RING2_MOUSE
ID RING2_MOUSE Reviewed; 336 AA.
AC Q9CQJ4; O35699; O35729; Q4FJV5; Q8C1X8;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=E3 ubiquitin-protein ligase RING2;
DE EC=2.3.2.27 {ECO:0000269|PubMed:15525528, ECO:0000269|PubMed:22325148, ECO:0000269|PubMed:24980959};
DE AltName: Full=RING finger protein 1B;
DE Short=RING1b;
DE AltName: Full=RING finger protein 2;
DE AltName: Full=RING-type E3 ubiquitin transferase RING2 {ECO:0000305};
GN Name=Rnf2; Synonyms=DinG, Ring1b;
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], AND INTERACTION WITH CBX2.
RC STRAIN=NIH Swiss;
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 MRNA].
RC STRAIN=C57BL/6J; TISSUE=B-cell, and Ovary;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 [5]
RP INTERACTION WITH RYBP AND RING1.
RX PubMed=10369680; DOI=10.1093/emboj/18.12.3404;
RA Garcia E., Marcos-Gutierrez C., del Mar Lorente M., Moreno J.C., Vidal M.;
RT "RYBP, a new repressor protein that interacts with components of the
RT mammalian Polycomb complex, and with the transcription factor YY1.";
RL EMBO J. 18:3404-3418(1999).
RN [6]
RP INTERACTION WITH CBX2; PCGF2; PHC1; PHC2; RNF1 AND BMI1, FUNCTION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=12183370; DOI=10.1242/dev.129.18.4171;
RA Suzuki M., Mizutani-Koseki Y., Fujimura Y., Miyagishima H., Kaneko T.,
RA Takada Y., Akasaka T., Tanzawa H., Takihara Y., Nakano M., Masumoto H.,
RA Vidal M., Isono K., Koseki H.;
RT "Involvement of the Polycomb-group gene Ring1B in the specification of the
RT anterior-posterior axis in mice.";
RL Development 129:4171-4183(2002).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
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 [8]
RP SUBCELLULAR LOCATION.
RX PubMed=15509584; DOI=10.1074/jbc.c400493200;
RA Fang J., Chen T., Chadwick B., Li E., Zhang Y.;
RT "Ring1b-mediated H2A ubiquitination associates with inactive X chromosomes
RT and is involved in initiation of X inactivation.";
RL J. Biol. Chem. 279:52812-52815(2004).
RN [9]
RP INTERACTION WITH PHC2.
RX PubMed=16024804; DOI=10.1128/mcb.25.15.6694-6706.2005;
RA Isono K., Fujimura Y., Shinga J., Yamaki M., O-Wang J., Takihara Y.,
RA Murahashi Y., Takada Y., Mizutani-Koseki Y., Koseki H.;
RT "Mammalian polyhomeotic homologues Phc2 and Phc1 act in synergy to mediate
RT polycomb repression of Hox genes.";
RL Mol. Cell. Biol. 25:6694-6706(2005).
RN [10]
RP INTERACTION WITH RYBP.
RX PubMed=19170609; DOI=10.1021/bi801933c;
RA Neira J.L., Roman-Trufero M., Contreras L.M., Prieto J., Singh G.,
RA Barrera F.N., Renart M.L., Vidal M.;
RT "The transcriptional repressor RYBP is a natively unfolded protein which
RT folds upon binding to DNA.";
RL Biochemistry 48:1348-1360(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, SUBUNIT, AND
RP INTERACTION WITH PCGF2; RYBP; RING1; PHC1; PHC3; PHC2; CBX7; CBX2 AND CBX8.
RX PubMed=22325148; DOI=10.1016/j.cell.2011.12.029;
RA Tavares L., Dimitrova E., Oxley D., Webster J., Poot R., Demmers J.,
RA Bezstarosti K., Taylor S., Ura H., Koide H., Wutz A., Vidal M.,
RA Elderkin S., Brockdorff N.;
RT "RYBP-PRC1 complexes mediate H2A ubiquitylation at polycomb target sites
RT independently of PRC2 and H3K27me3.";
RL Cell 148:664-678(2012).
RN [13]
RP FUNCTION, INTERACTION WITH PHC1; PCGF2; RYBP; CBX7; CBX4; CBX2 AND BMI1,
RP AND TISSUE SPECIFICITY.
