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Polycomb protein SUZ12 (Chromatin precipitated E2F target 9 protein) (ChET 9 protein) (Joined to JAZF1 protein) (Suppressor of zeste 12 protein homolog)

 SUZ12_HUMAN             Reviewed;         739 AA.
Q15022; Q96BD9;
11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 3.
12-SEP-2018, entry version 179.
RecName: Full=Polycomb protein SUZ12;
AltName: Full=Chromatin precipitated E2F target 9 protein;
Short=ChET 9 protein;
AltName: Full=Joined to JAZF1 protein;
AltName: Full=Suppressor of zeste 12 protein homolog;
Name=SUZ12; Synonyms=CHET9, JJAZ1, KIAA0160;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ILE-216.
TISSUE=Bone marrow;
PubMed=8590280; DOI=10.1093/dnares/2.4.167;
Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.;
"Prediction of the coding sequences of unidentified human genes. IV.
The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by
analysis of cDNA clones from human cell line KG-1.";
DNA Res. 2:167-174(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
DISEASE, AND CHROMOSOMAL TRANSLOCATION WITH JAZF1.
PubMed=11371647; DOI=10.1073/pnas.101132598;
Koontz J.I., Soreng A.L., Nucci M., Kuo F.C., Pauwels P.,
van Den Berghe H., Cin P.D., Fletcher J.A., Sklar J.;
"Frequent fusion of the JAZF1 and JJAZ1 genes in endometrial stromal
tumors.";
Proc. Natl. Acad. Sci. U.S.A. 98:6348-6353(2001).
[4]
INDUCTION.
PubMed=11564866; DOI=10.1128/MCB.21.20.6820-6832.2001;
Weinmann A.S., Bartley S.M., Zhang T., Zhang M.Q., Farnham P.J.;
"Use of chromatin immunoprecipitation to clone novel E2F target
promoters.";
Mol. Cell. Biol. 21:6820-6832(2001).
[5]
IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE PRC2
COMPLEX WITH EED; EZH2; RBBP4 AND RBBP7, AND METHYLTRANSFERASE
ACTIVITY OF THE PRC2 COMPLEX.
PubMed=12435631; DOI=10.1101/gad.1035902;
Kuzmichev A., Nishioka K., Erdjument-Bromage H., Tempst P.,
Reinberg D.;
"Histone methyltransferase activity associated with a human
multiprotein complex containing the Enhancer of Zeste protein.";
Genes Dev. 16:2893-2905(2002).
[6]
IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE PRC2
COMPLEX WITH EED; EZH2; RBBP4 AND RBBP7, AND METHYLTRANSFERASE
ACTIVITY OF THE PRC2 COMPLEX.
PubMed=12351676; DOI=10.1126/science.1076997;
Cao R., Wang L., Wang H., Xia L., Erdjument-Bromage H., Tempst P.,
Jones R.S., Zhang Y.;
"Role of histone H3 lysine 27 methylation in Polycomb-group
silencing.";
Science 298:1039-1043(2002).
[7]
INDUCTION.
PubMed=14532106; DOI=10.1093/emboj/cdg542;
Bracken A.P., Pasini D., Capra M., Prosperini E., Colli E., Helin K.;
"EZH2 is downstream of the pRB-E2F pathway, essential for
proliferation and amplified in cancer.";
EMBO J. 22:5323-5335(2003).
[8]
FUNCTION, INTERACTION WITH EZH2, METHYLTRANSFERASE ACTIVITY OF THE
PRC2 COMPLEX, AND DEVELOPMENTAL STAGE.
PubMed=15385962; DOI=10.1038/sj.emboj.7600402;
Pasini D., Bracken A.P., Jensen M.R., Lazzerini Denchi E., Helin K.;
"Suz12 is essential for mouse development and for EZH2 histone
methyltransferase activity.";
EMBO J. 23:4061-4071(2004).
