PCGF6_RAT
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 03-AUG-2022, entry version 121.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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 -!- PTM: Phosphorylated during mitosis. {ECO:0000250|UniProtKB:Q9BYE7}.
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DR EMBL; BC083820; AAH83820.1; -; mRNA.
DR RefSeq; NP_001013172.1; NM_001013154.1.
DR AlphaFoldDB; Q5XI70; -.
DR BMRB; Q5XI70; -.
DR SMR; Q5XI70; -.
DR STRING; 10116.ENSRNOP00000027450; -.
DR PaxDb; Q5XI70; -.
DR GeneID; 309457; -.
DR KEGG; rno:309457; -.
DR UCSC; RGD:1306904; rat.
DR CTD; 84108; -.
DR RGD; 1306904; Pcgf6.
DR VEuPathDB; HostDB:ENSRNOG00000020250; -.
DR eggNOG; KOG2660; Eukaryota.
DR HOGENOM; CLU_046427_4_0_1; -.
DR InParanoid; Q5XI70; -.
DR OMA; FSSNRCP; -.
DR OrthoDB; 1203951at2759; -.
DR PhylomeDB; Q5XI70; -.
DR TreeFam; TF324206; -.
DR Reactome; R-RNO-8953750; Transcriptional Regulation by E2F6.
DR PRO; PR:Q5XI70; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000020250; Expressed in testis and 20 other tissues.
DR Genevisible; Q5XI70; RN.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0031519; C:PcG protein complex; ISS:UniProtKB.
DR GO; GO:0035102; C:PRC1 complex; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0036353; P:histone H2A-K119 monoubiquitination; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
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 2: Evidence at transcript 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..351
FT /note="Polycomb group RING finger protein 6"
FT /id="PRO_0000055991"
FT ZN_FING 135..174
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 69..110
FT /evidence="ECO:0000255"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..37
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..101
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BYE7"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BYE7"
FT CROSSLNK 224
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BYE7"
FT CROSSLNK 235
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BYE7"
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