RX PubMed=22226355; DOI=10.1016/j.stem.2011.12.006;
RA Morey L., Pascual G., Cozzuto L., Roma G., Wutz A., Benitah S.A.,
RA Di Croce L.;
RT "Nonoverlapping functions of the Polycomb group Cbx family of proteins in
RT embryonic stem cells.";
RL Cell Stem Cell 10:47-62(2012).
RN [14]
RP INTERACTION WITH CHTOP.
RX PubMed=22872859; DOI=10.1074/mcp.m112.017194;
RA Fanis P., Gillemans N., Aghajanirefah A., Pourfarzad F., Demmers J.,
RA Esteghamat F., Vadlamudi R.K., Grosveld F., Philipsen S., van Dijk T.B.;
RT "Five friends of methylated chromatin target of protein-arginine-
RT methyltransferase[prmt]-1 (chtop), a complex linking arginine methylation
RT to desumoylation.";
RL Mol. Cell. Proteomics 11:1263-1273(2012).
RN [15]
RP FUNCTION, AND INTERACTION WITH AURKB.
RX PubMed=24034696; DOI=10.1016/j.molcel.2013.08.022;
RA Frangini A., Sjoberg M., Roman-Trufero M., Dharmalingam G., Haberle V.,
RA Bartke T., Lenhard B., Malumbres M., Vidal M., Dillon N.;
RT "The Aurora B kinase and the Polycomb protein Ring1B combine to regulate
RT active promoters in quiescent lymphocytes.";
RL Mol. Cell 51:647-661(2013).
RN [16]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF HIS-69.
RX PubMed=24980959; DOI=10.1038/cr.2014.85;
RA Xia P., Wang S., Huang G., Du Y., Zhu P., Li M., Fan Z.;
RT "RNF2 is recruited by WASH to ubiquitinate AMBRA1 leading to downregulation
RT of autophagy.";
RL Cell Res. 24:943-958(2014).
RN [17]
RP FUNCTION, INTERACTION WITH PCGF1; PCGF2; PCGF3; PCGF5 AND PCGF6, AND
RP SUBUNIT.
RX PubMed=28596365; DOI=10.1126/science.aal2512;
RA Almeida M., Pintacuda G., Masui O., Koseki Y., Gdula M., Cerase A.,
RA Brown D., Mould A., Innocent C., Nakayama M., Schermelleh L.,
RA Nesterova T.B., Koseki H., Brockdorff N.;
RT "PCGF3/5-PRC1 initiates Polycomb recruitment in X chromosome
RT inactivation.";
RL Science 356:1081-1084(2017).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-159 IN COMPLEX WITH BMI1 AND
RP ZINC IONS, FUNCTION, MONOUBIQUITINATION, 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).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates monoubiquitination
CC of 'Lys-119' of histone H2A (H2AK119Ub), thereby playing a central role
CC in histone code and gene regulation (PubMed:15525528, PubMed:22325148,
CC PubMed:28596365). H2AK119Ub gives a specific tag for epigenetic
CC transcriptional repression and participates in X chromosome
CC inactivation of female mammals (PubMed:15525528, PubMed:28596365). May
CC be involved in the initiation of both imprinted and random X
CC inactivation (PubMed:15525528). Essential component of a Polycomb group
CC (PcG) multiprotein PRC1-like complex, a complex class required to
CC maintain the transcriptionally repressive state of many genes,
CC including Hox genes, throughout development (PubMed:22325148,
CC PubMed:16710298). PcG PRC1 complex acts via chromatin remodeling and
CC modification of histones, rendering chromatin heritably changed in its
CC expressibility (PubMed:15525528, PubMed:22325148, PubMed:16710298). E3
CC ubiquitin-protein ligase activity is enhanced by BMI1/PCGF4
CC (PubMed:16710298). Acts as the main E3 ubiquitin ligase on histone H2A
CC of the PRC1 complex, while RING1 may rather act as a modulator of
CC RNF2/RING2 activity (PubMed:15525528, PubMed:16710298). Plays a role in
CC the transcriptional repression of genes that are required for
CC pluripotency in embryonic stem cells, thereby contributing to
CC differentiation of the ectodermal and endodermal germ layers
CC (PubMed:22226355). Association with the chromosomal DNA is cell-cycle
CC dependent. In resting B- and T-lymphocytes, interaction with AURKB
CC leads to block its activity, thereby maintaining transcription in
CC resting lymphocytes (PubMed:24034696). Also acts as a negative
CC regulator of autophagy by mediating ubiquitination of AMBRA1, leading
CC to its subsequent degradation (PubMed:24980959).
