Reviewed, UniProtKB/Swiss-Prot O43463 (SUV91_HUMAN)

Names and origin

Protein names

Recommended name:
    Histone-lysine N-methyltransferase SUV39H1
    EC=2.1.1.43
Alternative name(s):
    Suppressor of variegation 3-9 homolog 1
      Short name=Su(var)3-9 homolog 1
    Position-effect variegation 3-9 homolog
    Histone H3-K9 methyltransferase 1
    H3-K9-HMTase 1
    Lysine N-methyltransferase 1A

Gene names

Name:	SUV39H1
Synonyms:	KMT1A, SUV39H

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	412 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 using monomethylated H3 'Lys-9' as substrate. Also weakly methylates histone H1 (in vitro). H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions. H3 'Lys-9' trimethylation is also required to direct DNA methylation at pericentric repeats. SUV39H1 is targeted to histone H3 via its interaction with RB1 and is involved in many processes, such as repression of MYOD1-stimulated differentiation, regulation of the control switch for exiting the cell cycle and entering differentiaton, repression by the PML-RARA fusion protein, BMP-induced repression, repression of switch recombination to IgA and regulation of telomere length. Ref.15 Ref.19 Ref.22 Ref.23
Catalytic activity	S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N(6)-methyl-L-lysine. Ref.7
Enzyme regulation	Inhibited by S-adenosyl-L-homocysteine. Ref.20
Subunit structure	Interacts with H3 and H4 histones. Interacts with GFI1B, DNMT3B, CBX1, CBX4, MBD1, RUNX1, RUNX3, MYOD1, SMAD5 and RB1. Interacts with SBF1 through the SET domain. Interacts with HDAC1 and HDAC2 through the N-terminus and associates with the core histone deacetylase complex composed of HDAC1, HDAC2, RBBP4 and RBBP7. In case of infection, interacts with HTLV-1 Tax protein, leading to abrogate Tax transactivation of HTLV-1 LTR. Ref.22 Ref.1 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.16 Ref.17 Ref.18 Ref.24 Ref.25
Subcellular location	Nucleus. Centromere. Note= Associates with centromeric constitutive heterochromatin. Ref.6
Developmental stage	Accumulates during mitosis at centromeres during prometaphase, but dissociates from the centromere at the meta- to anaphase transition.
Domain	Although the SET domain contains the active site of enzymatic activity, both pre-SET and post-SET domains are required for methyltransferase activity. The SET domain also participates to stable binding to heterochromatin. Ref.17
Post-translational modification	Phosphorylated on serine residues, and to a lesser degree, on threonine residues. The phosphorylated form is stabilized by SBF1 and is less active in its transcriptional repressor function. Ref.6 Ref.21 Ref.26 Ref.27
Sequence similarities	Belongs to the histone-lysine methyltransferase family. Suvar3-9 subfamily. Contains 1 chromo domain. Contains 1 post-SET domain. Contains 1 pre-SET domain. Contains 1 SET domain.

Ontologies

Keywords
Biological process	Cell cycle Differentiation Host-virus interaction Transcription Transcription regulation
Cellular component	Centromere Chromosomal protein Nucleus
Ligand	S-adenosyl-L-methionine
Molecular function	Chromatin regulator Methyltransferase Repressor Transferase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW chromatin assembly or disassembly Inferred from electronic annotation. Source: InterPro chromatin modification Inferred from electronic annotation. Source: InterPro interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chromatin Inferred from electronic annotation. Source: InterPro chromosome, centromeric region Inferred from electronic annotation. Source: UniProtKB-KW condensed nuclear chromosome Ref.1 Traceable author statement. Source: ProtInc
Molecular function	chromatin binding Ref.1 Traceable author statement. Source: ProtInc histone lysine N-methyltransferase activity (H3-K9 specific) Ref.7 Inferred from direct assay. Source: UniProtKB protein binding Ref.7 Ref.9 Ref.11 Inferred from physical interaction. Source: IntAct zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	P68432	1	EBI-349968,EBI-79764	From a different organism.
CBX5	P45973	1	EBI-349968,EBI-78219
HDAC1	Q13547	2	EBI-349968,EBI-301834
HDAC2	Q92769	2	EBI-349968,EBI-301821
HIST1H3A	P68431	1	EBI-349968,EBI-79722
KIAA0409	O43159	1	EBI-349968,EBI-2008793
MBD1	Q9UIS9	2	EBI-349968,EBI-867196

