ID SUZ12_HUMAN Reviewed; 739 AA. AC Q15022; Q96BD9; DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 3. DT 27-MAR-2024, entry version 212. DE RecName: Full=Polycomb protein SUZ12; DE AltName: Full=Chromatin precipitated E2F target 9 protein; DE Short=ChET 9 protein; DE AltName: Full=Joined to JAZF1 protein; DE AltName: Full=Suppressor of zeste 12 protein homolog; GN Name=SUZ12; Synonyms=CHET9, JJAZ1, KIAA0160; 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 [LARGE SCALE MRNA], AND VARIANT ILE-216. RC TISSUE=Bone marrow; RX PubMed=8590280; DOI=10.1093/dnares/2.4.167; RA Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.; RT "Prediction of the coding sequences of unidentified human genes. IV. The RT coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of RT cDNA clones from human cell line KG-1."; RL DNA Res. 2:167-174(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Uterus; 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 DISEASE, AND CHROMOSOMAL TRANSLOCATION WITH JAZF1. RX PubMed=11371647; DOI=10.1073/pnas.101132598; RA Koontz J.I., Soreng A.L., Nucci M., Kuo F.C., Pauwels P., RA van Den Berghe H., Cin P.D., Fletcher J.A., Sklar J.; RT "Frequent fusion of the JAZF1 and JJAZ1 genes in endometrial stromal RT tumors."; RL Proc. Natl. Acad. Sci. U.S.A. 98:6348-6353(2001). RN [4] RP INDUCTION. RX PubMed=11564866; DOI=10.1128/mcb.21.20.6820-6832.2001; RA Weinmann A.S., Bartley S.M., Zhang T., Zhang M.Q., Farnham P.J.; RT "Use of chromatin immunoprecipitation to clone novel E2F target RT promoters."; RL Mol. Cell. Biol. 21:6820-6832(2001). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE PRC2 COMPLEX RP WITH EED; EZH2; RBBP4 AND RBBP7, AND METHYLTRANSFERASE ACTIVITY OF THE PRC2 RP COMPLEX. RX PubMed=12435631; DOI=10.1101/gad.1035902; RA Kuzmichev A., Nishioka K., Erdjument-Bromage H., Tempst P., Reinberg D.; RT "Histone methyltransferase activity associated with a human multiprotein RT complex containing the Enhancer of Zeste protein."; RL Genes Dev. 16:2893-2905(2002). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE PRC2 COMPLEX RP WITH EED; EZH2; RBBP4 AND RBBP7, AND METHYLTRANSFERASE ACTIVITY OF THE PRC2 RP COMPLEX. RX PubMed=12351676; DOI=10.1126/science.1076997; RA Cao R., Wang L., Wang H., Xia L., Erdjument-Bromage H., Tempst P., RA Jones R.S., Zhang Y.; RT "Role of histone H3 lysine 27 methylation in Polycomb-group silencing."; RL Science 298:1039-1043(2002). RN [7] RP INDUCTION. RX PubMed=14532106; DOI=10.1093/emboj/cdg542; RA Bracken A.P., Pasini D., Capra M., Prosperini E., Colli E., Helin K.; RT "EZH2 is downstream of the pRB-E2F pathway, essential for proliferation and RT amplified in cancer."; RL EMBO J. 22:5323-5335(2003). RN [8] RP FUNCTION, INTERACTION WITH EZH2, METHYLTRANSFERASE ACTIVITY OF THE PRC2 RP COMPLEX, AND DEVELOPMENTAL STAGE. RX PubMed=15385962; DOI=10.1038/sj.emboj.7600402; RA Pasini D., Bracken A.P., Jensen M.R., Lazzerini Denchi E., Helin K.; RT "Suz12 is essential for mouse development and for EZH2 histone RT methyltransferase activity."; RL EMBO J. 23:4061-4071(2004). RN [9] RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=15231737; DOI=10.1101/gad.1200204; RA Kirmizis A., Bartley S.M., Kuzmichev A., Margueron R., Reinberg D., RA Green R., Farnham P.J.; RT "Silencing of human polycomb target genes is associated with methylation of RT histone H3 Lys 27."; RL Genes Dev. 18:1592-1605(2004). RN [10] RP CHARACTERIZATION OF THE PRC2 AND PRC3 COMPLEXES INCLUDING EED; EZH2; RBBP4; RP RBBP7 AND SUZ12, AND METHYLTRANSFERASE ACTIVITY OF THE PRC2 AND PRC3 RP COMPLEXES. RX PubMed=15099518; DOI=10.1016/s1097-2765(04)00185-6; RA Kuzmichev A., Jenuwein T., Tempst P., Reinberg D.; RT "Different EZH2-containing complexes target methylation of histone H1 or RT nucleosomal histone H3."; RL Mol. Cell 14:183-193(2004). RN [11] RP FUNCTION, CHARACTERIZATION OF THE PRC2 COMPLEX INCLUDING AEBP2; EED; EZH2; RP RBBP4 AND SUZ12, AND METHYLTRANSFERASE ACTIVITY OF THE PRC2 COMPLEX. RX PubMed=15225548; DOI=10.1016/j.molcel.2004.06.020; RA Cao R., Zhang Y.; RT "SUZ12 is required for both the histone methyltransferase activity and the RT silencing function of the EED-EZH2 complex."; RL Mol. Cell 15:57-67(2004). RN [12] RP CHARACTERIZATION OF THE PRC4 COMPLEX INCLUDING EED; EZH2; RBBP4; RBBP7; RP SUZ12 AND SIRT1, METHYLTRANSFERASE ACTIVITY OF THE PRC4 COMPLEX, AND TISSUE RP SPECIFICITY. RX PubMed=15684044; DOI=10.1073/pnas.0409875102; RA Kuzmichev A., Margueron R., Vaquero A., Preissner T.S., Scher M., RA Kirmizis A., Ouyang X., Brockdorff N., Abate-Shen C., Farnham P.J., RA Reinberg D.; RT "Composition and histone substrates of polycomb repressive group complexes RT change during cellular differentiation."; RL Proc. Natl. Acad. Sci. U.S.A. 102:1859-1864(2005). RN [13] RP INTERACTION WITH EZH2. RX PubMed=16224021; DOI=10.1126/science.1118947; RA Cha T.