CC {ECO:0000269|PubMed:12183370, ECO:0000269|PubMed:15525528,
CC ECO:0000269|PubMed:16710298, ECO:0000269|PubMed:22226355,
CC ECO:0000269|PubMed:22325148, ECO:0000269|PubMed:24034696,
CC ECO:0000269|PubMed:24980959, ECO:0000269|PubMed:28596365}.
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:0000269|PubMed:15525528,
CC ECO:0000269|PubMed:22325148, ECO:0000269|PubMed:24980959};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:15525528, ECO:0000269|PubMed:22325148,
CC ECO:0000269|PubMed:24980959}.
CC -!- SUBUNIT: Component of chromatin-associated Polycomb (PcG) complexes
CC (PubMed:22325148). Component of a number of PRC1-like complexes; these
CC complexes contain either the polycomb group ring finger protein PCGF1,
CC or PCGF2, or PCGF3, or BMI1, or PCGF5, or PCGF6 (PubMed:28596365,
CC PubMed:16710298). Distinct PRC1-like complexes are composed of a RING1
CC subunit (RING1B or RING1A), one of the six PCGF proteins (PCGF1, PCGF2,
CC PCGF3, BMI1, PCGF5 or PCGF6), one PHC protein (PHC1, PHC2 or PHC3) and
CC one of the CBX proteins (CBX2, CBX4, CBX6, CBX7 or CBX8) (Probable).
CC Part of a complex that contains RNF2, UB2D3 and BMI1; within that
CC complex RNF2 and BMI1 form a tight heterodimer, where UB2D3 interacts
CC only with RNF2. The complex composed of RNF2, UB2D3 and BMI1 binds
CC nucleosomes, and has activity only with nucleosomal histone H2A (By
CC similarity). Part of a complex that contains PCGF5, RNF2 and UBE2D3.
CC Part of a complex that contains AUTS2, PCGF5, RNF2, CSNK2B AND RYBP (By
CC similarity). Interacts with CBX6 and CBX8 (By similarity). Interacts
CC with PHC1, PCGF2, RYBP, CBX7, CBX4, CBX2, RNF1/RING1, BMI1 and PHC2
CC (PubMed:12183370, PubMed:16024804, PubMed:16710298, PubMed:19170609,
CC PubMed:9312051, PubMed:10369680, PubMed:22325148, PubMed:22226355).
CC Interaction with RYBP and CBX7 is mutually exclusive; both compete for
CC the same binding site on RNF2 (PubMed:22325148). Component of
CC repressive BCOR complex containing a Polycomb group subcomplex at least
CC composed of RYBP, PCGF1, BCOR and RING1 (By similarity). Interacts with
CC CBX2 and PHC1 (PubMed:22226355). Interacts with CHTOP
CC (PubMed:22872859). Interacts with AURKB (PubMed:24034696). Part of the
CC E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX, TFDP1, CBX3,
CC BAT8, EUHMTASE1, RNF1/RING1, RNF2/RING2, MBLR, L3MBTL2 and YAF2 (By
CC similarity). Component of some MLL1/MLL complex, at least composed of
CC the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as
CC well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C,
CC KANSL1, LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2,
CC RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and
CC TEX10. Interacts with RYBP, HIP2 and TFCP2 (By similarity). Interacts
CC with NUPR1 (By similarity). {ECO:0000250|UniProtKB:Q99496,
CC ECO:0000269|PubMed:10369680, ECO:0000269|PubMed:12183370,
CC ECO:0000269|PubMed:16024804, ECO:0000269|PubMed:16710298,
CC ECO:0000269|PubMed:19170609, ECO:0000269|PubMed:22226355,
CC ECO:0000269|PubMed:22325148, ECO:0000269|PubMed:22872859,
CC ECO:0000269|PubMed:24034696, ECO:0000269|PubMed:28596365,
CC ECO:0000269|PubMed:9312051, ECO:0000305}.
