RING1_MACMU
ID RING1_MACMU Reviewed; 377 AA.
AC Q8WMN5;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=E3 ubiquitin-protein ligase RING1;
DE EC=2.3.2.27;
DE AltName: Full=Polycomb complex protein RING1;
DE AltName: Full=RING finger protein 1;
DE AltName: Full=RING-type E3 ubiquitin transferase RING1 {ECO:0000305};
GN Name=RING1;
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12557056; DOI=10.1007/s00251-002-0515-z;
RA Sudbrak R., Reinhardt R., Hennig S., Lehrach H., Gunther E., Walter L.;
RT "Comparative and evolutionary analysis of the rhesus macaque extended MHC
RT class II region.";
RL Immunogenetics 54:699-704(2003).
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 (By similarity). {ECO:0000250}.
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;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of chromatin-associated Polycomb (PcG) complexes.
CC Part of the E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX,
CC TFDP1, CBX3, BAT8, EUHMTASE1, RING1, RNF2/RING2 MBLR, L3MBTL2 and YAF2.
CC Interacts with CBX2 and PCGF6. Component of a PRC1-like complex.
CC Component of repressive BCOR complex containing Polycomb group
CC subcomplex at least composed of RYBP, PCGF1, BCOR and RNF2/RING2.
CC Interacts with PHC2, PCGF2, RNF2; CBX6, CBX7 and CBX8. Interacts with
CC BMI1 (By similarity). Interacts with MN1 (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q06587}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}.
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DR EMBL; AJ421778; CAD18905.1; -; Genomic_DNA.
DR RefSeq; NP_001108431.1; NM_001114959.1.
DR AlphaFoldDB; Q8WMN5; -.
DR SMR; Q8WMN5; -.
DR STRING; 9544.ENSMMUP00000005154; -.
DR GeneID; 718137; -.
DR KEGG; mcc:718137; -.
DR CTD; 6015; -.
DR eggNOG; KOG0311; Eukaryota.
DR InParanoid; Q8WMN5; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000006718; Unplaced.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0031519; C:PcG protein complex; ISS:UniProtKB.
DR GO; GO:0035102; C:PRC1 complex; ISS:UniProtKB.
DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0035518; P:histone H2A monoubiquitination; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR CDD; cd16739; RING-HC_RING1; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR032443; RAWUL.
DR InterPro; IPR043540; RING1/RING2.
DR InterPro; IPR042741; RING1_RING-HC.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR46076; PTHR46076; 1.
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 3: Inferred from homology;
KW Chromatin regulator; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..377
FT /note="E3 ubiquitin-protein ligase RING1"
FT /id="PRO_0000056385"
FT ZN_FING 19..59
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..205
FT /note="Necessary for transcriptional repression"
FT /evidence="ECO:0000250"
FT REGION 119..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..377
FT /note="Necessary for interaction with CBX2"
FT /evidence="ECO:0000250"
FT REGION 280..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 172..175
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q06587"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q06587"
FT MOD_RES 158
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q06587"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q06587"
FT MOD_RES 186
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q06587"
FT MOD_RES 191
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q06587"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q06587"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q06587"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q06587"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q06587"
SQ SEQUENCE 377 AA; 39100 MW; F406EC2487E5DE7D CRC64;
MDGTEIAVSP RSLHSELMCP ICLDMLKNTM TTKECLHRFC SDCIVTALRS GNKECPTCRK
KLVSKRSLRP DPNFDALISK IYPSREEYEA HQDRVLIRLS RLHNQQALSS SIEEGLRMQA
MHRAQRVRRP IPGSDQTTTM SGGEGEPGEG EGDGEDVSSD SAPDSAPGPA PKRPRGGGAG
GSSVGTGGGG TGGVGGGAGS EDSGDRGGTL GGGTLGPPSP PGAPSPPEPG GEIELVFRPH
PLLVEKGEYC QTRYVKTTGN ATVDHLSKYL ALRIALERRQ QQEAGEPGGP GGGASDTGGP
DGGGGEGGGA GGGDGPEEPA LPSLEGVSEK QYTIYIAPGG GAFTTLNGSL TLELVNEKFW
KVSRPLELCY APTKDPK
