CBX7_MOUSE
ID CBX7_MOUSE Reviewed; 158 AA.
AC Q8VDS3;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Chromobox protein homolog 7;
GN Name=Cbx7; Synonyms=D15Ertd417e;
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], FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION
RP WITH RING1.
RC STRAIN=CD-1;
RX PubMed=14647293; DOI=10.1038/ncb1077;
RA Gil J., Bernard D., Martinez D., Beach D.;
RT "Polycomb CBX7 has a unifying role in cellular lifespan.";
RL Nat. Cell Biol. 6:67-72(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
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 [3]
RP FUNCTION, INTERACTION WITH HISTONE H3K9ME3; H3K27ME3; H3K9ME2; H4K20ME1 AND
RP SSRNA, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF PHE-11
RP AND TRP-35.
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 [4]
RP STRUCTURE BY NMR OF 1-71 IN COMPLEX WITH HISTONE H3 DIMETHYLATED AT
RP 'LYS-27', FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP ARG-17; LYS-31 AND TRP-35.
RX PubMed=20541999; DOI=10.1016/j.molcel.2010.03.021;
RA Yap K.L., Li S., Munoz-Cabello A.M., Raguz S., Zeng L., Mujtaba S., Gil J.,
RA Walsh M.J., Zhou M.M.;
RT "Molecular interplay of the noncoding RNA ANRIL and methylated histone H3
RT lysine 27 by polycomb CBX7 in transcriptional silencing of INK4a.";
RL Mol. Cell 38:662-674(2010).
RN [5]
RP FUNCTION, INTERACTION WITH RNF2; PHC1 AND PCGF2, 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).
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 (PubMed:16537902, PubMed:22226355). PcG PRC1 complex acts
CC via chromatin remodeling and modification of histones; it mediates
CC monoubiquitination of histone H2A 'Lys-119', rendering chromatin
CC heritably changed in its expressibility. Promotes histone H3
CC trimethylation at 'Lys-9' (H3K9me3) (By similarity). Binds to histone
CC H3 trimethylated at 'Lys-9' (H3K9me3) or at 'Lys-27' (H3K27me3)
CC (PubMed:16537902, PubMed:22226355). Trimethylation at 'Lys-27'
CC (H3K27me3) is important for chromatin recruitment (PubMed:22226355,
CC PubMed:16537902). May possibly also bind trimethylated lysine residues
CC in other proteins (in vitro) (PubMed:16537902). Binds non-coding,
CC single-stranded RNA and double-stranded RNA (PubMed:20541999,
CC PubMed:16537902). Plays a role in the timely repression of
CC differentiation-specific genes in pluripotent embryonic stem cells to
CC maintain the undifferentiated state (PubMed:22226355). Regulator of
CC cellular lifespan by maintaining the repression of CDKN2A, but not by
CC inducing telomerase activity (PubMed:14647293).
CC {ECO:0000250|UniProtKB:O95931, ECO:0000269|PubMed:14647293,
CC ECO:0000269|PubMed:16537902, ECO:0000269|PubMed:20541999,
CC ECO:0000269|PubMed:22226355}.
CC -!- SUBUNIT: Component of a PRC1-like complex (PubMed:22226355). Distinct
CC PRC1-like core complexes are composed of a RING1 subunit (RING1B or
CC RING1A), one of the six PCGF proteins (PCGF1-6), one PHC protein (PHC1-
CC 3) and one of the CBX proteins (CBX2, CBX4, CBX6, CBX7 or CBX8)
CC (PubMed:22226355). The composition of the PRC1 complex may differ
CC between the PRC1 complex in pluripotent embryonic stem cells containing
CC RNF2, CBX7 and PCGF2, and the PRC1 complex in differentiating cells
CC containing RNF2, CBX2, CBX4 and BMI1 (PubMed:22226355). Interacts with
CC RING1 (PubMed:14647293). Interacts with RNF2, PHC1 and PCGF2
CC (PubMed:22226355). Interacts (via chromodomain) with histone H3K9Me3
CC and H3K27me3 (PubMed:16537902). Interacts with H3K9Me2 and H4K20Me1
CC (PubMed:16537902). Interacts (via chromodomain) with single-stranded
CC and double-stranded RNA; RNA binding seems to be required for the
CC localization to chromatin (PubMed:16537902). Interacts with PCGF1,
CC PCGF3, PCGF5 and PCGF6 (By similarity). {ECO:0000250|UniProtKB:O95931,
CC ECO:0000269|PubMed:14647293, ECO:0000269|PubMed:16537902,
CC ECO:0000269|PubMed:22226355}.
