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IID00688
 UniprotO00257
ProteinE3 SUMO-protein ligase CBX4
GeneCBX4
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS xml
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
560
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 8-65 Homo dimer :
 Evidence X-RAY 5epl B Reference
       Region 5epl B 8-63 order
       Region 5epl B 64-65 disorder
 Evidence X-RAY 5epl A Reference
       Region 5epl A 8-59 order
       Region 5epl A 60-65 disorder
Seq 8-65 Monomer :
 Evidence NMR 2k28 A Reference
       Region 2k28 A 8-65 order
 Evidence X-RAY 3i8z A Reference
       Region 3i8z A 8-10 disorder
       Region 3i8z A 11-60 order
       Region 3i8z A 61-62 disorder
Seqphosphorylation
    497-497 Phosphothreonine; by HIPK2
    467-467 Phosphoserine
    182-182 Phosphoserine
Seqacetylation
    149-149 N6-acetyllysine; alternate
 
Prediction
NeProc
Disorder 1-4,65-530
Order 5-64,531-560
ProS 65-94,119-125,132-138,149-153,163-169,185-201,260-265,412-418,461-479
AlphaFold
Disorder 1-7,68-83,85-85,87-165,167-251,253-257,267-533,535-537,556-560
Order 8-67,84-84,86-86,166-166,252-252,258-266,534-534,538-555
Pfam Hmmer
PF00385 11-60 1.3e-19
SEG 139-152 ,209-230 ,311-332 ,378-400 ,443-461 ,495-522
Function
Function in SwissProt
E3 SUMO-protein ligase which facilitates SUMO1 conjugation by UBE2I (PubMed:12679040). Involved in the sumoylation of HNRNPK, a p53/TP53 transcriptional coactivator, hence indirectly regulates p53/TP53 transcriptional activation resulting in p21/CDKN1A expression. Monosumoylates ZNF131 (PubMed:22825850).
Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development (PubMed:12167701, PubMed:19636380, PubMed:21282530). PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility (PubMed:12167701, PubMed:19636380, PubMed:21282530). Binds to histone H3 trimethylated at 'Lys-9' (H3K9me3) (By similarity). Plays a role in the lineage differentiation of the germ layers in embryonic development (By similarity).