CC -!- INTERACTION:
CC Q9CQJ4; P25916: Bmi1; NbExp=17; IntAct=EBI-927321, EBI-927401;
CC Q9CQJ4; Q9QXV1: Cbx8; NbExp=5; IntAct=EBI-927321, EBI-1216641;
CC Q9CQJ4; Q61177: Csnk2a1; NbExp=4; IntAct=EBI-927321, EBI-1216438;
CC Q9CQJ4; Q6ZQ88: Kdm1a; NbExp=3; IntAct=EBI-927321, EBI-1216284;
CC Q9CQJ4; Q6P1G2: Kdm2b; NbExp=4; IntAct=EBI-927321, EBI-1216214;
CC Q9CQJ4; P23798: Pcgf2; NbExp=15; IntAct=EBI-927321, EBI-926857;
CC Q9CQJ4; Q64028: Phc1; NbExp=7; IntAct=EBI-927321, EBI-927346;
CC Q9CQJ4; Q9QWH1: Phc2; NbExp=7; IntAct=EBI-927321, EBI-642357;
CC Q9CQJ4; O35730: Ring1; NbExp=3; IntAct=EBI-927321, EBI-929310;
CC Q9CQJ4; Q8CCI5: Rybp; NbExp=8; IntAct=EBI-927321, EBI-929290;
CC Q9CQJ4; Q9WTX5: Skp1; NbExp=4; IntAct=EBI-927321, EBI-1202363;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12183370,
CC ECO:0000269|PubMed:22325148, ECO:0000269|PubMed:24980959}. Cytoplasm
CC {ECO:0000269|PubMed:24980959}. Chromosome {ECO:0000269|PubMed:12183370,
CC ECO:0000269|PubMed:22325148}. Note=Enriched on inactive X chromosome
CC (Xi) in female trophoblast stem (TS) cells as well as differentiating
CC embryonic stem (ES) cells (PubMed:12183370). The enrichment on Xi is
CC transient during TS and ES cell differentiation. The association with
CC Xi is mitotically stable in non-differentiated TS cells
CC (PubMed:12183370). {ECO:0000269|PubMed:12183370}.
CC -!- TISSUE SPECIFICITY: Expressed in embryonic stem cells.
CC {ECO:0000269|PubMed:22226355}.
CC -!- PTM: Monoubiquitinated, by auto-ubiquitination (PubMed:16710298).
CC Polyubiquitinated in the presence of UBE2D3 (in vitro) (By similarity).
CC {ECO:0000250|UniProtKB:Q99496, ECO:0000269|PubMed:16710298}.
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DR EMBL; Y12880; CAA73380.1; -; mRNA.
DR EMBL; Y12783; CAA73321.1; -; mRNA.
DR EMBL; AK145767; BAE26638.1; -; mRNA.
DR EMBL; AK012358; BAB28186.1; -; mRNA.
DR EMBL; AK013124; BAB28663.1; -; mRNA.
DR EMBL; AK030319; BAC26898.1; -; mRNA.
DR EMBL; AK090066; BAC41075.1; -; mRNA.
DR EMBL; CT010297; CAJ18505.1; -; mRNA.
DR EMBL; BC020122; AAH20122.1; -; mRNA.
DR CCDS; CCDS15362.1; -.
DR RefSeq; NP_035407.1; NM_011277.2.
DR PDB; 2CKL; X-ray; 2.00 A; B=1-159.
DR PDBsum; 2CKL; -.
DR AlphaFoldDB; Q9CQJ4; -.
DR BMRB; Q9CQJ4; -.
DR SMR; Q9CQJ4; -.
DR BioGRID; 202919; 127.
DR DIP; DIP-36109N; -.
DR IntAct; Q9CQJ4; 58.
DR MINT; Q9CQJ4; -.
DR STRING; 10090.ENSMUSP00000075476; -.
DR iPTMnet; Q9CQJ4; -.
DR PhosphoSitePlus; Q9CQJ4; -.
DR EPD; Q9CQJ4; -.
DR jPOST; Q9CQJ4; -.
DR MaxQB; Q9CQJ4; -.
DR PaxDb; Q9CQJ4; -.
DR PeptideAtlas; Q9CQJ4; -.
DR PRIDE; Q9CQJ4; -.
DR ProteomicsDB; 253289; -.
DR Antibodypedia; 20609; 439 antibodies from 44 providers.
DR DNASU; 19821; -.
DR Ensembl; ENSMUST00000076110; ENSMUSP00000075476; ENSMUSG00000026484.
DR Ensembl; ENSMUST00000187048; ENSMUSP00000140896; ENSMUSG00000026484.
DR GeneID; 19821; -.
DR KEGG; mmu:19821; -.
DR UCSC; uc007cyx.1; mouse.
DR CTD; 6045; -.
DR MGI; MGI:1101759; Rnf2.
DR VEuPathDB; HostDB:ENSMUSG00000026484; -.
DR eggNOG; KOG0311; Eukaryota.
DR GeneTree; ENSGT00940000154499; -.
DR HOGENOM; CLU_056557_1_1_1; -.
DR InParanoid; Q9CQJ4; -.
DR OMA; PTEMTGD; -.
