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 10-MAY-2017, entry version 121.
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; Myomorpha;
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}.
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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 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 CDD; cd00162; RING; 1.
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 153 162 ipat:ZF_RING_1 [T]
FT MYHIT 137 176 iprf:ZF_RING_2 [T]
FT MYHIT 137 175 ismart:RING [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
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