PCGF2_MOUSE
ID PCGF2_MOUSE Reviewed; 342 AA.
AC P23798;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Polycomb group RING finger protein 2;
DE AltName: Full=DNA-binding protein Mel-18;
DE AltName: Full=Melanoma nuclear protein 18;
DE AltName: Full=RING finger protein 110;
DE AltName: Full=Zinc finger protein 144;
DE Short=Zfp-144;
GN Name=Pcgf2; Synonyms=Mel-18, Mel18, Rnf110, Zfp144, Znf144;
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], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP SUBCELLULAR LOCATION.
RX PubMed=2246278; DOI=10.1016/s0021-9258(17)45476-7;
RA Tagawa M., Sakamoto T., Shigemoto K., Matsubara H., Tamura Y., Ito T.,
RA Nakamura I., Okitsu A., Imai K., Taniguchi M.;
RT "Expression of novel DNA-binding protein with zinc finger structure in
RT various tumor cells.";
RL J. Biol. Chem. 265:20021-20026(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ILS, and ISS;
RX PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
RA Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RT "High-throughput sequence identification of gene coding variants within
RT alcohol-related QTLs.";
RL Mamm. Genome 12:657-663(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP FUNCTION.
RX PubMed=8521824; DOI=10.1002/j.1460-2075.1995.tb00254.x;
RA Kanno M., Hasegawa M., Ishida A., Isono K., Taniguchi M.;
RT "mel-18, a Polycomb group-related mammalian gene, encodes a transcriptional
RT negative regulator with tumor suppressive activity.";
RL EMBO J. 14:5672-5678(1995).
RN [5]
RP FUNCTION.
RX PubMed=8625838; DOI=10.1242/dev.122.5.1513;
RA Akasaka T., Kanno M., Balling R., Mieza M.A., Taniguchi M., Koseki H.;
RT "A role for mel-18, a Polycomb group-related vertebrate gene, during the
RT anteroposterior specification of the axial skeleton.";
RL Development 122:1513-1522(1996).
RN [6]
RP FUNCTION.
RX PubMed=11750047; DOI=10.1016/s0165-2478(01)00315-7;
RA Miyazaki K., Inoue H., Onai N., Ishihara H., Kanno M.;
RT "Chemokine-mediated thymopoiesis is regulated by a mammalian Polycomb group
RT gene, mel-18.";
RL Immunol. Lett. 80:139-143(2002).
RN [7]
RP SUBUNIT, AND PHOSPHORYLATION.
RX PubMed=12480532; DOI=10.1016/s0006-291x(02)02791-2;
RA Fujisaki S., Ninomiya Y., Ishihara H., Miyazaki M., Kanno R., Asahara T.,
RA Kanno M.;
RT "Dimerization of the Polycomb-group protein Mel-18 is regulated by PKC
RT phosphorylation.";
RL Biochem. Biophys. Res. Commun. 300:135-140(2003).
RN [8]
RP FUNCTION.
RX PubMed=15183898; DOI=10.1016/j.exphem.2004.03.001;
RA Kajiume T., Ninomiya Y., Ishihara H., Kanno R., Kanno M.;
RT "Polycomb group gene mel-18 modulates the self-renewal activity and cell
RT cycle status of hematopoietic stem cells.";
RL Exp. Hematol. 32:571-578(2004).
RN [9]
RP FUNCTION.
RX PubMed=15728456; DOI=10.4049/jimmunol.174.5.2507;
RA Miyazaki M., Kawamoto H., Kato Y., Itoi M., Miyazaki K., Masuda K.,
RA Tashiro S., Ishihara H., Igarashi K., Amagai T., Kanno R., Kanno M.;
RT "Polycomb group gene mel-18 regulates early T progenitor expansion by
RT maintaining the expression of Hes-1, a target of the Notch pathway.";
RL J. Immunol. 174:2507-2516(2005).
RN [10]
RP INTERACTION WITH PHC2.
RX PubMed=16024804; DOI=10.1128/mcb.25.15.6694-6706.2005;
RA Isono K., Fujimura Y., Shinga J., Yamaki M., O-Wang J., Takihara Y.,
RA Murahashi Y., Takada Y., Mizutani-Koseki Y., Koseki H.;
RT "Mammalian polyhomeotic homologues Phc2 and Phc1 act in synergy to mediate
RT polycomb repression of Hox genes.";
RL Mol. Cell. Biol. 25:6694-6706(2005).
