true2005-04-262024-03-27216RING2_HUMANInteractions of BCL7A with novel ring finger proteins.Dyer M.J.S.Abdul-Rauf M.Heward J.M.Cui X.Cleary M.L.Catovsky D.1997-01EMBL/GenBank/DDBJNUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1)BrainIdentification of Bap-1, a protein that binds to integrin and is involved in integrin-mediated signal transduction.Li S.-F.1999-04EMBL/GenBank/DDBJNUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1)Complete sequencing and characterization of 21,243 full-length human cDNAs.Ota T.Suzuki Y.Nishikawa T.Otsuki T.Sugiyama T.Irie R.Wakamatsu A.Hayashi K.Sato H.Nagai K.Kimura K.Makita H.Sekine M.Obayashi M.Nishi T.Shibahara T.Tanaka T.Ishii S.Yamamoto J.Saito K.Kawai Y.Isono Y.Nakamura Y.Nagahari K.Murakami K.Yasuda T.Iwayanagi T.Wagatsuma M.Shiratori A.Sudo H.Hosoiri T.Kaku Y.Kodaira H.Kondo H.Sugawara M.Takahashi M.Kanda K.Yokoi T.Furuya T.Kikkawa E.Omura Y.Abe K.Kamihara K.Katsuta N.Sato K.Tanikawa M.Yamazaki M.Ninomiya K.Ishibashi T.Yamashita H.Murakawa K.Fujimori K.Tanai H.Kimata M.Watanabe M.Hiraoka S.Chiba Y.Ishida S.Ono Y.Takiguchi S.Watanabe S.Yosida M.Hotuta T.Kusano J.Kanehori K.Takahashi-Fujii A.Hara H.Tanase T.-O.Nomura Y.Togiya S.Komai F.Hara R.Takeuchi K.Arita M.Imose N.Musashino K.Yuuki H.Oshima A.Sasaki N.Aotsuka S.Yoshikawa Y.Matsunawa H.Ichihara T.Shiohata N.Sano S.Moriya S.Momiyama H.Satoh N.Takami S.Terashima Y.Suzuki O.Nakagawa S.Senoh A.Mizoguchi H.Goto Y.Shimizu F.Wakebe H.Hishigaki H.Watanabe T.Sugiyama A.Takemoto M.Kawakami B.Yamazaki M.'Watanabe K.Kumagai A.Itakura S.Fukuzumi Y.Fujimori Y.Komiyama M.Tashiro H.Tanigami A.Fujiwara T.Ono T.Yamada K.Fujii Y.Ozaki K.Hirao M.Ohmori Y.Kawabata A.Hikiji T.Kobatake N.Inagaki H.Ikema Y.Okamoto S.Okitani R.Kawakami T.Noguchi S.Itoh T.Shigeta K.Senba T.Matsumura K.Nakajima Y.Mizuno T.Morinaga M.Sasaki M.Togashi T.Oyama M.Hata H.Watanabe M.'Komatsu T.Mizushima-Sugano J.Satoh T.Shirai Y.Takahashi Y.Nakagawa K.Okumura K.Nagase T.Nomura N.Kikuchi H.Masuho Y.Yamashita R.Nakai K.Yada T.Nakamura Y.'Ohara O.Isogai T.Sugano S.doi:10.1038/ng12852004Nat. Genet.3640-45NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2)The DNA sequence and biological annotation of human chromosome 1.Gregory S.G.Barlow K.F.McLay K.E.Kaul R.Swarbreck D.Dunham A.Scott C.E.Howe K.L.Woodfine K.Spencer C.C.A.Jones M.C.Gillson C.Searle S.Zhou Y.Kokocinski F.McDonald L.Evans R.Phillips K.Atkinson A.Cooper R.Jones C.Hall R.E.Andrews T.D.Lloyd C.Ainscough R.Almeida J.P.Ambrose K.D.Anderson F.Andrew R.W.Ashwell R.I.S.Aubin K.Babbage A.K.Bagguley C.L.Bailey J.Beasley H.Bethel G.Bird C.P.Bray-Allen S.Brown J.Y.Brown A.J.Buckley D.Burton J.Bye J.Carder C.Chapman J.C.Clark S.Y.Clarke G.Clee C.Cobley V.Collier R.E.Corby N.Coville G.J.Davies J.Deadman R.Dunn M.Earthrowl M.Ellington A.G.Errington H.Frankish A.Frankland J.French L.Garner P.Garnett J.Gay L.Ghori M.R.J.Gibson R.Gilby L.M.Gillett W.Glithero R.J.Grafham D.V.Griffiths C.Griffiths-Jones S.Grocock R.Hammond S.Harrison E.S.I.Hart E.Haugen E.Heath P.D.Holmes S.Holt K.Howden P.J.Hunt A.R.Hunt S.E.Hunter G.Isherwood J.James R.Johnson C.Johnson D.Joy A.Kay M.Kershaw J.K.Kibukawa M.Kimberley A.M.King A.Knights A.J.Lad H.Laird G.Lawlor S.Leongamornlert D.A.Lloyd D.M.Loveland