CBX8_MOUSE
ID CBX8_MOUSE Reviewed; 362 AA.
AC Q9QXV1;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Chromobox protein homolog 8;
DE AltName: Full=Polycomb 3 homolog;
DE Short=Pc3;
DE Short=mPc3;
GN Name=Cbx8; Synonyms=Pc3;
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 [GENOMIC DNA / MRNA].
RC STRAIN=129/SvJ;
RX PubMed=10721694; DOI=10.1016/s0378-1119(99)00540-5;
RA Hemenway C.S., Halligan B.W., Gould G.C.D., Levy L.S.;
RT "Identification and analysis of a third mouse Polycomb gene, MPc3.";
RL Gene 242:31-40(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 RECONSTITUTION OF A PRC1-LIKE COMPLEX, AND INTERACTION WITH RING1; RNF2;
RP BMI1 AND PHC2.
RX PubMed=16359901; DOI=10.1016/j.molcel.2005.12.002;
RA Cao R., Tsukada Y., Zhang Y.;
RT "Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene silencing.";
RL Mol. Cell 20:845-854(2005).
RN [4]
RP INTERACTION WITH MLLT3.
RX PubMed=11439343; DOI=10.1038/sj.onc.1204478;
RA Hemenway C.S., de Erkenez A.C., Gould G.C.D.;
RT "The polycomb protein MPc3 interacts with AF9, an MLL fusion partner in
RT t(9;11)(p22;q23) acute leukemias.";
RL Oncogene 20:3798-3805(2001).
RN [5]
RP INTERACTION WITH RNA, AND SUBCELLULAR 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229 AND SER-284, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110; SER-229; TYR-234 AND
RP SER-284, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, and
RC Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP STRUCTURE BY NMR OF 7-58.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RSGI RUH-055, a chromo domain from Mus musculus
RT cDNA.";
RL Submitted (OCT-2006) to the PDB data bank.
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. PcG PRC1 complex acts via chromatin remodeling and
CC modification of histones; it mediates monoubiquitination of histone H2A
CC 'Lys-119', rendering chromatin heritably changed in its expressibility
CC (By similarity). {ECO:0000250|UniProtKB:Q9HC52}.
CC -!- SUBUNIT: Component of a PRC1-like complex (PubMed:16359901). Interacts
CC with RING1, RNF2, PCGF1, PCGF2, PCGF3, BMI1, PCGF5, PCGF6 and PHC2
CC (PubMed:16359901). Interacts with histone H3 (By similarity). Interacts
CC with MLLT3 (Ref.8). Interacts with PHC2 (By similarity). Interacts (via
CC chromodomain) with single-stranded RNA (PubMed:16537902).
CC {ECO:0000250|UniProtKB:Q9HC52, ECO:0000269|PubMed:11439343,
CC ECO:0000269|PubMed:16359901, ECO:0000269|PubMed:16537902}.
CC -!- INTERACTION:
CC Q9QXV1; P25916: Bmi1; NbExp=3; IntAct=EBI-1216641, EBI-927401;
CC Q9QXV1; O35730: Ring1; NbExp=2; IntAct=EBI-1216641, EBI-929310;
CC Q9QXV1; Q9CQJ4: Rnf2; NbExp=5; IntAct=EBI-1216641, EBI-927321;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16537902}. Chromosome
CC {ECO:0000269|PubMed:16537902}. Note=Localizes to the inactivated X
CC chromosome in females. {ECO:0000269|PubMed:16537902}.
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DR EMBL; AF180370; AAF25615.1; -; mRNA.
DR EMBL; AF202116; AAF26713.1; -; Genomic_DNA.
DR EMBL; BC014815; AAH14815.1; -; mRNA.
DR CCDS; CCDS25709.1; -.
DR RefSeq; NP_038954.1; NM_013926.1.
DR PDB; 2DNV; NMR; -; A=8-58.
DR PDBsum; 2DNV; -.
DR AlphaFoldDB; Q9QXV1; -.
DR SMR; Q9QXV1; -.
DR BioGRID; 206027; 7.
DR IntAct; Q9QXV1; 5.