-L., Zhou B.P., Xia W., Wu Y., Yang C.-C., Chen C.-T., Ping B., RA Otte A.P., Hung M.-C.; RT "Akt-mediated phosphorylation of EZH2 suppresses methylation of lysine 27 RT in histone H3."; RL Science 310:306-310(2005). RN [14] RP INTERACTION WITH WDR77. RX PubMed=16712789; DOI=10.1016/j.bbrc.2006.05.014; RA Furuno K., Masatsugu T., Sonoda M., Sasazuki T., Yamamoto K.; RT "Association of Polycomb group SUZ12 with WD-repeat protein MEP50 that RT binds to histone H2A selectively in vitro."; RL Biochem. Biophys. Res. Commun. 345:1051-1058(2006). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-546, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [16] RP FUNCTION. RX PubMed=16618801; DOI=10.1101/gad.381706; RA Bracken A.P., Dietrich N., Pasini D., Hansen K.H., Helin K.; RT "Genome-wide mapping of Polycomb target genes unravels their roles in cell RT fate transitions."; RL Genes Dev. 20:1123-1136(2006). RN [17] RP METHYLTRANSFERASE ACTIVITY OF THE PRC2 COMPLEX, AND INTERACTION WITH RP HISTONE H1. RX PubMed=16431907; DOI=10.1074/jbc.m513425200; RA Martin C., Cao R., Zhang Y.; RT "Substrate preferences of the EZH2 histone methyltransferase complex."; RL J. Biol. Chem. 281:8365-8370(2006). RN [18] RP FUNCTION. RX PubMed=17344414; DOI=10.1101/gad.415507; RA Bracken A.P., Kleine-Kohlbrecher D., Dietrich N., Pasini D., Gargiulo G., RA Beekman C., Theilgaard-Moench K., Minucci S., Porse B.T., Marine J.-C., RA Hansen K.H., Helin K.; RT "The Polycomb group proteins bind throughout the INK4A-ARF locus and are RT disassociated in senescent cells."; RL Genes Dev. 21:525-530(2007). RN [19] RP DE NOVO DNA METHYLATION OF PRC2 TARGET GENES. RX PubMed=17200670; DOI=10.1038/ng1950; RA Schlesinger Y., Straussman R., Keshet I., Farkash S., Hecht M., RA Zimmerman J., Eden E., Yakhini Z., Ben-Shushan E., Reubinoff B.E., RA Bergman Y., Simon I., Cedar H.; RT "Polycomb-mediated methylation on Lys27 of histone H3 pre-marks genes for RT de novo methylation in cancer."; RL Nat. Genet. 39:232-236(2007). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-546 AND SER-583, AND RP IDENTIFICATION BY 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 [21] RP IDENTIFICATION IN THE PRC2/EZH1 COMPLEX. RX PubMed=19026781; DOI=10.1016/j.molcel.2008.11.004; RA Margueron R., Li G., Sarma K., Blais A., Zavadil J., Woodcock C.L., RA Dynlacht B.D., Reinberg D.; RT "Ezh1 and Ezh2 maintain repressive chromatin through different RT mechanisms."; RL Mol. Cell 32:503-518(2008). RN [22] RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE PRC2 COMPLEX, RP AND METHYLTRANSFERASE ACTIVITY OF THE PRC2 COMPLEX. RX PubMed=18086877; DOI=10.1128/mcb.01589-07; RA Cao R., Wang H., He J., Erdjument-Bromage H., Tempst P., Zhang Y.; RT "Role of hPHF1 in H3K27 methylation and Hox gene silencing."; RL Mol. Cell. Biol. 28:1862-1872(2008). RN [23] RP FUNCTION, INTERACTION WITH EED AND EZH2, INTERACTION OF THE PRC2 COMPLEX RP WITH PHF1, AND METHYLTRANSFERASE ACTIVITY OF THE PRC2 COMPLEX. RX PubMed=18285464; DOI=10.1128/mcb.02017-07; RA Sarma K., Margueron R., Ivanov A., Pirrotta V., Reinberg D.; RT "Ezh2 requires PHF1 to efficiently catalyze H3 lysine 27 trimethylation in RT vivo."; RL Mol. Cell. Biol. 28:2718-2731(2008). RN [24] RP SUMOYLATION AT LYS-72; LYS-73 AND LYS-75. RX PubMed=18628979; DOI=10.1371/journal.pone.0002704; RA Riising E.M., Boggio R., Chiocca S., Helin K., Pasini D.; RT "The polycomb repressive complex 2 is a potential target of SUMO RT modifications."; RL PLoS ONE 3:E2704-E2704(2008). RN [25] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-546, AND IDENTIFICATION BY RP 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 [26] RP TRANS-SPLICING. RX PubMed=18772439; DOI=10.1126/science.1156725; RA Li H., Wang J., Mor G., Sklar J.; RT "A neoplastic gene fusion mimics trans-splicing of RNAs in normal human RT cells."; RL Science 321:1357-1361(2008). RN [27] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [28] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-546, 