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IID00697
 UniprotO95983
ProteinMethyl-CpG-binding domain protein 3
GeneMBD3
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS xml
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
291
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 1-70 Monomer :
 Evidence NMR 2mb7 A Reference
       Region 2mb7 A 1-70 order
       Region 2mb7 A 1-1 high_rmsd
       Region 2mb7 A 24-26 high_rmsd
Seqphosphorylation
    144-144 Phosphoserine
    85-85 Phosphoserine
    56-56 Phosphoserine
 
Prediction
NeProc
Disorder 1-4,74-144,149-197,249-291
Order 5-73,145-148,198-248
ProS 1-4,74-99,109-117,123-144,149-185,249-272,283-291
AlphaFold
Disorder 1-2,71-104,109-109,111-112,114-115,117-119,122-131,258-291
Order 3-70,105-108,110-110,113-113,116-116,120-121,132-257
Pfam Hmmer
PF01429 1-72 1.6e-29
SEG 268-287
Function
Function in SwissProt
Acts as transcriptional repressor and plays a role in gene silencing. Does not bind to DNA by itself (PubMed:12124384). Binds to DNA with a preference for sites containing methylated CpG dinucleotides (in vitro). Binds to a lesser degree DNA containing unmethylated CpG dinucleotides (PubMed:24307175). Recruits histone deacetylases and DNA methyltransferases.
Biological Process
See also
Diagram with PDB data
MTA1/HDAC1The structure of HDAC1 in complex with the dimeric ELM2-SANT domain of MTA1 from the NuRD complex