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Q15022

- SUZ12_HUMAN

UniProt

Q15022 - SUZ12_HUMAN

Protein

Polycomb protein SUZ12

Gene

SUZ12

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 3 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    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.6 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei93 – 942Breakpoint for translocation to form JAZF1-SUZ12 oncogene

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri448 – 47124C2H2-typeAdd
    BLAST

    GO - Molecular functioni

    1. chromatin binding Source: Ensembl
    2. histone methyltransferase activity Source: MGI
    3. metal ion binding Source: UniProtKB-KW
    4. methylated histone binding Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. sequence-specific DNA binding Source: Ensembl

    GO - Biological processi

    1. histone ubiquitination Source: Ensembl
    2. negative regulation of cell differentiation Source: UniProtKB
    3. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
    4. positive regulation of cell proliferation Source: Ensembl
    5. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_169436. Oxidative Stress Induced Senescence.
    REACT_200808. PRC2 methylates histones and DNA.
    SignaLinkiQ15022.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Polycomb protein SUZ12
    Alternative name(s):
    Chromatin precipitated E2F target 9 protein
    Short name:
    ChET 9 protein
    Joined to JAZF1 protein
    Suppressor of zeste 12 protein homolog
    Gene namesi
    Name:SUZ12
    Synonyms:CHET9, JJAZ1, KIAA0160
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:17101. SUZ12.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. ESC/E(Z) complex Source: UniProtKB
    2. nucleoplasm Source: Reactome
    3. nucleus Source: UniProt
    4. sex chromatin Source: Ensembl

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    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.1 Publication

    Keywords - Diseasei

    Proto-oncogene

    Organism-specific databases

    Orphaneti97685. 17q11 microdeletion syndrome.
    PharmGKBiPA134936035.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 739739Polycomb protein SUZ12PRO_0000047057Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki72 – 72Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Cross-linki73 – 73Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Cross-linki75 – 75Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei546 – 5461Phosphoserine6 Publications
    Modified residuei583 – 5831Phosphoserine1 Publication

    Post-translational modificationi

    Sumoylated, probably by PIAS2.1 Publication

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ15022.
    PaxDbiQ15022.
    PRIDEiQ15022.

    Expressioni

    Tissue specificityi

    Overexpressed in breast and colon cancer.2 Publications

    Developmental stagei

    Expressed at low levels in quiescent cells. Expression rises at the G1/S phase transition.1 Publication

    Inductioni

    Expression is induced by E2F1, E2F2 and E2F3.2 Publications

    Gene expression databases

    ArrayExpressiQ15022.
    BgeeiQ15022.
    CleanExiHS_SUZ12.
    GenevestigatoriQ15022.

    Organism-specific databases

    HPAiHPA057436.

    Interactioni

    Subunit structurei

    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/BMAL1.10 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HDAC3O153797EBI-1264675,EBI-607682
    HLXQ147742EBI-1264675,EBI-6678255
    PML-RARQ151566EBI-1264675,EBI-867256

    Protein-protein interaction databases

    BioGridi117059. 331 interactions.
    DIPiDIP-38524N.
    IntActiQ15022. 25 interactions.
    STRINGi9606.ENSP00000316578.

    Structurei

    3D structure databases

    ProteinModelPortaliQ15022.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni563 – 63977VEFS-boxAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi7 – 5044Gly-richAdd
    BLAST
    Compositional biasi51 – 599Poly-Ser
    Compositional biasi60 – 678Poly-Ala

    Sequence similaritiesi

    Contains 1 C2H2-type zinc finger.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri448 – 47124C2H2-typeAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG313866.
    HOGENOMiHOG000047340.
    HOVERGENiHBG039522.
    InParanoidiQ15022.
    KOiK11463.
    OMAiPKMEQIQ.
    PhylomeDBiQ15022.
    TreeFamiTF323249.

