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Protein

Polycomb protein SUZ12

Gene

SUZ12

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri448 – 471C2H2-typeAdd BLAST24

GO - Molecular functioni

  • chromatin DNA binding Source: Ensembl
  • histone methyltransferase activity Source: MGI
  • metal ion binding Source: UniProtKB-KW
  • methylated histone binding Source: UniProtKB
  • RNA binding Source: Ensembl
  • RNA polymerase II core promoter sequence-specific DNA binding Source: Ensembl

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000178691-MONOMER.
ReactomeiR-HSA-212300. PRC2 methylates histones and DNA.
R-HSA-2559580. Oxidative Stress Induced Senescence.
R-HSA-3214841. PKMTs methylate histone lysines.
R-HSA-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.
SignaLinkiQ15022.
SIGNORiQ15022.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:17101. SUZ12.

Subcellular locationi

GO - Cellular componenti

  • ESC/E(Z) complex Source: UniProtKB
  • nucleolus Source: HPA
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • protein-DNA complex Source: Ensembl
  • sex chromatin Source: Ensembl
Complete GO annotation...

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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei93 – 94Breakpoint for translocation to form JAZF1-SUZ12 oncogene2

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

DisGeNETi23512.
OpenTargetsiENSG00000178691.
PharmGKBiPA134936035.

Chemistry databases

ChEMBLiCHEMBL3137286.

Polymorphism and mutation databases

BioMutaiSUZ12.
DMDMi116242808.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000470571 – 739Polycomb protein SUZ12Add BLAST739

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei20PhosphoserineCombined sources1
Cross-linki72Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Cross-linki73Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Cross-linki75Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei541PhosphoserineCombined sources1
Modified residuei546PhosphoserineCombined sources1
Modified residuei583PhosphoserineCombined sources1
Modified residuei726PhosphoserineCombined sources1

Post-translational modificationi

Sumoylated, probably by PIAS2.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ15022.
MaxQBiQ15022.
PaxDbiQ15022.
PeptideAtlasiQ15022.
PRIDEiQ15022.

PTM databases

iPTMnetiQ15022.
PhosphoSitePlusiQ15022.

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

BgeeiENSG00000178691.
CleanExiHS_SUZ12.
ExpressionAtlasiQ15022. baseline and differential.
GenevisibleiQ15022. HS.

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

GO - Molecular functioni

  • methylated histone binding Source: UniProtKB

Protein-protein interaction databases

BioGridi117059. 346 interactors.
DIPiDIP-38524N.
IntActiQ15022. 36 interactors.
STRINGi9606.ENSP00000316578.

Chemistry databases

BindingDBiQ15022.

Structurei

Secondary structure

1739
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni568 – 570Combined sources3
Helixi576 – 578Combined sources3
Helixi590 – 601Combined sources12
Beta strandi604 – 606Combined sources3
Helixi608 – 624Combined sources17
Helixi629 – 631Combined sources3
Helixi632 – 649Combined sources18
Helixi653 – 665Combined sources13
Helixi671 – 686Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5HYNX-ray2.95C/H/M/S558-685[»]
5IJ7X-ray2.62S/T545-725[»]
5IJ8X-ray2.99S/T545-725[»]
ProteinModelPortaliQ15022.
SMRiQ15022.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni563 – 639VEFS-boxAdd BLAST77

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi7 – 50Gly-richAdd BLAST44
Compositional biasi51 – 59Poly-Ser9
Compositional biasi60 – 67Poly-Ala8

Sequence similaritiesi

Contains 1 C2H2-type zinc finger.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri448 – 471C2H2-typeAdd BLAST24

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG2350. Eukaryota.
ENOG410YJ29. LUCA.
GeneTreeiENSGT00390000012364.
HOGENOMiHOG000047340.
HOVERGENiHBG039522.
InParanoidiQ15022.
KOiK11463.
OMAiPMETRTS.
OrthoDBiEOG091G012Q.
PhylomeDBiQ15022.
TreeFamiTF323249.

