RING1_HUMAN
ID RING1_HUMAN Reviewed; 406 AA.
AC Q06587; A8JZZ0; Q5JP96; Q5SQW2; Q86V19;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 209.
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=Really interesting new gene 1 protein;
GN Name=RING1; Synonyms=RNF1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=7681583; DOI=10.1073/pnas.90.6.2112;
RA Lovering R., Hanson I.M., Borden K.L.B., Martin S., O'Reilly N.J.,
RA Evan G.I., Rahman D., Pappin D.J.C., Trowsdale J., Freemont P.S.;
RT "Identification and preliminary characterization of a protein motif related
RT to the zinc finger.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:2112-2116(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye, and Skin;
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 CHARACTERIZATION, AND INTERACTION WITH PHC2.
RX PubMed=9199346; DOI=10.1128/mcb.17.7.4105;
RA Satijn D.P.E., Gunster M.J., van der Vlag J., Hamer K.M., Schul W.,
RA Alkema M.J., Saurin A.J., Freemont P.S., van Driel R., Otte A.P.;
RT "RING1 is associated with the polycomb group protein complex and acts as a
RT transcriptional repressor.";
RL Mol. Cell. Biol. 17:4105-4113(1997).
RN [7]
RP CHARACTERIZATION.
RX PubMed=9858531; DOI=10.1128/mcb.19.1.57;
RA Satijn D.P.E., Otte A.P.;
RT "RING1 interacts with multiple Polycomb-group proteins and displays
RT tumorigenic activity.";
RL Mol. Cell. Biol. 19:57-68(1999).
RN [8]
RP INTERACTION WITH PCGF6.
RX PubMed=12167161; DOI=10.1046/j.1365-2443.2002.00565.x;
RA Akasaka T., Takahashi N., Suzuki M., Koseki H., Bodmer R., Koga H.;
RT "MBLR, a new RING finger protein resembling mammalian Polycomb gene
RT products, is regulated by cell cycle-dependent phosphorylation.";
RL Genes Cells 7:835-850(2002).
RN [9]
RP IDENTIFICATION IN A PRC1-LIKE HPRC-H COMPLEX.
RX PubMed=12167701; DOI=10.1128/mcb.22.17.6070-6078.2002;
RA Levine S.S., Weiss A., Erdjument-Bromage H., Shao Z., Tempst P.,
RA Kingston R.E.;
RT "The core of the polycomb repressive complex is compositionally and
RT functionally conserved in flies and humans.";
RL Mol. Cell. Biol. 22:6070-6078(2002).
RN [10]
RP IDENTIFICATION IN COMPLEX WITH E2F6; TFDP1; MAX; MGA; EUHMTASE1; BAT8;
RP CBX3; RNF2; MBLR; L3MBTL2 AND YAF2.
RX PubMed=12004135; DOI=10.1126/science.1069861;
RA Ogawa H., Ishiguro K., Gaubatz S., Livingston D.M., Nakatani Y.;
RT "A complex with chromatin modifiers that occupies E2F- and Myc-responsive
RT genes in G0 cells.";
RL Science 296:1132-1136(2002).
RN [11]
RP IDENTIFICATION IN A PRC1-LIKE COMPLEX WITH RNF2; BMI1 AND PHC2.
RX PubMed=15386022; DOI=10.1038/nature02985;
RA Wang H., Wang L., Erdjument-Bromage H., Vidal M., Tempst P., Jones R.S.,
RA Zhang Y.;
RT "Role of histone H2A ubiquitination in Polycomb silencing.";
RL Nature 431:873-878(2004).
RN [12]
RP FUNCTION.
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 [13]
RP INTERACTION WITH RYBP; PCGF1; BCOR AND RNF2.
RX PubMed=16943429; DOI=10.1128/mcb.00630-06;
RA Gearhart M.D., Corcoran C.M., Wamstad J.A., Bardwell V.J.;
RT "Polycomb group and SCF ubiquitin ligases are found in a novel BCOR complex
RT that is recruited to BCL6 targets.";
RL Mol. Cell. Biol. 26:6880-6889(2006).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38; SER-187 AND SER-190, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [16]
RP IDENTIFICATION IN A PRC1-LIKE COMPLEX, AND INTERACTION WITH PCGF2.