    Family and domain databases

    InterProiIPR019135. Polycomb_protein_VEFS-Box.
    IPR015880. Znf_C2H2-like.
    [Graphical view]
    PfamiPF09733. VEFS-Box. 1 hit.
    [Graphical view]
    SMARTiSM00355. ZnF_C2H2. 1 hit.
    [Graphical view]
    PROSITEiPS00028. ZINC_FINGER_C2H2_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q15022-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAPQKHGGGG GGGSGPSAGS GGGGFGGSAA VAAATASGGK SGGGSCGGGG    50
    SYSASSSSSA AAAAGAAVLP VKKPKMEHVQ ADHELFLQAF EKPTQIYRFL 100
    RTRNLIAPIF LHRTLTYMSH RNSRTNIKRK TFKVDDMLSK VEKMKGEQES 150
    HSLSAHLQLT FTGFFHKNDK PSPNSENEQN SVTLEVLLVK VCHKKRKDVS 200
    CPIRQVPTGK KQVPLNPDLN QTKPGNFPSL AVSSNEFEPS NSHMVKSYSL 250
    LFRVTRPGRR EFNGMINGET NENIDVNEEL PARRKRNRED GEKTFVAQMT 300
    VFDKNRRLQL LDGEYEVAMQ EMEECPISKK RATWETILDG KRLPPFETFS 350
    QGPTLQFTLR WTGETNDKST APIAKPLATR NSESLHQENK PGSVKPTQTI 400
    AVKESLTTDL QTRKEKDTPN ENRQKLRIFY QFLYNNNTRQ QTEARDDLHC 450
    PWCTLNCRKL YSLLKHLKLC HSRFIFNYVY HPKGARIDVS INECYDGSYA 500
    GNPQDIHRQP GFAFSRNGPV KRTPITHILV CRPKRTKASM SEFLESEDGE 550
    VEQQRTYSSG HNRLYFHSDT CLPLRPQEME VDSEDEKDPE WLREKTITQI 600
    EEFSDVNEGE KEVMKLWNLH VMKHGFIADN QMNHACMLFV ENYGQKIIKK 650
    NLCRNFMLHL VSMHDFNLIS IMSIDKAVTK LREMQQKLEK GESASPANEE 700
    ITEEQNGTAN GFSEINSKEK ALETDSVSGV SKQSKKQKL 739
    Length:739
    Mass (Da):83,055
    Last modified:October 17, 2006 - v3
    Checksum:iA8830EBC3FD38D56
    GO

    Sequence cautioni

    The sequence BAA09931.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti216 – 2161N → I.1 Publication
    Corresponds to variant rs17339444 [ dbSNP | Ensembl ].
    VAR_028100

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D63881 mRNA. Translation: BAA09931.2. Different initiation.
    BC015704 mRNA. Translation: AAH15704.1.
    CCDSiCCDS11270.1.
    RefSeqiNP_056170.2. NM_015355.2.
    UniGeneiHs.462732.

    Genome annotation databases

    EnsembliENST00000322652; ENSP00000316578; ENSG00000178691.
    GeneIDi23512.
    KEGGihsa:23512.
    UCSCiuc002hgs.2. human.

    Polymorphism databases

    DMDMi116242808.

    Keywords - Coding sequence diversityi

    Chromosomal rearrangement, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D63881 mRNA. Translation: BAA09931.2 . Different initiation.
    BC015704 mRNA. Translation: AAH15704.1 .
    CCDSi CCDS11270.1.
    RefSeqi NP_056170.2. NM_015355.2.
    UniGenei Hs.462732.

    3D structure databases

    ProteinModelPortali Q15022.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117059. 331 interactions.
    DIPi DIP-38524N.
    IntActi Q15022. 25 interactions.
    STRINGi 9606.ENSP00000316578.

    Polymorphism databases

    DMDMi 116242808.

    Proteomic databases

    MaxQBi Q15022.
    PaxDbi Q15022.
    PRIDEi Q15022.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000322652 ; ENSP00000316578 ; ENSG00000178691 .
    GeneIDi 23512.
    KEGGi hsa:23512.
    UCSCi uc002hgs.2. human.

    Organism-specific databases

    CTDi 23512.
    GeneCardsi GC17P030264.
    HGNCi HGNC:17101. SUZ12.
    HPAi HPA057436.
    MIMi 606245. gene.
    neXtProti NX_Q15022.
    Orphaneti 97685. 17q11 microdeletion syndrome.
    PharmGKBi PA134936035.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG313866.
    HOGENOMi HOG000047340.
    HOVERGENi HBG039522.
    InParanoidi Q15022.
    KOi K11463.
    OMAi PKMEQIQ.
    PhylomeDBi Q15022.
    TreeFami TF323249.

    Enzyme and pathway databases

    Reactomei REACT_169436. Oxidative Stress Induced Senescence.
    REACT_200808. PRC2 methylates histones and DNA.
    SignaLinki Q15022.

    Miscellaneous databases

    GeneWikii SUZ12.
    GenomeRNAii 23512.
    NextBioi 45931.
    PROi Q15022.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15022.
    Bgeei Q15022.
    CleanExi HS_SUZ12.
    Genevestigatori Q15022.

    Family and domain databases

    InterProi IPR019135. Polycomb_protein_VEFS-Box.
    IPR015880. Znf_C2H2-like.
    [Graphical view ]
    Pfami PF09733. VEFS-Box. 1 hit.
    [Graphical view ]
    SMARTi SM00355. ZnF_C2H2. 1 hit.
    [Graphical view ]
    PROSITEi PS00028. ZINC_FINGER_C2H2_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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."
      Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.
      DNA Res. 2:167-174(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ILE-216.
      Tissue: Bone marrow.
    2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Uterus.
    3. Cited for: DISEASE, CHROMOSOMAL TRANSLOCATION WITH JAZF1.
    4. "Use of chromatin immunoprecipitation to clone novel E2F target promoters."
      Weinmann A.S., Bartley S.M., Zhang T., Zhang M.Q., Farnham P.J.
      Mol. Cell. Biol. 21:6820-6832(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    5. "Histone methyltransferase activity associated with a human multiprotein complex containing the Enhancer of Zeste protein."
      Kuzmichev A., Nishioka K., Erdjument-Bromage H., Tempst P., Reinberg D.
      Genes Dev. 16:2893-2905(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE PRC2 COMPLEX WITH EED; EZH2; RBBP4 AND RBBP7, METHYLTRANSFERASE ACTIVITY OF THE PRC2 COMPLEX.
    6. "Role of histone H3 lysine 27 methylation in Polycomb-group silencing."
      Cao R., Wang L., Wang H., Xia L., Erdjument-Bromage H., Tempst P., Jones R.S., Zhang Y.
      Science 298:1039-1043(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE PRC2 COMPLEX WITH EED; EZH2; RBBP4 AND RBBP7, METHYLTRANSFERASE ACTIVITY OF THE PRC2 COMPLEX.
    7. "EZH2 is downstream of the pRB-E2F pathway, essential for proliferation and amplified in cancer."
      Bracken A.P., Pasini D., Capra M., Prosperini E., Colli E., Helin K.
      EMBO J. 22:5323-5335(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    8. "Suz12 is essential for mouse development and for EZH2 histone methyltransferase activity."
      Pasini D., Bracken A.P., Jensen M.R., Lazzerini Denchi E., Helin K.
      EMBO J. 23:4061-4071(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH EZH2, METHYLTRANSFERASE ACTIVITY OF THE PRC2 COMPLEX, DEVELOPMENTAL STAGE.
    9. "Silencing of human polycomb target genes is associated with methylation of histone H3 Lys 27."
      Kirmizis A., Bartley S.M., Kuzmichev A., Margueron R., Reinberg D., Green R., Farnham P.J.
      Genes Dev. 18:1592-1605(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    10. "Different EZH2-containing complexes target methylation of histone H1 or nucleosomal histone H3."
      Kuzmichev A., Jenuwein T., Tempst P., Reinberg D.
      Mol. Cell 14:183-193(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF THE PRC2 AND PRC3 COMPLEXES INCLUDING EED; EZH2; RBBP4; RBBP7 AND SUZ12, METHYLTRANSFERASE ACTIVITY OF THE PRC2 AND PRC3 COMPLEXES.
    11. "SUZ12 is required for both the histone methyltransferase activity and the silencing function of the EED-EZH2 complex."
      Cao R., Zhang Y.
      Mol. Cell 15:57-67(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CHARACTERIZATION OF THE PRC2 COMPLEX INCLUDING AEBP2; EED; EZH2; RBBP4 AND SUZ12, METHYLTRANSFERASE ACTIVITY OF THE PRC2 COMPLEX.
    12. "Composition and histone substrates of polycomb repressive group complexes change during cellular differentiation."
      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.
      Proc. Natl. Acad. Sci. U.S.A. 102:1859-1864(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF THE PRC4 COMPLEX INCLUDING EED; EZH2; RBBP4; RBBP7; SUZ12 AND SIRT1, METHYLTRANSFERASE ACTIVITY OF THE PRC4 COMPLEX, TISSUE SPECIFICITY.
    13. "Akt-mediated phosphorylation of EZH2 suppresses methylation of lysine 27 in histone H3."
      Cha T.-L., Zhou B.P., Xia W., Wu Y., Yang C.-C., Chen C.-T., Ping B., Otte A.P., Hung M.-C.
      Science 310:306-310(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EZH2.
    14. "Association of Polycomb group SUZ12 with WD-repeat protein MEP50 that binds to histone H2A selectively in vitro."
      Furuno K., Masatsugu T., Sonoda M., Sasazuki T., Yamamoto K.
      Biochem. Biophys. Res. Commun. 345:1051-1058(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH WDR77.
    15. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-546, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "Genome-wide mapping of Polycomb target genes unravels their roles in cell fate transitions."
      Bracken A.P., Dietrich N., Pasini D., Hansen K.H., Helin K.
      Genes Dev. 20:1123-1136(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    17. "Substrate preferences of the EZH2 histone methyltransferase complex."
      Martin C., Cao R., Zhang Y.
      J. Biol. Chem. 281:8365-8370(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLTRANSFERASE ACTIVITY OF THE PRC2 COMPLEX, INTERACTION WITH HISTONE H1.
    18. "The Polycomb group proteins bind throughout the INK4A-ARF locus and are disassociated in senescent cells."
      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.
      Genes Dev. 21:525-530(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    19. "Polycomb-mediated methylation on Lys27 of histone H3 pre-marks genes for de novo methylation in cancer."
      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.
      Nat. Genet. 39:232-236(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: DE NOVO DNA METHYLATION OF PRC2 TARGET GENES.
    20. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-546 AND SER-583, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. "Ezh1 and Ezh2 maintain repressive chromatin through different mechanisms."
      Margueron R., Li G., Sarma K., Blais A., Zavadil J., Woodcock C.L., Dynlacht B.D., Reinberg D.
      Mol. Cell 32:503-518(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE PRC2/EED-EZH1 COMPLEX.
    22. "Role of hPHF1 in H3K27 methylation and Hox gene silencing."
      Cao R., Wang H., He J., Erdjument-Bromage H., Tempst P., Zhang Y.
      Mol. Cell. Biol. 28:1862-1872(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE PRC2 COMPLEX, METHYLTRANSFERASE ACTIVITY OF THE PRC2 COMPLEX.
    23. "Ezh2 requires PHF1 to efficiently catalyze H3 lysine 27 trimethylation in vivo."
      Sarma K., Margueron R., Ivanov A., Pirrotta V., Reinberg D.
      Mol. Cell. Biol. 28:2718-2731(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH EED AND EZH2, INTERACTION OF THE PRC2 COMPLEX WITH PHF1, METHYLTRANSFERASE ACTIVITY OF THE PRC2 COMPLEX.
    24. "The polycomb repressive complex 2 is a potential target of SUMO modifications."
      Riising E.M., Boggio R., Chiocca S., Helin K., Pasini D.
      PLoS ONE 3:E2704-E2704(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION AT LYS-72; LYS-73 AND LYS-75.
    25. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-546, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    26. "A neoplastic gene fusion mimics trans-splicing of RNAs in normal human cells."
      Li H., Wang J., Mor G., Sklar J.
      Science 321:1357-1361(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: TRANS-SPLICING.
    27. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-546, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    29. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      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.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-546, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    30. "Corepressor protein CDYL functions as a molecular bridge between polycomb repressor complex 2 and repressive chromatin mark trimethylated histone lysine 27."
      Zhang Y., Yang X., Gui B., Xie G., Zhang D., Shang Y., Liang J.
      J. Biol. Chem. 286:42414-42425(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CDYL.
    31. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-546, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiSUZ12_HUMAN
    AccessioniPrimary (citable) accession number: Q15022
    Secondary accession number(s): Q96BD9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 11, 2003
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 136 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    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).1 Publication

    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).1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3