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 [29] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-546, AND IDENTIFICATION BY RP 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 [30] RP INTERACTION WITH CDYL. RX PubMed=22009739; DOI=10.1074/jbc.m111.271064; RA Zhang Y., Yang X., Gui B., Xie G., Zhang D., Shang Y., Liang J.; RT "Corepressor protein CDYL functions as a molecular bridge between polycomb RT repressor complex 2 and repressive chromatin mark trimethylated histone RT lysine 27."; RL J. Biol. Chem. 286:42414-42425(2011). RN [31] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-546, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [32] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-541; SER-546 AND RP SER-726, AND 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 [33] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [34] RP INVOLVEMENT IN IMMAS, VARIANT IMMAS VAL-610, CHARACTERIZATION OF VARIANT RP IMMAS VAL-610, AND FUNCTION. RX PubMed=28229514; DOI=10.1002/humu.23200; RA Imagawa E., Higashimoto K., Sakai Y., Numakura C., Okamoto N., RA Matsunaga S., Ryo A., Sato Y., Sanefuji M., Ihara K., Takada Y., RA Nishimura G., Saitsu H., Mizuguchi T., Miyatake S., Nakashima M., RA Miyake N., Soejima H., Matsumoto N.; RT "Mutations in genes encoding polycomb repressive complex 2 subunits cause RT Weaver syndrome."; RL Hum. Mutat. 38:637-648(2017). RN [35] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-75; LYS-223 AND LYS-390, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [36] RP INTERACTION WITH ARMC12. RX PubMed=30026490; DOI=10.1038/s41467-018-05286-2; RA Li D., Song H., Mei H., Fang E., Wang X., Yang F., Li H., Chen Y., RA Huang K., Zheng L., Tong Q.; RT "Armadillo repeat containing 12 promotes neuroblastoma progression through RT interaction with retinoblastoma binding protein 4."; RL Nat. Commun. 9:2829-2829(2018). RN [37] RP INTERACTION WITH EZHIP. RX PubMed=30923826; DOI=10.1093/neuonc/noz058; RA Huebner J.M., Mueller T., Papageorgiou D.N., Mauermann M., Krijgsveld J., RA Russell R.B., Ellison D.W., Pfister S.M., Pajtler K.W., Kool M.; RT "EZHIP / CXorf67 mimics K27M mutated oncohistones and functions as an RT intrinsic inhibitor of PRC2 function in aggressive posterior fossa RT ependymoma."; RL Neuro-oncol. 21:878-889(2019). RN [38] {ECO:0007744|PDB:5WAI, ECO:0007744|PDB:5WAK} RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 76-545 IN COMPLEX WITH RBBP4; RP AEBP2 AND JARID2, FUNCTION, IDENTIFICATION IN THE PRC2 COMPLEX, INTERACTION RP WITH AEBP2; PHF19; JARID2 AND EPOP, SUBCELLULAR LOCATION, AND MUTAGENESIS RP OF PHE-86 AND PHE-90. RX PubMed=29499137; DOI=10.1016/j.molcel.2018.01.039; RA Chen S., Jiao L., Shubbar M., Yang X., Liu X.; RT "Unique Structural Platforms of Suz12 Dictate Distinct Classes of PRC2 for RT Chromatin Binding."; RL Mol. Cell 69:840-852.e5(2018). RN [39] {ECO:0007744|PDB:6NQ3} RP X-RAY CRYSTALLOGRAPHY (2.89 ANGSTROMS) OF 76-545 IN COMPLEX WITH RBBP4; RP PHF19 AND JARID2, FUNCTION, IDENTIFICATION IN THE PRC2 COMPLEX, SUBCELLULAR RP LOCATION, AND MUTAGENESIS OF 195-LYS--LYS-197; ARG-196; TRP-334 AND RP GLY-518. RX PubMed=31959557; DOI=10.1016/j.molcel.2019.12.019; RA Chen S., Jiao L., Liu X., Yang X., Liu X.; RT "A Dimeric Structural Scaffold for PRC2-PCL Targeting to CpG Island RT Chromatin."; RL Mol. Cell 77:1265-1278.e7(2020). RN [40] RP VARIANT IMMAS HIS-599, AND INVOLVEMENT IN IMMAS. RX PubMed=30019515; DOI=10.1111/cge.13415; RA Imagawa E., Albuquerque E.V.A., Isidor B., Mitsuhashi S., Mizuguchi T., RA Miyatake S., Takata A., Miyake N., Boguszewski M.C.S., Boguszewski C.L., RA Lerario A.M., Funari M.A., Jorge A.A.L., Matsumoto N.; RT "Novel SUZ12 mutations in Weaver-like syndrome."; RL Clin. Genet. 94:461-466(2018). RN [41] RP VARIANTS IMMAS GLN-535; LEU-603 AND 654-ARG--LEU-739 DEL. RX PubMed=31736240; DOI=10.1002/ajmg.c.31748; RG C.A.U.S.E.S. Study; RA Cyrus S.S., Cohen A.S.A., Agbahovbe R., Avela K., Yeung K.S., Chung B.H.Y., RA Luk H.M., Tkachenko N., Choufani S., Weksberg R., Lopez-Rangel E., RA Brown K., Saenz M.S., Svihovec S., McCandless S.E., Bird L.M., Garcia A.G., RA Gambello M.J., McWalter K., Schnur R.E., An J., Jones S.J.M., Bhalla S.K., RA Pinz H., Braddock S.R., Gibson W.T.; RT "Rare SUZ12 variants commonly cause an overgrowth phenotype."; RL Am. J. Med. Genet. C. Semin. Med. Genet. 181:532-547(2019). CC -!