[9]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=15231737; DOI=10.1101/gad.1200204;
Kirmizis A., Bartley S.M., Kuzmichev A., Margueron R., Reinberg D.,
Green R., Farnham P.J.;
"Silencing of human polycomb target genes is associated with
methylation of histone H3 Lys 27.";
Genes Dev. 18:1592-1605(2004).
[10]
CHARACTERIZATION OF THE PRC2 AND PRC3 COMPLEXES INCLUDING EED; EZH2;
RBBP4; RBBP7 AND SUZ12, AND METHYLTRANSFERASE ACTIVITY OF THE PRC2 AND
PRC3 COMPLEXES.
PubMed=15099518; DOI=10.1016/S1097-2765(04)00185-6;
Kuzmichev A., Jenuwein T., Tempst P., Reinberg D.;
"Different EZH2-containing complexes target methylation of histone H1
or nucleosomal histone H3.";
Mol. Cell 14:183-193(2004).
[11]
FUNCTION, CHARACTERIZATION OF THE PRC2 COMPLEX INCLUDING AEBP2; EED;
EZH2; RBBP4 AND SUZ12, AND METHYLTRANSFERASE ACTIVITY OF THE PRC2
COMPLEX.
PubMed=15225548; DOI=10.1016/j.molcel.2004.06.020;
Cao R., Zhang Y.;
"SUZ12 is required for both the histone methyltransferase activity and
the silencing function of the EED-EZH2 complex.";
Mol. Cell 15:57-67(2004).
[12]
CHARACTERIZATION OF THE PRC4 COMPLEX INCLUDING EED; EZH2; RBBP4;
RBBP7; SUZ12 AND SIRT1, METHYLTRANSFERASE ACTIVITY OF THE PRC4
COMPLEX, AND TISSUE SPECIFICITY.
PubMed=15684044; DOI=10.1073/pnas.0409875102;
Kuzmichev A., Margueron R., Vaquero A., Preissner T.S., Scher M.,
Kirmizis A., Ouyang X., Brockdorff N., Abate-Shen C., Farnham P.J.,
Reinberg D.;
"Composition and histone substrates of polycomb repressive group
complexes change during cellular differentiation.";
Proc. Natl. Acad. Sci. U.S.A. 102:1859-1864(2005).
[13]
INTERACTION WITH EZH2.
PubMed=16224021; DOI=10.1126/science.1118947;
Cha T.-L., Zhou B.P., Xia W., Wu Y., Yang C.-C., Chen C.-T., Ping B.,
Otte A.P., Hung M.-C.;
"Akt-mediated phosphorylation of EZH2 suppresses methylation of lysine
27 in histone H3.";
Science 310:306-310(2005).
[14]
INTERACTION WITH WDR77.
PubMed=16712789; DOI=10.1016/j.bbrc.2006.05.014;
Furuno K., Masatsugu T., Sonoda M., Sasazuki T., Yamamoto K.;
"Association of Polycomb group SUZ12 with WD-repeat protein MEP50 that
binds to histone H2A selectively in vitro.";
Biochem. Biophys. Res. Commun. 345:1051-1058(2006).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-546, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[16]
FUNCTION.
PubMed=16618801; DOI=10.1101/gad.381706;
Bracken A.P., Dietrich N., Pasini D., Hansen K.H., Helin K.;
"Genome-wide mapping of Polycomb target genes unravels their roles in
cell fate transitions.";
Genes Dev. 20:1123-1136(2006).
[17]
METHYLTRANSFERASE ACTIVITY OF THE PRC2 COMPLEX, AND INTERACTION WITH
HISTONE H1.
PubMed=16431907; DOI=10.1074/jbc.M513425200;
Martin C., Cao R., Zhang Y.;
"Substrate preferences of the EZH2 histone methyltransferase
complex.";
J. Biol. Chem. 281:8365-8370(2006).
[18]
FUNCTION.
PubMed=17344414; DOI=10.1101/gad.415507;
Bracken A.P., Kleine-Kohlbrecher D., Dietrich N., Pasini D.,
Gargiulo G., Beekman C., Theilgaard-Moench K., Minucci S., Porse B.T.,
Marine J.-C., Hansen K.H., Helin K.;
"The Polycomb group proteins bind throughout the INK4A-ARF locus and
are disassociated in senescent cells.";
Genes Dev. 21:525-530(2007).
