IDEAL List

IDEAL

IID00688
UniprotO00257
ProteinE3 SUMO-protein ligase CBX4
GeneCBX4
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS xml rdf

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

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.