- FUNCTION: Polycomb group (PcG) protein. Component of the PRC2 complex, CC which methylates 'Lys-9' (H3K9me) and 'Lys-27' (H3K27me) of histone H3, CC leading to transcriptional repression of the affected target gene CC (PubMed:15225548, PubMed:15231737, PubMed:15385962, PubMed:16618801, CC PubMed:17344414, PubMed:18285464, PubMed:28229514, PubMed:29499137, CC PubMed:31959557). The PRC2 complex may also serve as a recruiting CC platform for DNA methyltransferases, thereby linking two epigenetic CC repression systems (PubMed:12435631, PubMed:12351676, PubMed:15385962, CC PubMed:15099518, PubMed:15225548, PubMed:15684044, PubMed:16431907, CC PubMed:18086877, PubMed:18285464). Genes repressed by the PRC2 complex CC include HOXC8, HOXA9, MYT1 and CDKN2A (PubMed:15231737, CC PubMed:16618801, PubMed:17200670, PubMed:31959557). CC {ECO:0000269|PubMed:12351676, ECO:0000269|PubMed:12435631, CC ECO:0000269|PubMed:15099518, ECO:0000269|PubMed:15225548, CC ECO:0000269|PubMed:15231737, ECO:0000269|PubMed:15385962, CC ECO:0000269|PubMed:15684044, ECO:0000269|PubMed:16431907, CC ECO:0000269|PubMed:16618801, ECO:0000269|PubMed:17200670, CC ECO:0000269|PubMed:17344414, ECO:0000269|PubMed:18086877, CC ECO:0000269|PubMed:18285464, ECO:0000269|PubMed:28229514, CC ECO:0000269|PubMed:29499137, ECO:0000269|PubMed:31959557}. CC -!- SUBUNIT: Component of the PRC2 complex, which consists of the core CC subunits EED, EZH1 or EZH2, SUZ12, and RBBP4, and various combinations CC of accessory subunits including AEBP2, JARID2, PHF19, MTF2 and EPOP CC (PubMed:12435631, PubMed:12351676, PubMed:15385962, PubMed:15099518, CC PubMed:15225548, PubMed:15684044, PubMed:16224021, PubMed:19026781, CC PubMed:18285464, PubMed:29499137, PubMed:31959557). Within the complex, CC interacts (via C2H2 zinc finger domain) with JARID2 and EPOP; JARID2 CC and EPOP compete for SUZ12 binding (PubMed:29499137). Also interacts CC with AEBP2 and PHF19 (PubMed:29499137). Forms a monomeric PRC2.2 (class CC 2) complex consisting of at least SUZ12, RBBP4, AEBP2 and JARID2 CC (PubMed:29499137). Forms a dimeric PRC2.1 (class 1, PRC-PCL) complex CC consisting of at least SUZ12, RBBP4, and PHF19 or MTF2; PHF19 and MTF2 CC stabilize the dimeric structure which enhances PRC2 interaction with CC chromatin (PubMed:31959557). The minimum components required for CC methyltransferase activity of the PRC2/EZH2 complex are EED, EZH2 and CC SUZ12 (PubMed:12435631, PubMed:12351676, PubMed:15385962, CC PubMed:15099518, PubMed:15225548, PubMed:15684044, PubMed:16431907, CC PubMed:18086877, PubMed:18285464). The PRC2 complex may also interact CC with DNMT1, DNMT3A, DNMT3B and PHF1 via the EZH2 subunit and with SIRT1 CC via the SUZ12 subunit (PubMed:15684044, PubMed:18285464). Interacts CC with WDR77 (PubMed:16712789). Interacts with histone H1 CC (PubMed:16431907). Interacts with CDYL (PubMed:22009739). Interacts CC with BMAL1 (By similarity). Interacts with EZHIP (via C-terminal CC region) (PubMed:30923826). Interacts with ARMC12 (PubMed:30026490). CC {ECO:0000250|UniProtKB:Q80U70, ECO:0000269|PubMed:12351676, CC ECO:0000269|PubMed:12435631, ECO:0000269|PubMed:15099518, CC ECO:0000269|PubMed:15225548, ECO:0000269|PubMed:15385962, CC ECO:0000269|PubMed:15684044, ECO:0000269|PubMed:16224021, CC ECO:0000269|PubMed:16431907, ECO:0000269|PubMed:16712789, CC ECO:0000269|PubMed:18086877, ECO:0000269|PubMed:18285464, CC ECO:0000269|PubMed:19026781, ECO:0000269|PubMed:22009739, CC ECO:0000269|PubMed:29499137, ECO:0000269|PubMed:30026490, CC ECO:0000269|PubMed:30923826, ECO:0000269|PubMed:31959557}. CC -!- INTERACTION: CC Q15022; O75530: EED; NbExp=10; IntAct=EBI-1264675, EBI-923794; CC Q15022; Q15910: EZH2; NbExp=27; IntAct=EBI-1264675, EBI-530054; CC Q15022; O15379: HDAC3; NbExp=7; IntAct=EBI-1264675, EBI-607682; CC Q15022; Q92833-1: JARID2; NbExp=7; IntAct=EBI-1264675, EBI-15825247; CC Q15022; Q15156: PML-RAR; NbExp=6; IntAct=EBI-1264675, EBI-867256; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15231737, CC ECO:0000269|PubMed:29499137, ECO:0000269|PubMed:31959557}. CC Note=Localizes to chromatin as part of the PRC2 complex. CC {ECO:0000269|PubMed:29499137, ECO:0000269|PubMed:31959557}. CC -!- TISSUE SPECIFICITY: Overexpressed in breast and colon cancer. CC {ECO:0000269|PubMed:15231737, ECO:0000269|PubMed:15684044}. CC -!- DEVELOPMENTAL STAGE: Expressed at low levels in quiescent cells. CC Expression rises at the G1/S phase transition. CC {ECO:0000269|PubMed:15385962}. CC -!