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DescriptionRecName: Full=Polycomb group RING finger protein 6; AltName: Full=Mel18 and Bmi1-like RING finger; AltName: Full=RING finger protein 134;
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MyHits synonymsPCGF6_MOUSE , Q99NA9 , 0D29B7FE065B5448
match map segment
ismart:RING iprf:ZF_RING_2 ipat:ZF_RING_1  
Legends: 1, Phosphoserine. {ECO:0000250|UniProtKB:Q9BYE7}; 2, Phosphoserine. {ECO:0000244|PubMed:21183079}; 3, ZN_FING RING-type. {ECO:0000255|PROSITE- ProRule:PRU00175}; 4, COILED {ECO:0000255}; 5, COMPBIAS Pro-rich; 6, COMPBIAS Glu-rich; 7, ismart:RING [T]; 8, iprf:ZF_RING_2 [T]; 9, ipat:ZF_RING_1 [T].
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   02-NOV-2016, entry version 118.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, AND IDENTIFICATION
RP   BY 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
RT   expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Transcriptional repressor. May modulate the levels of
CC       histone H3K4Me3 by activating KDM5D histone demethylase. Component
CC       of a Polycomb group (PcG) multiprotein PRC1-like complex, a
CC       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
CC       histone H2A 'Lys-119', rendering chromatin heritably changed in
CC       its expressibility (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of a PRC1-like complex. Interacts with
CC       BMI1/PCGF4, RING1 and RNF2. Interacts with KDM5D. Interacts with
CC       CBX4, CBX6, CBX7 and CBX8 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in ovary, testis, stomach, liver,
CC       thymus and kidney (at protein level).
CC       {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}.
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC       {ECO:0000255|PROSITE-ProRule:PRU00175}.
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   UniGene; Mm.35413; -.
DR   ProteinModelPortal; Q99NA9; -.
DR   SMR; Q99NA9; -.
DR   BioGrid; 214431; 7.
DR   IntAct; Q99NA9; 6.
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   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   eggNOG; KOG2660; Eukaryota.
DR   eggNOG; ENOG410XPCN; LUCA.
DR   GeneTree; ENSGT00550000074463; -.
DR   HOGENOM; HOG000231946; -.
DR   HOVERGEN; HBG052826; -.
DR   InParanoid; Q99NA9; -.
DR   KO; K11470; -.
DR   OMA; IGANEDT; -.
DR   OrthoDB; EOG091G0EC9; -.
DR   PhylomeDB; Q99NA9; -.
DR   TreeFam; TF324206; -.
DR   PRO; PR:Q99NA9; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   Bgee; ENSMUSG00000025050; -.
DR   CleanEx; MM_PCGF6; -.
DR   Genevisible; Q99NA9; MM.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0031519; C:PcG protein complex; ISS:UniProtKB.
DR   GO; GO:0035102; C:PRC1 complex; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; ISO:MGI.
DR   GO; GO:0019904; F:protein domain specific binding; ISA:MGI.
DR   GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR   GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; ISO:MGI.
DR   GO; GO:0001227; F:transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding; IDA:NTNU_SB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:NTNU_SB.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR029071; Ubiquitin-rel_dom.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
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; Complete proteome; Metal-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Repressor; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1    353       Polycomb group RING finger protein 6.
FT                                /FTId=PRO_0000055990.
FT   ZN_FING     137    176       RING-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00175}.
FT   COILED       71    112       {ECO:0000255}.
FT   COMPBIAS     24     42       Pro-rich.
FT   COMPBIAS     82    123       Glu-rich.
FT   MOD_RES      34     34       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9BYE7}.
FT   MOD_RES     118    118       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       137    175       ismart:RING [T]
FT   MYHIT       137    176       iprf:ZF_RING_2 [T]
FT   MYHIT       153    162       ipat:ZF_RING_1 [T]
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
//