RING1_RAT
ID RING1_RAT Reviewed; 406 AA.
AC Q6MGB6; Q4KMC1; Q63510;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 138.
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; Synonyms=Rnf1;
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 GENOMIC DNA], AND ALTERNATIVE SPLICING
RP (ISOFORM 2).
RC STRAIN=Brown Norway;
RX PubMed=15060004; DOI=10.1101/gr.1987704;
RA Hurt P., Walter L., Sudbrak R., Klages S., Mueller I., Shiina T., Inoko H.,
RA Lehrach H., Guenther E., Reinhardt R., Himmelbauer H.;
RT "The genomic sequence and comparative analysis of the rat major
RT histocompatibility complex.";
RL Genome Res. 14:631-639(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Brown Norway; TISSUE=Lung;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 30-78.
RC STRAIN=Lewis;
RX PubMed=8662089; DOI=10.1007/bf02602588;
RA Walter L., Fischer K., Guenther E.;
RT "Physical mapping of the Ring1, Ring2, Ke6, Ke4, Rxrb, Col11a2 and RT1.Hb
RT genes of the rat major histocompatibility complex.";
RL Immunogenetics 44:218-221(1996).
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 BMI1, PHC2, PCGF2, RNF2; CBX6, CBX7 and CBX8 (By
CC similarity). Interacts with MN1 (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q06587}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6MGB6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6MGB6-2; Sequence=VSP_017698;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH98635.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BX883042; CAE83930.1; -; Genomic_DNA.
DR EMBL; BC098635; AAH98635.2; ALT_INIT; mRNA.
DR EMBL; X95474; CAA64746.1; -; Genomic_DNA.
DR RefSeq; NP_997714.2; NM_212549.2. [Q6MGB6-1]
DR AlphaFoldDB; Q6MGB6; -.
DR SMR; Q6MGB6; -.
DR STRING; 10116.ENSRNOP00000000543; -.
DR iPTMnet; Q6MGB6; -.
DR PhosphoSitePlus; Q6MGB6; -.
DR jPOST; Q6MGB6; -.
DR PaxDb; Q6MGB6; -.
DR GeneID; 309626; -.
DR KEGG; rno:309626; -.
DR UCSC; RGD:3576; rat. [Q6MGB6-1]
DR CTD; 6015; -.
DR RGD; 3576; Ring1.
DR VEuPathDB; HostDB:ENSRNOG00000000467; -.
DR eggNOG; KOG0311; Eukaryota.
DR HOGENOM; CLU_056557_1_0_1; -.
DR InParanoid; Q6MGB6; -.
DR OMA; LYYAPTM; -.
DR OrthoDB; 1319463at2759; -.
DR PhylomeDB; Q6MGB6; -.
DR TreeFam; TF105501; -.
DR Reactome; R-RNO-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-RNO-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-RNO-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-RNO-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-RNO-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-RNO-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR Reactome; R-RNO-8943724; Regulation of PTEN gene transcription.
DR Reactome; R-RNO-8953750; Transcriptional Regulation by E2F6.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q6MGB6; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Bgee; ENSRNOG00000000467; Expressed in pancreas and 20 other tissues.
DR ExpressionAtlas; Q6MGB6; baseline and differential.
DR Genevisible; Q6MGB6; RN.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0016604; C:nuclear body; ISO:RGD.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
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:0001739; C:sex chromatin; ISO:RGD.
DR GO; GO:0000151; C:ubiquitin ligase complex; ISO:RGD.
DR GO; GO:0003682; F:chromatin binding; ISO:RGD.
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:0097027; F:ubiquitin-protein transferase activator activity; ISO:RGD.
DR GO; GO:0009952; P:anterior/posterior pattern specification; ISO:RGD.
DR GO; GO:0048593; P:camera-type eye morphogenesis; ISO:RGD.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0035518; P:histone H2A monoubiquitination; ISO:RGD.
DR GO; GO:0016574; P:histone ubiquitination; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
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 2: Evidence at transcript level;
KW Alternative splicing; Chromatin regulator; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..406
FT /note="E3 ubiquitin-protein ligase RING1"
FT /id="PRO_0000056387"
FT ZN_FING 48..88
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 30..234
FT /note="Necessary for transcriptional repression"
FT /evidence="ECO:0000250"
FT REGION 151..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..406
FT /note="Necessary for interaction with CBX2"
FT /evidence="ECO:0000250"
FT REGION 309..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 201..204
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOD_RES 24
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q06587"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q06587"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q06587"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q06587"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q06587"
FT MOD_RES 215
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q06587"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q06587"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q06587"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q06587"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q06587"
FT VAR_SEQ 1..29
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_017698"
FT CONFLICT 65
FT /note="L -> C (in Ref. 3; CAA64746)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 406 AA; 42661 MW; 61CC002752031C9F CRC64;
MTTPANAQNA SKTWELSLYE LHRTPQEAIM DGTEIAVSPR SLHSELMCPI CLDMLKNTMT
TKECLHRFCS DCIVTALRSG NKECPTCRKK LVSKRSLRPD PNFDALISKI YPSREEYEAH
QDRVLIRLSR LHNQQALSSS IEEGLRMQAM HRAQRVRRPM PGSDQTTTMS GGEGEPGEGE
GDGEDISSDS APDSAPGPAP KRPRGGGAGG SSVGTGGGAA GGACGGAGSE DSGDRGGTLG
GGTLGPPSPP GAPSPPEPGG EIELVFRPHP LLVEKGEYCQ TRYVKTTGNA TVDHLSKYLA
LRIALERRQQ QETVEPGGPG GGASDTGGPD GGGGERGVSG GGEGPEEPAL PSLEGVSEKQ
YTIYIAPGGG AFTTLNGSLT LELVNEKFWK VSRPLELCYA PTKDPK
