ID CBX4_MOUSE Reviewed; 551 AA. AC O55187; Q149G5; Q149G6; DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 12-DEC-2006, sequence version 2. DT 29-OCT-2014, entry version 111. DE RecName: Full=E3 SUMO-protein ligase CBX4; DE EC=6.3.2.-; DE AltName: Full=Chromobox protein homolog 4; DE AltName: Full=Polycomb 2 homolog; DE Short=Pc2; DE Short=mPc2; GN Name=Cbx4; Synonyms=Pc2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=9367786; DOI=10.1006/jmbi.1997.1372; RA Alkema M.J., Jacobs J., Voncken J.W., Jenkins N.A., Copeland N.G., RA Satijn D.P.E., Otte A.P., Berns A., van Lohuizen M.; RT "MPc2, a new murine homolog of the Drosophila polycomb protein is a RT member of the mouse polycomb transcriptional repressor complex."; RL J. Mol. Biol. 273:993-1003(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP INTERACTION WITH H3-K9ME3. RX PubMed=16537902; DOI=10.1128/MCB.26.7.2560-2569.2006; RA Bernstein E., Duncan E.M., Masui O., Gil J., Heard E., Allis C.D.; RT "Mouse polycomb proteins bind differentially to methylated histone H3 RT and RNA and are enriched in facultative heterochromatin."; RL Mol. Cell. Biol. 26:2560-2569(2006). RN [4] RP INTERACTION WITH CHTOP. RX PubMed=22872859; DOI=10.1074/mcp.M112.017194; RA Fanis P., Gillemans N., Aghajanirefah A., Pourfarzad F., Demmers J., RA Esteghamat F., Vadlamudi R.K., Grosveld F., Philipsen S., RA van Dijk T.B.; RT "Five friends of methylated chromatin target of protein-arginine- RT methyltransferase[prmt]-1 (chtop), a complex linking arginine RT methylation to desumoylation."; RL Mol. Cell. Proteomics 11:1263-1273(2012). CC -!- FUNCTION: E3 SUMO-protein ligase which facilitates SUMO1 CC conjugation by UBE2I. Involved in the sumoylation of HNRNPK, a CC p53/TP53 transcriptional coactivator, hence indirectly regulates CC p53/TP53 transcriptional activation resulting in p21/CDKN1A CC expression. CC -!- FUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1- CC like complex, a complex class required to maintain the CC transcriptionally repressive state of many genes, including Hox CC genes, throughout development. PcG PRC1 complex acts via chromatin CC remodeling and modification of histones; it mediates CC monoubiquitination of histone H2A 'Lys-119', rendering chromatin CC heritably changed in its expressibility. CC -!- PATHWAY: Protein modification; protein sumoylation. CC -!- SUBUNIT: Interacts with SUV39H1 and HIPK2. Interacts with CSNK2B CC (By similarity). Component of a PRC1-like complex. Interacts with CC histone H3-K9Me3. Interacts with CHTOP. {ECO:0000250, CC ECO:0000269|PubMed:16537902, ECO:0000269|PubMed:22872859}. CC -!- SUBCELLULAR LOCATION: Nucleus. Nucleus speckle {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O55187-1; Sequence=Displayed; CC Name=2; CC IsoId=O55187-2; Sequence=VSP_022009; CC Note=No experimental confirmation available.; CC -!- DOMAIN: The polyhistidine repeat may act as a targeting signal to CC nuclear speckles. {ECO:0000250}. CC -!