[19]
DE NOVO DNA METHYLATION OF PRC2 TARGET GENES.
PubMed=17200670; DOI=10.1038/ng1950;
Schlesinger Y., Straussman R., Keshet I., Farkash S., Hecht M.,
Zimmerman J., Eden E., Yakhini Z., Ben-Shushan E., Reubinoff B.E.,
Bergman Y., Simon I., Cedar H.;
"Polycomb-mediated methylation on Lys27 of histone H3 pre-marks genes
for de novo methylation in cancer.";
Nat. Genet. 39:232-236(2007).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-546 AND SER-583, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[21]
IDENTIFICATION IN THE PRC2/EED-EZH1 COMPLEX.
PubMed=19026781; DOI=10.1016/j.molcel.2008.11.004;
Margueron R., Li G., Sarma K., Blais A., Zavadil J., Woodcock C.L.,
Dynlacht B.D., Reinberg D.;
"Ezh1 and Ezh2 maintain repressive chromatin through different
mechanisms.";
Mol. Cell 32:503-518(2008).
[22]
IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE PRC2
COMPLEX, AND METHYLTRANSFERASE ACTIVITY OF THE PRC2 COMPLEX.
PubMed=18086877; DOI=10.1128/MCB.01589-07;
Cao R., Wang H., He J., Erdjument-Bromage H., Tempst P., Zhang Y.;
"Role of hPHF1 in H3K27 methylation and Hox gene silencing.";
Mol. Cell. Biol. 28:1862-1872(2008).
[23]
FUNCTION, INTERACTION WITH EED AND EZH2, INTERACTION OF THE PRC2
COMPLEX WITH PHF1, AND METHYLTRANSFERASE ACTIVITY OF THE PRC2 COMPLEX.
PubMed=18285464; DOI=10.1128/MCB.02017-07;
Sarma K., Margueron R., Ivanov A., Pirrotta V., Reinberg D.;
"Ezh2 requires PHF1 to efficiently catalyze H3 lysine 27
trimethylation in vivo.";
Mol. Cell. Biol. 28:2718-2731(2008).
[24]
SUMOYLATION AT LYS-72; LYS-73 AND LYS-75.
PubMed=18628979; DOI=10.1371/journal.pone.0002704;
Riising E.M., Boggio R., Chiocca S., Helin K., Pasini D.;
"The polycomb repressive complex 2 is a potential target of SUMO
modifications.";
PLoS ONE 3:E2704-E2704(2008).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-546, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[26]
TRANS-SPLICING.
PubMed=18772439; DOI=10.1126/science.1156725;
Li H., Wang J., Mor G., Sklar J.;
"A neoplastic gene fusion mimics trans-splicing of RNAs in normal
human cells.";
Science 321:1357-1361(2008).
[27]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-546, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-546, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[30]
INTERACTION WITH CDYL.
PubMed=22009739; DOI=10.1074/jbc.M111.271064;
Zhang Y., Yang X., Gui B., Xie G., Zhang D., Shang Y., Liang J.;
"Corepressor protein CDYL functions as a molecular bridge between
polycomb repressor complex 2 and repressive chromatin mark
trimethylated histone lysine 27.";
J. Biol. Chem. 286:42414-42425(2011).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-546, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-541; SER-546 AND
SER-726, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[33]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[34]
INVOLVEMENT IN DISEASE, VARIANT VAL-610, CHARACTERIZATION OF VARIANT
VAL-610, AND FUNCTION.
PubMed=28229514; DOI=10.1002/humu.23200;
Imagawa E., Higashimoto K., Sakai Y., Numakura C., Okamoto N.,
Matsunaga S., Ryo A., Sato Y., Sanefuji M., Ihara K., Takada Y.,
Nishimura G., Saitsu H., Mizuguchi T., Miyatake S., Nakashima M.,
Miyake N., Soejima H., Matsumoto N.;
"Mutations in genes encoding polycomb repressive complex 2 subunits
cause Weaver syndrome.";
Hum. Mutat. 38:637-648(2017).