J.Lovell J.Lush M.J.Lyne R.Martin S.Mashreghi-Mohammadi M.Matthews L.Matthews N.S.W.McLaren S.Milne S.Mistry S.Moore M.J.F.Nickerson T.O'Dell C.N.Oliver K.Palmeiri A.Palmer S.A.Parker A.Patel D.Pearce A.V.Peck A.I.Pelan S.Phelps K.Phillimore B.J.Plumb R.Rajan J.Raymond C.Rouse G.Saenphimmachak C.Sehra H.K.Sheridan E.Shownkeen R.Sims S.Skuce C.D.Smith M.Steward C.Subramanian S.Sycamore N.Tracey A.Tromans A.Van Helmond Z.Wall M.Wallis J.M.White S.Whitehead S.L.Wilkinson J.E.Willey D.L.Williams H.Wilming L.Wray P.W.Wu Z.Coulson A.Vaudin M.Sulston J.E.Durbin R.M.Hubbard T.Wooster R.Dunham I.Carter N.P.McVean G.Ross M.T.Harrow J.Olson M.V.Beck S.Rogers J.Bentley D.R.doi:10.1038/nature047272006Nature441315-321NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]Mural R.J.Istrail S.Sutton G.G.Florea L.Halpern A.L.Mobarry C.M.Lippert R.Walenz B.Shatkay H.Dew I.Miller J.R.Flanigan M.J.Edwards N.J.Bolanos R.Fasulo D.Halldorsson B.V.Hannenhalli S.Turner R.Yooseph S.Lu F.Nusskern D.R.Shue B.C.Zheng X.H.Zhong F.Delcher A.L.Huson D.H.Kravitz S.A.Mouchard L.Reinert K.Remington K.A.Clark A.G.Waterman M.S.Eichler E.E.Adams M.D.Hunkapiller M.W.Myers E.W.Venter J.C.2005-07EMBL/GenBank/DDBJNUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).The MGC Project Teamdoi:10.1101/gr.25965042004Genome Res.142121-2127NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1)E3 ligase activity of RING finger proteins that interact with Hip-2, a human ubiquitin-conjugating enzyme.Lee S.-J.Choi J.-Y.Sung Y.-M.Park H.Rhim H.Kang S.doi:10.1016/s0014-5793(01)02689-82001FEBS Lett.50361-64INTERACTION WITH HIP2FUNCTIONMUTAGENESIS OF CYS-51; CYS-54 AND HIS-69Binding of the RING polycomb proteins to specific target genes in complex with the grainyhead-like family of developmental transcription factors.Tuckfield A.Clouston D.R.Wilanowski T.M.Zhao L.-L.Cunningham J.M.Jane S.M.doi:10.1128/mcb.22.6.1936-1946.20022002Mol. Cell. Biol.221936-1946INTERACTION WITH TFCP2The core of the polycomb repressive complex is compositionally and functionally conserved in flies and humans.Levine S.S.Weiss A.Erdjument-Bromage H.Shao Z.Tempst P.Kingston R.E.doi:10.1128/mcb.22.17.6070-6078.20022002Mol. Cell. Biol.226070-6078IDENTIFICATION IN A PRC1-LIKE HPRC-H COMPLEXA complex with chromatin modifiers that occupies E2F- and Myc-responsive genes in G0 cells.Ogawa H.Ishiguro K.Gaubatz S.Livingston D.M.Nakatani Y.doi:10.1126/science.10698612002Science2961132-1136IDENTIFICATION IN COMPLEX WITH E2F6; TFDP1; MAX; MGA; EUHMTASE1; BAT8; CBX3; RNF1; MBLR; L3MBTL2 AND YAF2Role of histone H2A ubiquitination in Polycomb silencing.Wang H.Wang L.Erdjument-Bromage H.Vidal M.Tempst P.Jones R.S.Zhang Y.doi:10.1038/nature029852004Nature431873-878IDENTIFICATION BY MASS SPECTROMETRYIDENTIFICATION IN A PRC1-LIKE COMPLEX WITH RING1; PHC2 AND BMI1FUNCTIONCATALYTIC ACTIVITYPATHWAYMUTAGENESIS OF HIS-69 AND ARG-70Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF.Dou Y.Milne T.A.Tackett A.J.Smith E.R.Fukuda A.Wysocka J.Allis C.D.Chait B.T.Hess J.L.Roeder R.G.doi:10.1016/j.cell.2005.04.0312005Cell121873-885IDENTIFICATION IN THE MLL1/MLL COMPLEXRole of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene silencing.Cao R.Tsukada Y.Zhang