- SIMILARITY: Contains 1 chromo domain. {ECO:0000255|PROSITE- CC ProRule:PRU00053}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U63387; AAB96874.1; -; mRNA. DR EMBL; BC117801; AAI17802.1; -; mRNA. DR EMBL; BC117802; AAI17803.1; -; mRNA. DR CCDS; CCDS25710.1; -. [O55187-1] DR RefSeq; NP_031651.2; NM_007625.2. [O55187-1] DR UniGene; Mm.268070; -. DR UniGene; Mm.471550; -. DR ProteinModelPortal; O55187; -. DR SMR; O55187; 11-60. DR BioGrid; 198537; 5. DR IntAct; O55187; 2. DR PhosphoSite; O55187; -. DR MaxQB; O55187; -. DR PRIDE; O55187; -. DR Ensembl; ENSMUST00000026665; ENSMUSP00000026665; ENSMUSG00000039989. [O55187-1] DR GeneID; 12418; -. DR KEGG; mmu:12418; -. DR UCSC; uc007mpv.2; mouse. [O55187-1] DR CTD; 8535; -. DR MGI; MGI:1195985; Cbx4. DR eggNOG; NOG281109; -. DR GeneTree; ENSGT00530000063056; -. DR HOGENOM; HOG000231219; -. DR HOVERGEN; HBG005257; -. DR InParanoid; O55187; -. DR KO; K11452; -. DR OMA; KWAHGAG; -. DR OrthoDB; EOG7PCJGP; -. DR TreeFam; TF106456; -. DR Reactome; REACT_188970; Oxidative Stress Induced Senescence. DR UniPathway; UPA00886; -. DR NextBio; 281212; -. DR PRO; PR:O55187; -. DR Bgee; O55187; -. DR CleanEx; MM_CBX4; -. DR ExpressionAtlas; O55187; baseline and differential. DR Genevestigator; O55187; -. DR GO; GO:0016604; C:nuclear body; IDA:MGI. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0031519; C:PcG protein complex; ISS:UniProtKB. DR GO; GO:0035102; C:PRC1 complex; ISS:UniProtKB. DR GO; GO:0003682; F:chromatin binding; IDA:MGI. DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW. DR GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB. DR GO; GO:0051219; F:phosphoprotein binding; IPI:MGI. DR GO; GO:0003727; F:single-stranded RNA binding; IDA:UniProtKB. DR GO; GO:0032183; F:SUMO binding; IDA:MGI. DR GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:MGI. DR GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW. DR GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI. DR GO; GO:0016925; P:protein sumoylation; IMP:MGI. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR InterPro; IPR017984; Chromo_dom_subgr. DR InterPro; IPR023780; Chromo_domain. DR InterPro; IPR000953; Chromo_domain/shadow. DR InterPro; IPR016197; Chromodomain-like. DR InterPro; IPR023779; Chromodomain_CS. DR Pfam; PF00385; Chromo; 1. DR PRINTS; PR00504; CHROMODOMAIN. DR SMART; SM00298; CHROMO; 1. DR SUPFAM; SSF54160; SSF54160; 1. DR PROSITE; PS00598; CHROMO_1; 1. DR PROSITE; PS50013; CHROMO_2; 1. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Chromatin regulator; KW Complete proteome; Isopeptide bond; Ligase; Nucleus; KW Reference proteome; Repressor; Transcription; KW Transcription regulation; Ubl conjugation; Ubl conjugation pathway. FT CHAIN 1 551 E3 SUMO-protein ligase CBX4. FT /FTId=PRO_0000080207. FT DOMAIN 11 69 Chromo. {ECO:0000255|PROSITE- FT ProRule:PRU00053}. FT COMPBIAS 383 395 Poly-His. FT MOD_RES 149 149 N6-acetyllysine. {ECO:0000250}. FT CROSSLNK 490 490 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO). FT {ECO:0000250}. FT VAR_SEQ 1 66 Missing (in isoform 2). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_022009. FT CONFLICT 77 77 K -> N (in Ref. 1; AAB96874). FT {ECO:0000305}. FT CONFLICT 144 145 PG -> AR (in Ref. 1; AAB96874). FT {ECO:0000305}. SQ SEQUENCE 551 AA; 60523 MW; 382F8305FD803CF3 CRC64; MELPAVGEHV FAVESIEKKR IRKGRVEYLV KWRGWSPKYN TWEPEENILD PRLLIAFQNR ERQEQLMGYR KRGPKPKPLV VQVPTFARRS NVLTGLQDSS ADNRAKLELG TQGKGQGHQY ELNSKKHHQY QPHSKERSGK PPPPGKSGKY YYQLNSKKHH PYQPDPKMYD LQYQGGHKEA PSPTCPDLGT KSHPPDKWAH GAAAKGYLGA VKPLGGGAGA PGKGSEKGPP NGMTPAPKEA VTGNGIGGKM KIVKNKNKNG RIVIVMSKYM ENGMQAVKIK SGEAAEGEAR SPSHKKRAAE ERHPQGDRTF KKAAGASEEK KAEVPCKRRE EEALVSGDAQ PQDLGSRKLS PTKEAFGEQP LQLTTKPDLL AWDPARSSHP PAHHHHHHHH HHHHHTVGLN LSHARKRCLS ETHGEREPCK KRLTARSIST PTCLGGSPVS EHPANVSPTA ASLPQPEVIL LDSDLDEPID LRCVKMRSDA GEPPSTLQVK PEAPAVAAVV APAPASEKPP AEAQEEPVEP LSEFKPFFGN IIITDVTANC LTVTFKEYVT V //