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IID00565
UniprotQ13547
ProteinHistone deacetylase 1
GeneHDAC1
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
482
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 1-376 Hetero trimer : IID00563Complex
 Evidence X-RAY 5icn B Reference
       Region 5icn B 1-7 disorder
       Region 5icn B 8-376 order
Seq 1-482 Hetero tetramer : IID00563Complex
 Evidence X-RAY 4bkx B Reference
       Region 4bkx B 1-7 disorder
       Region 4bkx B 8-376 order
       Region 4bkx B 377-482 disorder
Seq 413-422 Hetero dimer : IID00130Complex
 Evidence X-RAY 7sme B Reference
       Region 7sme B 413-422 order
SeqProS verified 413-422 Hetero dimer : IID00130Complex
       Region 7sme B 413-422 order
       Region 4bkx B 377-482 disorder
Seqphosphorylation
    406-406 Phosphoserine
    423-423 Phosphoserine; by CK2
    421-421 Phosphoserine; by CK2
    409-409 Phosphoserine
    393-393 Phosphoserine
Seqacetylation
    220-220 N6-acetyllysine
    74-74 N6-acetyllysine; alternate
 
Prediction
NeProc
Disorder 1-7,391-482
Order 8-390
ProS 391-391,399-423,428-439
AlphaFold
Disorder 1-7,376-383,388-388,390-400,403-405,418-482
Order 8-375,384-387,389-389,401-402,406-417
Pfam Hmmer
PF00850 10-321 4.4e-194
SEG 13-27 ,390-402 ,417-430 ,443-471
Function
Function in SwissProt
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 and TSHZ3 (PubMed:12837748, PubMed:16285960, 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 by mediating decrotonylation ((2E)-butenoyl) of histones (PubMed:28497810).
Biological Process
Diagram with PDB data
HDAC1/RBL1p107 pocket domain complexed with HDAC1 peptide
See also
Diagram with PDB data
MXD1/Sin3bStructure of the complex of the Mad1-Sin3B interaction domains
REST/Sin3bSolution structure of the NRSF/REST-mSin3B PAH1 complex
MTA1/HDAC1The structure of HDAC1 in complex with the dimeric ELM2-SANT domain of MTA1 from the NuRD complex