ID A0A0D9RB09_CHLSB Unreviewed; 406 AA.
AC A0A0D9RB09;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=E3 ubiquitin-protein ligase RING1 {ECO:0000256|ARBA:ARBA00019738};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE AltName: Full=Polycomb complex protein RING1 {ECO:0000256|ARBA:ARBA00032615};
DE AltName: Full=RING finger protein 1 {ECO:0000256|ARBA:ARBA00032292};
DE AltName: Full=RING-type E3 ubiquitin transferase RING1 {ECO:0000256|ARBA:ARBA00030911};
GN Name=RING1 {ECO:0000313|Ensembl:ENSCSAP00000005798.1};
OS Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000005798.1, ECO:0000313|Proteomes:UP000029965};
RN [1] {ECO:0000313|Ensembl:ENSCSAP00000005798.1, ECO:0000313|Proteomes:UP000029965}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCSAP00000005798.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
CC -!- FUNCTION: Constitutes one of the E3 ubiquitin-protein ligases that
CC mediate monoubiquitination of 'Lys-119' of histone H2A, thereby playing
CC a central role in histone code and gene regulation. H2A 'Lys-119'
CC ubiquitination gives a specific tag for epigenetic transcriptional
CC repression and participates in X chromosome inactivation of female
CC mammals. Essential component of a Polycomb group (PcG) multiprotein
CC PRC1-like complex, a complex class required to maintain the
CC transcriptionally repressive state of many genes, including Hox genes,
CC throughout development. PcG PRC1 complex acts via chromatin remodeling
CC and modification of histones, rendering chromatin heritably changed in
CC its expressibility. Compared to RNF2/RING2, it does not have the main
CC E3 ubiquitin ligase activity on histone H2A, and it may rather act as a
CC modulator of RNF2/RING2 activity. {ECO:0000256|ARBA:ARBA00025085}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000256|ARBA:ARBA00004324}.
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DR EMBL; AC241459; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_007971152.1; XM_007972961.1.
DR AlphaFoldDB; A0A0D9RB09; -.
DR STRING; 60711.ENSCSAP00000005798; -.
DR Ensembl; ENSCSAT00000007624.1; ENSCSAP00000005798.1; ENSCSAG00000009538.1.
DR GeneID; 103221674; -.
DR KEGG; csab:103221674; -.
DR CTD; 6015; -.
DR eggNOG; KOG0311; Eukaryota.
DR GeneTree; ENSGT00940000161022; -.
DR OMA; GAEDNCD; -.
DR OrthoDB; 460116at2759; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 103221674; 2 hits in 16 CRISPR screens.
DR Proteomes; UP000029965; Chromosome 17.
DR Bgee; ENSCSAG00000009538; Expressed in pituitary gland and 7 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR GO; GO:0035102; C:PRC1 complex; IEA:Ensembl.
DR GO; GO:0001739; C:sex chromatin; IEA:Ensembl.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0097027; F:ubiquitin-protein transferase activator activity; IEA:Ensembl.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IEA:Ensembl.
DR GO; GO:0048593; P:camera-type eye morphogenesis; IEA:Ensembl.
DR GO; GO:0006338; P:chromatin remodeling; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:Ensembl.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd17166; RAWUL_RING1; 1.
DR CDD; cd16740; RING-HC_RING2; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR032443; RAWUL.
DR InterPro; IPR043540; RING1/RING2.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR46076:SF2; E3 UBIQUITIN-PROTEIN LIGASE RING1; 1.
DR PANTHER; PTHR46076; E3 UBIQUITIN-PROTEIN LIGASE RING1 / RING 2 FAMILY MEMBER; 1.
DR Pfam; PF16207; RAWUL; 1.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000029965};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 48..88
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 148..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 406 AA; 42383 MW; 69597D656DDB8CBF CRC64;
MTTPANAQNA SKTWELSLYE LHRTPQEAIM DGTEIAVSPR SLHSELMCPI CLDMLKNTMT
TKECLHRFCS DCIVTALRSG NKECPTCRKK LVSKRSLRPD PNFDALISKI YPSREEYEAH
QDRVLIRLSR LHNQQALSSS IEEGLRMQAM HRAQRVRRPI PGSDQTTTMS GGEGEPGEGE
GDGEDVSSDS APDSAPGPAP KRPRGGGAGG SSVGTGGGGT GGVGGGAGSE DSGDRGGTLG
GGTLGPPSPP GAPSPPEPGG EIELVFRPHP LLVEKGEYCQ TRYVKTTGNA TVDHLSKYLA
LRIALERRQQ QEAGEPGGPG GGASDTGGPD GGGGEGGGAG GGDGPEEPAL PSLEGVSEKQ
YTIYIAPGGG AFTTLNGSLT LELVNEKFWK VSRPLELCYA PTKDPK
//