[35]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-75; LYS-223 AND LYS-390, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: Polycomb group (PcG) protein. Component of the PRC2/EED-
EZH2 complex, which methylates 'Lys-9' (H3K9me) and 'Lys-27'
(H3K27me) of histone H3, leading to transcriptional repression of
the affected target gene. The PRC2/EED-EZH2 complex may also serve
as a recruiting platform for DNA methyltransferases, thereby
linking two epigenetic repression systems. Genes repressed by the
PRC2/EED-EZH2 complex include HOXC8, HOXA9, MYT1 and CDKN2A.
{ECO:0000269|PubMed:15225548, ECO:0000269|PubMed:15231737,
ECO:0000269|PubMed:15385962, ECO:0000269|PubMed:16618801,
ECO:0000269|PubMed:17344414, ECO:0000269|PubMed:18285464,
ECO:0000269|PubMed:28229514}.
-!- SUBUNIT: Component of the PRC2/EED-EZH2 complex, which includes
EED, EZH2, SUZ12, RBBP4 and RBBP7 and possibly AEBP2. The minimum
components required for methyltransferase activity of the
PRC2/EED-EZH2 complex are EED, EZH2 and SUZ12. Component of the
PRC2/EED-EZH1 complex, which includes EED, EZH1, SUZ12, RBBP4 and
AEBP2. The PRC2 complex may also interact with DNMT1, DNMT3A,
DNMT3B and PHF1 via the EZH2 subunit and with SIRT1 via the SUZ12
subunit. Interacts with WDR77. Interacts with histone H1.
Interacts with CDYL. Interacts with ARNTL/BMAL1.
{ECO:0000269|PubMed:12351676, ECO:0000269|PubMed:12435631,
ECO:0000269|PubMed:15385962, ECO:0000269|PubMed:16224021,
ECO:0000269|PubMed:16431907, ECO:0000269|PubMed:16712789,
ECO:0000269|PubMed:18086877, ECO:0000269|PubMed:18285464,
ECO:0000269|PubMed:19026781, ECO:0000269|PubMed:22009739}.
-!- INTERACTION:
O75530:EED; NbExp=8; IntAct=EBI-1264675, EBI-923794;
Q15910:EZH2; NbExp=22; IntAct=EBI-1264675, EBI-530054;
O15379:HDAC3; NbExp=7; IntAct=EBI-1264675, EBI-607682;
Q14774:HLX; NbExp=2; IntAct=EBI-1264675, EBI-6678255;
Q92833-1:JARID2; NbExp=7; IntAct=EBI-1264675, EBI-15825247;
Q15156:PML-RAR; NbExp=6; IntAct=EBI-1264675, EBI-867256;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15231737}.
-!- TISSUE SPECIFICITY: Overexpressed in breast and colon cancer.
{ECO:0000269|PubMed:15231737, ECO:0000269|PubMed:15684044}.
-!- DEVELOPMENTAL STAGE: Expressed at low levels in quiescent cells.
Expression rises at the G1/S phase transition.
{ECO:0000269|PubMed:15385962}.
-!- INDUCTION: Expression is induced by E2F1, E2F2 and E2F3.
{ECO:0000269|PubMed:11564866, ECO:0000269|PubMed:14532106}.
-!- PTM: Sumoylated, probably by PIAS2. {ECO:0000269|PubMed:18628979}.
-!- DISEASE: Note=A chromosomal aberration involving SUZ12 may be a
cause of endometrial stromal tumors. Translocation
t(7;17)(p15;q21) with JAZF1. The translocation generates the
JAZF1-SUZ12 oncogene consisting of the N-terminus part of JAZF1
and the C-terminus part of SUZ12. It is frequently found in all
cases of endometrial stromal tumors, except in endometrial stromal
sarcomas, where it is rarer. {ECO:0000269|PubMed:11371647}.
