RING1_MOUSE
ID RING1_MOUSE Reviewed; 406 AA.
AC O35730; Q3U242; Q3U333; Q4FK33; Q63ZX8; Q921Z8;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 179.
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};
DE AltName: Full=Transcription repressor Ring1A;
GN Name=Ring1; Synonyms=Ring1A, Rnf1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN TRANSCRIPTION
RP REPRESSION, INTERACTION WITH CBX2, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=Swiss Webster / NIH; TISSUE=Embryo;
RX PubMed=9312051; DOI=10.1093/emboj/16.19.5930;
RA Schoorlemmer J., Marcos-Gutierrez C., Were F., Martinez R., Garcia E.,
RA Satijn D.P.E., Otte A.P., Vidal M.;
RT "Ring1A is a transcriptional repressor that interacts with the Polycomb-M33
RT protein and is expressed at rhombomere boundaries in the mouse hindbrain.";
RL EMBO J. 16:5930-5942(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=129/SvJ;
RA Rowen L., Qin S., Madan A., Loretz C., James R., Dors M., Mix L., Hall J.,
RA Lasky S., Hood L.;
RT "Sequence of the mouse major histocomaptibility locus class II region.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=NOD;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J.,
RA Wiemann S., Schick M., Korn B.;
RT "Cloning of mouse full open reading frames in Gateway(R) system entry
RT vector (pDONR201).";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=Czech II; TISSUE=Embryo, and Mammary gland;
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 [6]
RP ENZYME ACTIVITY, AND FUNCTION.
RX PubMed=15525528; DOI=10.1016/j.devcel.2004.10.005;
RA de Napoles M., Mermoud J.E., Wakao R., Tang Y.A., Endoh M., Appanah R.,
RA Nesterova T.B., Silva J., Otte A.P., Vidal M., Koseki H., Brockdorff N.;
RT "Polycomb group proteins Ring1A/B link ubiquitylation of histone H2A to
RT heritable gene silencing and X inactivation.";
RL Dev. Cell 7:663-676(2004).
RN [7]
RP RECONSTITUTION OF A PRC1-LIKE COMPLEX, AND INTERACTION WITH BMI1; CBX8 AND
RP PHC2.
RX PubMed=16359901; DOI=10.1016/j.molcel.2005.12.002;
RA Cao R., Tsukada Y., Zhang Y.;
RT "Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene silencing.";
RL Mol. Cell 20:845-854(2005).
RN [8]
RP FUNCTION, INTERACTION WITH BMI1, AND SUBUNIT.
RX PubMed=16710298; DOI=10.1038/sj.emboj.7601144;
RA Buchwald G., van der Stoop P., Weichenrieder O., Perrakis A.,
RA van Lohuizen M., Sixma T.K.;
RT "Structure and E3-ligase activity of the Ring-Ring complex of polycomb
RT proteins Bmi1 and Ring1b.";
RL EMBO J. 25:2465-2474(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 ECO:0000269|PubMed:15525528, ECO:0000269|PubMed:16710298,
CC ECO:0000269|PubMed:9312051}.
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 -!- INTERACTION:
CC O35730; P25916: Bmi1; NbExp=4; IntAct=EBI-929310, EBI-927401;
CC O35730; Q9QXV1: Cbx8; NbExp=2; IntAct=EBI-929310, EBI-1216641;
CC O35730; Q9QWH1: Phc2; NbExp=2; IntAct=EBI-929310, EBI-642357;
CC O35730; Q9CQJ4: Rnf2; NbExp=3; IntAct=EBI-929310, EBI-927321;
CC O35730; Q8CCI5: Rybp; NbExp=4; IntAct=EBI-929310, EBI-929290;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O35730-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O35730-2; Sequence=VSP_017695;
CC Name=3;
CC IsoId=O35730-3; Sequence=VSP_017696, VSP_017697;
CC -!- DEVELOPMENTAL STAGE: Expressed in cells of the central nervous system
CC (CNS) from 8.5 to 11.5 dpc. Expressed in the hindbrain (in the
CC rhombomere boundaries) at 10.5 dpc. Expressed in CNS (ventricular zone
CC and spinal cord), peripheral nervous system (PNS, sensory cranial and
CC spinal ganglia), olfactory and tongue epithelia at 13.5 dpc. Expressed
CC in CNS, thymus, various epithelial cell types including the olfactory,
CC tooth and tongue epithelia at 15.5 dpc. {ECO:0000269|PubMed:9312051}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH09070.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Y12881; CAA73381.1; -; mRNA.
DR EMBL; AF100956; AAC69901.1; -; Genomic_DNA.
DR EMBL; AK154962; BAE32956.1; -; mRNA.
DR EMBL; AK155509; BAE33300.1; -; mRNA.
DR EMBL; CT010219; CAJ18427.1; -; mRNA.
DR EMBL; BC009070; AAH09070.1; ALT_INIT; mRNA.
