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Overview

Uniprot IDO00257
Protein NameE3 SUMO-protein ligase CBX4
Gene NameCBX4
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
223 GAAGAPGKGSEKGPP
227 APGKGSEKGPPNGMM

Function

E3 SUMO-protein ligase that catalyzes sumoylation of target proteins by promoting the transfer of SUMO from the E2 enzyme to the substrate (PubMed:12679040, PubMed:22467880, PubMed:22825850). Also acts as a histone reader, which specifically recognizes and binds histone H3 trimethylated at 'Lys-9' and 'Lys-27' (H3K9me3 and H3K27me3, respectively) via its chromo domain (By similarity). Catalyzes sumoylation of HNRNPK, a p53/TP53 transcriptional coactivator, hence indirectly regulates p53/TP53 transcriptional activation resulting in p21/CDKN1A expression (PubMed:22825850). Acts as a regulator of brown adipocyte differentiation by mediating sumoylation of PRDM16, thereby preventing PRDM16 ubiquitination and degradation (By similarity). Monosumoylates ZNF131 (PubMed:22467880). 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). Plays a role in the lineage differentiation of the germ layers in embryonic development (By similarity)

Protein Sequence

10 MELPAVGEHV 20 FAVESIEKKR 30 IRKGRVEYLV 40 KWRGWSPKYN 50 TWEPEENILD 60 PRLLIAFQNR 70 ERQEQLMGYR 80 KRGPKPKPLV 90 VQVPTFARRS 100 NVLTGLQDSS 110 TDNRAKLDLG 120 AQGKGQGHQY 130 ELNSKKHHQY 140 QPHSKERAGK 150 PPPPGKSGKY 160 YYQLNSKKHH 170 PYQPDPKMYD 180 LQYQGGHKEA 190 PSPTCPDLGA 200 KSHPPDKWAQ 210 GAGAKGYLGA 220 VKPLAGAAGA 230 PGKGSEKGPP 240 NGMMPAPKEA 250 VTGNGIGGKM 260 KIVKNKNKNG 270 RIVIVMSKYM 280 ENGMQAVKIK 290 SGEVAEGEAR 300 SPSHKKRAAD 310 ERHPPADRTF 320 KKAAGAEEKK 330 VEAPPKRREE 340 EVSGVSDPQP 350 QDAGSRKLSP 360 TKEAFGEQPL 370 QLTTKPDLLA 380 WDPARNTHPP 390 SHHPHPHPHH 400 HHHHHHHHHH 410 AVGLNLSHVR 420 KRCLSETHGE 430 REPCKKRLTA 440 RSISTPTCLG 450 GSPAAERPAD 460 LPPAAALPQP 470 EVILLDSDLD 480 EPIDLRCVKT 490 RSEAGEPPSS 500 LQVKPETPAS 510 AAVAVAAAAA 520 PTTTAEKPPA 530 EAQDEPAESL 540 SEFKPFFGNI 550 IITDVTANCL 560 TVTFKEYVTV

Gene Ontology

Classification GO ID Description
Cellular Component GO:0000785 chromatin
Cellular Component GO:0016604 nuclear body
Cellular Component GO:0016607 nuclear speck
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0031519 PcG protein complex
Cellular Component GO:0035102 PRC1 complex
Molecular Function GO:0003682 chromatin binding
Molecular Function GO:0019899 enzyme binding
Molecular Function GO:0061628 histone H3K27me3 reader activity
Molecular Function GO:0051219 phosphoprotein binding
Molecular Function GO:0003727 single-stranded RNA binding
Molecular Function GO:0032183 SUMO binding
Molecular Function GO:0061665 SUMO ligase activity
Molecular Function GO:0019789 SUMO transferase activity
Molecular Function GO:0000976 transcription cis-regulatory region binding
Molecular Function GO:0003714 transcription corepressor activity
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0031507 heterochromatin formation
Biological Process GO:0043066 negative regulation of apoptotic process
Biological Process GO:0045892 negative regulation of DNA-templated transcription
Biological Process GO:0032435 negative regulation of proteasomal ubiquitin-dependent protein catabolic process
Biological Process GO:0000122 negative regulation of transcription by RNA polymerase II
Biological Process GO:0090336 positive regulation of brown fat cell differentiation
Biological Process GO:0050821 protein stabilization
Biological Process GO:0016925 protein sumoylation

Reference

[1] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.