PCGF6_MOUSE
ID PCGF6_MOUSE Reviewed; 353 AA.
AC Q99NA9;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Polycomb group RING finger protein 6;
DE AltName: Full=Mel18 and Bmi1-like RING finger;
DE AltName: Full=RING finger protein 134;
GN Name=Pcgf6; Synonyms=Mblr, Rnf134;
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, AND DEVELOPMENTAL STAGE.
RC TISSUE=Thymus;
RX PubMed=12167161; DOI=10.1046/j.1365-2443.2002.00565.x;
RA Akasaka T., Takahashi N., Suzuki M., Koseki H., Bodmer R., Koga H.;
RT "MBLR, a new RING finger protein resembling mammalian Polycomb gene
RT products, is regulated by cell cycle-dependent phosphorylation.";
RL Genes Cells 7:835-850(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
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).
CC -!- FUNCTION: Transcriptional repressor. May modulate the levels of histone
CC H3K4Me3 by activating KDM5D histone demethylase. Component of a
CC Polycomb group (PcG) multiprotein PRC1-like complex, a complex class
CC required to maintain the transcriptionally repressive state of many
CC genes, including Hox genes, throughout development. PcG PRC1 complex
CC acts via chromatin remodeling and modification of histones; it mediates
CC monoubiquitination of histone H2A 'Lys-119', rendering chromatin
CC heritably changed in its expressibility. Within the PRC1-like complex,
CC regulates RNF2 ubiquitin ligase activity.
CC {ECO:0000250|UniProtKB:Q9BYE7}.
CC -!- SUBUNIT: Component of a PRC1-like complex. Interacts with BMI1/PCGF4,
CC RING1 and RNF2. Interacts with KDM5D. Interacts with CBX4, CBX6, CBX7
CC and CBX8. {ECO:0000250|UniProtKB:Q9BYE7}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BYE7}.
CC -!- TISSUE SPECIFICITY: Expressed in ovary, testis, stomach, liver, thymus
CC and kidney (at protein level). {ECO:0000269|PubMed:12167161}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryo at 10.5 dpc.
CC {ECO:0000269|PubMed:12167161}.
CC -!- PTM: Phosphorylated during mitosis. {ECO:0000250|UniProtKB:Q9BYE7}.
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DR EMBL; AB047007; BAB40780.1; -; mRNA.
DR EMBL; BC016195; AAH16195.1; -; mRNA.
DR EMBL; BC089460; AAH89460.1; -; mRNA.
DR CCDS; CCDS29885.1; -.
DR RefSeq; NP_081930.1; NM_027654.3.
DR AlphaFoldDB; Q99NA9; -.
DR BMRB; Q99NA9; -.
DR SMR; Q99NA9; -.
DR BioGRID; 214431; 10.
DR IntAct; Q99NA9; 6.
DR MINT; Q99NA9; -.
DR STRING; 10090.ENSMUSP00000026032; -.
DR iPTMnet; Q99NA9; -.
DR PhosphoSitePlus; Q99NA9; -.
DR EPD; Q99NA9; -.
DR MaxQB; Q99NA9; -.
DR PaxDb; Q99NA9; -.
DR PeptideAtlas; Q99NA9; -.
DR PRIDE; Q99NA9; -.
DR ProteomicsDB; 288069; -.
DR Antibodypedia; 31521; 162 antibodies from 22 providers.
DR DNASU; 71041; -.
DR Ensembl; ENSMUST00000026032; ENSMUSP00000026032; ENSMUSG00000025050.
DR GeneID; 71041; -.
DR KEGG; mmu:71041; -.
DR UCSC; uc008hul.1; mouse.
DR CTD; 84108; -.
DR MGI; MGI:1918291; Pcgf6.
DR VEuPathDB; HostDB:ENSMUSG00000025050; -.
DR eggNOG; KOG2660; Eukaryota.
DR GeneTree; ENSGT00940000158034; -.
DR HOGENOM; CLU_046427_4_0_1; -.
DR InParanoid; Q99NA9; -.
DR OMA; FSSNRCP; -.
DR OrthoDB; 1203951at2759; -.
DR PhylomeDB; Q99NA9; -.
DR TreeFam; TF324206; -.
DR Reactome; R-MMU-8953750; Transcriptional Regulation by E2F6.
DR BioGRID-ORCS; 71041; 3 hits in 77 CRISPR screens.
DR ChiTaRS; Pcgf6; mouse.
DR PRO; PR:Q99NA9; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q99NA9; protein.
DR Bgee; ENSMUSG00000025050; Expressed in animal zygote and 252 other tissues.
DR ExpressionAtlas; Q99NA9; baseline and differential.
DR Genevisible; Q99NA9; MM.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0036353; P:histone H2A-K119 monoubiquitination; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR038037; PCGF6.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR10825:SF74; PTHR10825:SF74; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..353
FT /note="Polycomb group RING finger protein 6"
FT /id="PRO_0000055990"
FT ZN_FING 137..176
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 71..112
FT /evidence="ECO:0000255"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..39
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..103
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BYE7"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 226
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BYE7"
FT CROSSLNK 237
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BYE7"
SQ SEQUENCE 353 AA; 39820 MW; 0D29B7FE065B5448 CRC64;
MDEAETDATE NKRASEAKRA SAMPPPPPPP PPISPPALIP APAAGEEGPA SLGQAGAAGC
SRSRPPALEP ERSLGRLRGR FEDYDEELEE EEEMEEEEEE EEEMSHFSLR LESGRADSED
EEERLINLVE LTPYILCSIC KGYLIDATTI TECLHTFCKS CIVRHFYYSN RCPKCNIVVH
QTQPLYNIRL DRQLQDIVYK LVINLEEREK KQMHDFYKER GLEVPKPAAP QPVPSSKGKT
KKVLESVFRI PPELDMSLLL EFIGANEDTG HFKPLEKKFV RVSGEATIGH VEKFLRRKMG
LDPACQVDII CGDHLLERYQ TLREIRRAIG DTAMQDGLLV LHYGLVVSPL KIT