- INDUCTION: Expression is induced by E2F1, E2F2 and E2F3. CC {ECO:0000269|PubMed:11564866, ECO:0000269|PubMed:14532106}. CC -!- PTM: Sumoylated, probably by PIAS2. {ECO:0000269|PubMed:18628979}. CC -!- DISEASE: Note=A chromosomal aberration involving SUZ12 may be a cause CC of endometrial stromal tumors. Translocation t(7;17)(p15;q21) with CC JAZF1. The translocation generates the JAZF1-SUZ12 oncogene consisting CC of the N-terminus part of JAZF1 and the C-terminus part of SUZ12. It is CC frequently found in all cases of endometrial stromal tumors, except in CC endometrial stromal sarcomas, where it is rarer. CC {ECO:0000269|PubMed:11371647}. CC -!- DISEASE: Imagawa-Matsumoto syndrome (IMMAS) [MIM:618786]: An autosomal CC dominant syndrome characterized by generalized overgrowth, dysmorphic CC features, musculoskeletal abnormalities, developmental delay and CC intellectual disability. Some patients have genitourinary and CC structural brain abnormalities. {ECO:0000269|PubMed:28229514, CC ECO:0000269|PubMed:30019515, ECO:0000269|PubMed:31736240}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- MISCELLANEOUS: Under hypoxic conditions, the precursor SUZ12 RNA CC undergoes regulated trans-splicing with the JAZF1 RNA, resulting in a CC chimeric isoform which may be protective against apoptosis. The CC chimeric transcript is characterized by JAZF1 exons 1-3 joined to SUZ12 CC exon 2-16. The chimeric transcript is expressed primarily in the CC endometrium from late secretory and early proliferative phases of the CC menstrual cycle, but not in normal myometrium at any phase of the CC cycle. Its expression is slightly induced by low levels of CC progesterone, but suppressed by both estrogen and high levels of CC progesterone (PubMed:18772439). {ECO:0000305|PubMed:18772439}. CC -!- SIMILARITY: Belongs to the VEFS (VRN2-EMF2-FIS2-SU(Z)12) family. CC {ECO:0000305}. CC -!- CAUTION: Two variants of the PRC2 complex have been described, termed CC PRC3 and PRC4. Each of the three complexes may include a different CC complement of EED isoforms, although the precise sequences of the CC isoforms in each complex have not been determined. The PRC2 and PRC4 CC complexes may also methylate 'Lys-26' of histone H1 in addition to CC 'Lys-27' of histone H3 (PubMed:15099518, PubMed:15684044), although CC other studies have demonstrated no methylation of 'Lys-26' of histone CC H1 by PRC2 (PubMed:16431907). {ECO:0000305|PubMed:16431907}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA09931.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/41039/JJAZ1"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D63881; BAA09931.2; ALT_INIT; mRNA. DR EMBL; BC015704; AAH15704.1; -; mRNA. DR CCDS; CCDS11270.1; -. DR RefSeq; NP_056170.2; NM_015355.3. DR PDB; 4W2R; X-ray; 2.81 A; S/T=545-725. DR PDB; 5HYN; X-ray; 2.95 A; C/H/M/S=558-685. DR PDB; 5IJ7; X-ray; 2.62 A; S/T=545-725. DR PDB; 5IJ8; X-ray; 2.99 A; S/T=545-725. DR PDB; 5LS6; X-ray; 3.47 A; C/F/I/L=558-685. DR PDB; 5WAI; X-ray; 2.90 A; B/F=76-545. DR PDB; 5WAK; X-ray; 3.20 A; B=76-545. DR PDB; 5WG6; X-ray; 3.90 A; A/C=543-695. DR PDB; 6B3W; X-ray; 3.05 A; S/T=545-725. DR PDB; 6C23; EM; 3.90 A; A/M/Q=1-739. DR PDB; 6C24; EM; 3.50 A; A/M/Q=1-739. DR PDB; 6NQ3; X-ray; 2.89 A; B/F=76-545. DR PDB; 6WKR; EM; 3.50 A; A=1-739. DR PDB; 7AT8; EM; 4.40 A; C=1-739. DR PDB; 7KSO; EM; 3.90 A; C=1-739. DR PDB; 7KSR; EM; 4.10 A; C=1-739. DR PDB; 7KTP; EM; 4.80 A; C=1-739. DR PDB; 7TD5; X-ray; 2.99 A; C/H=561-739. DR PDB; 8FYH; EM; 3.40 A; B/H=1-739. DR PDBsum; 4W2R; -. DR PDBsum; 5HYN; -. DR PDBsum; 5IJ7; -. DR PDBsum; 5IJ8; -. DR PDBsum; 5LS6; -. DR PDBsum; 5WAI; -. DR PDBsum; 5WAK; -. DR PDBsum; 5WG6; -. DR PDBsum; 6B3W; -. DR PDBsum; 6C23; -. DR PDBsum; 6C24; -. DR PDBsum; 6NQ3; -. DR PDBsum; 6WKR; -. DR PDBsum; 7AT8; -. DR PDBsum; 7KSO; -. DR PDBsum; 7KSR; -. DR PDBsum; 7KTP; -. DR PDBsum; 7TD5; -. DR PDBsum; 8FYH; -. DR AlphaFoldDB; Q15022; -. DR EMDB; EMD-11910; -. DR EMDB; EMD-11912; -. DR EMDB; EMD-21707; -. DR EMDB; EMD-23021; -. DR EMDB; EMD-23022; -. DR EMDB; EMD-23024; -. DR EMDB; EMD-23025; -. DR EMDB; EMD-23103; -. DR EMDB; EMD-29578; -. DR EMDB; EMD-29647; -. DR EMDB; EMD-29656; -. DR EMDB; EMD-7334; -. DR EMDB; EMD-7335; -. DR SMR; Q15022; -. DR BioGRID; 117059; 633. DR ComplexPortal; CPX-2196; Polycomb repressive complex 2.1, EZH1-RBBP4-PCL3-PALI1 variant. DR ComplexPortal; CPX-2198; Polycomb