SUZ12_HUMAN
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 03-AUG-2022, entry version 203.
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 ARNTL/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=25; 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 and 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="http://atlasgeneticsoncology.org/Genes/JJAZ1ID41039ch17q11.html";
CC ---------------------------------------------------------------------------
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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 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 AlphaFoldDB; Q15022; -.
DR SMR; Q15022; -.
DR BioGRID; 117059; 609.
DR CORUM; Q15022; -.
DR DIP; DIP-38524N; -.
DR IntAct; Q15022; 78.
DR MINT; Q15022; -.
DR STRING; 9606.ENSP00000316578; -.
DR BindingDB; Q15022; -.
DR ChEMBL; CHEMBL3137286; -.
DR ChEMBL; CHEMBL3137287; -.
DR ChEMBL; CHEMBL3301388; -.
DR GlyGen; Q15022; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q15022; -.
DR PhosphoSitePlus; Q15022; -.
DR BioMuta; SUZ12; -.
DR DMDM; 116242808; -.
DR EPD; Q15022; -.
DR jPOST; Q15022; -.
DR MassIVE; Q15022; -.
DR MaxQB; Q15022; -.
DR PaxDb; Q15022; -.
DR PeptideAtlas; Q15022; -.
DR PRIDE; Q15022; -.
DR ProteomicsDB; 60374; -.
DR Antibodypedia; 27067; 379 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 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; 516359at2759; -.
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; 157 hits in 1089 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 211 other tissues.
DR ExpressionAtlas; Q15022; baseline and differential.
DR Genevisible; Q15022; HS.
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:0032993; C:protein-DNA complex; IEA:Ensembl.
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: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:0003723; F:RNA 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:0009048; P:dosage compensation by inactivation of X chromosome; IEA:Ensembl.
DR GO; GO:0016574; P:histone ubiquitination; 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 InterPro; IPR019135; Polycomb_protein_VEFS-Box.
DR Pfam; PF09733; VEFS-Box; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
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; unknown pathological
FT 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 'Lys-
FT 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