-!- DISEASE: Note=Defects in EED are associated with Weaver syndrome
(WVS): A syndrome of accelerated growth and osseous maturation,
unusual craniofacial appearance, hoarse and low-pitched cry, and
hypertonia with camptodactyly. Distinguishing features of Weaver
syndrome include broad forehead and face, ocular hypertelorism,
prominent wide philtrum, micrognathia, deep horizontal chin
groove, and deep-set nails. In addition, carpal bone development
is advanced over the rest of the hand.
{ECO:0000269|PubMed:28229514}.
-!- MISCELLANEOUS: Under hypoxic conditions, the precursor SUZ12 RNA
undergoes regulated trans-splicing with the JAZF1 RNA, resulting
in a chimeric isoform which may be protective against apoptosis.
The chimeric transcript is characterized by JAZF1 exons 1-3 joined
to SUZ12 exon 2-16. The chimeric transcript is expressed primarily
in the endometrium from late secretory and early proliferative
phases of the menstrual cycle, but not in normal myometrium at any
phase of the cycle. Its expression is slightly induced by low
levels of progesterone, but suppressed by both estrogen and high
levels of progesterone (PubMed:18772439).
{ECO:0000305|PubMed:18772439}.
-!- SIMILARITY: Belongs to the VEFS (VRN2-EMF2-FIS2-SU(Z)12) family.
{ECO:0000305}.
-!- CAUTION: Two variants of the PRC2 complex have been described,
termed PRC3 and PRC4. Each of the three complexes may include a
different complement of EED isoforms, although the precise
sequences of the isoforms in each complex have not been
determined. The PRC2 and PRC4 complexes may also methylate 'Lys-
26' of histone H1 in addition to 'Lys-27' of histone H3
(PubMed:15099518 and PubMed:15684044), although other studies have
demonstrated no methylation of 'Lys-26' of histone H1 by PRC2
(PubMed:16431907). {ECO:0000305|PubMed:16431907}.
-!- SEQUENCE CAUTION:
Sequence=BAA09931.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/JJAZ1ID41039ch17q11.html";
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EMBL; D63881; BAA09931.2; ALT_INIT; mRNA.
EMBL; BC015704; AAH15704.1; -; mRNA.
CCDS; CCDS11270.1; -.
RefSeq; NP_056170.2; NM_015355.3.
UniGene; Hs.462732; -.
PDB; 4W2R; X-ray; 2.81 A; S/T=545-725.
PDB; 5HYN; X-ray; 2.95 A; C/H/M/S=558-685.
PDB; 5IJ7; X-ray; 2.62 A; S/T=545-725.
PDB; 5IJ8; X-ray; 2.99 A; S/T=545-725.
PDB; 5LS6; X-ray; 3.47 A; C/F/I/L=558-685.
PDB; 5WAI; X-ray; 2.90 A; B/F=76-545.
PDB; 5WAK; X-ray; 3.20 A; B=76-545.
PDB; 5WG6; X-ray; 3.90 A; A/C=543-695.
PDB; 6B3W; X-ray; 3.05 A; S/T=545-725.
PDB; 6C23; EM; 3.90 A; A/M/Q=1-739.
PDB; 6C24; EM; 3.50 A; A/M/Q=1-739.
PDBsum; 4W2R; -.
PDBsum; 5HYN; -.
PDBsum; 5IJ7; -.
PDBsum; 5IJ8; -.
PDBsum; 5LS6; -.
PDBsum; 5WAI; -.
PDBsum; 5WAK; -.
PDBsum; 5WG6; -.
PDBsum; 6B3W; -.
PDBsum; 6C23; -.
PDBsum; 6C24; -.
ProteinModelPortal; Q15022; -.
SMR; Q15022; -.
BioGrid; 117059; 351.
CORUM; Q15022; -.
DIP; DIP-38524N; -.
IntAct; Q15022; 39.
MINT; Q15022; -.
STRING; 9606.ENSP00000316578; -.