DR STRING; 10090.ENSMUSP00000026663; -.
DR iPTMnet; Q9QXV1; -.
DR PhosphoSitePlus; Q9QXV1; -.
DR EPD; Q9QXV1; -.
DR jPOST; Q9QXV1; -.
DR MaxQB; Q9QXV1; -.
DR PaxDb; Q9QXV1; -.
DR PeptideAtlas; Q9QXV1; -.
DR PRIDE; Q9QXV1; -.
DR ProteomicsDB; 265685; -.
DR Antibodypedia; 19753; 698 antibodies from 38 providers.
DR DNASU; 30951; -.
DR Ensembl; ENSMUST00000026663; ENSMUSP00000026663; ENSMUSG00000025578.
DR GeneID; 30951; -.
DR KEGG; mmu:30951; -.
DR UCSC; uc007mpu.1; mouse.
DR CTD; 57332; -.
DR MGI; MGI:1353589; Cbx8.
DR VEuPathDB; HostDB:ENSMUSG00000025578; -.
DR eggNOG; KOG2748; Eukaryota.
DR GeneTree; ENSGT00940000158476; -.
DR HOGENOM; CLU_042051_0_1_1; -.
DR InParanoid; Q9QXV1; -.
DR OMA; HPENHGH; -.
DR OrthoDB; 1628171at2759; -.
DR PhylomeDB; Q9QXV1; -.
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; 30951; 0 hits in 112 CRISPR screens.
DR ChiTaRS; Cbx8; mouse.
DR EvolutionaryTrace; Q9QXV1; -.
DR PRO; PR:Q9QXV1; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9QXV1; protein.
DR Bgee; ENSMUSG00000025578; Expressed in embryonic brain and 201 other tissues.
DR Genevisible; Q9QXV1; MM.
DR GO; GO:0000785; C:chromatin; 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; IDA:MGI.
DR GO; GO:0035102; C:PRC1 complex; ISS:UniProtKB.
DR GO; GO:0000151; C:ubiquitin ligase complex; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0035064; F:methylated histone binding; ISO:MGI.
DR GO; GO:0003727; F:single-stranded RNA binding; IDA:UniProtKB.
DR GO; GO:0097027; F:ubiquitin-protein transferase activator activity; IDA:MGI.
DR GO; GO:0031507; P:heterochromatin assembly; ISS:MGI.
DR GO; GO:0016574; P:histone ubiquitination; IDA:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0032967; P:positive regulation of collagen biosynthetic process; ISO:MGI.
DR GO; GO:0045739; P:positive regulation of DNA repair; ISO:MGI.
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 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 3D-structure; Chromatin regulator; Chromosome; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..362
FT /note="Chromobox protein homolog 8"
FT /id="PRO_0000080216"
FT DOMAIN 11..69
FT /note="Chromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT REGION 90..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HC52"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 234
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HC52"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 305
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HC52"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HC52"
FT STRAND 16..30
FT /evidence="ECO:0007829|PDB:2DNV"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:2DNV"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:2DNV"
FT HELIX 51..58
FT /evidence="ECO:0007829|PDB:2DNV"
SQ SEQUENCE 362 AA; 39860 MW; EE047F57483741B2 CRC64;
MELSAVGERV FAAEALLKRR IRKGRMEYLV KWKGWSQKYS TWEPEENILD ARLLAAFEER
EREMELYGPK KRGPKPKTFL LKAQAKAKAK TYEFRSDSTR GIRIPYPGRS PQDLASTSRA
REGLRNTGLP PPGSSTSTCR ADPPRDRDRE RDRGTSRVDD KPSSPGDSSK KRGPKPRKEP
LDPSQRPLGE PSAGLGEYLK GRKLDETSSG TGKFPAGHSV IQLARRQDSD LVQYGVTSPS
SAEASSKLAV DTFPARVIKH RAAFLEAKGQ GALDPGGARV RHSSGTPASV GSLYRDMGAQ
GGRPSLIARI PVARILGDPE EESWSPSLTN LEKVVVTDVT SNFLTVTIKE SNTDQGFFKE
KR
