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Chromobox protein homolog 8 (Polycomb 3 homolog) (Pc3) (mPc3)

 CBX8_MOUSE              Reviewed;         362 AA.
Q9QXV1;
29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
20-JUN-2018, entry version 145.
RecName: Full=Chromobox protein homolog 8;
AltName: Full=Polycomb 3 homolog;
Short=Pc3;
Short=mPc3;
Name=Cbx8; Synonyms=Pc3;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
STRAIN=129/SvJ;
PubMed=10721694; DOI=10.1016/S0378-1119(99)00540-5;
Hemenway C.S., Halligan B.W., Gould G.C.D., Levy L.S.;
"Identification and analysis of a third mouse Polycomb gene, MPc3.";
Gene 242:31-40(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
RECONSTITUTION OF A PRC1-LIKE COMPLEX, AND INTERACTION WITH RING1;
RNF2; BMI1 AND PHC2.
PubMed=16359901; DOI=10.1016/j.molcel.2005.12.002;
Cao R., Tsukada Y., Zhang Y.;
"Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene
silencing.";
Mol. Cell 20:845-854(2005).
[4]
INTERACTION WITH MLLT3.
PubMed=11439343; DOI=10.1038/sj.onc.1204478;
Hemenway C.S., de Erkenez A.C., Gould G.C.D.;
"The polycomb protein MPc3 interacts with AF9, an MLL fusion partner
in t(9;11)(p22;q23) acute leukemias.";
Oncogene 20:3798-3805(2001).
[5]
INTERACTION WITH RNA, AND SUBCELLULAR LOCATION.
PubMed=16537902; DOI=10.1128/MCB.26.7.2560-2569.2006;
Bernstein E., Duncan E.M., Masui O., Gil J., Heard E., Allis C.D.;
"Mouse polycomb proteins bind differentially to methylated histone H3
and RNA and are enriched in facultative heterochromatin.";
Mol. Cell. Biol. 26:2560-2569(2006).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229 AND SER-284, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110; SER-229; TYR-234
AND SER-284, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, and
Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[8]
STRUCTURE BY NMR OF 7-58.
RIKEN structural genomics initiative (RSGI);
"Solution structure of RSGI RUH-055, a chromo domain from Mus musculus
cDNA.";
Submitted (OCT-2006) to the PDB data bank.
-!- FUNCTION: 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. 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 (By similarity).
{ECO:0000250|UniProtKB:Q9HC52}.
-!- SUBUNIT: Component of a PRC1-like complex (PubMed:16359901).
Interacts with RING1, RNF2, PCGF1, PCGF2, PCGF3, BMI1, PCGF5,
PCGF6 and PHC2 (PubMed:16359901). Interacts with histone H3 (By
similarity). Interacts with MLLT3 (Ref.8). Interacts with PHC2 (By
similarity). Interacts (via chromodomain) with single-stranded RNA
(PubMed:16537902). {ECO:0000250|UniProtKB:Q9HC52,
ECO:0000269|PubMed:11439343, ECO:0000269|PubMed:16359901,
ECO:0000269|PubMed:16537902}.
-!- INTERACTION:
P25916:Bmi1; NbExp=3; IntAct=EBI-1216641, EBI-927401;
O35730:Ring1; NbExp=2; IntAct=EBI-1216641, EBI-929310;
Q9CQJ4:Rnf2; NbExp=5; IntAct=EBI-1216641, EBI-927321;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16537902}.
Chromosome {ECO:0000269|PubMed:16537902}. Note=Localizes to the
inactivated X chromosome in females.
{ECO:0000269|PubMed:16537902}.
-----------------------------------------------------------------------
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EMBL; AF180370; AAF25615.1; -; mRNA.
EMBL; AF202116; AAF26713.1; -; Genomic_DNA.
EMBL; BC014815; AAH14815.1; -; mRNA.
CCDS; CCDS25709.1; -.
RefSeq; NP_038954.1; NM_013926.1.
UniGene; Mm.99953; -.
PDB; 2DNV; NMR; -; A=8-58.
PDBsum; 2DNV; -.
ProteinModelPortal; Q9QXV1; -.
SMR; Q9QXV1; -.
BioGrid; 206027; 7.
IntAct; Q9QXV1; 5.
STRING; 10090.ENSMUSP00000026663; -.
iPTMnet; Q9QXV1; -.
PhosphoSitePlus; Q9QXV1; -.
