Q15022 (SUZ12_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	SUZ12
Synonyms:	CHET9, JJAZ1, KIAA0160

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	739 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Ref.5 Ref.6 Ref.8 Ref.13 Ref.14 Ref.17 Ref.21 Ref.22 Ref.23
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 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 (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 process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Chromosomal rearrangement Polymorphism
Disease	Proto-oncogene
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Chromatin regulator Repressor
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	histone ubiquitination Inferred from electronic annotation. Source: Compara 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: Compara positive regulation of cell proliferation Inferred from electronic annotation. Source: Compara transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	ESC/E(Z) complex Inferred from direct assay PubMed 20075857PubMed 23104054PubMed 23273982. Source: UniProtKB sex chromatin Inferred from electronic annotation. Source: Compara
Molecular_function	chromatin binding Inferred from electronic annotation. Source: Compara histone methyltransferase activity Inferred from mutant phenotype Ref.8. Source: MGI methylated histone residue binding Inferred from direct assay PubMed 21029866. Source: UniProtKB sequence-specific DNA binding Inferred from electronic annotation. Source: Compara zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HDAC3	O15379	7	EBI-1264675,EBI-607682
PML-RAR	Q15156	6	EBI-1264675,EBI-867256

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 739	739	Polycomb protein SUZ12		PRO_0000047057
Regions
	Zinc finger	448 – 471	24	C2H2-type
	Region	563 – 639	77	VEFS-box
	Compositional bias	7 – 50	44	Gly-rich
	Compositional bias	51 – 59	9	Poly-Ser
	Compositional bias	60 – 67	8	Poly-Ala
Sites
	Site	93 – 94	2	Breakpoint for translocation to form JAZF1-SUZ12 oncogene
Amino acid modifications
	Modified residue	546	1	Phosphoserine Ref.15 Ref.20 Ref.25 Ref.27 Ref.28 Ref.29
	Modified residue	583	1	Phosphoserine Ref.20
	Cross-link	72		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.24
	Cross-link	73		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.24
	Cross-link	75		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.24
Natural variations
	Natural variant	216	1	N → I. Ref.1 Corresponds to variant rs17339444 [ dbSNP | Ensembl ].		VAR_028100

Sequences

	Sequence		Length	Mass (Da)
	Q15022 [UniParc]. Last modified October 17, 2006. Version 3. Checksum: A8830EBC3FD38D56	FASTA	739	83,055
	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

References

	« Hide 'large scale' referencesShow '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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[28]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[29]	"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, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases
EMBL GenBank DDBJ	D63881 mRNA. Translation: BAA09931.2. Different initiation. BC015704 mRNA. Translation: AAH15704.1.
IPI	IPI00299526.
RefSeq	NP_056170.2. NM_015355.2.
UniGene	Hs.741396.
3D structure databases
ProteinModelPortal	Q15022.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-38524N.
IntAct	Q15022. 19 interactions.
STRING	9606.ENSP00000316578.
Polymorphism databases
DMDM	116242808.
Proteomic databases
PaxDb	Q15022.
PRIDE	Q15022.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000322652; ENSP00000316578; ENSG00000178691.
GeneID	23512.
KEGG	hsa:23512.
UCSC	uc002hgs.2. human.
Organism-specific databases
CTD	23512.
GeneCards	GC17P030264.
HGNC	HGNC:17101. SUZ12.
MIM	606245. gene.
neXtProt	NX_Q15022.
Orphanet	97685. 17q11 microdeletion syndrome.
PharmGKB	PA134936035.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG313866.
HOGENOM	HOG000047340.
HOVERGEN	HBG039522.
InParanoid	Q15022.
KO	K11463.
OMA	PKMEQIQ.
OrthoDB	EOG4GTKCD.
PhylomeDB	Q15022.
Gene expression databases
Bgee	Q15022.
CleanEx	HS_SUZ12.
Genevestigator	Q15022.
GermOnline	ENSG00000178691. Homo sapiens.
Family and domain databases
InterPro	IPR019135. Polycomb_protein_VEFS-Box. IPR015880. Znf_C2H2-like. [Graphical view]
Pfam	PF09733. VEFS-Box. 1 hit. [Graphical view]
SMART	SM00355. ZnF_C2H2. 1 hit. [Graphical view]
PROSITE	PS00028. ZINC_FINGER_C2H2_1. 1 hit. PS50157. ZINC_FINGER_C2H2_2. False negative. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	23512.
NextBio	45931.
SOURCE	Search...

Entry information

Entry name

SUZ12_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 121 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.