CBX4
entrez
8535
canonical
uniprot
O00257
canonical
ensembl
ENSG00000141582
resolver
ensp
ENSP00000269397
resolver
genesymbol
CBX4
resolver
hgnc
HGNC:1554
resolver
uniprot
A0A0S2Z5B2
resolver
uniprot
B1PJR7
resolver
uniprot
Q6TPI8
resolver
uniprot
Q96C04
resolver
uniprot_entry
A0A0S2Z5B2_HUMAN
resolver
uniprot_entry
CBX4_HUMAN
resolver
uniprot_sec
B1PJR7
resolver
uniprot_sec
Q6TPI8
resolver
uniprot_sec
Q96C04
resolver
amino_acid_sequence
MELPAVGEHVFAVESIEKKRIRKGRVEYLVKWRGWSPKYNTWEPEENILDPRLLIAFQNRERQEQLMGYRKRGPKPKPLVVQVPTFARRSNVLTGLQDSSTDNRAKLDLGAQGKGQGHQYELNSKKHHQYQPHSKERAGKPPPPGKSGKYYYQLNSKKHHPYQPDPKMYDLQYQGGHKEAPSPTCPDLGAKSHPPDKWAQGAGAKGYLGAVKPLAGAAGAPGKGSEKGPPNGMMPAPKEAVTGNGIGGKMKIVKNKNKNGRIVIVMSKYMENGMQAVKIKSGEVAEGEARSPSHKKRAADERHPPADRTFKKAAGAEEKKVEAPPKRREEEVSGVSDPQPQDAGSRKLSPTKEAFGEQPLQLTTKPDLLAWDPARNTHPPSHHPHPHPHHHHHHHHHHHHAVGLNLSHVRKRCLSETHGEREPCKKRLTARSISTPTCLGGSPAAERPADLPPAAALPQPEVILLDSDLDEPIDLRCVKTRSEAGEPPSSLQVKPETPASAAVAVAAAAAPTTTAEKPPAEAQDEPAESLSEFKPFFGNIIITDVTANCLTVTFKEYVTV
uniprot
proteins
ec_number
2.3.2.-
uniprot
proteins
function
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 ZBTB35 (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). {ECO:0000250|UniProtKB:O55187, ECO:0000269|PubMed:12167701, ECO:0000269|PubMed:12679040, ECO:0000269|PubMed:19636380, ECO:0000269|PubMed:21282530, ECO:0000269|PubMed:22467880, ECO:0000269|PubMed:22825850}.; FUNCTION: (Microbial infection) Plays a critical for EV71 infection through SUMOylation E3 ligase function. Enhances the stability of EV71 RNA-directed RNA polymerase by regulating its SUMOylation and 'Lys-63'-linked ubiquitination. {ECO:0000269|PubMed:41859455}.
uniprot
proteins
mass_dalton
61368
uniprot
proteins
mutagenesis
MUTAGEN 16; /note="I->F: Reduced interaction with H3C15, H3C1 and RNF2."; /evidence="ECO:0000269|PubMed:18927235"; MUTAGEN 434; /note="S->A: Abolishes interaction with YWHAZ and YWHAE; impairs interaction with PCGF6 and BMI1; no effect on interaction with RNF2."; /evidence="ECO:0000269|PubMed:21282530"; MUTAGEN 494; /note="K->R: No effect on ZBTB35 sumoylation."; /evidence="ECO:0000269|PubMed:22467880"; MUTAGEN 497; /note="T->A: Small decrease in ZBTB35 sumoylation."; /evidence="ECO:0000269|PubMed:22467880
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein sumoylation. {ECO:0000269|PubMed:12679040, ECO:0000269|PubMed:22467880, ECO:0000269|PubMed:22825850}.
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated. Ubiquitination regulates the function of the Polycomb group (PcG) multiprotein PRC1-like complex. Deubiquitinated by USP26. {ECO:0000269|PubMed:28839133}.; PTM: Phosphorylated on Thr-497 by HIPK2 upon DNA damage. This phosphorylation stimulates E3 SUMO-protein ligase activity and promotes sumoylation on Lys-494, as well as sumoylation of other target proteins, such as HNRNPK. {ECO:0000269|PubMed:12679040, ECO:0000269|PubMed:15592428, ECO:0000269|PubMed:17018294}.
uniprot
proteins
pubmed
12101246
uniprot
proteins
pubmed
12167701
uniprot
proteins
pubmed
12679040
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15592428
uniprot
proteins
pubmed
16061479
uniprot
proteins
pubmed
16625196
uniprot
proteins
pubmed
17018294
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18927235
uniprot
proteins
pubmed
19266028
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19636380
uniprot
proteins
pubmed
21282530
uniprot
proteins
pubmed
22467880
uniprot
proteins
pubmed
22825850
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25218447
uniprot
proteins
pubmed
25755297
uniprot
proteins
pubmed
25772364
uniprot
proteins
pubmed
27211601
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
28839133
uniprot
proteins
pubmed
28842558
uniprot
proteins
pubmed
41859455
uniprot
proteins
pubmed
9199346
uniprot
proteins
pubmed
9315667
uniprot
proteins
sequence_length
560
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:41859455}. Nucleus {ECO:0000269|PubMed:12679040, ECO:0000269|PubMed:17018294, ECO:0000269|PubMed:18927235, ECO:0000269|PubMed:21282530}. Nucleus speckle {ECO:0000269|PubMed:19266028}. Note=Localization to nuclear polycomb bodies is required for ZBTB35 sumoylation (PubMed:22467880). Localized in distinct foci on chromatin (PubMed:18927235). {ECO:0000269|PubMed:18927235, ECO:0000269|PubMed:22467880}.
uniprot
proteins