, ECO:0000269|PubMed:17341466, ECO:0000269|PubMed:17369852, ECO:0000269|PubMed:17373667, ECO:0000269|PubMed:17548428, ECO:0000269|PubMed:17704056, ECO:0000269|PubMed:17872950, ECO:0000269|PubMed:17996965, ECO:0000269|PubMed:18093978, ECO:0000269|PubMed:19049980, ECO:0000269|PubMed:19061646, ECO:0000269|PubMed:19081374, ECO:0000269|PubMed:19182791, ECO:0000269|PubMed:19343227, ECO:0000269|PubMed:21549307, ECO:0000269|PubMed:21829689}.
Tissue SpecificityUbiquitous, with higher levels in heart, pancreas and testis, and lower levels in kidney and brain.
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