SUZ12_DROME
ID SUZ12_DROME Reviewed; 900 AA.
AC Q9NJG9; Q8T9D8; Q9VW55;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Polycomb protein Su(z)12;
DE AltName: Full=Suppressor 12 of zeste protein;
GN Name=Su(z)12; ORFNames=CG8013;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE (ISOFORM 1), CHARACTERIZATION, AND MUTANT SU(Z)12-2.
RX PubMed=11546753; DOI=10.1242/dev.128.17.3371;
RA Birve A., Sengupta A.K., Beuchle D., Larsson J., Kennison J.A.,
RA Rasmuson-Lestander A., Mueller J.;
RT "Su(z)12, a novel Drosophila Polycomb group gene that is conserved in
RT vertebrates and plants.";
RL Development 128:3371-3379(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP IDENTIFICATION IN AN ESC/E(Z) COMPLEX WITH CAF1-55; ESC; E(Z) AND HDAC1,
RP AND METHYLTRANSFERASE ACTIVITY OF THE COMPLEX.
RX PubMed=12408863; DOI=10.1016/s0092-8674(02)00975-3;
RA Czermin B., Melfi R., McCabe D., Seitz V., Imhof A., Pirrotta V.;
RT "Drosophila Enhancer of zeste/ESC complexes have a histone H3
RT methyltransferase activity that marks chromosomal Polycomb sites.";
RL Cell 111:185-196(2002).
RN [6]
RP IDENTIFICATION IN AN ESC/E(Z) COMPLEX WITH CAF1-55; ESC AND E(Z), AND
RP METHYLTRANSFERASE ACTIVITY OF THE COMPLEX.
RX PubMed=12408864; DOI=10.1016/s0092-8674(02)00976-5;
RA Mueller J., Hart C.M., Francis N.J., Vargas M.L., Sengupta A., Wild B.,
RA Miller E.L., O'Connor M.B., Kingston R.E., Simon J.A.;
RT "Histone methyltransferase activity of a Drosophila Polycomb group
RT repressor complex.";
RL Cell 111:197-208(2002).
RN [7]
RP IDENTIFICATION IN AN ESC/E(Z) COMPLEX WITH CAF1-55; ESC; E(Z); PCL AND
RP HDAC1.
RX PubMed=12697833; DOI=10.1128/mcb.23.9.3352-3362.2003;
RA Tie F., Prasad-Sinha J., Birve A., Rasmuson-Lestander A., Harte P.J.;
RT "A 1-megadalton ESC/E(Z) complex from Drosophila that contains polycomblike
RT and RPD3.";
RL Mol. Cell. Biol. 23:3352-3362(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-547, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
CC -!- FUNCTION: Polycomb group (PcG) protein. While PcG proteins are
CC generally required to maintain the transcriptionally repressive state
CC of homeotic genes throughout development, this protein is specifically
CC required during the first 6 hours of embryogenesis to establish the
CC repressed state. Component of the Esc/E(z) complex, which methylates
CC 'Lys-9' (H3K9me) and 'Lys-27' (H3K27me) of histone H3, leading to
CC transcriptional repression of the affected target gene. The Esc/E(z)
CC complex is necessary but not sufficient for the repression of homeotic
CC target genes, suggesting that the recruitment of the distinct PRC1
CC complex is also required.
CC -!- SUBUNIT: Component of the Esc/E(z) complex, composed of Caf1-55, esc,
CC E(z), Su(z)12, and possibly pho. The Esc/E(z) complex may also
CC associate with Pcl and HDAC1/Rpd3 during early embryogenesis. This
CC complex is distinct from the PRC1 complex, which contains many other
CC PcG proteins like Pc, Ph, Psc, Su(z)2. The two complexes however
CC cooperate and interact together during the first 3 hours of development
CC to establish PcG silencing. Interacts with corto in vitro.
CC {ECO:0000269|PubMed:12408863, ECO:0000269|PubMed:12408864,
CC ECO:0000269|PubMed:12697833}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=B;
CC IsoId=Q9NJG9-1; Sequence=Displayed;
CC Name=2; Synonyms=A;
CC IsoId=Q9NJG9-2; Sequence=VSP_007033, VSP_007034;
CC -!- SIMILARITY: Belongs to the VEFS (VRN2-EMF2-FIS2-SU(Z)12) family.
CC {ECO:0000305}.
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DR EMBL; AF149047; AAF73149.1; -; mRNA.
DR EMBL; AE014296; AAF49094.2; -; Genomic_DNA.
DR EMBL; AE014296; AAN11641.1; -; Genomic_DNA.
DR EMBL; AY069809; AAL39954.1; -; mRNA.
DR RefSeq; NP_652059.1; NM_143802.3. [Q9NJG9-2]
DR RefSeq; NP_730465.1; NM_168826.2. [Q9NJG9-1]
DR PDB; 2YB8; X-ray; 2.30 A; A=79-91.
DR PDBsum; 2YB8; -.
DR AlphaFoldDB; Q9NJG9; -.
DR SMR; Q9NJG9; -.
DR BioGRID; 71118; 19.
DR IntAct; Q9NJG9; 12.
DR MINT; Q9NJG9; -.
DR STRING; 7227.FBpp0074686; -.
DR iPTMnet; Q9NJG9; -.