repressive complex 2.1,EZH2-RBBP4-PCL3-PALI1 variant. DR ComplexPortal; CPX-2204; Polycomb repressive complex 2.1, EZH2-RBBP4-PCL1-PALI1 variant. DR ComplexPortal; CPX-2205; Polycomb repressive complex 2.1, EZH1-RBBP7-PCL1-EPOP variant. DR ComplexPortal; CPX-2209; Polycomb repressive complex 2.2, EZH2-RBBP4 variant. DR ComplexPortal; CPX-2212; Polycomb repressive complex 2.2, EZH1-RBBP7 variant. DR ComplexPortal; CPX-2213; Polycomb repressive complex 2.2, EZH2-RBBP7 variant. DR ComplexPortal; CPX-2307; Polycomb repressive complex 2.1, EZH1-RBBP7-PCL1-PALI1 variant. DR ComplexPortal; CPX-2309; Polycomb repressive complex 2.1, EZH1-RBBP7-PCL2-PALI1 variant. DR ComplexPortal; CPX-2310; Polycomb repressive complex 2.1, EZH1-RBBP4-PCL2-PALI1 variant. DR ComplexPortal; CPX-2311; Polycomb repressive complex 2.1, EZH2-RBBP7-PCL1-PALI1 variant. DR ComplexPortal; CPX-2312; Polycomb repressive complex 2.1, EZH2-RBBP4-PCL2-PALI1 variant. DR ComplexPortal; CPX-2314; Polycomb repressive complex 2.1,EZH2-RBBP7-PCL2-PALI1 variant. DR ComplexPortal; CPX-2316; Polycomb repressive complex 2.1,EZH2-RBBP7-PCL3-PALI1 variant. DR ComplexPortal; CPX-2317; Polycomb repressive complex 2.1, EZH1-RBBP4-PCL1-EPOP variant. DR ComplexPortal; CPX-2318; Polycomb repressive complex 2.1, EZH1-RBBP4-PCL2-EPOP variant. DR ComplexPortal; CPX-2320; Polycomb repressive complex 2.1, EZH1-RBBP7-PCL2-EPOP variant. DR ComplexPortal; CPX-2322; Polycomb repressive complex 2.1, EZH1-RBBP4-PCL3-EPOP variant. DR ComplexPortal; CPX-2323; Polycomb repressive complex 2.1, EZH1-RBBP7-PCL3-EPOP variant. DR ComplexPortal; CPX-2324; Polycomb repressive complex 2.1, EZH2-RBBP4-PCL1-EPOP variant. DR ComplexPortal; CPX-2325; Polycomb repressive complex 2.1, EZH2-RBBP7-PCL1-EPOP variant. DR ComplexPortal; CPX-2326; Polycomb repressive complex 2.1, EZH2-RBBP4-PCL2-EPOP variant. DR ComplexPortal; CPX-2327; Polycomb repressive complex 2.1, EZH2-RBBP7-PCL2-EPOP variant. DR ComplexPortal; CPX-2328; Polycomb repressive complex 2.1, EZH2-RBBP4-PCL3-EPOP variant. DR ComplexPortal; CPX-2329; Polycomb repressive complex 2.1, EZH2-RBBP7-PCL3-EPOP variant. DR ComplexPortal; CPX-2330; Polycomb repressive complex 2.2, EZH1-RBBP4 variant. DR ComplexPortal; CPX-2569; Polycomb repressive complex 2.1, EZH1-RBBP4-PCL1-PALI1 variant. DR ComplexPortal; CPX-2570; Polycomb repressive complex 2.1, EZH1-RBBP7-PCL3-PALI1 variant. DR CORUM; Q15022; -. DR DIP; DIP-38524N; -. DR IntAct; Q15022; 80. DR MINT; Q15022; -. DR STRING; 9606.ENSP00000316578; -. DR BindingDB; Q15022; -. DR ChEMBL; CHEMBL2189118; -. DR GlyCosmos; Q15022; 1 site, 1 glycan. DR GlyGen; Q15022; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q15022; -. DR PhosphoSitePlus; Q15022; -. DR SwissPalm; Q15022; -. DR BioMuta; SUZ12; -. DR DMDM; 116242808; -. DR EPD; Q15022; -. DR jPOST; Q15022; -. DR MassIVE; Q15022; -. DR MaxQB; Q15022; -. DR PaxDb; 9606-ENSP00000316578; -. DR PeptideAtlas; Q15022; -. DR ProteomicsDB; 60374; -. DR Pumba; Q15022; -. DR Antibodypedia; 27067; 459 antibodies from 38 providers. DR DNASU; 23512; -. DR Ensembl; ENST00000322652.10; ENSP00000316578.5; ENSG00000178691.11. DR GeneID; 23512; -. DR KEGG; hsa:23512; -. DR MANE-Select; ENST00000322652.10; ENSP00000316578.5; NM_015355.4; NP_056170.2. DR UCSC; uc002hgs.3; human. DR AGR; HGNC:17101; -. DR CTD; 23512; -. DR DisGeNET; 23512; -. DR GeneCards; SUZ12; -. DR HGNC; HGNC:17101; SUZ12. DR HPA; ENSG00000178691; Low tissue specificity. DR MalaCards; SUZ12; -. DR MIM; 606245; gene. DR MIM; 618786; phenotype. DR neXtProt; NX_Q15022; -. DR OpenTargets; ENSG00000178691; -. DR Orphanet; 213711; Endometrial stromal sarcoma. DR Orphanet; 3447; Weaver syndrome. DR PharmGKB; PA134936035; -. DR VEuPathDB; HostDB:ENSG00000178691; -. DR eggNOG; KOG2350; Eukaryota. DR GeneTree; ENSGT00390000012364; -. DR InParanoid; Q15022; -. DR OMA; RNEKMFG; -. DR OrthoDB; 3107244at2759; -. DR PhylomeDB; Q15022; -. DR TreeFam; TF323249; -. DR PathwayCommons; Q15022; -. DR Reactome; R-HSA-212300; PRC2 methylates histones and DNA. DR Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence. DR Reactome; R-HSA-3214841; PKMTs methylate histone lysines. DR Reactome; R-HSA-4551638; SUMOylation of chromatin organization proteins. DR Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis. DR Reactome; R-HSA-8943724; Regulation of PTEN gene transcription. DR Reactome; R-HSA-8953750; Transcriptional Regulation by E2F6. DR