EPD; Q9QXV1; -.
MaxQB; Q9QXV1; -.
PaxDb; Q9QXV1; -.
PeptideAtlas; Q9QXV1; -.
PRIDE; Q9QXV1; -.
Ensembl; ENSMUST00000026663; ENSMUSP00000026663; ENSMUSG00000025578.
GeneID; 30951; -.
KEGG; mmu:30951; -.
UCSC; uc007mpu.1; mouse.
CTD; 57332; -.
MGI; MGI:1353589; Cbx8.
eggNOG; ENOG410IPQ7; Eukaryota.
eggNOG; ENOG410XRRX; LUCA.
GeneTree; ENSGT00530000063056; -.
HOGENOM; HOG000233642; -.
HOVERGEN; HBG003608; -.
InParanoid; Q9QXV1; -.
KO; K11455; -.
OMA; QCGVASP; -.
OrthoDB; EOG091G0MFV; -.
PhylomeDB; Q9QXV1; -.
TreeFam; TF106456; -.
Reactome; R-MMU-2559580; Oxidative Stress Induced Senescence.
Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins.
Reactome; R-MMU-4551638; SUMOylation of chromatin organization proteins.
Reactome; R-MMU-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
Reactome; R-MMU-8943724; Regulation of PTEN gene transcription.
EvolutionaryTrace; Q9QXV1; -.
PRO; PR:Q9QXV1; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000025578; -.
CleanEx; MM_CBX8; -.
Genevisible; Q9QXV1; MM.
GO; GO:0000792; C:heterochromatin; IDA:UniProtKB.
GO; GO:0000790; C:nuclear chromatin; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0031519; C:PcG protein complex; IDA:MGI.
GO; GO:0035102; C:PRC1 complex; ISS:UniProtKB.
GO; GO:0000151; C:ubiquitin ligase complex; IDA:MGI.
GO; GO:0035064; F:methylated histone binding; ISO:MGI.
GO; GO:0003727; F:single-stranded RNA binding; IDA:UniProtKB.
GO; GO:0097027; F:ubiquitin-protein transferase activator activity; IDA:MGI.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
GO; GO:0006342; P:chromatin silencing; ISS:MGI.
GO; GO:0016574; P:histone ubiquitination; IDA:MGI.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
GO; GO:0008284; P:positive regulation of cell proliferation; ISO:MGI.
GO; GO:0032967; P:positive regulation of collagen biosynthetic process; ISO:MGI.
GO; GO:0045739; P:positive regulation of DNA repair; ISO:MGI.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd00024; CHROMO; 1.
InterPro; IPR033773; CBX7_C.
InterPro; IPR016197; Chromo-like_dom_sf.
InterPro; IPR000953; Chromo/chromo_shadow_dom.
InterPro; IPR023780; Chromo_domain.
InterPro; IPR023779; Chromodomain_CS.
Pfam; PF17218; CBX7_C; 1.
Pfam; PF00385; Chromo; 1.
SMART; SM00298; CHROMO; 1.
SUPFAM; SSF54160; SSF54160; 1.
PROSITE; PS00598; CHROMO_1; 1.
PROSITE; PS50013; CHROMO_2; 1.
1: Evidence at protein level;
3D-structure; Chromatin regulator; Chromosome; Complete proteome;
Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription;
Transcription regulation.
CHAIN 1 362 Chromobox protein homolog 8.
/FTId=PRO_0000080216.
DOMAIN 11 69 Chromo. {ECO:0000255|PROSITE-
ProRule:PRU00053}.
MOD_RES 110 110 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 164 164 Phosphoserine.
{ECO:0000250|UniProtKB:Q9HC52}.
MOD_RES 229 229 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 234 234 Phosphotyrosine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 238 238 Phosphoserine.
{ECO:0000250|UniProtKB:Q9HC52}.
MOD_RES 284 284 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 305 305 Phosphoserine.
{ECO:0000250|UniProtKB:Q9HC52}.
MOD_RES 325 325 Phosphoserine.
{ECO:0000250|UniProtKB:Q9HC52}.
STRAND 16 30 {ECO:0000244|PDB:2DNV}.
STRAND 42 44 {ECO:0000244|PDB:2DNV}.
TURN 45 47 {ECO:0000244|PDB:2DNV}.
HELIX 51 58 {ECO:0000244|PDB:2DNV}.
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


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