RX PubMed=19636380; DOI=10.1371/journal.pone.0006380;
RA Maertens G.N., El Messaoudi-Aubert S., Racek T., Stock J.K., Nicholls J.,
RA Rodriguez-Niedenfuhr M., Gil J., Peters G.;
RT "Several distinct polycomb complexes regulate and co-localize on the INK4a
RT tumor suppressor locus.";
RL PLoS ONE 4:E6380-E6380(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-220, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-248 AND SER-254, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [20]
RP IDENTIFICATION IN A PRC1-LIKE COMPLEX, INTERACTION WITH CBX6; CBX7 AND
RP CBX8, AND SUBCELLULAR LOCATION.
RX PubMed=21282530; DOI=10.1074/mcp.m110.002642;
RA Vandamme J., Volkel P., Rosnoblet C., Le Faou P., Angrand P.O.;
RT "Interaction proteomics analysis of polycomb proteins defines distinct PRC1
RT Complexes in mammalian cells.";
RL Mol. Cell. Proteomics 0:0-0(2011).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38; SER-140 AND SER-229, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-24; SER-38; SER-187; THR-215;
RP THR-220; SER-229 AND SER-232, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [23]
RP INTERACTION WITH MN1.
RX PubMed=31839203; DOI=10.1016/j.ajhg.2019.11.011;
RA Miyake N., Takahashi H., Nakamura K., Isidor B., Hiraki Y., Koshimizu E.,
RA Shiina M., Sasaki K., Suzuki H., Abe R., Kimura Y., Akiyama T.,
RA Tomizawa S.I., Hirose T., Hamanaka K., Miyatake S., Mitsuhashi S.,
RA Mizuguchi T., Takata A., Obo K., Kato M., Ogata K., Matsumoto N.;
RT "Gain-of-function MN1 truncation variants cause a recognizable syndrome
RT with craniofacial and brain abnormalities.";
RL Am. J. Hum. Genet. 106:13-25(2020).
RN [24]
RP VARIANT GLN-95.
RX PubMed=25725044; DOI=10.1136/jmedgenet-2014-102813;
RA Blanchard M.G., Willemsen M.H., Walker J.B., Dib-Hajj S.D., Waxman S.G.,
RA Jongmans M.C., Kleefstra T., van de Warrenburg B.P., Praamstra P.,
RA Nicolai J., Yntema H.G., Bindels R.J., Meisler M.H., Kamsteeg E.J.;
RT "De novo gain-of-function and loss-of-function mutations of SCN8A in
RT patients with intellectual disabilities and epilepsy.";
RL J. Med. Genet. 52:330-337(2015).
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. {ECO:0000269|PubMed:16359901}.
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 Interacts with BMI1 (By similarity). Part of the E2F6.com-1 complex in
CC G0 phase composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EUHMTASE1,
CC RING1, RNF2/RING2 MBLR, L3MBTL2 and YAF2. Interacts with CBX2 and
CC PCGF6. Component of a PRC1-like complex. Component of repressive BCOR
CC complex containing Polycomb group subcomplex at least composed of RYBP,
CC PCGF1, BCOR and RNF2/RING2. Interacts with PCGF2, RNF2; CBX6, CBX7 and
CC CBX8. Interacts with PHC2 (By similarity). Interacts with MN1
CC (PubMed:31839203). {ECO:0000250, ECO:0000269|PubMed:31839203}.