CC -!- INTERACTION:
CC Q8VDS3; Q9NZI8: IGF2BP1; Xeno; NbExp=2; IntAct=EBI-1216533, EBI-1053892;
CC Q8VDS3; Q9HCE1: MOV10; Xeno; NbExp=4; IntAct=EBI-1216533, EBI-1055820;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14647293,
CC ECO:0000269|PubMed:16537902, ECO:0000269|PubMed:20541999}. Chromosome
CC {ECO:0000269|PubMed:16537902, ECO:0000269|PubMed:22226355}.
CC Note=Requires trimethylation at 'Lys-27' (H3K27me3) for the
CC localization to chromatin (PubMed:22226355). Localizes to facultative
CC heterochromatin and to the inactivated X chromosome in females
CC (PubMed:16537902). {ECO:0000269|PubMed:16537902,
CC ECO:0000269|PubMed:22226355}.
CC -!- TISSUE SPECIFICITY: Expressed in embryonic stem cells.
CC {ECO:0000269|PubMed:16537902, ECO:0000269|PubMed:22226355}.
CC -!- DEVELOPMENTAL STAGE: In embryonic fibroblast cultured in vitro,
CC expression gradually decreases with passage number and totally
CC disappears in senescent cells.
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DR EMBL; AY453793; AAR26721.1; -; mRNA.
DR EMBL; BC021398; AAH21398.1; -; mRNA.
DR CCDS; CCDS37143.1; -.
DR RefSeq; NP_659060.1; NM_144811.3.
DR PDB; 2KVM; NMR; -; A=1-71.
DR PDB; 4X3K; X-ray; 1.45 A; A/B=7-66.
DR PDB; 4X3S; X-ray; 1.60 A; A/B=7-66.
DR PDB; 4X3T; X-ray; 2.14 A; A/B/C/D/E/F=7-66.
DR PDB; 4X3U; X-ray; 1.63 A; A/B=7-66.
DR PDB; 5EJW; X-ray; 2.60 A; A=1-71.
DR PDBsum; 2KVM; -.
DR PDBsum; 4X3K; -.
DR PDBsum; 4X3S; -.
DR PDBsum; 4X3T; -.
DR PDBsum; 4X3U; -.
DR PDBsum; 5EJW; -.
DR AlphaFoldDB; Q8VDS3; -.
DR BMRB; Q8VDS3; -.
DR SMR; Q8VDS3; -.
DR BioGRID; 206690; 28.
DR DIP; DIP-38616N; -.
DR IntAct; Q8VDS3; 30.
DR STRING; 10090.ENSMUSP00000105245; -.
DR ChEMBL; CHEMBL3826868; -.
DR iPTMnet; Q8VDS3; -.
DR PhosphoSitePlus; Q8VDS3; -.
DR MaxQB; Q8VDS3; -.
DR PaxDb; Q8VDS3; -.
DR PRIDE; Q8VDS3; -.
DR ProteomicsDB; 279933; -.
DR Antibodypedia; 26564; 141 antibodies from 29 providers.
DR DNASU; 52609; -.
DR Ensembl; ENSMUST00000109615; ENSMUSP00000105244; ENSMUSG00000053411.
DR Ensembl; ENSMUST00000109616; ENSMUSP00000105245; ENSMUSG00000053411.
