PCGF1_BOVIN
ID PCGF1_BOVIN Reviewed; 259 AA.
AC Q2YDF9;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Polycomb group RING finger protein 1;
GN Name=PCGF1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the Polycomb group (PcG) multiprotein BCOR
CC complex, a complex required to maintain the transcriptionally
CC repressive state of some genes, such as BCL6 and the cyclin-dependent
CC kinase inhibitor, CDKN1A. Transcriptional repressor that may be
CC targeted to the DNA by BCL6; this transcription repressor activity may
CC be related to PKC signaling pathway. Represses CDKN1A expression by
CC binding to its promoter, and this repression is dependent on the
CC retinoic acid response element (RARE element). Promotes cell cycle
CC progression and enhances cell proliferation as well. May have a
CC positive role in tumor cell growth by down-regulating CDKN1A. Component
CC of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex
CC class required to maintain the transcriptionally repressive state of
CC many genes, including Hox genes, throughout development. PcG PRC1
CC complex acts via chromatin remodeling and modification of histones; it
CC mediates monoubiquitination of histone H2A 'Lys-119', rendering
CC chromatin heritably changed in its expressibility. Within the PRC1-like
CC complex, regulates RNF2 ubiquitin ligase activity. Regulates the
CC expression of DPPA4 and NANOG in the NT2 embryonic carcinoma cells.
CC {ECO:0000250|UniProtKB:Q9BSM1}.
CC -!- SUBUNIT: Interacts with BCORL1, forming heterodimers (By similarity).
CC The PCGF1-BCORL1 heterodimeric complex interacts with the KDM2B-SKP1
CC heterodimeric complex to form a homotetrameric polycomb repression
CC complex 1 (PRC1.1) (By similarity). Component of the repressive BCOR
CC complex containing a Polycomb group subcomplex at least composed of
CC RYBP, RING1 and RNF2/RING2 (By similarity). Specifically interacts with
CC BCOR, RING1 and RNF2/RING2 (By similarity). Component of a PRC1-like
CC complex (By similarity). Interacts with CBX6, CBX7 and CBX8 (By
CC similarity). Interacts with DPPA4, NANOG, POU5F1 and RYBP (By
CC similarity). {ECO:0000250|UniProtKB:Q9BSM1}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BSM1}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI10243.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC110242; AAI10243.1; ALT_INIT; mRNA.
DR RefSeq; NP_001039912.2; NM_001046447.2.
DR AlphaFoldDB; Q2YDF9; -.
DR SMR; Q2YDF9; -.
DR STRING; 9913.ENSBTAP00000022090; -.
DR PaxDb; Q2YDF9; -.
DR GeneID; 539040; -.
DR KEGG; bta:539040; -.
DR CTD; 84759; -.
DR eggNOG; KOG2660; Eukaryota.
DR InParanoid; Q2YDF9; -.
DR OrthoDB; 1203951at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0031519; C:PcG protein 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 Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR032443; RAWUL.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF16207; RAWUL; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9BSM1"
FT CHAIN 2..259
FT /note="Polycomb group RING finger protein 1"
FT /id="PRO_0000277854"
FT ZN_FING 47..86
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 86..247
FT /note="Necessary for repressor activity"
FT /evidence="ECO:0000250"
FT REGION 150..255
FT /note="Required for the interaction with the KDM2B-SKP1
FT heterodimeric complex"
FT /evidence="ECO:0000250|UniProtKB:Q9BSM1"
FT REGION 167..255
FT /note="RING-finger and WD40-associated ubiquitin-like
FT domain (RAWUL); sufficient for interaction with BCOR and
FT BCORL1"
FT /evidence="ECO:0000250|UniProtKB:Q9BSM1"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9BSM1"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BSM1"
FT CROSSLNK 24
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BSM1"
FT CROSSLNK 88
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BSM1"
SQ SEQUENCE 259 AA; 30324 MW; A36F58C0CE46797D CRC64;
MASPQGGQIA IAMRLRNQLQ SVYKMDPLRN EEEVRVKIKD LNEHIVCCLC AGYFVDATTI
TECLHTFCKS CIVKYLQTSK YCPMCNIKIH ETQPLLNHKL DRVMQDIVYK LVPGLQDSEE
KRIREFYQSR GLDRVTQPSG EEPALSNLGL PFSSFDHSKA HYYRYDEQLS LCLERLSSGK
DKNKSILQNK YVRCSVRAEV RHLRRVLCHR LMLNPQHVQL LFDNEVLPDH MTMKQIWLSH
WFGKPSPLLL QYSVKEKRR
