Legends: 1, Phosphoserine. {ECO:0000250|UniProtKB:Q9BYE7}; 2, ZN_FING RING-type. {ECO:0000255|PROSITE- ProRule:PRU00175}; 3, COILED {ECO:0000255}; 4, COMPBIAS Pro-rich; 5, ipat:ZF_RING_1 [T]; 6, iprf:ZF_RING_2 [T]; 7, ismart:RING [T].
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ID PCGF6_RAT Reviewed; 351 AA.
AC Q5XI70;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 05-OCT-2016, entry version 92.
DE RecName: Full=Polycomb group RING finger protein 6;
DE AltName: Full=RING finger protein 134;
GN Name=Pcgf6; Synonyms=Rnf134;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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).
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 -!- PTM: Phosphorylated during mitosis. {ECO:0000250}.
CC -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC {ECO:0000255|PROSITE-ProRule:PRU00175}.
DR EMBL; BC083820; AAH83820.1; -; mRNA.
DR RefSeq; NP_001013172.1; NM_001013154.1.
DR UniGene; Rn.16897; -.
DR ProteinModelPortal; Q5XI70; -.
DR STRING; 10116.ENSRNOP00000027450; -.
DR PaxDb; Q5XI70; -.
DR PRIDE; Q5XI70; -.
DR Ensembl; ENSRNOT00000027450; ENSRNOP00000027450; ENSRNOG00000020250.
DR GeneID; 309457; -.
DR KEGG; rno:309457; -.
DR UCSC; RGD:1306904; rat.
DR CTD; 84108; -.
DR RGD; 1306904; Pcgf6.
DR eggNOG; KOG2660; Eukaryota.
DR eggNOG; ENOG410XPCN; LUCA.
DR GeneTree; ENSGT00550000074463; -.
DR HOGENOM; HOG000231946; -.
DR HOVERGEN; HBG052826; -.
DR InParanoid; Q5XI70; -.
DR KO; K11470; -.
DR OMA; IGANEDT; -.
DR OrthoDB; EOG091G0EC9; -.
DR PhylomeDB; Q5XI70; -.
DR TreeFam; TF324206; -.
DR PRO; PR:Q5XI70; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000020250; -.
DR Genevisible; Q5XI70; RN.
DR GO; GO:0031519; C:PcG protein complex; ISS:UniProtKB.
DR GO; GO:0035102; C:PRC1 complex; ISS:UniProtKB.
DR GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0001227; F:transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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 2: Evidence at transcript level;
KW Coiled coil; Complete proteome; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1 351 Polycomb group RING finger protein 6.
FT /FTId=PRO_0000055991.
FT ZN_FING 135 174 RING-type. {ECO:0000255|PROSITE-
FT ProRule:PRU00175}.
FT COILED 69 110 {ECO:0000255}.
FT COMPBIAS 25 68 Pro-rich.
FT COMPBIAS 65 121 Glu-rich.
FT MOD_RES 32 32 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q9BYE7}.
FT MOD_RES 116 116 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q9BYE7}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 151 160 ipat:ZF_RING_1 [T]
FT MYHIT 135 174 iprf:ZF_RING_2 [T]
FT MYHIT 135 173 ismart:RING [T]
SQ SEQUENCE 351 AA; 39706 MW; ABD5B92FFAED7462 CRC64;
MEEAETDATE NKRASEAKRA SAMLPPPPPP ISPPALIPAP AAGEEGPASL AQAGAPGCSR
SRPPELEPER SLGRLRGRFE DYDEELEEDE EMEEEEEEEE EMSHFSLRLE SGRADSEDEE
ERLINLVELT PYILCSICKG YLIDATTITE CLHTFCKSCI VRHFYYSNRC PKCNIVVHQT
QPLYNIRLDR QLQDIVYKLV VNLEEREKKQ MHDFYKERGL EVPKPAVPQP VPASKGRTKK
ALESVFRIPP ELDVSLLLEF IGANEDTGHF KPLEKKFVRV SGEATIGHVE KFLRRKMGLD
PACQVDIICG DHLLERYQTL REIRRAIGDT AMQDGLLVLH YGLVVSPLKI T
//
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