DR GeneID; 52609; -.
DR KEGG; mmu:52609; -.
DR UCSC; uc007wuv.1; mouse.
DR CTD; 23492; -.
DR MGI; MGI:1196439; Cbx7.
DR VEuPathDB; HostDB:ENSMUSG00000053411; -.
DR eggNOG; KOG2748; Eukaryota.
DR GeneTree; ENSGT00940000158365; -.
DR HOGENOM; CLU_042051_1_1_1; -.
DR InParanoid; Q8VDS3; -.
DR OrthoDB; 1628171at2759; -.
DR PhylomeDB; Q8VDS3; -.
DR TreeFam; TF106456; -.
DR BioGRID-ORCS; 52609; 0 hits in 60 CRISPR screens.
DR ChiTaRS; Cbx7; mouse.
DR EvolutionaryTrace; Q8VDS3; -.
DR PRO; PR:Q8VDS3; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8VDS3; protein.
DR Bgee; ENSMUSG00000053411; Expressed in yolk sac and 148 other tissues.
DR ExpressionAtlas; Q8VDS3; baseline and differential.
DR Genevisible; Q8VDS3; MM.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0000792; C:heterochromatin; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO: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; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
DR GO; GO:0003727; F:single-stranded RNA binding; IDA:UniProtKB.
DR GO; GO:0032183; F:SUMO binding; IBA:GO_Central.
DR GO; GO:0061665; F:SUMO ligase activity; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; ISO:MGI.
DR GO; GO:0016925; P:protein sumoylation; IBA:GO_Central.
DR GO; GO:0048733; P:sebaceous gland development; IMP:MGI.
DR InterPro; IPR043000; CBX7.
DR InterPro; IPR033773; CBX7_C.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR017984; Chromo_dom_subgr.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR023779; Chromodomain_CS.
DR PANTHER; PTHR47277; PTHR47277; 2.
DR Pfam; PF17218; CBX7_C; 1.
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 3D-structure; Chromatin regulator; Chromosome; Nucleus; Reference proteome;
KW Repressor; RNA-binding; Transcription; Transcription regulation.
FT CHAIN 1..158
FT /note="Chromobox protein homolog 7"
FT /id="PRO_0000080213"
FT DOMAIN 11..69
FT /note="Chromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT REGION 60..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 11
FT /note="F->A: Abolishes binding to trimethylated histone
FT H3."
FT /evidence="ECO:0000269|PubMed:16537902"
FT MUTAGEN 17
FT /note="R->A,Q: Strongly reduced RNA binding. Prevents
FT cellular senescence and promotes continued cell division."
FT /evidence="ECO:0000269|PubMed:20541999"
FT MUTAGEN 31
FT /note="K->A: Strongly reduced RNA binding."
FT /evidence="ECO:0000269|PubMed:20541999"
FT MUTAGEN 35
FT /note="W->A: Strongly reduced binding to methylated histone
FT H3 (H3K27me3). Causes premature cellular senescence."
FT /evidence="ECO:0000269|PubMed:16537902,
FT ECO:0000269|PubMed:20541999"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:2KVM"
FT STRAND 10..22
FT /evidence="ECO:0007829|PDB:4X3K"
FT STRAND 25..32
FT /evidence="ECO:0007829|PDB:4X3K"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:4X3K"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:4X3K"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:4X3K"
FT HELIX 51..65
FT /evidence="ECO:0007829|PDB:4X3K"
SQ SEQUENCE 158 AA; 18109 MW; A40021F05B16BEAF CRC64;
MELSAIGEQV FAVESIRKKR VRKGKVEYLV KWKGWPPKYS TWEPEEHILD PRLVMAYEEK
EERDRASGYR KRGPKPRRLL LQESAAPDVV QTPGDWEPME QAPEEEAEAD LTNGPPPWTP
TLPSSEVTVT DITANSVTVT FREAQAAEGF FRDRNEKL
