CBX2_MOUSE
ID CBX2_MOUSE Reviewed; 519 AA.
AC P30658; A2ABG2; O35731; Q8CIA0;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Chromobox protein homolog 2;
DE AltName: Full=M33;
DE AltName: Full=Modifier 3 protein;
GN Name=Cbx2; Synonyms=M33;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=1352241; DOI=10.1242/dev.114.4.921;
RA Pearce J.J.H., Singh P.B., Gaunt S.J.;
RT "The mouse has a Polycomb-like chromobox gene.";
RL Development 114:921-930(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH RING1, DEVELOPMENTAL STAGE,
RP AND SUBCELLULAR LOCATION.
RC TISSUE=Embryo;
RX PubMed=9312051; DOI=10.1093/emboj/16.19.5930;
RA Schoorlemmer J., Marcos-Gutierrez C., Were F., Martinez R., Garcia E.,
RA Satijn D.P.E., Otte A.P., Vidal M.;
RT "Ring1A is a transcriptional repressor that interacts with the Polycomb-M33
RT protein and is expressed at rhombomere boundaries in the mouse hindbrain.";
RL EMBO J. 16:5930-5942(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION, INTERACTION WITH HISTONE H3K9ME3 AND H3K27ME3, AND SUBCELLULAR
RP LOCATION.
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 and
RT RNA and are enriched in facultative heterochromatin.";
RL Mol. Cell. Biol. 26:2560-2569(2006).
RN [7]
RP FUNCTION, INTERACTION WITH RNF2, AND TISSUE SPECIFICITY.
RX PubMed=22226355; DOI=10.1016/j.stem.2011.12.006;
RA Morey L., Pascual G., Cozzuto L., Roma G., Wutz A., Benitah S.A.,
RA Di Croce L.;
RT "Nonoverlapping functions of the Polycomb group Cbx family of proteins in
RT embryonic stem cells.";
RL Cell Stem Cell 10:47-62(2012).
RN [8]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-248, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1-like
CC complex, a complex class required to maintain the transcriptionally
CC repressive state of many genes, including Hox genes, throughout
CC development (By similarity). PcG PRC1 complex acts via chromatin
CC remodeling and modification of histones; it mediates monoubiquitination
CC of histone H2A 'Lys-119', rendering chromatin heritably changed in its
CC expressibility (By similarity). Binds to histone H3 trimethylated at
CC 'Lys-9' (H3K9me3) or at 'Lys-27' (H3K27me3) (PubMed:16537902). Plays a
CC role in the lineage differentiation of the germ layers in embryonic
CC development (PubMed:22226355). Involved in sexual development, acting
CC as activator of NR5A1 expression (By similarity).
CC {ECO:0000250|UniProtKB:Q14781, ECO:0000269|PubMed:16537902,
CC ECO:0000269|PubMed:22226355}.
CC -!- SUBUNIT: Component of a PRC1-like complex (By similarity). The
CC composition of the PRC1 complex may differ between the PRC1 complex in
CC pluripotent embryonic stem cells containing RNF2, CBX7 and PCGF2, and
CC the PRC1 complex in differentiating cells containing RNF2, CBX2, CBX4
CC and BMI1 (PubMed:22226355). Interacts with RING1/RNF2 (PubMed:9312051,
CC PubMed:22226355). Interacts (via chromodomain) with histone H3K9Me3 and
CC H3K27me3 (PubMed:16537902). May interact with H3C15 and H3C1 (By
CC similarity). {ECO:0000250|UniProtKB:Q14781,
CC ECO:0000269|PubMed:16537902, ECO:0000269|PubMed:22226355,
CC ECO:0000269|PubMed:9312051}.
CC -!- INTERACTION:
CC P30658; Q60848: Hells; NbExp=2; IntAct=EBI-360174, EBI-3043887;
CC P30658; Q8CCI5: Rybp; NbExp=3; IntAct=EBI-360174, EBI-929290;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:9312051}.
CC Chromosome {ECO:0000269|PubMed:16537902}. Note=Localizes to the
CC inactivated X chromosome in females. {ECO:0000269|PubMed:16537902}.
CC -!- TISSUE SPECIFICITY: Expressed in embryoid bodies.
CC {ECO:0000269|PubMed:22226355}.
CC -!- DEVELOPMENTAL STAGE: Expressed in most embryonic tissues except the
CC heart from 8.5 to 11.5 dpc. Expressed in central nervous system (CNS,
CC ventricular zone and spinal cord), peripheral nervous system (PNS,
CC sensory cranial and spinal ganglia), olfactory and tongue epithelia,
CC lung, gastrointestinal duct and urogenital system at 13.5 dpc.
CC Expressed in CNS, thymus, various epithelial cell types including the
CC olfactory, tooth and tongue epithelia at 15.5 dpc.
CC {ECO:0000269|PubMed:9312051}.
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DR EMBL; X62537; CAA44398.1; -; mRNA.
DR EMBL; Y13274; CAA73723.1; -; mRNA.
DR EMBL; AL662835; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466558; EDL34680.1; -; Genomic_DNA.