RN [11]
RP INTERACTION WITH RNF2 AND CBX7, 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: Transcriptional repressor (PubMed:8521824). Binds
CC specifically to the DNA sequence 5'-GACTNGACT-3' (PubMed:8521824). Has
CC tumor suppressor activity (PubMed:8521824). May play a role in control
CC of cell proliferation and/or neural cell development (Probable).
CC Regulates proliferation of early T progenitor cells by maintaining
CC expression of HES1(PubMed:15728456). Also plays a role in antero-
CC posterior specification of the axial skeleton and negative regulation
CC of the self-renewal activity of hematopoietic stem cells
CC (PubMed:8625838, PubMed:15183898). Component of a Polycomb group (PcG)
CC multiprotein PRC1-like complex, a complex class required to maintain
CC the transcriptionally repressive state of many genes, including Hox
CC genes, throughout development. 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. Within the PRC1-like complex, regulates RNF2 ubiquitin
CC ligase activity (By similarity). {ECO:0000250|UniProtKB:P35227,
CC ECO:0000269|PubMed:11750047, ECO:0000269|PubMed:15183898,
CC ECO:0000269|PubMed:15728456, ECO:0000269|PubMed:8521824,
CC ECO:0000269|PubMed:8625838, ECO:0000305}.
CC -!- SUBUNIT: Exists as both a monomer and homodimer (PubMed:12480532).
CC Component of a PRC1-like complex. Interacts with CBX8, RING1 AND RNF2
CC (By similarity). Interacts with CBX7 (PubMed:22226355). Interacts with
CC PHC2 (PubMed:16024804). {ECO:0000250|UniProtKB:P35227,
CC ECO:0000269|PubMed:12480532, ECO:0000269|PubMed:22226355}.
CC -!- INTERACTION:
CC P23798; Q60848: Hells; NbExp=2; IntAct=EBI-926857, EBI-3043887;
CC P23798; Q64028: Phc1; NbExp=4; IntAct=EBI-926857, EBI-927346;
CC P23798; Q9QWH1: Phc2; NbExp=5; IntAct=EBI-926857, EBI-642357;
CC P23798; Q9CQJ4: Rnf2; NbExp=15; IntAct=EBI-926857, EBI-927321;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:2246278}.
CC -!- TISSUE SPECIFICITY: Expressed in embryonic stem cells
CC (PubMed:22226355). Expressed in a variety of tumor cells and in neural
CC tissues (PubMed:2246278). {ECO:0000269|PubMed:22226355,
CC ECO:0000269|PubMed:2246278}.
CC -!- DEVELOPMENTAL STAGE: Developmentally regulated.
CC {ECO:0000269|PubMed:2246278}.
CC -!- PTM: Phosphorylated. Homodimer formation is regulated by
CC phosphorylation with only unphosphorylated proteins forming homodimers.
CC {ECO:0000269|PubMed:12480532}.
CC -!- DISEASE: Note=Probably related to tumorigenesis since it is expressed
CC strongly in most tumor cell lines.
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DR EMBL; D90085; BAA14122.1; -; mRNA.
DR EMBL; AF483502; AAL90776.1; -; mRNA.
DR EMBL; AF483503; AAL90777.1; -; mRNA.
DR EMBL; BC016419; AAH16419.1; -; mRNA.
DR CCDS; CCDS25327.1; -.
DR PIR; A37991; A37991.
DR RefSeq; NP_001156779.1; NM_001163307.1.
DR RefSeq; NP_001156780.1; NM_001163308.1.
DR RefSeq; NP_033571.1; NM_009545.2.
DR RefSeq; XP_011247274.1; XM_011248972.2.
DR RefSeq; XP_011247275.1; XM_011248973.2.
DR RefSeq; XP_011247277.1; XM_011248975.2.
DR RefSeq; XP_017169992.1; XM_017314503.1.
DR AlphaFoldDB; P23798; -.
DR SMR; P23798; -.
DR BioGRID; 204639; 14.
DR CORUM; P23798; -.
DR DIP; DIP-37645N; -.
DR IntAct; P23798; 14.
DR MINT; P23798; -.
DR STRING; 10090.ENSMUSP00000018681; -.