DR OrthoDB; 1319463at2759; -.
DR PhylomeDB; Q9CQJ4; -.
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; 19821; 6 hits in 75 CRISPR screens.
DR ChiTaRS; Rnf2; mouse.
DR EvolutionaryTrace; Q9CQJ4; -.
DR PRO; PR:Q9CQJ4; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9CQJ4; protein.
DR Bgee; ENSMUSG00000026484; Expressed in undifferentiated genital tubercle and 264 other tissues.
DR ExpressionAtlas; Q9CQJ4; baseline and differential.
DR Genevisible; Q9CQJ4; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0000791; C:euchromatin; IDA:MGI.
DR GO; GO:0000792; C:heterochromatin; IDA:MGI.
DR GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0031519; C:PcG protein complex; IDA:UniProtKB.
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:0071535; F:RING-like zinc finger domain binding; ISO:MGI.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0009948; P:anterior/posterior axis specification; IMP:MGI.
DR GO; GO:0001702; P:gastrulation with mouth forming second; IMP:MGI.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:0007281; P:germ cell development; IMP:CACAO.
DR GO; GO:0035518; P:histone H2A monoubiquitination; ISS:UniProtKB.
DR GO; GO:0036353; P:histone H2A-K119 monoubiquitination; IMP:UniProtKB.
DR GO; GO:0016574; P:histone ubiquitination; IDA:MGI.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:MGI.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR032443; RAWUL.
DR InterPro; IPR043540; RING1/RING2.
DR InterPro; IPR037937; RING2.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR46076; PTHR46076; 1.
DR PANTHER; PTHR46076:SF4; PTHR46076:SF4; 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 3D-structure; Acetylation; Chromosome; Cytoplasm; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q99496"
FT CHAIN 2..336
FT /note="E3 ubiquitin-protein ligase RING2"
FT /id="PRO_0000056039"
FT ZN_FING 51..91
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 2..179
FT /note="Interaction with HIP2"
FT /evidence="ECO:0000250|UniProtKB:Q99496"
FT REGION 93..98
FT /note="Interaction with nucleosomes via an acidic patch on
FT histone H2A and histone H2B"
FT /evidence="ECO:0000250|UniProtKB:Q99496"
FT REGION 157..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q99496"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99496"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99496"
FT MOD_RES 168
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99496"
FT CROSSLNK 112
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT CROSSLNK 249
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q99496"
FT CROSSLNK 323
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q99496"
FT MUTAGEN 69
FT /note="H->Y: Loss of ubiquitin ligase activity."
FT /evidence="ECO:0000269|PubMed:24980959"
FT CONFLICT 253
FT /note="N -> H (in Ref. 2; BAC41075)"
FT /evidence="ECO:0000305"
FT CONFLICT 299
FT /note="S -> T (in Ref. 2; BAC41075)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="V -> L (in Ref. 2; BAC41075)"
FT /evidence="ECO:0000305"
FT CONFLICT 332..336
FT /note="TKEHK -> FTASGNVR (in Ref. 1; CAA73380)"
FT /evidence="ECO:0000305"
FT HELIX 21..25
FT /evidence="ECO:0007829|PDB:2CKL"
FT HELIX 46..49
FT /evidence="ECO:0007829|PDB:2CKL"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:2CKL"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:2CKL"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:2CKL"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:2CKL"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:2CKL"
FT HELIX 73..81
FT /evidence="ECO:0007829|PDB:2CKL"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:2CKL"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:2CKL"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:2CKL"
FT HELIX 104..113
FT /evidence="ECO:0007829|PDB:2CKL"
SQ SEQUENCE 336 AA; 37623 MW; 84BA5B3E044DB7EC CRC64;
MSQAVQTNGT QPLSKTWELS LYELQRTPQE AITDGLEIVV SPRSLHSELM CPICLDMLKN
TMTTKECLHR FCADCIITAL RSGNKECPTC RKKLVSKRSL RPDPNFDALI SKIYPSRDEY
EAHQERVLAR INKHNNQQAL SHSIEEGLKI QAMNRLQRGK KQQIENGSGA EDNGDSSHCS
NASTHSNQEA GPSNKRTKTS DDSGLELDNN NAAVAIDPVM DGASEIELVF RPHPTLMEKD
DSAQTRYIKT SGNATVDHLS KYLAVRLALE ELRSKGESNQ MNLDTASEKQ YTIYIATASG
QFTVLNGSFS LELVSEKYWK VNKPMELYYA PTKEHK