DR PaxDb; Q9NJG9; -.
DR PRIDE; Q9NJG9; -.
DR DNASU; 48071; -.
DR EnsemblMetazoa; FBtr0074916; FBpp0074685; FBgn0020887. [Q9NJG9-2]
DR EnsemblMetazoa; FBtr0074917; FBpp0074686; FBgn0020887. [Q9NJG9-1]
DR GeneID; 48071; -.
DR KEGG; dme:Dmel_CG8013; -.
DR CTD; 48071; -.
DR FlyBase; FBgn0020887; Su(z)12.
DR VEuPathDB; VectorBase:FBgn0020887; -.
DR eggNOG; KOG2350; Eukaryota.
DR GeneTree; ENSGT00390000012364; -.
DR InParanoid; Q9NJG9; -.
DR OMA; RNEKMFG; -.
DR PhylomeDB; Q9NJG9; -.
DR Reactome; R-DME-212300; PRC2 methylates histones and DNA.
DR Reactome; R-DME-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-DME-8943724; Regulation of PTEN gene transcription.
DR SignaLink; Q9NJG9; -.
DR BioGRID-ORCS; 48071; 1 hit in 1 CRISPR screen.
DR ChiTaRS; Su(z)12; fly.
DR EvolutionaryTrace; Q9NJG9; -.
DR GenomeRNAi; 48071; -.
DR PRO; PR:Q9NJG9; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0020887; Expressed in egg cell and 22 other tissues.
DR Genevisible; Q9NJG9; DM.
DR GO; GO:0000785; C:chromatin; NAS:UniProtKB.
DR GO; GO:0035098; C:ESC/E(Z) complex; IDA:FlyBase.
DR GO; GO:0035097; C:histone methyltransferase complex; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; NAS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140718; P:facultative heterochromatin assembly; IC:FlyBase.
DR GO; GO:2001229; P:negative regulation of response to gamma radiation; IMP:FlyBase.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; NAS:UniProtKB.
DR GO; GO:0022008; P:neurogenesis; IMP:FlyBase.
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; Alternative splicing; Chromatin regulator;
KW Developmental protein; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Zinc; Zinc-finger.
FT CHAIN 1..900
FT /note="Polycomb protein Su(z)12"
FT /id="PRO_0000047059"
FT ZN_FING 411..434
FT /note="C2H2-type"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..603
FT /note="VEFS-box"
FT REGION 678..900
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..717
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 731..775
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 832..864
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 547
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT VAR_SEQ 806..855
FT /note="NTVLNKRQRYSDGSPGTGIGNGHGGGSGSGANRNKSNNHSLPATSNNASS
FT -> VEQAADAPEVLTHSDNAVDVGIIDDECGGFGAVGVMNGVASPVANNCVGN (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_007033"
FT VAR_SEQ 856..900
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_007034"
FT MUTAGEN 274
FT /note="G->D: In Su(z)12-2; induces larval lethality; when
FT homozygous."
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:2YB8"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:2YB8"
SQ SEQUENCE 900 AA; 100104 MW; 53BA0D83C49EC92F CRC64;
MAPAKKREKD SNPDGSAANG IIGLTHGAPD ASNAGSTVPP TAEGQVKLNG HQQEQELFLQ
AFEKPTQIYR YLRNRHETNP IFLNRTLSYM KERMSRNNKK RISFQVNSML ESITQKSEAV
SQNYLHVIYD SLHEKLPARL DNESGEDLLQ EQLLCEAGES VSVETTLYKI TRSKRKDSTL
DFQELLSKCS QIVYNPKDRV GEHATISIPL QTMRPMGEQH TLYKLLFRIK VLSPSTCNDE
NAETPPNKRS RPNEKMFGSE LILYEKSSGF ITEGEYEAML QPLNSTSIKS FSPKKCTWET
MPDSYIPLSL TYDVYQQSPM LKFHLTLSNE QLPEMISAPE LQRYVQHLDA VAEMNYNNNN
YNNNNNCSGL KNGSGGGNST VCKTTPEHIQ IVYNFMYSNN TRQQTEYTQE LNCPWCGLDC
LRLYALLKHL KLCHARFNFT YQPAGSGARI DVTINDAYDG SYAGSPYDLA GPSGSSFART
CGPVRRTSVT SLMVCRPRRQ KTCLDEFLEL DEDEISNQRS YITGHNRLYH HTETCLPVHP
KELDIDSEGE SDPLWLRQKT IQMIDEFSDV NEGEKELMKL WNLHVMRHGF VGDCQLPIAC
EMFLDAKGTE IVRKNLYRNF ILHMCSLFDY GLIAAETVYK TVQKLQGLLS KYAAGQELMQ
RQREEQLKYW LDVGMHKKQE DPKTLKSPQK PAPPADQAST SSASTSGSGS GSSSMQPPKR
MPAHLKRGSA ASSPGVQSKG TENGTNGSNS SSSNSKNVAK KSADQPLSTL ANTRERRSEY
GQKRNVSGSR LAATPASKRK LSSKDNTVLN KRQRYSDGSP GTGIGNGHGG GSGSGANRNK
SNNHSLPATS NNASSSSSNS KRAIARRRST SERTKASGST GGGAGGVRTR LSVPAKYERR