Reactome; R-HSA-9609690; HCMV Early Events. DR Reactome; R-HSA-9710421; Defective pyroptosis. DR SignaLink; Q15022; -. DR SIGNOR; Q15022; -. DR BioGRID-ORCS; 23512; 161 hits in 1174 CRISPR screens. DR ChiTaRS; SUZ12; human. DR GeneWiki; SUZ12; -. DR GenomeRNAi; 23512; -. DR Pharos; Q15022; Tbio. DR PRO; PR:Q15022; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q15022; Protein. DR Bgee; ENSG00000178691; Expressed in trabecular bone tissue and 213 other cell types or tissues. DR ExpressionAtlas; Q15022; baseline and differential. DR GO; GO:0005677; C:chromatin silencing complex; IEA:Ensembl. DR GO; GO:0035098; C:ESC/E(Z) complex; IDA:UniProtKB. DR GO; GO:0016604; C:nuclear body; IDA:HPA. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; HDA:UniProtKB. DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:Ensembl. DR GO; GO:0016586; C:RSC-type complex; IBA:GO_Central. DR GO; GO:0001739; C:sex chromatin; IEA:Ensembl. DR GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central. DR GO; GO:0008047; F:enzyme activator activity; IMP:UniProtKB. DR GO; GO:0042054; F:histone methyltransferase activity; IMP:MGI. DR GO; GO:0106222; F:lncRNA binding; IEA:Ensembl. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB. DR GO; GO:1990841; F:promoter-specific chromatin binding; IEA:Ensembl. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:Ensembl. DR GO; GO:0001222; F:transcription corepressor binding; IPI:ARUK-UCL. DR GO; GO:0008283; P:cell population proliferation; IEA:Ensembl. DR GO; GO:0140718; P:facultative heterochromatin formation; IEA:Ensembl. DR GO; GO:0045596; P:negative regulation of cell differentiation; IMP:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl. DR GO; GO:0048709; P:oligodendrocyte differentiation; IEA:Ensembl. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl. DR GO; GO:0060816; P:random inactivation of X chromosome; IEA:Ensembl. DR CDD; cd21551; VEFS-box_SUZ12; 1. DR CDD; cd21750; ZnB-Zn_SUZ12; 1. DR IDEAL; IID00725; -. DR InterPro; IPR019135; Polycomb_protein_VEFS-Box. DR PANTHER; PTHR22597; POLYCOMB GROUP PROTEIN; 1. DR PANTHER; PTHR22597:SF0; POLYCOMB PROTEIN SUZ12; 1. DR Pfam; PF09733; VEFS-Box; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1. DR Genevisible; Q15022; HS. PE 1: Evidence at protein level; KW 3D-structure; Chromatin regulator; Chromosomal rearrangement; KW Disease variant; Intellectual disability; Isopeptide bond; Metal-binding; KW Nucleus; Phosphoprotein; Proto-oncogene; Reference proteome; Repressor; KW Transcription; Transcription regulation; Ubl conjugation; Zinc; KW Zinc-finger. FT CHAIN 1..739 FT /note="Polycomb protein SUZ12" FT /id="PRO_0000047057" FT ZN_FING 448..471 FT /note="C2H2-type" FT REGION 1..23 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 79..106 FT /note="Interaction with JARID2 and EPOP" FT /evidence="ECO:0000269|PubMed:29499137" FT REGION 146..363 FT /note="Interaction with AEBP2 and PHF19" FT /evidence="ECO:0000269|PubMed:29499137" FT REGION 378..399 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 563..639 FT /note="VEFS-box" FT REGION 687..739 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 698..739 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 93..94 FT /note="Breakpoint for translocation to form JAZF1-SUZ12 FT oncogene" FT MOD_RES 20 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 541 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 546 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 583 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18220336" FT MOD_RES 726 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT CROSSLNK 72 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000269|PubMed:18628979" FT CROSSLNK 73 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000269|PubMed:18628979" FT CROSSLNK 75 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO); alternate" FT /evidence="ECO:0000269|PubMed:18628979" FT CROSSLNK 75 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 223 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 390 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VARIANT 216 FT /note="N -> I (in dbSNP:rs17339444)" FT /evidence="ECO:0000269|PubMed:8590280" FT /id="VAR_028100" FT VARIANT 535 FT /note="R -> Q (in IMMAS; uncertain significance)" FT /evidence="ECO:0000269|PubMed:31736240" FT /id="VAR_083817" FT VARIANT 599 FT /note="Q -> H (in IMMAS; dbSNP:rs1567840381)" FT /evidence="ECO:0000269|PubMed:30019515" FT /id="VAR_083818" FT VARIANT 603 FT /note="F -> L (in IMMAS; dbSNP:rs1598192095)" FT /evidence="ECO:0000269|PubMed:31736240" FT /id="VAR_083819" FT VARIANT 610 FT /note="E -> V (in IMMAS; decreased trimethylation of FT 'Lys-27' of histone H3; no effect on interaction with EZH2; FT dbSNP:rs1131692177)" FT /evidence="ECO:0000269|PubMed:28229514" FT /id="VAR_078318" FT VARIANT 654..739 FT /note="Missing (in IMMAS)" FT /evidence="ECO:0000269|PubMed:31736240" FT /id="VAR_083820" FT MUTAGEN 86 FT /note="F->A: Fails to interact with JARID2; when associated FT with A-90." FT /evidence="ECO:0000269|PubMed:29499137" FT MUTAGEN 90 FT /note="F->A: Fails to interact with JARID2; when associated FT with A-86." FT /evidence="ECO:0000269|PubMed:29499137" FT MUTAGEN 195..197 FT /note="KRK->DDD: Fails to form a PRC2.1 dimer. Reduced FT H3K27me3 enrichment on PRC2 target genes." FT /evidence="ECO:0000269|PubMed:31959557" FT MUTAGEN 196 FT /note="R->A: Fails to form a PRC2.1 dimer." FT /evidence="ECO:0000269|PubMed:31959557" FT MUTAGEN 334 FT /note="W->A: Fails to interact with PHF19. The PRC2.1 dimer FT forms but is unstable." FT /evidence="ECO:0000269|PubMed:31959557" FT MUTAGEN 518 FT /note="G->W: No effect on interaction with PHF19. The FT PRC2.1 dimer forms but is unstable." FT /evidence="ECO:0000269|PubMed:31959557" FT HELIX 80..82 FT /evidence="ECO:0007829|PDB:6NQ3" FT HELIX 83..106 FT /evidence="ECO:0007829|PDB:6NQ3" FT HELIX 112..114 FT /evidence="ECO:0007829|PDB:6NQ3" FT HELIX 116..121 FT /evidence="ECO:0007829|PDB:6NQ3" FT HELIX 128..131 FT /evidence="ECO:0007829|PDB:6NQ3" FT HELIX 136..142 FT /evidence="ECO:0007829|PDB:6NQ3" FT STRAND 157..160 FT /evidence="ECO:0007829|PDB:6NQ3" FT STRAND 185..193 FT /evidence="ECO:0007829|PDB:6NQ3" FT STRAND 198..200 FT /evidence="ECO:0007829|PDB:6NQ3" FT STRAND 203..207 FT /evidence="ECO:0007829|PDB:5WAI" FT STRAND 229..232 FT /evidence="ECO:0007829|PDB:6NQ3" FT HELIX 234..236 FT /evidence="ECO:0007829|PDB:6NQ3" FT HELIX 241..243 FT /evidence="ECO:0007829|PDB:5WAI" FT STRAND 245..253 FT /evidence="ECO:0007829|PDB:6NQ3" FT STRAND 296..302 FT /evidence="ECO:0007829|PDB:5WAI" FT STRAND 312..316 FT /evidence="ECO:0007829|PDB:6NQ3" FT STRAND 354..358 FT /evidence="ECO:0007829|PDB:6NQ3" FT STRAND 370..372 FT /evidence="ECO:0007829|PDB:6NQ3" FT TURN 376..378 FT /evidence="ECO:0007829|PDB:5WAK" FT STRAND 427..434 FT /evidence="ECO:0007829|PDB:6NQ3" FT STRAND 437..441 FT /evidence="ECO:0007829|PDB:6NQ3" FT STRAND 446..449 FT /evidence="ECO:0007829|PDB:6C24" FT TURN 451..453 FT /evidence="ECO:0007829|PDB:6NQ3" FT HELIX 460..470 FT /evidence="ECO:0007829|PDB:6NQ3" FT TURN 471..473 FT /evidence="ECO:0007829|PDB:6NQ3" FT STRAND 474..481 FT /evidence="ECO:0007829|PDB:6NQ3" FT STRAND 484..491 FT /evidence="ECO:0007829|PDB:6NQ3" FT HELIX 506..508 FT /evidence="ECO:0007829|PDB:6NQ3" FT STRAND 516..518 FT /evidence="ECO:0007829|PDB:5WAI" FT STRAND 525..531 FT /evidence="ECO:0007829|PDB:6NQ3" FT HELIX 541..543 FT /evidence="ECO:0007829|PDB:5WAI" FT HELIX 544..547 FT /evidence="ECO:0007829|PDB:6C24" FT TURN 568..570 FT /evidence="ECO:0007829|PDB:5IJ7" FT HELIX 576..578 FT /evidence="ECO:0007829|PDB:5IJ7" FT HELIX 590..601 FT /evidence="ECO:0007829|PDB:5IJ7" FT STRAND 604..606 FT /evidence="ECO:0007829|PDB:5IJ7" FT HELIX 608..624 FT /evidence="ECO:0007829|PDB:5IJ7" FT HELIX 629..631 FT /evidence="ECO:0007829|PDB:5IJ7" FT HELIX 632..649 FT /evidence="ECO:0007829|PDB:5IJ7" FT HELIX 653..665 FT /evidence="ECO:0007829|PDB:5IJ7" FT HELIX 671..686 FT /evidence="ECO:0007829|PDB:5IJ7" SQ SEQUENCE 739 AA; 83055 MW; A8830EBC3FD38D56 CRC64; MAPQKHGGGG GGGSGPSAGS GGGGFGGSAA VAAATASGGK SGGGSCGGGG SYSASSSSSA AAAAGAAVLP VKKPKMEHVQ ADHELFLQAF EKPTQIYRFL RTRNLIAPIF LHRTLTYMSH RNSRTNIKRK TFKVDDMLSK VEKMKGEQES HSLSAHLQLT FTGFFHKNDK PSPNSENEQN SVTLEVLLVK VCHKKRKDVS CPIRQVPTGK KQVPLNPDLN QTKPGNFPSL AVSSNEFEPS NSHMVKSYSL LFRVTRPGRR EFNGMINGET NENIDVNEEL PARRKRNRED GEKTFVAQMT VFDKNRRLQL LDGEYEVAMQ EMEECPISKK RATWETILDG KRLPPFETFS QGPTLQFTLR WTGETNDKST APIAKPLATR NSESLHQENK PGSVKPTQTI AVKESLTTDL QTRKEKDTPN ENRQKLRIFY QFLYNNNTRQ QTEARDDLHC PWCTLNCRKL YSLLKHLKLC HSRFIFNYVY HPKGARIDVS INECYDGSYA GNPQDIHRQP GFAFSRNGPV KRTPITHILV CRPKRTKASM SEFLESEDGE VEQQRTYSSG HNRLYFHSDT CLPLRPQEME VDSEDEKDPE WLREKTITQI EEFSDVNEGE KEVMKLWNLH VMKHGFIADN QMNHACMLFV ENYGQKIIKK NLCRNFMLHL VSMHDFNLIS IMSIDKAVTK LREMQQKLEK GESASPANEE ITEEQNGTAN GFSEINSKEK ALETDSVSGV SKQSKKQKL //