DR EMBL; BC082771; AAH82771.1; -; mRNA.
DR CCDS; CCDS50070.1; -. [O35730-1]
DR RefSeq; NP_033092.3; NM_009066.3. [O35730-1]
DR AlphaFoldDB; O35730; -.
DR SMR; O35730; -.
DR BioGRID; 202894; 38.
DR IntAct; O35730; 33.
DR MINT; O35730; -.
DR STRING; 10090.ENSMUSP00000025183; -.
DR iPTMnet; O35730; -.
DR PhosphoSitePlus; O35730; -.
DR EPD; O35730; -.
DR MaxQB; O35730; -.
DR PaxDb; O35730; -.
DR PeptideAtlas; O35730; -.
DR PRIDE; O35730; -.
DR ProteomicsDB; 255148; -. [O35730-1]
DR ProteomicsDB; 255149; -. [O35730-2]
DR ProteomicsDB; 255150; -. [O35730-3]
DR Antibodypedia; 1772; 577 antibodies from 36 providers.
DR DNASU; 19763; -.
DR Ensembl; ENSMUST00000025183; ENSMUSP00000025183; ENSMUSG00000024325. [O35730-1]
DR GeneID; 19763; -.
DR KEGG; mmu:19763; -.
DR UCSC; uc008cas.2; mouse. [O35730-1]
DR CTD; 6015; -.
DR MGI; MGI:1101770; Ring1.
DR VEuPathDB; HostDB:ENSMUSG00000024325; -.
DR eggNOG; KOG0311; Eukaryota.
DR GeneTree; ENSGT00940000161022; -.
DR HOGENOM; CLU_056557_1_0_1; -.
DR InParanoid; O35730; -.
DR OMA; LYYAPTM; -.
DR OrthoDB; 1319463at2759; -.
DR PhylomeDB; O35730; -.
DR TreeFam; TF105501; -.
DR Reactome; R-MMU-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-MMU-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-MMU-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-MMU-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-MMU-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR Reactome; R-MMU-8943724; Regulation of PTEN gene transcription.
DR Reactome; R-MMU-8953750; Transcriptional Regulation by E2F6.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 19763; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Ring1; mouse.
DR PRO; PR:O35730; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; O35730; protein.
DR Bgee; ENSMUSG00000024325; Expressed in embryonic brain and 213 other tissues.
DR Genevisible; O35730; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; IDA:MGI.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0031519; C:PcG protein complex; IDA:MGI.
DR GO; GO:0035102; C:PRC1 complex; ISO:MGI.
DR GO; GO:0001739; C:sex chromatin; IDA:MGI.
DR GO; GO:0000151; C:ubiquitin ligase complex; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
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; IDA:MGI.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IMP:MGI.
DR GO; GO:0048593; P:camera-type eye morphogenesis; IGI:MGI.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0035518; P:histone H2A monoubiquitination; ISO:MGI.
DR GO; GO:0016574; P:histone ubiquitination; IDA:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
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 1: Evidence at protein 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_0000056386"
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 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:0000269|PubMed:9312051"
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:0007744|PubMed:21183079"
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:0000303|Ref.4"
FT /id="VSP_017695"
FT VAR_SEQ 153..183
FT /note="AQRVRRPMPGSDQTATMSGGEGEPGEGEGDG -> CGEPETLLPMGLVWSTG
FT LIVCIRAARWRPCS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_017696"
FT VAR_SEQ 184..406
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_017697"
FT CONFLICT 54
FT /note="M -> V (in Ref. 4; CAJ18427)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="F -> L (in Ref. 4; CAJ18427 and 5; AAH09070)"
FT /evidence="ECO:0000305"
FT CONFLICT 314
FT /note="T -> A (in Ref. 3; BAE33300, 4 and 5; AAH09070)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 406 AA; 42631 MW; 4F274E976974A2D8 CRC64;
MTTPANAQNA SKTWELSLYE LHRTPQEAIM DGTEIAVSPR SLHSELMCPI CLDMLKNTMT
TKECLHRFCS DCIVTALRSG NKECPTCRKK LVSKRSLRPD PNFDALISKI YPSREEYEAH
QDRVLIRLSR LHNQQALSSS IEEGLRMQAM HRAQRVRRPM PGSDQTATMS GGEGEPGEGE
GDGEDVSSDS APDSAPGPAP KRPRGAGAGA SSVGTGGGAA GGACGGAGSE DSGDRGGTLG
GGTLGPPSPP GAPSPPEPGG EIELVFRPHP LLVEKGEYCQ TRYVKTTGNA TVDHLSKYLA
LRIALERRQQ QETTEPGGPG GGASDTGGPD GGGGERGVAG GGEGPEEPAL PSLEGVSEKQ
YTIYIAPGGG AFTTLNGSLT LELVNEKFWK VSRPLELCYA PTKDPK