BindingDB; Q15022; -.
ChEMBL; CHEMBL3137287; -.
iPTMnet; Q15022; -.
PhosphoSitePlus; Q15022; -.
BioMuta; SUZ12; -.
DMDM; 116242808; -.
EPD; Q15022; -.
MaxQB; Q15022; -.
PaxDb; Q15022; -.
PeptideAtlas; Q15022; -.
PRIDE; Q15022; -.
ProteomicsDB; 60374; -.
Ensembl; ENST00000322652; ENSP00000316578; ENSG00000178691.
GeneID; 23512; -.
KEGG; hsa:23512; -.
UCSC; uc002hgs.3; human.
CTD; 23512; -.
DisGeNET; 23512; -.
EuPathDB; HostDB:ENSG00000178691.10; -.
GeneCards; SUZ12; -.
HGNC; HGNC:17101; SUZ12.
HPA; HPA057436; -.
MalaCards; SUZ12; -.
MIM; 606245; gene.
neXtProt; NX_Q15022; -.
OpenTargets; ENSG00000178691; -.
PharmGKB; PA134936035; -.
eggNOG; KOG2350; Eukaryota.
eggNOG; ENOG410YJ29; LUCA.
GeneTree; ENSGT00390000012364; -.
HOGENOM; HOG000047340; -.
HOVERGEN; HBG039522; -.
InParanoid; Q15022; -.
KO; K11463; -.
OMA; AMQEMEE; -.
OrthoDB; EOG091G012Q; -.
PhylomeDB; Q15022; -.
TreeFam; TF323249; -.
Reactome; R-HSA-212300; PRC2 methylates histones and DNA.
Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
Reactome; R-HSA-4551638; SUMOylation of chromatin organization proteins.
Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
Reactome; R-HSA-8943724; Regulation of PTEN gene transcription.
Reactome; R-HSA-8953750; Transcriptional Regulation by E2F6.
SignaLink; Q15022; -.
SIGNOR; Q15022; -.
ChiTaRS; SUZ12; human.
GeneWiki; SUZ12; -.
GenomeRNAi; 23512; -.
PRO; PR:Q15022; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000178691; Expressed in 236 organ(s), highest expression level in female gonad.
CleanEx; HS_SUZ12; -.
ExpressionAtlas; Q15022; baseline and differential.
Genevisible; Q15022; HS.
GO; GO:0035098; C:ESC/E(Z) complex; IDA:UniProtKB.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0032993; C:protein-DNA complex; IEA:Ensembl.
GO; GO:0016586; C:RSC-type complex; IBA:GO_Central.
GO; GO:0001739; C:sex chromatin; IEA:Ensembl.
GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
GO; GO:0042054; F:histone methyltransferase activity; IMP:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
GO; GO:1990841; F:promoter-specific chromatin binding; IEA:Ensembl.
GO; GO:0003723; F:RNA binding; IEA:Ensembl.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0070734; P:histone H3-K27 methylation; IEA:GOC.
GO; GO:0016574; P:histone ubiquitination; IEA:Ensembl.
GO; GO:0045596; P:negative regulation of cell differentiation; IMP:UniProtKB.
GO; GO:0070317; P:negative regulation of G0 to G1 transition; TAS:Reactome.
GO; GO:0045814; P:negative regulation of gene expression, epigenetic; TAS:Reactome.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR019135; Polycomb_protein_VEFS-Box.
Pfam; PF09733; VEFS-Box; 1.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
1: Evidence at protein level;
3D-structure; Chromatin regulator; Chromosomal rearrangement;
Complete proteome; Isopeptide bond; Metal-binding; Nucleus;
Phosphoprotein; Polymorphism; Proto-oncogene; Reference proteome;
Repressor; Transcription; Transcription regulation; Ubl conjugation;
Zinc; Zinc-finger.
CHAIN 1 739 Polycomb protein SUZ12.
/FTId=PRO_0000047057.
ZN_FING 448 471 C2H2-type.
REGION 563 639 VEFS-box.