DR iPTMnet; P23798; -.
DR PhosphoSitePlus; P23798; -.
DR EPD; P23798; -.
DR MaxQB; P23798; -.
DR PaxDb; P23798; -.
DR PeptideAtlas; P23798; -.
DR PRIDE; P23798; -.
DR ProteomicsDB; 287966; -.
DR Antibodypedia; 72907; 258 antibodies from 34 providers.
DR DNASU; 22658; -.
DR Ensembl; ENSMUST00000018681; ENSMUSP00000018681; ENSMUSG00000018537.
DR Ensembl; ENSMUST00000103148; ENSMUSP00000099437; ENSMUSG00000018537.
DR Ensembl; ENSMUST00000169807; ENSMUSP00000126967; ENSMUSG00000018537.
DR Ensembl; ENSMUST00000179765; ENSMUSP00000137517; ENSMUSG00000018537.
DR GeneID; 22658; -.
DR KEGG; mmu:22658; -.
DR UCSC; uc007lel.2; mouse.
DR CTD; 7703; -.
DR MGI; MGI:99161; Pcgf2.
DR VEuPathDB; HostDB:ENSMUSG00000018537; -.
DR eggNOG; KOG2660; Eukaryota.
DR GeneTree; ENSGT00940000159730; -.
DR HOGENOM; CLU_046427_0_0_1; -.
DR InParanoid; P23798; -.
DR OMA; MDIAYIL; -.
DR OrthoDB; 1344247at2759; -.
DR PhylomeDB; P23798; -.
DR TreeFam; TF324206; -.
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-8953750; Transcriptional Regulation by E2F6.
DR BioGRID-ORCS; 22658; 2 hits in 78 CRISPR screens.
DR ChiTaRS; Pcgf2; mouse.
DR PRO; PR:P23798; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P23798; protein.
DR Bgee; ENSMUSG00000018537; Expressed in undifferentiated genital tubercle and 205 other tissues.
DR ExpressionAtlas; P23798; baseline and differential.
DR Genevisible; P23798; MM.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; IDA:MGI.
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:UniProtKB.
DR GO; GO:0035102; C:PRC1 complex; ISS:UniProtKB.
DR GO; GO:0001739; C:sex chromatin; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IBA:GO_Central.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IMP:MGI.
DR GO; GO:0097190; P:apoptotic signaling pathway; IGI:MGI.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IDA:MGI.
DR GO; GO:0048706; P:embryonic skeletal system development; IGI:MGI.
DR GO; GO:0048704; P:embryonic skeletal system morphogenesis; IGI:MGI.
DR GO; GO:0016573; P:histone acetylation; IGI:MGI.
DR GO; GO:0036353; P:histone H2A-K119 monoubiquitination; ISS:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IGI:MGI.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IGI:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:MGI.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR032443; RAWUL.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF16207; RAWUL; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..342
FT /note="Polycomb group RING finger protein 2"
FT /id="PRO_0000055985"
FT ZN_FING 18..57
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 237..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 81..95
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 241..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 237
FT /note="Phosphothreonine; by PKA"
FT /evidence="ECO:0000255"
FT MOD_RES 334
FT /note="Phosphothreonine; by PKA"
FT /evidence="ECO:0000255"
FT CROSSLNK 51
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P35227"
FT CROSSLNK 88
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P35227"
SQ SEQUENCE 342 AA; 37723 MW; C23031B8B9E30108 CRC64;
MHRTTRIKIT ELNPHLMCAL CGGYFIDATT IVECLHSFCK TCIVRYLETN KYCPMCDVQV
HKTRPLLSIR SDKTLQDIVY KLVPGLFKDE MKRRRDFYAA YPLTEVPNGS NEDRGEVLEQ
EKGALGDDEI VSLSIEFYEG VRDREEKKNL TENGDGDKEK TGVRFLRCPA AMTVMHLAKF
LRNKMDVPSK YKVEILYEDE PLKEYYTLMD IAYIYPWRRN GPLPLKYRVQ PACKRLTLPT
VPTPSEGTNT SGASECESVS DKAPSPATLP ATSSSLPSPA TPSHGSPSSH GPPATHPTSP
TPPSTAAGTT TATNGGTSNC LQTPSSTSRG RKMTVNGAPC PP
