O55187 · CBX4_MOUSE

  • Protein
    E3 SUMO-protein ligase CBX4
  • Gene
    Cbx4
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

E3 SUMO-protein ligase which facilitates SUMO1 conjugation by UBE2I. Involved in the sumoylation of HNRNPK, a p53/TP53 transcriptional coactivator, hence indirectly regulates p53/TP53 transcriptional activation resulting in p21/CDKN1A expression.
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 (By similarity).
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 (By similarity).
Binds to histone H3 trimethylated at 'Lys-9' (H3K9me3) (PubMed:16537902).
Plays a role in the lineage differentiation of the germ layers in embryonic development (PubMed:22226355).

Pathway

Protein modification; protein sumoylation.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentnuclear body
Cellular Componentnuclear speck
Cellular Componentnucleoplasm
Cellular Componentnucleus
Cellular ComponentPcG protein complex
Cellular ComponentPRC1 complex
Molecular Functionchromatin binding
Molecular Functionenzyme binding
Molecular Functionmethylated histone binding
Molecular Functionphosphoprotein binding
Molecular Functionsingle-stranded RNA binding
Molecular FunctionSUMO binding
Molecular FunctionSUMO ligase activity
Molecular FunctionSUMO transferase activity
Molecular Functiontranscription cis-regulatory region binding
Biological Processchromatin organization
Biological Processnegative regulation of transcription by RNA polymerase II
Biological Processprotein sumoylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    E3 SUMO-protein ligase CBX4
  • EC number
  • Alternative names
    • Chromobox protein homolog 4
    • E3 SUMO-protein transferase CBX4
    • Polycomb 2 homolog (Pc2; mPc2)

Gene names

    • Name
      Cbx4
    • Synonyms
      Pc2

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    O55187
  • Secondary accessions
    • Q149G5
    • Q149G6

Proteomes

Organism-specific databases

Subcellular Location

PTM/Processing

Features

Showing features for chain, cross-link, modified residue.

TypeIDPosition(s)Description
ChainPRO_00000802071-551E3 SUMO-protein ligase CBX4
Cross-link77Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link106Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link114Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link125Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue149N6-acetyllysine; alternate
Cross-link149Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate
Cross-link157Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link167Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link178Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue182Phosphoserine
Cross-link191Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link205Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link212Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link223Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link249Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link268Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link278Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link280Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link321Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link353Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link366Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue463Phosphoserine
Cross-link490Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
Cross-link490Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate

Post-translational modification

Ubiquitinated. Ubiquitination regulates the function of the Polycomb group (PcG) multiprotein PRC1-like complex. Deubiquitinated by USP26.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed in embryoid bodies.

Gene expression databases

Interaction

Subunit

Interacts with SUV39H1 and HIPK2 (By similarity).
Interacts with CSNK2B (By similarity).
Component of a PRC1-like complex (By similarity).
The composition of the PRC1 complex differs between the PRC1 complex in pluripotent embryonic stem cells containing RNF2, CBX7 and PCGF2, and the PRC1 complex in differentiating cells containing RNF2, CBX2, CBX4 and BMI1 (PubMed:22226355).
Interacts with RNF2 (PubMed:22226355).
Interacts (via chromodomain) with histone H3K9Me3 and single-stranded RNA (ssRNA) (PubMed:16537902).
Interacts with CHTOP (PubMed:22872859).
May interact with H3C15 and H3C1 (By similarity).
Interacts with PRDM1 (By similarity).

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain11-69Chromo
Region125-152Disordered
Region172-193Disordered
Region216-244Disordered
Region281-399Disordered
Compositional bias283-336Basic and acidic residues
Compositional bias380-399Basic residues
Region430-451Disordered

Domain

The polyhistidine repeat may act as a targeting signal to nuclear speckles.

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

O55187-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    551
  • Mass (Da)
    60,523
  • Last updated
    2006-12-12 v2
  • Checksum
    382F8305FD803CF3
MELPAVGEHVFAVESIEKKRIRKGRVEYLVKWRGWSPKYNTWEPEENILDPRLLIAFQNRERQEQLMGYRKRGPKPKPLVVQVPTFARRSNVLTGLQDSSADNRAKLELGTQGKGQGHQYELNSKKHHQYQPHSKERSGKPPPPGKSGKYYYQLNSKKHHPYQPDPKMYDLQYQGGHKEAPSPTCPDLGTKSHPPDKWAHGAAAKGYLGAVKPLGGGAGAPGKGSEKGPPNGMTPAPKEAVTGNGIGGKMKIVKNKNKNGRIVIVMSKYMENGMQAVKIKSGEAAEGEARSPSHKKRAAEERHPQGDRTFKKAAGASEEKKAEVPCKRREEEALVSGDAQPQDLGSRKLSPTKEAFGEQPLQLTTKPDLLAWDPARSSHPPAHHHHHHHHHHHHHTVGLNLSHARKRCLSETHGEREPCKKRLTARSISTPTCLGGSPVSEHPANVSPTAASLPQPEVILLDSDLDEPIDLRCVKMRSDAGEPPSTLQVKPEAPAVAAVVAPAPASEKPPAEAQEEPVEPLSEFKPFFGNIIITDVTANCLTVTFKEYVTV

O55187-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Features

Showing features for alternative sequence, sequence conflict, compositional bias.

TypeIDPosition(s)Description
Alternative sequenceVSP_0220091-66in isoform 2
Sequence conflict77in Ref. 1; AAB96874
Sequence conflict144-145in Ref. 1; AAB96874
Compositional bias283-336Basic and acidic residues
Compositional bias380-399Basic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U63387
EMBL· GenBank· DDBJ
AAB96874.1
EMBL· GenBank· DDBJ
mRNA
BC117801
EMBL· GenBank· DDBJ
AAI17802.1
EMBL· GenBank· DDBJ
mRNA
BC117802
EMBL· GenBank· DDBJ
AAI17803.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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