COMPBIAS 7 50 Gly-rich.
COMPBIAS 51 59 Poly-Ser.
COMPBIAS 60 67 Poly-Ala.
SITE 93 94 Breakpoint for translocation to form
JAZF1-SUZ12 oncogene.
MOD_RES 20 20 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 541 541 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 546 546 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 583 583 Phosphoserine.
{ECO:0000244|PubMed:18220336}.
MOD_RES 726 726 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 72 72 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:18628979}.
CROSSLNK 73 73 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:18628979}.
CROSSLNK 75 75 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000269|PubMed:18628979}.
CROSSLNK 75 75 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 223 223 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 390 390 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VARIANT 216 216 N -> I (in dbSNP:rs17339444).
{ECO:0000269|PubMed:8590280}.
/FTId=VAR_028100.
VARIANT 610 610 E -> V (found in a patient with Weaver
syndrome; decreased trimethylation of
'Lys-27' of histone H3; no effect on
interaction with EZH2;
dbSNP:rs1131692177).
{ECO:0000269|PubMed:28229514}.
/FTId=VAR_078318.
HELIX 80 106 {ECO:0000244|PDB:5WAI}.
HELIX 112 114 {ECO:0000244|PDB:5WAI}.
HELIX 116 121 {ECO:0000244|PDB:5WAI}.
HELIX 128 131 {ECO:0000244|PDB:5WAI}.
HELIX 134 136 {ECO:0000244|PDB:5WAI}.
HELIX 137 146 {ECO:0000244|PDB:5WAI}.
STRAND 156 165 {ECO:0000244|PDB:5WAI}.
STRAND 185 192 {ECO:0000244|PDB:5WAI}.
STRAND 203 207 {ECO:0000244|PDB:5WAI}.
STRAND 229 233 {ECO:0000244|PDB:5WAI}.
HELIX 241 243 {ECO:0000244|PDB:5WAI}.
STRAND 245 254 {ECO:0000244|PDB:5WAI}.
STRAND 296 302 {ECO:0000244|PDB:5WAI}.
STRAND 312 318 {ECO:0000244|PDB:5WAI}.
STRAND 354 362 {ECO:0000244|PDB:5WAI}.
STRAND 370 372 {ECO:0000244|PDB:5WAK}.
TURN 376 378 {ECO:0000244|PDB:5WAK}.
STRAND 427 434 {ECO:0000244|PDB:5WAI}.
STRAND 437 443 {ECO:0000244|PDB:5WAI}.
STRAND 446 449 {ECO:0000244|PDB:6C24}.
TURN 451 453 {ECO:0000244|PDB:5WAI}.
HELIX 460 470 {ECO:0000244|PDB:5WAI}.
TURN 471 473 {ECO:0000244|PDB:5WAI}.
STRAND 474 481 {ECO:0000244|PDB:5WAI}.
STRAND 484 491 {ECO:0000244|PDB:5WAI}.
TURN 503 506 {ECO:0000244|PDB:6C24}.
STRAND 507 509 {ECO:0000244|PDB:6C24}.
STRAND 516 518 {ECO:0000244|PDB:5WAI}.
STRAND 525 531 {ECO:0000244|PDB:5WAI}.
HELIX 541 543 {ECO:0000244|PDB:5WAI}.
HELIX 544 547 {ECO:0000244|PDB:6C24}.
TURN 568 570 {ECO:0000244|PDB:5IJ7}.
HELIX 576 578 {ECO:0000244|PDB:5IJ7}.
HELIX 590 601 {ECO:0000244|PDB:5IJ7}.
STRAND 604 606 {ECO:0000244|PDB:5IJ7}.
HELIX 608 624 {ECO:0000244|PDB:5IJ7}.
HELIX 629 631 {ECO:0000244|PDB:5IJ7}.
HELIX 632 649 {ECO:0000244|PDB:5IJ7}.
HELIX 653 665 {ECO:0000244|PDB:5IJ7}.
HELIX 671 686 {ECO:0000244|PDB:5IJ7}.
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


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