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 412	412	Histone-lysine N-methyltransferase SUV39H1		PRO_0000186057
Regions
	Domain	43 – 101	59	Chromo
	Domain	179 – 240	62	Pre-SET
	Domain	242 – 370	129	SET
	Domain	396 – 412	17	Post-SET
Amino acid modifications
	Modified residue	391	1	Phosphoserine Ref.21 Ref.26 Ref.27
Experimental info
	Mutagenesis	64	1	W → A: Abolishes methyltransferase activity Ref.20
	Mutagenesis	67	1	Y → A: Abolishes methyltransferase activity Ref.20
	Mutagenesis	320	1	H → R: Strongly increases methylation of histone H3 Ref.7
	Mutagenesis	324	1	H → L or K: Abolishes methylation of histone H3 Ref.7
	Mutagenesis	326	1	C → A: Abolishes methylation of histone H3 Ref.7
	Sequence conflict	213	1	L → P in BAD96791. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	O43463-1 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: AF6F959AD20C6C76	FASTA	412	47,907
	10 20 30 40 50 60 MAENLKGCSV CCKSSWNQLQ DLCRLAKLSC PALGISKRNL YDFEVEYLCD YKKIREQEYY 70 80 90 100 110 120 LVKWRGYPDS ESTWEPRQNL KCVRILKQFH KDLERELLRR HHRSKTPRHL DPSLANYLVQ 130 140 150 160 170 180 KAKQRRALRR WEQELNAKRS HLGRITVENE VDLDGPPRAF VYINEYRVGE GITLNQVAVG 190 200 210 220 230 240 CECQDCLWAP TGGCCPGASL HKFAYNDQGQ VRLRAGLPIY ECNSRCRCGY DCPNRVVQKG 250 260 270 280 290 300 IRYDLCIFRT DDGRGWGVRT LEKIRKNSFV MEYVGEIITS EEAERRGQIY DRQGATYLFD 310 320 330 340 350 360 LDYVEDVYTV DAAYYGNISH FVNHSCDPNL QVYNVFIDNL DERLPRIAFF ATRTIRAGEE 370 380 390 400 410 LTFDYNMQVD PVDMESTRMD SNFGLAGLPG SPKKRVRIEC KCGTESCRKY LF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Functional mammalian homologues of the Drosophila PEV-modifier Su(var)3-9 encode centromere-associated proteins which complex with the heterochromatin component M31." Aagaard L., Laible G., Selenko P., Schmid M., Dorn R., Schotta G., Kuhfittig S., Wolf A., Lebersorger A., Singh P.B., Reuter G., Jenuwein T. EMBO J. 18:1923-1938(1999) [PubMed: 10202156] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH CBX1. Tissue: B-cell.
[2]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R. Nature 434:325-337(2005) [PubMed: 15772651] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung.
[6]	"Mitotic phosphorylation of SUV39H1, a novel component of active centromeres, coincides with transient accumulation at mammalian centromeres." Aagaard L., Schmid M., Warburton P., Jenuwein T. J. Cell Sci. 113:817-829(2000) [PubMed: 10671371] [Abstract] Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION.
[7]	"Regulation of chromatin structure by site-specific histone H3 methyltransferases." Rea S., Eisenhaber F., O'Carroll D., Strahl B.D., Sun Z.-W., Schmid M., Opravil S., Mechtler K., Ponting C.P., Allis C.D., Jenuwein T. Nature 406:593-599(2000) [PubMed: 10949293] [Abstract] Cited for: ENZYME ACTIVITY, MUTAGENESIS OF HIS-320; HIS-324 AND CYS-326.
[8]	"Set domain-dependent regulation of transcriptional silencing and growth control by SUV39H1, a mammalian ortholog of Drosophila Su(var)3-9." Firestein R., Cui X., Huie P., Cleary M.L. Mol. Cell. Biol. 20:4900-4909(2000) [PubMed: 10848615] [Abstract] Cited for: INTERACTION WITH SBF1.
