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IID00488
 UniprotQ92769
ProteinHistone deacetylase 2
GeneHDAC2
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS xml
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
488
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 7-375 Homo trimer :
 Evidence X-RAY 5ix0 C Reference
       Region 5ix0 C 7-9 disorder
       Region 5ix0 C 10-375 order
 Evidence X-RAY 5ix0 B Reference
       Region 5ix0 B 7-9 disorder
       Region 5ix0 B 10-375 order
 Evidence X-RAY 5ix0 A Reference
       Region 5ix0 A 7-375 order
Seq 7-376 Monomer :
 Evidence X-RAY 3max C Reference
       Region 3max C 9-374 order
 Evidence X-RAY 3max B Reference
       Region 3max B 9-10 disorder
       Region 3max B 11-374 order
 Evidence X-RAY 3max A Reference
       Region 3max A 9-374 order
 Evidence X-RAY 4ly1 C Reference
       Region 4ly1 C 8-8 disorder
       Region 4ly1 C 9-374 order
       Region 4ly1 C 375-376 disorder
 Evidence X-RAY 4ly1 B Reference
       Region 4ly1 B 8-8 disorder
       Region 4ly1 B 9-375 order
       Region 4ly1 B 376-376 disorder
 Evidence X-RAY 4ly1 A Reference
       Region 4ly1 A 8-375 order
       Region 4ly1 A 376-376 disorder
 Evidence X-RAY 4lxz C Reference
       Region 4lxz C 8-8 disorder
       Region 4lxz C 9-376 order
 Evidence X-RAY 4lxz B Reference
       Region 4lxz B 8-8 disorder
       Region 4lxz B 9-375 order
       Region 4lxz B 376-376 disorder
 Evidence X-RAY 4lxz A Reference
       Region 4lxz A 8-375 order
       Region 4lxz A 376-376 disorder
 Evidence X-RAY 5ix0 C Reference
       Region 5ix0 C 7-9 disorder
       Region 5ix0 C 10-375 order
 Evidence X-RAY 5ix0 B Reference
       Region 5ix0 B 7-9 disorder
       Region 5ix0 B 10-375 order
 Evidence X-RAY 5ix0 A Reference
       Region 5ix0 A 7-375 order
 Evidence X-RAY 5iwg C Reference
       Region 5iwg C 8-9 disorder
       Region 5iwg C 10-375 order
 Evidence X-RAY 5iwg B Reference
       Region 5iwg B 8-9 disorder
       Region 5iwg B 10-375 order
 Evidence X-RAY 5iwg A Reference
       Region 5iwg A 8-375 order
Seqphosphorylation
    424-424 Phosphoserine
    422-422 Phosphoserine
    407-407 Phosphoserine
    394-394 Phosphoserine
Seqacetylation
    221-221 N6-acetyllysine
    75-75 N6-acetyllysine; alternate
 
Prediction
NeProc
Disorder 1-8,392-443,472-488
Order 9-391,444-471
ProS 392-392,400-424,429-437
AlphaFold
Disorder 1-7,376-384,389-389,391-406,409-411,417-417,419-487
Order 8-375,385-388,390-390,407-408,412-416,418-418,488-488
Pfam Hmmer
PF00850 11-322 9e-189
SEG 14-28 ,392-403 ,418-431 ,448-469
Function
Function in SwissProt
Responsible 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. Forms transcriptional repressor complexes by associating with MAD, SIN3, YY1 and N-COR. Interacts in the late S-phase of DNA-replication with DNMT1 in the other transcriptional repressor complex composed of DNMT1, DMAP1, PCNA, CAF1. Deacetylates TSHZ3 and regulates its transcriptional repressor 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. May be involved in the transcriptional repression of circadian target genes, such as PER1, mediated by CRY1 through histone deacetylation. Involved in MTA1-mediated transcriptional corepression of TFF1 and CDKN1A.
Biological Process
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
PHF12/MORF4L1Structural Basis for Molecular Interactions Involving MRG Domains: Implications in Chromatin Biology