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E3 SUMO-protein ligase CBX4 (EC 6.3.2.-) (Chromobox protein homolog 4) (Polycomb 2 homolog) (Pc2) (mPc2)

 CBX4_MOUSE              Reviewed;         551 AA.
O55187; Q149G5; Q149G6;
24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
12-DEC-2006, sequence version 2.
05-DEC-2018, entry version 147.
RecName: Full=E3 SUMO-protein ligase CBX4;
EC=2.3.2.-;
AltName: Full=Chromobox protein homolog 4;
AltName: Full=E3 SUMO-protein transferase CBX4 {ECO:0000305};
AltName: Full=Polycomb 2 homolog;
Short=Pc2;
Short=mPc2;
Name=Cbx4; Synonyms=Pc2;
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 [MRNA] (ISOFORM 1).
PubMed=9367786; DOI=10.1006/jmbi.1997.1372;
Alkema M.J., Jacobs J., Voncken J.W., Jenkins N.A., Copeland N.G.,
Satijn D.P.E., Otte A.P., Berns A., van Lohuizen M.;
"MPc2, a new murine homolog of the Drosophila polycomb protein is a
member of the mouse polycomb transcriptional repressor complex.";
J. Mol. Biol. 273:993-1003(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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]
FUNCTION, AND INTERACTION WITH HISTONE H3K9ME3 AND SSRNA.
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).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=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).
[5]
INTERACTION WITH RNF2, AND TISSUE SPECIFICITY.
PubMed=22226355; DOI=10.1016/j.stem.2011.12.006;
Morey L., Pascual G., Cozzuto L., Roma G., Wutz A., Benitah S.A.,
Di Croce L.;
"Nonoverlapping functions of the Polycomb group Cbx family of proteins
in embryonic stem cells.";
Cell Stem Cell 10:47-62(2012).
[6]
INTERACTION WITH CHTOP.
PubMed=22872859; DOI=10.1074/mcp.M112.017194;
Fanis P., Gillemans N., Aghajanirefah A., Pourfarzad F., Demmers J.,
Esteghamat F., Vadlamudi R.K., Grosveld F., Philipsen S.,
van Dijk T.B.;
"Five friends of methylated chromatin target of protein-arginine-
methyltransferase[prmt]-1 (chtop), a complex linking arginine
methylation to desumoylation.";
Mol. Cell. Proteomics 11:1263-1273(2012).
-!- FUNCTION: E3 SUMO-protein ligase which facilitates SUMO1
conjugation by UBE2I. Involved in the sumoylation of HNRNPK, a
p53/TP53 transcriptional coactivator, hence indirectly regulates
p53/TP53 transcriptional activation resulting in p21/CDKN1A
expression. {ECO:0000250|UniProtKB:O00257}.
-!- 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 (By similarity). 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).
Binds to histone H3 trimethylated at 'Lys-9' (H3K9me3)
(PubMed:16537902). Plays a role in the lineage differentiation of
the germ layers in embryonic development (PubMed:22226355).
{ECO:0000250|UniProtKB:O00257, ECO:0000269|PubMed:16537902,
ECO:0000269|PubMed:22226355}.
-!- PATHWAY: Protein modification; protein sumoylation.
-!- SUBUNIT: Interacts with SUV39H1 and HIPK2 (By similarity).
Interacts with CSNK2B (By similarity). Component of a PRC1-like
complex (By similarity). The composition of the PRC1 complex
differs between the PRC1 complex in pluripotent embryonic stem
cells containing RNF2, CBX7 and PCGF2, and the PRC1 complex in
differentiating cells containing RNF2, CBX2, CBX4 and BMI1
(PubMed:22226355). Interacts with RNF2 (PubMed:22226355).
Interacts (via chromodomain) with histone H3K9Me3 and single-
stranded RNA (ssRNA) (PubMed:16537902). Interacts with CHTOP
(PubMed:22872859). May interact with HIST2H3A and HIST1H3A (By
similarity). {ECO:0000250|UniProtKB:O00257,
ECO:0000269|PubMed:16537902, ECO:0000269|PubMed:22226355,
ECO:0000269|PubMed:22872859}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O00257}.
Nucleus speckle {ECO:0000250|UniProtKB:O00257}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O55187-1; Sequence=Displayed;
Name=2;
IsoId=O55187-2; Sequence=VSP_022009;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in embryoid bodies.
{ECO:0000269|PubMed:22226355}.
-!- DOMAIN: The polyhistidine repeat may act as a targeting signal to
nuclear speckles. {ECO:0000250}.
-----------------------------------------------------------------------
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EMBL; U63387; AAB96874.1; -; mRNA.
EMBL; BC117801; AAI17802.1; -; mRNA.
EMBL; BC117802; AAI17803.1; -; mRNA.
CCDS; CCDS25710.1; -. [O55187-1]
RefSeq; NP_031651.2; NM_007625.2. [O55187-1]
UniGene; Mm.268070; -.
UniGene; Mm.471550; -.
ProteinModelPortal; O55187; -.