[9]	"Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins." Lachner M., O'Carroll D., Rea S., Mechtler K., Jenuwein T. Nature 410:116-120(2001) [PubMed: 11242053] [Abstract] Cited for: INTERACTION WITH HISTONE H3 AND HISTONE H4.
[10]	"Rb targets histone H3 methylation and HP1 to promoters." Nielsen S.J., Schneider R., Bauer U.-M., Bannister A.J., Morrison A., O'Carroll D., Firestein R., Cleary M.L., Jenuwein T., Herrera R.E., Kouzarides T. Nature 412:561-565(2001) [PubMed: 11484059] [Abstract] Cited for: INTERACTION WITH RB1.
[11]	"Methyl-CpG binding domain 1 (MBD1) interacts with the Suv39h1-HP1 heterochromatic complex for DNA methylation-based transcriptional repression." Fujita N., Watanabe S., Ichimura T., Tsuruzoe S., Shinkai Y., Tachibana M., Chiba T., Nakao M. J. Biol. Chem. 278:24132-24138(2003) [PubMed: 12711603] [Abstract] Cited for: INTERACTION WITH MBD1.
[12]	"Selective interactions between vertebrate polycomb homologs and the SUV39H1 histone lysine methyltransferase suggest that histone H3-K9 methylation contributes to chromosomal targeting of Polycomb group proteins." Sewalt R.G.A.B., Lachner M., Vargas M., Hamer K.M., den Blaauwen J.L., Hendrix T., Melcher M., Schweizer D., Jenuwein T., Otte A.P. Mol. Cell. Biol. 22:5539-5553(2002) [PubMed: 12101246] [Abstract] Cited for: INTERACTION WITH CBX4.
[13]	"SUV39H1 interacts with AML1 and abrogates AML1 transactivity. AML1 is methylated in vivo." Chakraborty S., Sinha K.K., Senyuk V., Nucifora G. Oncogene 22:5229-5237(2003) [PubMed: 12917624] [Abstract] Cited for: INTERACTION WITH RUNX1.
[14]	"pRb2/p130-E2F4/5-HDAC1-SUV39H1-p300 and pRb2/p130-E2F4/5-HDAC1-SUV39H1-DNMT1 multimolecular complexes mediate the transcription of estrogen receptor-alpha in breast cancer." Macaluso M., Cinti C., Russo G., Russo A., Giordano A. Oncogene 22:3511-3517(2003) [PubMed: 12789259] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH HDAC1.
[15]	"A Suv39h-dependent mechanism for silencing S-phase genes in differentiating but not in cycling cells." Ait-Si-Ali S., Guasconi V., Fritsch L., Yahi H., Sekhri R., Naguibneva I., Robin P., Cabon F., Polesskaya A., Harel-Bellan A. EMBO J. 23:605-615(2004) [PubMed: 14765126] [Abstract] Cited for: FUNCTION.
[16]	"Suv39h histone methyltransferases interact with Smads and cooperate in BMP-induced repression." Frontelo P., Leader J.E., Yoo N., Potocki A.C., Crawford M., Kulik M., Lechleider R.J. Oncogene 23:5242-5251(2004) [PubMed: 15107829] [Abstract] Cited for: INTERACTION WITH SMAD5.
[17]	"A glue for heterochromatin maintenance: stable SUV39H1 binding to heterochromatin is reinforced by the SET domain." Krouwels I.M., Wiesmeijer K., Abraham T.E., Molenaar C., Verwoerd N.P., Tanke H.J., Dirks R.W. J. Cell Biol. 170:537-549(2005) [PubMed: 16103223] [Abstract] Cited for: DOMAIN, INTERACTION WITH CBX1.
[18]	"Gfi1b alters histone methylation at target gene promoters and sites of gamma-satellite containing heterochromatin." Vassen L., Fiolka K., Moeroey T. EMBO J. 25:2409-2419(2006) [PubMed: 16688220] [Abstract] Cited for: INTERACTION WITH GFI1B.