Y.doi:10.1016/j.molcel.2005.12.0022005Mol. Cell20845-854FUNCTIONPolycomb group and SCF ubiquitin ligases are found in a novel BCOR complex that is recruited to BCL6 targets.Gearhart M.D.Corcoran C.M.Wamstad J.A.Bardwell V.J.doi:10.1128/mcb.00630-062006Mol. Cell. Biol.266880-6889INTERACTION WITH RYBP; PCGF1; BCOR AND RING1Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.Gauci S.Helbig A.O.Slijper M.Krijgsveld J.Heck A.J.Mohammed S.doi:10.1021/ac90043092009Anal. Chem.814493-4501ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS]IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Several distinct polycomb complexes regulate and co-localize on the INK4a tumor suppressor locus.Maertens G.N.El Messaoudi-Aubert S.Racek T.Stock J.K.Nicholls J.Rodriguez-Niedenfuhr M.Gil J.Peters G.doi:10.1371/journal.pone.00063802009PLoS ONE4E6380IDENTIFICATION IN A PRC1-LIKE COMPLEXINTERACTION WITH PCGF2Initial characterization of the human central proteome.Burkard T.R.Planyavsky M.Kaupe I.Breitwieser F.P.Buerckstuemmer T.Bennett K.L.Superti-Furga G.Colinge J.doi:10.1186/1752-0509-5-172011BMC Syst. Biol.517IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Interaction proteomics analysis of polycomb proteins defines distinct PRC1 Complexes in mammalian cells.Vandamme J.Volkel P.Rosnoblet C.Le Faou P.Angrand P.O.doi:10.1074/mcp.m110.0026422011Mol. Cell. ProteomicsIDENTIFICATION IN A PRC1-LIKE COMPLEXINTERACTION WITH CBX4; CBX6; CBX7 AND CBX8SUBCELLULAR LOCATIONToward a comprehensive characterization of a human cancer cell phosphoproteome.Zhou H.Di Palma S.Preisinger C.Peng M.Polat A.N.Heck A.J.Mohammed S.doi:10.1021/pr300630k2013J. Proteome Res.12260-271PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143 AND SER-168IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]ErythroleukemiaAn AUTS2-polycomb complex activates gene expression in the CNS.Gao Z.Lee P.Stafford J.M.von Schimmelmann M.Schaefer A.Reinberg D.doi:10.1038/nature139212014Nature516349-354FUNCTIONSUBCELLULAR LOCATIONIDENTIFICATION IN A COMPLEX WITH PCGF5; AUTS2; CSNK2B AND RYBPIDENTIFICATION BY MASS SPECTROMETRYMUTAGENESIS OF SER-41 AND SER-168PHOSPHORYLATION AT SER-41 AND SER-168The variant Polycomb Repressor Complex 1 component PCGF1 interacts with a pluripotency sub-network that includes DPPA4, a regulator of embryogenesis.Oliviero G.Munawar N.Watson A.Streubel G.Manning G.Bardwell V.Bracken A.P.Cagney G.doi:10.1038/srep183882015Sci. Rep.518388IDENTIFICATION BY MASS SPECTROMETRYINTERACTION WITH PCGF1Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.Hendriks I.A.Lyon D.Young C.Jensen L.J.Vertegaal A.C.Nielsen M.L.doi:10.1038/nsmb.33662017Nat. Struct. Mol. Biol.24325-336SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-249 AND LYS-323IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Intrinsically disordered chromatin protein NUPR1 binds to the C-terminal region of Polycomb RING1B.Santofimia-Castano P.Rizzuti B.Pey A.L.Soubeyran P.Vidal M.Urrutia R.Iovanna J.L.Neira J.L.doi:10.1073/pnas.16199321142017Proc. Natl. Acad. Sci. U.S.A.114E6332-E6341INTERACTION WITH NUPR1Rare deleterious de novo missense variants in Rnf2/Ring2 are associated with a neurodevelopmental disorder with unique clinical features.Luo X.Schoch K.Jangam S.V.Bhavana V.H.Graves H.K.Kansagra S.Jasien J.M.Stong N.Keren B.Mignot C.Ravelli C.Bellen H.J.Wangler M.F.Shashi V.Yamamoto S.Undiagnosed Diseases Networkdoi:10.1093/hmg/ddab1102021Hum. Mol. Genet.301283-1292INVOLVEMENT IN LUSYAMVARIANTS LUSYAM HIS-70 AND ARG-82FUNCTIONStructure of a Bmi-1-Ring1B polycomb group ubiquitin ligase complex.Li Z.Cao R.Wang M.Myers M.P.Zhang Y.Xu R.M.doi:10.1074/jbc.m6024612002006J. Biol. Chem.28120643-20649X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 15-114 IN COMPLEX WITH BMI1 AND ZINC IONSFUNCTIONIDENTIFICATION BY MASS SPECTROMETRYSUBUNITRing1B contains a ubiquitin-like docking module for interaction with Cbx proteins.Bezsonova I.Walker J.R.Bacik J.P.Duan S.Dhe-Paganon S.Arrowsmith C.H.doi:10.1021/bi901131u2009Biochemistry4810542-10548X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 220-330INTERACTION WITH CBX7MUTAGENESIS OF TYR-262Polycomb group targeting through different binding partners of RING1B C-terminal domain.Wang R.Taylor A.B.Leal B.Z.Chadwell L.V.Ilangovan U.Robinson A.K.Schirf V.Hart P.J.Lafer E.M.Demeler B.Hinck A.P.McEwen D.G.Kim C.A.doi:10.1016/j.str.2010.04.0132010Structure18966-975X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 223-333 IN COMPLEXES WITH CBX7 AND RYBPFUNCTIONMUTAGENESIS OF TYR-247; HIS-258 AND TYR-262Recognition of UbcH5c and the nucleosome by the Bmi1/Ring1b ubiquitin ligase complex.Bentley M.L.Corn J.E.Dong K.C.Phung Q.Cheung T.K.Cochran A.G.doi:10.1038/emboj.2011.2432011EMBO J.303285-3297X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 1-116 IN COMPLEX WITH ZINC IONS; BMI1 AND UB2D3FUNCTIONCATALYTIC ACTIVITYPATHWAYMUTAGENESIS OF ASP-56 AND 97-LYS-ARG-98Crystal structure of the PRC1 ubiquitylation module bound to the nucleosome.McGinty R.K.Henrici R.C.Tan S.doi:10.1038/nature138902014Nature514591-596X-RAY CRYSTALLOGRAPHY (3.28 ANGSTROMS) OF 2-116 IN COMPLEX WITH ZINC IONS; THE NUCLEOSOME; BMI1 AND UB2D3FUNCTIONMUTAGENESIS OF ARG-81; LYS-93; LYS-97 AND ARG-98BMI1-RING1B is an autoinhibited RING E3 ubiquitin ligase.Taherbhoy A.M.Huang O.W.Cochran A.G.doi:10.1038/ncomms86212015Nat. Commun.67621X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-116 IN COMPLEX WITH ZINC IONS; UB2D3 AND PCGF5SUBUNITFUNCTIONCATALYTIC ACTIVITYPATHWAY2.50B=15-1141.70A/C=223-3332.00A=220-3301.70A/C/E/G/I/K=223-3332.65C=1-1163.28L/N=2-1162.00B/E=1-1161.70A=10-1163.09A/B=10-116A=10-1163.05N=16-116815Non-canonical polycomb repressive complex 1.1, RING2-PCGF1-YAF2 variantNon-canonical polycomb repressive complex 1.2, RNF2-RYBP variantNon-canonical polycomb repressive complex 1.2, RNF2-YAF2 variantNon-canonical polycomb repressive complex 1.4, RNF2-YAF2 variantNon-canonical polycomb repressive complex 1.3, RING2-RYBP-CKIIA2 variantNon-canonical polycomb repressive complex 1.3, RING2-RYBP-CKIIA1-A2 variantNon-canonical polycomb repressive complex 1.3, RING2-RYBP-CKIIA1 variantNon-canonical polycomb repressive complex 1.3, RING2-YAF2-CKIIA2 variantNon-canonical polycomb repressive complex 1.3, RING2-YAF2-CKIIA1-A2 variantNon-canonical polycomb repressive complex 1.3, RING2-YAF2-CKIIA1 variantNon-canonical polycomb repressive complex 1.6, RING2-RYBP variantNon-canonical polycomb repressive complex 1.6, RING2-YAF2 variantNon-canonical polycomb repressive complex 1.4, RNF2-RYBP variantNon-canonical polycomb repressive complex 1.1, RING2-PCGF1-RYBP variantPolycomb repressive complex 1, RING2-PCGF2-CBX2-PHC1 variantPolycomb repressive complex 1, RING2-PCGF2-CBX2-PHC2 variantPolycomb repressive complex 1, RING2-PCGF2-CBX2-PHC3 variantPolycomb repressive complex 1, RING2-PCGF2-CBX4-PHC1 variantPolycomb repressive complex 1, RING2-PCGF2-CBX4-PHC3 variantPolycomb repressive complex 1, RING2-PCGF2-CBX4-PHC2 variantPolycomb repressive complex 1, RING2-PCGF2-CBX6-PHC1 variantPolycomb repressive complex 1, RING2-PCGF2-CBX6-PHC2 variantPolycomb repressive complex 1, RING2-PCGF2-CBX6-PHC3 variantPolycomb repressive complex 1, RING2-PCGF2-CBX7-PHC1 variantPolycomb repressive complex 1, RING2-PCGF2-CBX7-PHC2 variantPolycomb repressive complex 1, RING2-PCGF2-CBX7-PHC3 variantPolycomb repressive complex 1, RING2-PCGF2-CBX8-PHC1 variantPolycomb repressive complex 1, RING2-PCGF2-CBX8-PHC2 variantPolycomb repressive complex 1, RING2-PCGF2-CBX8-PHC3 variantPolycomb repressive complex 1, RING2-PCGF4-CBX2-PHC1 variantPolycomb repressive complex 1, RING2-PCGF4-CBX2-PHC2 variantPolycomb repressive complex 1, RING2-PCGF4-CBX2-PHC3 variantPolycomb repressive complex 1, RING2-PCGF4-CBX4-PHC1 variantPolycomb repressive complex 1, RING2-PCGF4-CBX4-PHC2 variantPolycomb repressive complex 1, RING2-PCGF4-CBX4-PHC3 variantPolycomb repressive complex 1, RING2-PCGF4-CBX6-PHC1 variantPolycomb repressive complex 1, RING2-PCGF4-CBX6-PHC2 variantPolycomb repressive complex 1, RING2-PCGF4-CBX6-PHC3 variantPolycomb repressive complex 1, RING2-PCGF4-CBX7-PHC1 variantPolycomb repressive complex 1, RING2-PCGF4-CBX7-PHC2 variantPolycomb repressive complex 1, RING2-PCGF4-CBX7-PHC3 variantPolycomb repressive complex 1, RING2-PCGF4-CBX8-PHC1 variantPolycomb repressive complex 1, RING2-PCGF4-CBX8-PHC2 variantPolycomb repressive complex 1, RING2-PCGF4-CBX8-PHC3 variantNon-canonical polycomb repressive complex 1.5, RING2-RYBP-CKIIA2 variantNon-canonical polycomb repressive complex 1.5, RING2-RYBP-CKIIA1-A2 variantNon-canonical polycomb repressive complex 1.5, RING2-RYBP-CKIIA1 variantNon-canonical polycomb repressive complex 1.5, RING2-YAF2-CKIIA2 variantNon-canonical polycomb repressive complex 1.5, RING2-YAF2-CKIIA1-A2 variantNon-canonical polycomb repressive complex 1.5, RING2-YAF2-CKIIA1 variant1261 site, 1 glycan3 sites, 1 O-linked glycan (3 sites)485 antibodies from 44 providershumanRNF2Low tissue specificitygenephenotypeNon-specific syndromic intellectual disabilityEukaryota2681Oxidative Stress Induced SenescenceSUMOylation of DNA damage response and repair proteinsSUMOylation of transcription cofactorsSUMOylation of chromatin organization proteinsSUMOylation of RNA binding proteinsSUMOylation of DNA methylation proteinsRUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not knownRegulation of PTEN gene transcriptionTranscriptional Regulation by E2F615 hits in 1195 CRISPR screenshumanTbioProteinExpressed in primordial germ cell in gonad and 110 other cell types or tissuesbaseline and differentialRAWUL_RING2RING-HC_RING2Zinc/RING finger domain, C3HC4 (zinc finger)RAWULRING1/RING2RING2_RAWUL_domZnf_RINGZnf_RING/FYVE/PHDZnf_RING_CSE3 UBIQUITIN-PROTEIN LIGASE RING1 / RING 