Family and domain databases

InterProiIPR019135. Polycomb_protein_VEFS-Box.
[Graphical view]
PfamiPF09733. VEFS-Box. 1 hit.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q15022-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPQKHGGGG GGGSGPSAGS GGGGFGGSAA VAAATASGGK SGGGSCGGGG
60 70 80 90 100
SYSASSSSSA AAAAGAAVLP VKKPKMEHVQ ADHELFLQAF EKPTQIYRFL
110 120 130 140 150
RTRNLIAPIF LHRTLTYMSH RNSRTNIKRK TFKVDDMLSK VEKMKGEQES
160 170 180 190 200
HSLSAHLQLT FTGFFHKNDK PSPNSENEQN SVTLEVLLVK VCHKKRKDVS
210 220 230 240 250
CPIRQVPTGK KQVPLNPDLN QTKPGNFPSL AVSSNEFEPS NSHMVKSYSL
260 270 280 290 300
LFRVTRPGRR EFNGMINGET NENIDVNEEL PARRKRNRED GEKTFVAQMT
310 320 330 340 350
VFDKNRRLQL LDGEYEVAMQ EMEECPISKK RATWETILDG KRLPPFETFS
360 370 380 390 400
QGPTLQFTLR WTGETNDKST APIAKPLATR NSESLHQENK PGSVKPTQTI
410 420 430 440 450
AVKESLTTDL QTRKEKDTPN ENRQKLRIFY QFLYNNNTRQ QTEARDDLHC
460 470 480 490 500
PWCTLNCRKL YSLLKHLKLC HSRFIFNYVY HPKGARIDVS INECYDGSYA
510 520 530 540 550
GNPQDIHRQP GFAFSRNGPV KRTPITHILV CRPKRTKASM SEFLESEDGE
560 570 580 590 600
VEQQRTYSSG HNRLYFHSDT CLPLRPQEME VDSEDEKDPE WLREKTITQI
610 620 630 640 650
EEFSDVNEGE KEVMKLWNLH VMKHGFIADN QMNHACMLFV ENYGQKIIKK
660 670 680 690 700
NLCRNFMLHL VSMHDFNLIS IMSIDKAVTK LREMQQKLEK GESASPANEE
710 720 730
ITEEQNGTAN GFSEINSKEK ALETDSVSGV SKQSKKQKL
Length:739
Mass (Da):83,055
Last modified:October 17, 2006 - v3
Checksum:iA8830EBC3FD38D56
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_028100216N → I.1 PublicationCorresponds to variant rs17339444dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D63881 mRNA. Translation: BAA09931.2. Different initiation.
BC015704 mRNA. Translation: AAH15704.1.
CCDSiCCDS11270.1.
RefSeqiNP_056170.2. NM_015355.3.
UniGeneiHs.462732.

Genome annotation databases

EnsembliENST00000322652; ENSP00000316578; ENSG00000178691.
GeneIDi23512.
KEGGihsa:23512.
UCSCiuc002hgs.3. human.

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:
EMBLi
GenBanki
DDBJi
Links Updated
D63881 mRNA. Translation: BAA09931.2. Different initiation.
BC015704 mRNA. Translation: AAH15704.1.
CCDSiCCDS11270.1.
RefSeqiNP_056170.2. NM_015355.3.
UniGeneiHs.462732.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5HYNX-ray2.95C/H/M/S558-685[»]
5IJ7X-ray2.62S/T545-725[»]
5IJ8X-ray2.99S/T545-725[»]
ProteinModelPortaliQ15022.
SMRiQ15022.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117059. 346 interactors.
DIPiDIP-38524N.
IntActiQ15022. 36 interactors.
STRINGi9606.ENSP00000316578.

Chemistry databases

BindingDBiQ15022.
ChEMBLiCHEMBL3137286.

PTM databases

iPTMnetiQ15022.
PhosphoSitePlusiQ15022.

Polymorphism and mutation databases

BioMutaiSUZ12.
DMDMi116242808.

Proteomic databases

EPDiQ15022.
MaxQBiQ15022.
PaxDbiQ15022.
PeptideAtlasiQ15022.
PRIDEiQ15022.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000322652; ENSP00000316578; ENSG00000178691.
GeneIDi23512.
KEGGihsa:23512.
UCSCiuc002hgs.3. human.

Organism-specific databases

CTDi23512.
DisGeNETi23512.
GeneCardsiSUZ12.
HGNCiHGNC:17101. SUZ12.
HPAiHPA057436.
MIMi606245. gene.
neXtProtiNX_Q15022.
OpenTargetsiENSG00000178691.
PharmGKBiPA134936035.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2350. Eukaryota.
ENOG410YJ29. LUCA.
GeneTreeiENSGT00390000012364.
HOGENOMiHOG000047340.
HOVERGENiHBG039522.
InParanoidiQ15022.
KOiK11463.
OMAiPMETRTS.
OrthoDBiEOG091G012Q.
PhylomeDBiQ15022.
TreeFamiTF323249.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000178691-MONOMER.
ReactomeiR-HSA-212300. PRC2 methylates histones and DNA.
R-HSA-2559580. Oxidative Stress Induced Senescence.
R-HSA-3214841. PKMTs methylate histone lysines.
R-HSA-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.
SignaLinkiQ15022.
SIGNORiQ15022.

Miscellaneous databases

ChiTaRSiSUZ12. human.
GeneWikiiSUZ12.
GenomeRNAii23512.
PROiQ15022.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000178691.
CleanExiHS_SUZ12.
ExpressionAtlasiQ15022. baseline and differential.
GenevisibleiQ15022. HS.

Family and domain databases

InterProiIPR019135. Polycomb_protein_VEFS-Box.
[Graphical view]
PfamiPF09733. VEFS-Box. 1 hit.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 30, 2016
This is version 160 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

3D-structure, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.