SMR; O55187; -.
BioGrid; 198537; 25.
IntAct; O55187; 20.
STRING; 10090.ENSMUSP00000026665; -.
iPTMnet; O55187; -.
PhosphoSitePlus; O55187; -.
EPD; O55187; -.
MaxQB; O55187; -.
PaxDb; O55187; -.
PeptideAtlas; O55187; -.
PRIDE; O55187; -.
Ensembl; ENSMUST00000026665; ENSMUSP00000026665; ENSMUSG00000039989. [O55187-1]
GeneID; 12418; -.
KEGG; mmu:12418; -.
UCSC; uc007mpv.2; mouse. [O55187-1]
CTD; 8535; -.
MGI; MGI:1195985; Cbx4.
eggNOG; ENOG410IPQ6; Eukaryota.
eggNOG; ENOG410ZQCR; LUCA.
GeneTree; ENSGT00940000160081; -.
HOGENOM; HOG000231219; -.
HOVERGEN; HBG005257; -.
InParanoid; O55187; -.
KO; K11452; -.
OMA; VLQQKWV; -.
OrthoDB; EOG091G06XV; -.
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-3899300; SUMOylation of transcription cofactors.
Reactome; R-MMU-4551638; SUMOylation of chromatin organization proteins.
Reactome; R-MMU-4570464; SUMOylation of RNA binding 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.
UniPathway; UPA00886; -.
PRO; PR:O55187; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000039989; Expressed in 275 organ(s), highest expression level in olfactory epithelium.
CleanEx; MM_CBX4; -.
Genevisible; O55187; MM.
GO; GO:0016604; C:nuclear body; IDA:MGI.
GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0031519; C:PcG protein complex; ISS:UniProtKB.
GO; GO:0035102; C:PRC1 complex; ISS:UniProtKB.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
GO; GO:0051219; F:phosphoprotein binding; IPI:MGI.
GO; GO:0003727; F:single-stranded RNA binding; IDA:UniProtKB.
GO; GO:0032183; F:SUMO binding; IDA:MGI.
GO; GO:0019789; F:SUMO transferase activity; EXP:Reactome.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:MGI.
GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0016925; P:protein sumoylation; IMP:MGI.
CDD; cd00024; CHROMO; 1.
InterPro; IPR033773; CBX7_C.
InterPro; IPR016197; Chromo-like_dom_sf.
InterPro; IPR000953; Chromo/chromo_shadow_dom.
InterPro; IPR017984; Chromo_dom_subgr.
InterPro; IPR023780; Chromo_domain.
InterPro; IPR023779; Chromodomain_CS.
Pfam; PF17218; CBX7_C; 1.
Pfam; PF00385; Chromo; 1.
PRINTS; PR00504; CHROMODOMAIN.
SMART; SM00298; CHROMO; 1.
SUPFAM; SSF54160; SSF54160; 1.
PROSITE; PS00598; CHROMO_1; 1.
PROSITE; PS50013; CHROMO_2; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Chromatin regulator;
Complete proteome; Isopeptide bond; Nucleus; Phosphoprotein;
Reference proteome; Repressor; Transcription;
Transcription regulation; Transferase; Ubl conjugation;
Ubl conjugation pathway.
CHAIN 1 551 E3 SUMO-protein ligase CBX4.
/FTId=PRO_0000080207.
DOMAIN 11 69 Chromo. {ECO:0000255|PROSITE-
ProRule:PRU00053}.
COMPBIAS 383 395 Poly-His.
MOD_RES 149 149 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:O00257}.
MOD_RES 182 182 Phosphoserine.
{ECO:0000250|UniProtKB:O00257}.
MOD_RES 463 463 Phosphoserine.
{ECO:0000250|UniProtKB:O00257}.
CROSSLNK 77 77 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O00257}.
CROSSLNK 106 106 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O00257}.
CROSSLNK 114 114 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O00257}.
CROSSLNK 125 125 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O00257}.
CROSSLNK 149 149 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:O00257}.
CROSSLNK 157 157 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O00257}.
CROSSLNK 167 167 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O00257}.
CROSSLNK 178 178 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O00257}.
CROSSLNK 191 191 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O00257}.
CROSSLNK 205 205 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O00257}.
CROSSLNK 212 212 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O00257}.
CROSSLNK 223 223 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O00257}.
CROSSLNK 249 249 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O00257}.
CROSSLNK 268 268 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O00257}.
CROSSLNK 278 278 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O00257}.
CROSSLNK 280 280 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O00257}.
CROSSLNK 321 321 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O00257}.
CROSSLNK 353 353 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O00257}.
CROSSLNK 366 366 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O00257}.
CROSSLNK 490 490 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000250}.
CROSSLNK 490 490 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:O00257}.
VAR_SEQ 1 66 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_022009.
CONFLICT 77 77 K -> N (in Ref. 1; AAB96874).
{ECO:0000305}.
CONFLICT 144 145 PG -> AR (in Ref. 1; AAB96874).
{ECO:0000305}.
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


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