CC -!- INTERACTION:
CC Q06587; P35226: BMI1; NbExp=22; IntAct=EBI-752313, EBI-2341576;
CC Q06587; P55212: CASP6; NbExp=3; IntAct=EBI-752313, EBI-718729;
CC Q06587; O95503: CBX6; NbExp=6; IntAct=EBI-752313, EBI-3951758;
CC Q06587; O95931: CBX7; NbExp=5; IntAct=EBI-752313, EBI-3923843;
CC Q06587; Q9HC52: CBX8; NbExp=18; IntAct=EBI-752313, EBI-712912;
CC Q06587; G5E9A7: DMWD; NbExp=3; IntAct=EBI-752313, EBI-10976677;
CC Q06587; P13473-2: LAMP2; NbExp=3; IntAct=EBI-752313, EBI-21591415;
CC Q06587; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-752313, EBI-10271199;
CC Q06587; Q9BSM1: PCGF1; NbExp=9; IntAct=EBI-752313, EBI-749901;
CC Q06587; P35227: PCGF2; NbExp=13; IntAct=EBI-752313, EBI-2129767;
CC Q06587; Q3KNV8: PCGF3; NbExp=5; IntAct=EBI-752313, EBI-2339807;
CC Q06587; Q3KNV8-2: PCGF3; NbExp=3; IntAct=EBI-752313, EBI-12818023;
CC Q06587; Q86SE9: PCGF5; NbExp=8; IntAct=EBI-752313, EBI-2827999;
CC Q06587; Q9BYE7: PCGF6; NbExp=4; IntAct=EBI-752313, EBI-1048026;
CC Q06587; Q99496: RNF2; NbExp=6; IntAct=EBI-752313, EBI-722416;
CC Q06587; Q8N488: RYBP; NbExp=20; IntAct=EBI-752313, EBI-752324;
CC Q06587; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-752313, EBI-5235340;
CC Q06587; P04637: TP53; NbExp=7; IntAct=EBI-752313, EBI-366083;
CC Q06587; P51668: UBE2D1; NbExp=6; IntAct=EBI-752313, EBI-743540;
CC Q06587; P62837: UBE2D2; NbExp=4; IntAct=EBI-752313, EBI-347677;
CC Q06587; Q9Y2X8: UBE2D4; NbExp=4; IntAct=EBI-752313, EBI-745527;
CC Q06587; P61086: UBE2K; NbExp=9; IntAct=EBI-752313, EBI-473850;
CC Q06587; P51784: USP11; NbExp=4; IntAct=EBI-752313, EBI-306876;
CC Q06587; Q93009: USP7; NbExp=5; IntAct=EBI-752313, EBI-302474;
CC Q06587; Q8IY57: YAF2; NbExp=7; IntAct=EBI-752313, EBI-2842031;
CC Q06587; Q8IY57-5: YAF2; NbExp=8; IntAct=EBI-752313, EBI-12111538;
CC Q06587; Q96PE6: ZIM3; NbExp=3; IntAct=EBI-752313, EBI-18199075;
CC Q06587-2; Q8N488: RYBP; NbExp=3; IntAct=EBI-7065222, EBI-752324;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21282530}. Nucleus
CC speckle {ECO:0000269|PubMed:21282530}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q06587-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q06587-2; Sequence=VSP_017694;
CC -!- MISCELLANEOUS: The hPRC-H complex purification reported by
CC PubMed:12167701 probably presents a mixture of different PRC1-like
CC complexes.
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DR EMBL; Z14000; CAA78389.1; -; mRNA.
DR EMBL; BT007352; AAP36016.1; -; mRNA.
DR EMBL; AK289355; BAF82044.1; -; mRNA.
DR EMBL; AL031228; CAA20235.1; -; Genomic_DNA.
DR EMBL; AL031228; CAI95620.1; -; Genomic_DNA.
DR EMBL; AL645940; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL713971; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL844527; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR547129; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR759733; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR759786; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR847841; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002922; AAH02922.2; -; mRNA.
DR EMBL; BC051866; AAH51866.1; -; mRNA.
DR CCDS; CCDS34424.1; -. [Q06587-1]
DR PIR; A47380; A47380.
DR RefSeq; NP_002922.2; NM_002931.3. [Q06587-1]
DR AlphaFoldDB; Q06587; -.
DR SMR; Q06587; -.
DR BioGRID; 111947; 166.
DR CORUM; Q06587; -.
DR DIP; DIP-42043N; -.
DR IntAct; Q06587; 115.
DR MINT; Q06587; -.
DR STRING; 9606.ENSP00000363787; -.
DR GlyGen; Q06587; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q06587; -.
DR PhosphoSitePlus; Q06587; -.
DR BioMuta; RING1; -.
DR DMDM; 90110053; -.
DR EPD; Q06587; -.
DR jPOST; Q06587; -.
DR MassIVE; Q06587; -.
DR MaxQB; Q06587; -.
DR PaxDb; Q06587; -.
DR PeptideAtlas; Q06587; -.
DR PRIDE; Q06587; -.
DR ProteomicsDB; 58462; -. [Q06587-1]
DR ProteomicsDB; 58463; -. [Q06587-2]
DR TopDownProteomics; Q06587-1; -. [Q06587-1]
DR TopDownProteomics; Q06587-2; -. [Q06587-2]
DR Antibodypedia; 1772; 577 antibodies from 36 providers.
DR DNASU; 6015; -.
