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IID00387
 UniprotQ15291
ProteinRetinoblastoma-binding protein 5
GeneRBBP5
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
 Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
538
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 330-356 Hetero heptamer : IID00389Complex
 Evidence X-RAY 5f6k F Reference
       Region 5f6k F 330-338 disorder
       Region 5f6k F 339-355 order
       Region 5f6k F 356-356 disorder
 Evidence X-RAY 5f6k D Reference
       Region 5f6k D 330-335 disorder
       Region 5f6k D 336-354 order
       Region 5f6k D 355-356 disorder
Seq 330-356 Hetero trimer : IID00379Complex,Q9UBL3
 Evidence X-RAY 5f6l J Reference
       Region 5f6l J 330-335 disorder
       Region 5f6l J 336-354 order
       Region 5f6l J 355-356 disorder
Seq 330-356 Hetero tetramer : IID00389Complex
 Evidence X-RAY 5f6k D Reference
       Region 5f6k D 330-335 disorder
       Region 5f6k D 336-354 order
       Region 5f6k D 355-356 disorder
Seq 330-356 Hetero trimer : IID00389Complex
 Evidence X-RAY 5f6k F Reference
       Region 5f6k F 330-338 disorder
       Region 5f6k F 339-355 order
       Region 5f6k F 356-356 disorder
Seq 344-355 Hetero dimer : Q9UBL3
 Evidence X-RAY 4x8p B Reference
       Region 4x8p B 344-355 order
Seq 347-356 Hetero dimer : Q9UBL3
 Evidence X-RAY 4x8n B Reference
       Region 4x8n B 347-356 order
Seq 371-381 Hetero trimer : IID00377Complex
 Evidence X-RAY 3p4f B Reference
       Region 3p4f B 371-372 disorder
       Region 3p4f B 373-381 order
SeqProS possible 344-356 This region is described to be disordered in the free state. (PubMed=20716525) Hetero dimer : Q9UBL3
       Region 4x8p B 344-355 order
SeqProS possible 344-356 This region is described to be disordered in the free state. (PubMed=20716525) Hetero dimer : Q9UBL3
       Region 4x8n B 347-356 order
SeqProS possible 373-381 This region is described to be disordered in the free state. (PubMed=20716525) Hetero trimer : IID00377Complex
       Region 3p4f B 373-381 order
Seqphosphorylation
    525-525 Phosphoserine
    497-497 Phosphoserine; by CDK1
    389-389 Phosphoserine
    388-388 Phosphoserine
    350-350 Phosphoserine
    252-252 Phosphothreonine; by CDK1
 
Prediction
NeProc
Disorder 366-538
Order 1-365
ProS 366-388,396-418,454-471,497-538
AlphaFold
Disorder 1-10,357-371,405-451,463-464,472-538
Order 11-356,372-404,452-462,465-471
Pfam Hmmer
PF00400 56-94 3.8e-07
SEG 309-320 ,344-358
Function
Function in SwissProt
In embryonic stem (ES) cells, plays a crucial role in the differentiation potential, particularly along the neural lineage, regulating gene induction and H3 'Lys-4' methylation at key developmental loci, including that mediated by retinoic acid (By similarity). Does not affect ES cell self-renewal (By similarity). Component or associated component of some histone methyltransferase complexes which regulates transcription through recruitment of those complexes to gene promoters (PubMed:19131338). As part of the MLL1/MLL complex, involved in mono-, di- and trimethylation at 'Lys-4' of histone H3 (PubMed:19556245). Histone H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation (PubMed:19556245). In association with ASH2L and WDR5, stimulates the histone methyltransferase activities of KMT2A, KMT2B, KMT2C, KMT2D, SETD1A and SETD1B (PubMed:22266653, PubMed:21220120).