DR EMBL; BC035199; AAH35199.1; -; mRNA.
DR CCDS; CCDS25708.1; -.
DR PIR; S23796; S23796.
DR RefSeq; NP_031649.2; NM_007623.3.
DR AlphaFoldDB; P30658; -.
DR BMRB; P30658; -.
DR SMR; P30658; -.
DR BioGRID; 198535; 19.
DR CORUM; P30658; -.
DR DIP; DIP-690N; -.
DR IntAct; P30658; 17.
DR MINT; P30658; -.
DR STRING; 10090.ENSMUSP00000026662; -.
DR iPTMnet; P30658; -.
DR PhosphoSitePlus; P30658; -.
DR EPD; P30658; -.
DR MaxQB; P30658; -.
DR PaxDb; P30658; -.
DR PeptideAtlas; P30658; -.
DR PRIDE; P30658; -.
DR ProteomicsDB; 265684; -.
DR Antibodypedia; 32656; 310 antibodies from 30 providers.
DR DNASU; 12416; -.
DR Ensembl; ENSMUST00000026662; ENSMUSP00000026662; ENSMUSG00000025577.
DR GeneID; 12416; -.
DR KEGG; mmu:12416; -.
DR UCSC; uc007mpt.1; mouse.
DR CTD; 84733; -.
DR MGI; MGI:88289; Cbx2.
DR VEuPathDB; HostDB:ENSMUSG00000025577; -.
DR eggNOG; KOG2748; Eukaryota.
DR GeneTree; ENSGT00940000158816; -.
DR HOGENOM; CLU_027573_0_0_1; -.
DR InParanoid; P30658; -.
DR OMA; FQQNKGP; -.
DR OrthoDB; 1628171at2759; -.
DR TreeFam; TF106456; -.
DR Reactome; R-MMU-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-MMU-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-MMU-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-MMU-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-MMU-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR Reactome; R-MMU-8943724; Regulation of PTEN gene transcription.
DR BioGRID-ORCS; 12416; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Cbx2; mouse.
DR PRO; PR:P30658; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P30658; protein.
DR Bgee; ENSMUSG00000025577; Expressed in gastrula and 191 other tissues.
DR Genevisible; P30658; MM.
DR GO; GO:0000791; C:euchromatin; IDA:MGI.
DR GO; GO:0000792; C:heterochromatin; IDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0031519; C:PcG protein complex; IDA:MGI.
DR GO; GO:0035102; C:PRC1 complex; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0045137; P:development of primary sexual characteristics; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR InterPro; IPR042796; CBX2.
DR InterPro; IPR033773; CBX7_C.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR023779; Chromodomain_CS.
DR PANTHER; PTHR46860; PTHR46860; 1.
DR Pfam; PF17218; CBX7_C; 1.
DR Pfam; PF00385; Chromo; 1.
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 Chromatin regulator; Chromosome; DNA-binding; Isopeptide bond; Methylation;
KW Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..519
FT /note="Chromobox protein homolog 2"
FT /id="PRO_0000080202"
FT DOMAIN 12..70
FT /note="Chromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DNA_BIND 75..87
FT /note="A.T hook"
FT REGION 60..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 164..169
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 72..89
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 248
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q14781"
FT MOD_RES 248
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14781"
FT CROSSLNK 147
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14781"
FT CROSSLNK 154
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14781"
FT CONFLICT 1
FT /note="M -> EF (in Ref. 2; CAA73723)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="V -> A (in Ref. 1; CAA44398)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="S -> G (in Ref. 2; CAA73723)"
FT /evidence="ECO:0000305"
FT CONFLICT 133
FT /note="R -> G (in Ref. 2; CAA73723)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 519 AA; 54918 MW; F89EF3CEF14ACA72 CRC64;
MEELSSVGEQ VFAAECILSK RLRKGKLEYL VKWRGWSSKH NSWEPEENIL DPRLLLAFQK
KEHEKEVQNR KRGKRPRGRP RKHTVTSSCS RRSKLKEPDA PSKSKSSSSS SSSTSSSSSS
DEEEDDSDLD SKRGPRGRET HPVPQKKAQI LVAKPELKDP IRKKRGRKPL PPEQKAARRP
VSLAKVLKTT RKDLGTSAAK LPPPLSAPVA GLAALKAHTK EACGGPSTMA TPENLASLMK
GMAGSPSRGG IWQSSIVHYM NRMSQSQVQA ASRLALKAQA TNKCGLGLDL KVRTQKGGEL
GGSPAGGKVP KAPGGGAAEQ QRGNHSGSPG AQLAPTQELS LQVLDLQSVK NGVPGVGLLA
RHAPAKAIPA TNPATGKGPG SGPTGANMTN APTDNNKGEK LTCKATALPA PSVKRDTVKS
VAASGGQEGH TAPGEGRKPP ALSELSTGEE NSSSDSDPDS TSLPSAAQNL SVAIQTSQDW
KPTRSLIEHV FVTDVTANLI TVTVKESPTS VGFFNLRHY