DR Ensembl; ENST00000374656.5; ENSP00000363787.4; ENSG00000204227.5. [Q06587-1]
DR Ensembl; ENST00000383212.4; ENSP00000372699.4; ENSG00000206287.5. [Q06587-1]
DR Ensembl; ENST00000415941.2; ENSP00000412190.2; ENSG00000226788.3. [Q06587-1]
DR Ensembl; ENST00000427374.2; ENSP00000400572.2; ENSG00000231115.3. [Q06587-1]
DR Ensembl; ENST00000430233.2; ENSP00000396271.2; ENSG00000228520.3. [Q06587-1]
DR Ensembl; ENST00000436128.2; ENSP00000396439.2; ENSG00000235107.3. [Q06587-1]
DR GeneID; 6015; -.
DR KEGG; hsa:6015; -.
DR MANE-Select; ENST00000374656.5; ENSP00000363787.4; NM_002931.4; NP_002922.2.
DR UCSC; uc003odk.4; human. [Q06587-1]
DR CTD; 6015; -.
DR DisGeNET; 6015; -.
DR GeneCards; RING1; -.
DR HGNC; HGNC:10018; RING1.
DR HPA; ENSG00000204227; Low tissue specificity.
DR MIM; 602045; gene.
DR neXtProt; NX_Q06587; -.
DR OpenTargets; ENSG00000204227; -.
DR PharmGKB; PA34393; -.
DR VEuPathDB; HostDB:ENSG00000204227; -.
DR eggNOG; KOG0311; Eukaryota.
DR GeneTree; ENSGT00940000161022; -.
DR HOGENOM; CLU_056557_1_0_1; -.
DR InParanoid; Q06587; -.
DR OMA; MIVGEVL; -.
DR PhylomeDB; Q06587; -.
DR TreeFam; TF105501; -.
DR PathwayCommons; Q06587; -.
DR Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-HSA-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-HSA-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-HSA-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-HSA-4655427; SUMOylation of DNA methylation proteins.
DR Reactome; R-HSA-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR Reactome; R-HSA-8943724; Regulation of PTEN gene transcription.
DR Reactome; R-HSA-8953750; Transcriptional Regulation by E2F6.
DR SignaLink; Q06587; -.
DR SIGNOR; Q06587; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 6015; 25 hits in 1130 CRISPR screens.
DR ChiTaRS; RING1; human.
DR GeneWiki; RING1; -.
DR GenomeRNAi; 6015; -.
DR Pharos; Q06587; Tbio.
DR PRO; PR:Q06587; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q06587; protein.
DR Bgee; ENSG00000204227; Expressed in pituitary gland and 94 other tissues.
DR ExpressionAtlas; Q06587; baseline and differential.
DR Genevisible; Q06587; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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; IDA:UniProtKB.
DR GO; GO:0001739; C:sex chromatin; IEA:Ensembl.
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:0097027; F:ubiquitin-protein transferase activator activity; IEA:Ensembl.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IEA:Ensembl.
DR GO; GO:0048593; P:camera-type eye morphogenesis; IEA:Ensembl.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0035518; P:histone H2A monoubiquitination; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
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_0000056384"
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 148..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:0000255"
FT MOD_RES 24
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 215
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 220
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT VAR_SEQ 1..29
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7681583, ECO:0000303|Ref.2"
FT /id="VSP_017694"
FT VARIANT 95
FT /note="R -> Q (in dbSNP:rs1204881780)"
FT /evidence="ECO:0000269|PubMed:25725044"
FT /id="VAR_076618"
SQ SEQUENCE 406 AA; 42429 MW; 6959787479DE9DAB CRC64;
MTTPANAQNA SKTWELSLYE LHRTPQEAIM DGTEIAVSPR SLHSELMCPI CLDMLKNTMT
TKECLHRFCS DCIVTALRSG NKECPTCRKK LVSKRSLRPD PNFDALISKI YPSREEYEAH
QDRVLIRLSR LHNQQALSSS IEEGLRMQAM HRAQRVRRPI PGSDQTTTMS GGEGEPGEGE
GDGEDVSSDS APDSAPGPAP KRPRGGGAGG SSVGTGGGGT GGVGGGAGSE DSGDRGGTLG
GGTLGPPSPP GAPSPPEPGG EIELVFRPHP LLVEKGEYCQ TRYVKTTGNA TVDHLSKYLA
LRIALERRQQ QEAGEPGGPG GGASDTGGPD GCGGEGGGAG GGDGPEEPAL PSLEGVSEKQ
YTIYIAPGGG AFTTLNGSLT LELVNEKFWK VSRPLELCYA PTKDPK