2 FAMILY MEMBERE3 UBIQUITIN-PROTEIN LIGASE RING2RAWULzf-C3HC4_2RINGRING/U-boxZF_RING_1ZF_RING_2HSE3 ubiquitin-protein ligase RING22.3.2.27Huntingtin-interacting protein 2-interacting protein 3HIP2-interacting protein 3Protein DinGRING finger protein 1BRING1bRING finger protein 2RING finger protein BAP-1RING-type E3 ubiquitin transferase RING2RNF2BAP1DINGHIPI3RING1BE3 ubiquitin-protein ligase that mediates monoubiquitination of 'Lys-119' of histone H2A (H2AK119Ub), thereby playing a central role in histone code and gene regulation (PubMed:15386022, PubMed:16359901, PubMed:25519132, PubMed:33864376, PubMed:21772249, PubMed:25355358, PubMed:26151332). H2AK119Ub gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. May be involved in the initiation of both imprinted and random X inactivation (By similarity). Essential component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development (PubMed:16359901, PubMed:26151332). PcG PRC1 complex acts via chromatin remodeling and modification of histones, rendering chromatin heritably changed in its expressibility (PubMed:26151332). E3 ubiquitin-protein ligase activity is enhanced by BMI1/PCGF4 (PubMed:21772249). Acts as the main E3 ubiquitin ligase on histone H2A of the PRC1 complex, while RING1 may rather act as a modulator of RNF2/RING2 activity (Probable). Association with the chromosomal DNA is cell-cycle dependent. In resting B- and T-lymphocytes, interaction with AURKB leads to block its activity, thereby maintaining transcription in resting lymphocytes (By similarity). Also acts as a negative regulator of autophagy by mediating ubiquitination of AMBRA1, leading to its subsequent degradation (By similarity).Component of chromatin-associated Polycomb (PcG) complexes. Component of a number of PRC1-like complexes; these complexes contain either the polycomb group ring finger protein PCGF1, or PCGF2, or PCGF3, or PCGF4, or PCGF5, or PCGF6 (PubMed:12167701, PubMed:15386022, PubMed:19636380, PubMed:21282530, PubMed:26687479, PubMed:26151332). Part of a complex that contains RNF2, UB2D3 and BMI1; within that complex RNF2 and BMI1 form a tight heterodimer, where UB2D3 interacts only with RNF2 (PubMed:21772249, PubMed:25355358). The complex composed of RNF2, UB2D3 and BMI1 binds nucleosomes, and has activity only with nucleosomal histone H2A (PubMed:21772249). Part of a complex that contains PCGF5, RNF2 and UBE2D3 (PubMed:26151332). Part of a complex that contains AUTS2, PCGF5, RNF2, CSNK2B and RYBP (PubMed:25519132). Interacts with RYBP, PCGF2, CBX4, CBX6, CBX7 and CBX8 (PubMed:19636380, PubMed:21282530, PubMed:19791798, PubMed:20696397). Interacts with RNF1/RING1, BMI1 and PHC2 (PubMed:15386022, PubMed:16714294). Interaction with RYBP and CBX7 is mutually exclusive; both compete for the same binding site on RNF2 (By similarity). Component of repressive BCOR complex containing a Polycomb group subcomplex at least composed of RYBP, PCGF1, BCOR and RING1 (PubMed:16943429). Interacts with CBX2 and PHC1. Interacts with CHTOP. Interacts with AURKB (By similarity). Part of the E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EUHMTASE1, RNF1/RING1, RNF2/RING2, MBLR, L3MBTL2 and YAF2 (PubMed:12004135). Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10 (PubMed:15960975). Interacts with RYBP, HIP2 and TFCP2 (PubMed:11513855, PubMed:11865070, PubMed:20696397). Interacts with NUPR1 (PubMed:28720707).Enriched on inactive X chromosome (Xi) in female trophoblast stem (TS) cells as well as differentiating embryonic stem (ES) cells. The enrichment on Xi is transient during TS and ES cell differentiation. The association with Xi is mitotically stable in non-differentiated TS cells.Monoubiquitinated, by auto-ubiquitination (By similarity). Polyubiquitinated in the presence of UBE2D3 (in vitro) (PubMed:26151332).The disease is caused by variants affecting the gene represented in this entry.The hPRC-H complex purification reported probably presents a mixture of different PRC1-like complexes.Removed1E3 ubiquitin-protein ligase RING2375242336RING-type5191Interaction with HIP2179Interaction with nucleosomes via an acidic patch on histone H2A and histone H2B9398Disordered157208Polar residues194N-acetylserinePhosphoserine41Phosphoserine143Phosphoserine168Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)112Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)249Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)323In isoform 2.84155In LUSYAM.H70In LUSYAM; uncertain significance.R82No effect on ubiquitin ligase activity on histone H2A.ADStrong decrease in HIP2-binding; when associated with S-54.WStrong decrease in HIP2-binding; when associated with W-51.S54Loss of ubiquitin ligase activity on histone H2A.K56Loss of HIP2-binding and loss of ubiquitin ligase activity on histone H2A.Y69Loss of ubiquitin ligase activity on histone H2A.CDecreases ubiquitin ligase activity on histone H2A.A81Mildly decreases ubiquitin ligase activity on histone H2A.ALoss of ubiquitin ligase activity on histone H2A.AA97Strongly decreases ubiquitin ligase activity on histone H2A.ANearly abolishes ubiquitin ligase activity on histone H2A.ADecreases ubiquitin ligase activity on histone H2A.EReduced interaction with CBX7.A247Reduced interaction with CBX7.A258Reduced interaction with CBX7.A262131621253739424547495255575964656772738083889099100102104113225232234236246251256277283285288290291296302304311318321325331false2false6false7false21false5false2false7false15false11false4false2false5false2false15false16false5false3false9false6false3false6false20false4false4false6false4false6false6false3false4false5false5ABCB1ATXN1AUTS2BMI1CBX4CBX4CBX6CBX7CBX8CSNK2A1CSNK2BH2AC17KAT8PCGF1PCGF2PCGF3PCGF3PCGF5PCGF6PSEN2RING1RYBPUBE2D1UBE2D2UBE2D3UBE2D4UBE2E2UBE2E3UBE2KUSP11USP7YAF21997-05-01137655af7e7116797aca5bbb819d92b0e566611MSQAVQTNGTQPLSKTWELSLYELQRTPQEAITDGLEIVVSPRSLHSELMCPICLDMLKNTMTTKECLHRFCADCIITALRSGNKECPTCRKKLVSKRSLRPDPNFDALISKIYPSRDEYEAHQERVLARINKHNNQQALSHSIEEGLKIQAMNRLQRGKKQQIENGSGAEDNGDSSHCSNASTHSNQEAGPSNKRTKTSDDSGLELDNNNAAMAIDPVMDGASEIELVFRPHPTLMEKDDSAQTRYIKTSGNATVDHLSKYLAVRLALEELRSKGESNQMNLDTASEKQYTIYIATASGQFTVLNGSFSLELVSEKYWKVNKPMELYYAPTKEHK2MSQAVQTNGTQPLSKTWELSLYELQRTPQEAITDGLEIVVSPRSLHSELMCPICLDMLKNTMTTKECLHRFCADCIITALRSGLQRGKKQQIENGSGAEDNGDSSHCSNASTHSNQEAGPSNKRTKTSDDSGLELDNNNAAMAIDPVMDGASEIELVFRPHPTLMEKDDSAQTRYIKTSGNATVDHLSKYLAVRLALEELRSKGESNQMNLDTASEKQYTIYIATASGQFTVLNGSFSLELVSEKYWKVNKPMELYYAPTKEHKtruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetrue