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Q15022 (SUZ12_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:SUZ12
Synonyms:CHET9, JJAZ1, KIAA0160
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length739 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.8 Ref.9 Ref.11 Ref.16 Ref.18 Ref.23

Subunit structure

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. Ref.5 Ref.6 Ref.8 Ref.13 Ref.14 Ref.17 Ref.21 Ref.22 Ref.23 Ref.30

Subcellular location

Nucleus Ref.9.

Tissue specificity

Overexpressed in breast and colon cancer. Ref.9 Ref.12

Developmental stage

Expressed at low levels in quiescent cells. Expression rises at the G1/S phase transition. Ref.8

Induction

Expression is induced by E2F1, E2F2 and E2F3. Ref.4 Ref.7

Post-translational modification

Sumoylated, probably by PIAS2. Ref.24

Involvement in disease

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. Ref.3

Miscellaneous

Under hypoxic conditions, the precursor SUZ12 RNA undergoes regulated trans-splicing with the JAZF1 RNA, resulting in a chimeric isoform whichmay 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 (Ref.26).

Sequence similarities

Belongs to the VEFS (VRN2-EMF2-FIS2-SU(Z)12) family.

Contains 1 C2H2-type zinc finger.

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 (Ref.10 and Ref.12), although other studies have demonstrated no methylation of 'Lys-26' of histone H1 by PRC2 (Ref.17).

Sequence caution

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

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityChromosomal rearrangement
Polymorphism
   DiseaseProto-oncogene
   DomainZinc-finger
   LigandMetal-binding
Zinc
   Molecular functionChromatin regulator
Repressor
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processhistone ubiquitination

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell differentiation

Inferred from mutant phenotype PubMed 19847889. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentESC/E(Z) complex

Inferred from direct assay PubMed 20075857PubMed 23104054PubMed 23273982. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

sex chromatin

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionchromatin binding

Inferred from electronic annotation. Source: Ensembl

histone methyltransferase activity

Inferred from mutant phenotype Ref.8. Source: MGI

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

methylated histone residue binding

Inferred from direct assay PubMed 21029866. Source: UniProtKB

sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 739739Polycomb protein SUZ12
PRO_0000047057

Regions

Zinc finger448 – 47124C2H2-type
Region563 – 63977VEFS-box
Compositional bias7 – 5044Gly-rich
Compositional bias51 – 599Poly-Ser
Compositional bias60 – 678Poly-Ala

Sites

Site93 – 942Breakpoint for translocation to form JAZF1-SUZ12 oncogene

Amino acid modifications

Modified residue5461Phosphoserine Ref.15 Ref.20 Ref.25 Ref.28 Ref.29 Ref.31
Modified residue5831Phosphoserine Ref.20
Cross-link72Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.24
Cross-link73Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.24
Cross-link75Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.24

Natural variations

Natural variant2161N → I. Ref.1
Corresponds to variant rs17339444 [ dbSNP | Ensembl ].
VAR_028100

Sequences

Sequence LengthMass (Da)Tools
Q15022 [UniParc].

Last modified October 17, 2006. Version 3.
Checksum: A8830EBC3FD38D56

FASTA73983,055
        10         20         30         40         50         60 
MAPQKHGGGG GGGSGPSAGS GGGGFGGSAA VAAATASGGK SGGGSCGGGG SYSASSSSSA 

        70         80         90        100        110        120 
AAAAGAAVLP VKKPKMEHVQ ADHELFLQAF EKPTQIYRFL RTRNLIAPIF LHRTLTYMSH 

       130        140        150        160        170        180 
RNSRTNIKRK TFKVDDMLSK VEKMKGEQES HSLSAHLQLT FTGFFHKNDK PSPNSENEQN 

       190        200        210        220        230        240 
SVTLEVLLVK VCHKKRKDVS CPIRQVPTGK KQVPLNPDLN QTKPGNFPSL AVSSNEFEPS 

       250        260        270        280        290        300 
NSHMVKSYSL LFRVTRPGRR EFNGMINGET NENIDVNEEL PARRKRNRED GEKTFVAQMT 

       310        320        330        340        350        360 
VFDKNRRLQL LDGEYEVAMQ EMEECPISKK RATWETILDG KRLPPFETFS QGPTLQFTLR 

       370        380        390        400        410        420 
WTGETNDKST APIAKPLATR NSESLHQENK PGSVKPTQTI AVKESLTTDL QTRKEKDTPN 

       430        440        450        460        470        480 
ENRQKLRIFY QFLYNNNTRQ QTEARDDLHC PWCTLNCRKL YSLLKHLKLC HSRFIFNYVY 

       490        500        510        520        530        540 
HPKGARIDVS INECYDGSYA GNPQDIHRQP GFAFSRNGPV KRTPITHILV CRPKRTKASM 

       550        560        570        580        590        600 
SEFLESEDGE VEQQRTYSSG HNRLYFHSDT CLPLRPQEME VDSEDEKDPE WLREKTITQI 

       610        620        630        640        650        660 
EEFSDVNEGE KEVMKLWNLH VMKHGFIADN QMNHACMLFV ENYGQKIIKK NLCRNFMLHL 

       670        680        690        700        710        720 
VSMHDFNLIS IMSIDKAVTK LREMQQKLEK GESASPANEE ITEEQNGTAN GFSEINSKEK 

       730 
ALETDSVSGV SKQSKKQKL 

« Hide

References

« Hide 'large scale' references
[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]"Frequent fusion of the JAZF1 and JJAZ1 genes in endometrial stromal tumors."
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.
Proc. Natl. Acad. Sci. U.S.A. 98:6348-6353(2001) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D63881 mRNA. Translation: BAA09931.2. Different initiation.
BC015704 mRNA. Translation: AAH15704.1.
RefSeqNP_056170.2. NM_015355.2.
UniGeneHs.462732.

3D structure databases

ProteinModelPortalQ15022.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117059. 52 interactions.
DIPDIP-38524N.
IntActQ15022. 25 interactions.
STRING9606.ENSP00000316578.

Polymorphism databases

DMDM116242808.

Proteomic databases

PaxDbQ15022.
PRIDEQ15022.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000322652; ENSP00000316578; ENSG00000178691.
GeneID23512.
KEGGhsa:23512.
UCSCuc002hgs.2. human.

Organism-specific databases

CTD23512.
GeneCardsGC17P030264.
HGNCHGNC:17101. SUZ12.
HPAHPA057436.
MIM606245. gene.
neXtProtNX_Q15022.
Orphanet97685. 17q11 microdeletion syndrome.
PharmGKBPA134936035.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG313866.
HOGENOMHOG000047340.
HOVERGENHBG039522.
InParanoidQ15022.
KOK11463.
OMAPKMEQIQ.
PhylomeDBQ15022.
TreeFamTF323249.

Enzyme and pathway databases

ReactomeREACT_120956. Cellular responses to stress.
SignaLinkQ15022.

Gene expression databases

ArrayExpressQ15022.
BgeeQ15022.
CleanExHS_SUZ12.
GenevestigatorQ15022.

Family and domain databases

InterProIPR019135. Polycomb_protein_VEFS-Box.
IPR015880. Znf_C2H2-like.
[Graphical view]
PfamPF09733. VEFS-Box. 1 hit.
[Graphical view]
SMARTSM00355. ZnF_C2H2. 1 hit.
[Graphical view]
PROSITEPS00028. ZINC_FINGER_C2H2_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiSUZ12.
GenomeRNAi23512.
NextBio45931.
PROQ15022.
SOURCESearch...

Entry information

Entry nameSUZ12_HUMAN
AccessionPrimary (citable) accession number: Q15022
Secondary accession number(s): Q96BD9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2003
Last sequence update: October 17, 2006
Last modified: April 16, 2014
This is version 131 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM