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IID50144
 UniprotP61965
ProteinWD repeat-containing protein 5
GeneWdr5
OrganismMus musculus
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
334
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 1-334 Hetero trimer : IID50152Complex,P68433
 Evidence X-RAY 2xl3 B Reference
       Region 2xl3 B 1-30 disorder
       Region 2xl3 B 31-334 order
 Evidence X-RAY 2xl3 A Reference
       Region 2xl3 A 1-31 disorder
       Region 2xl3 A 32-334 order
Seq 1-334 Hetero dimer : IID50152Complex
 Evidence X-RAY 2xl2 B Reference
       Region 2xl2 B 1-30 disorder
       Region 2xl2 B 31-334 order
 Evidence X-RAY 2xl2 A Reference
       Region 2xl2 A 1-30 disorder
       Region 2xl2 A 31-334 order
Seqacetylation
    2-2 N-acetylalanine
    112-112 N6-acetyllysine
 
Prediction
NeProc
Disorder 1-23
Order 24-334
ProS 23-23
AlphaFold
Disorder 1-28,30-30
Order 29-29,31-334
Pfam Hmmer
PF00400 35-73 9.5e-12
PF00400 77-115 1.9e-11
PF00400 119-157 4.6e-13
PF00400 161-199 2.6e-12
PF00400 203-242 9.8e-07
PF00400 246-287 2e-07
SEG 2-15
Function
Function in SwissProt
Contributes to histone modification (By similarity). May position the N-terminus of histone H3 for efficient trimethylation at 'Lys-4' (By similarity). As part of the MLL1/MLL complex it is involved in methylation and dimethylation at 'Lys-4' of histone H3 (By similarity). H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation (By similarity). As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues (By similarity). May regulate osteoblasts differentiation (PubMed:11551928). In association with RBBP5 and ASH2L, stimulates the histone methyltransferase activities of KMT2A, KMT2B, KMT2C, KMT2D, SETD1A and SETD1B (By similarity).