[19]	"The histone methyltransferase Suv39h1 increases class switch recombination specifically to IgA." Bradley S.P., Kaminski D.A., Peters A.H.F.M., Jenuwein T., Stavnezer J. J. Immunol. 177:1179-1188(2006) [PubMed: 16818776] [Abstract] Cited for: FUNCTION.
[20]	"Catalytic properties and kinetic mechanism of human recombinant Lys-9 histone H3 methyltransferase SUV39H1: participation of the chromodomain in enzymatic catalysis." Chin H.G., Patnaik D., Esteve P.-O., Jacobsen S.E., Pradhan S. Biochemistry 45:3272-3284(2006) [PubMed: 16519522] [Abstract] Cited for: ENZYME REGULATION, MUTAGENESIS OF TRP-64 AND TYR-67.
[21]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391, MASS SPECTROMETRY. Tissue: Epithelium.
[22]	"Histone methyltransferase Suv39h1 represses MyoD-stimulated myogenic differentiation." Mal A.K. EMBO J. 25:3323-3334(2006) [PubMed: 16858404] [Abstract] Cited for: FUNCTION, INTERACTION WITH MYOD1.
[23]	"Recruitment of the histone methyltransferase SUV39H1 and its role in the oncogenic properties of the leukemia-associated PML-retinoic acid receptor fusion protein." Carbone R., Botrugno O.A., Ronzoni S., Insinga A., Di Croce L., Pelicci P.G., Minucci S. Mol. Cell. Biol. 26:1288-1296(2006) [PubMed: 16449642] [Abstract] Cited for: FUNCTION.
[24]	"RUNX1 associates with histone deacetylases and SUV39H1 to repress transcription." Reed-Inderbitzin E., Moreno-Miralles I., Vanden-Eynden S.K., Xie J., Lutterbach B., Durst-Goodwin K.L., Luce K.S., Irvin B.J., Cleary M.L., Brandt S.J., Hiebert S.W. Oncogene 25:5777-5786(2006) [PubMed: 16652147] [Abstract] Cited for: INTERACTION WITH RUNX1 AND RUNX3.
[25]	"SUV39H1 interacts with HTLV-1 Tax and abrogates Tax transactivation of HTLV-1 LTR." Kamoi K., Yamamoto K., Misawa A., Miyake A., Ishida T., Tanaka Y., Mochizuki M., Watanabe T. Retrovirology 3:5-5(2006) [PubMed: 16409643] [Abstract] Cited for: INTERACTION WITH HTLV-1 TAX.
[26]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391, MASS SPECTROMETRY. Tissue: Epithelium.
[27]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF019968 mRNA. Translation: AAB92224.1. CR541746 mRNA. Translation: CAG46546.1. AK223071 mRNA. Translation: BAD96791.1. AF196970 Genomic DNA. No translation available. BC006238 mRNA. Translation: AAH06238.1.
RefSeq	NP_003164.1.
UniGene	Hs.522639
3D structure databases
HSSP	HSSP built from PDB template 1ML9 based on UniProtKB Q8X225.
ModBase	Search...
Protein-protein interaction databases
IntAct	O43463. 10 interactions.
PTM databases
PhosphoSite	O43463.
Proteomic databases
PRIDE	O43463.
Genome annotation databases
Ensembl	ENSG00000101945. Homo sapiens. [Contig view]
GeneID	6839.
KEGG	hsa:6839.
Organism-specific databases
GeneCards	GC0XP048439.
H-InvDB	HIX0016781.
HGNC	HGNC:11479. SUV39H1.
MIM	300254. gene.
PharmGKB	PA36264.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	O43463.
HOVERGEN	O43463.
Gene expression databases
ArrayExpress	O43463.
CleanEx	HS_SUV39H1.
GermOnline	ENSG00000101945. Homo s