Q9EQQ0 (SUV92_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone-lysine N-methyltransferase SUV39H2
EC=2.1.1.43

Alternative name(s):
Histone H3-K9 methyltransferase 2
Short name=H3-K9-HMTase 2
Suppressor of variegation 3-9 homolog 2
Short name=Su(var)3-9 homolog 2

Gene names

Name:

Suv39h2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	477 AA.
Sequence status	Complete.
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. 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 cell cycle regulation, transcriptional repression and regulation of telomere length. May participate in regulation of higher-order chromatin organization during spermatogenesis. Ref.4 Ref.5 Ref.6 Ref.7
Catalytic activity	S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
Subunit structure	Interacts with SMAD5 By similarity.
Subcellular location	Nucleus. Chromosome. Chromosome › centromere. Note: Associates with centromeric constitutive heterochromatin during most stages of spermato- and spermiogenesis. Predominantly accumulates at the sex chromosomes present at the XY body.
Tissue specificity	Testis specific; predominant expression in type B spermatogonia and preleptotene spermatocytes.
Developmental stage	Strong expression in early embryos with a peak at E10.5. Expression is down-regulated at E17.5, and is nearly absent during postnatal development. In adult testes, prominent expression in late but not early spermatocytes.
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 By similarity.
Disruption phenotype	Mice lacking Suv39h1 and Suv39h2 display severely impaired viability and chromosomal instabilities that are associated with an increased tumor risk and perturbed chromosome interactions during male meiosis. They also show a higher level of histone H3 with phosphorylated 'Ser-10' and a reduced number of cells in G1 phase and an increased portion of cells with aberrant nuclear morphologies. Ref.4
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.
Sequence caution	The sequence AAF73152.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Cell cycle Differentiation Transcription Transcription regulation
Cellular component	Centromere Chromosome Nucleus
Ligand	S-adenosyl-L-methionine
Molecular function	Chromatin regulator Methyltransferase Repressor Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW chromatin assembly or disassembly Inferred from sequence or structural similarity. Source: UniProtKB chromatin remodeling Inferred from sequence or structural similarity. Source: UniProtKB male meiosis Inferred from expression pattern Ref.1. Source: UniProtKB regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	chromosome, centromeric region Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear heterochromatin Inferred from direct assay Ref.1. Source: MGI
Molecular_function	chromatin binding Inferred from direct assay Ref.1. Source: UniProtKB histone methyltransferase activity (H3-K9 specific) Inferred from sequence or structural similarity. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 477	477	Histone-lysine N-methyltransferase SUV39H2		PRO_0000186060
Regions
	Domain	118 – 176	59	Chromo
	Domain	256 – 314	59	Pre-SET
	Domain	316 – 444	129	SET
	Domain	461 – 477	17	Post-SET
Amino acid modifications
	Modified residue	448	1	Phosphoserine By similarity
	Modified residue	451	1	Phosphoserine By similarity
	Modified residue	455	1	Phosphoserine By similarity
Experimental info
	Sequence conflict	3	1	T → A in BAC38921. Ref.2
	Sequence conflict	131	1	Missing in AAF73152. Ref.1
	Sequence conflict	323	1	K → R in BAB29948. Ref.2
	Sequence conflict	323	1	K → R in BAC38921. Ref.2
	Sequence conflict	325	1	S → N in AAF73152. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9EQQ0 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 4008D46CF0F07006	FASTA	477	54,098
	10 20 30 40 50 60 MATARAKARG SEAGARCHRA PGPPPRPKAR RTARRRRAET LTARRSRPSA GERRAGSQRA 70 80 90 100 110 120 WSGAPRAAVF GDECARGALF KAWCVPCLVS LDTLQELCRK EKLTCKSIGI TKRNLNNYEV 130 140 150 160 170 180 EYLCDYKVAK GVEYYLVKWK GWPDSTNTWE PLRNLRCPQL LRQFSDDKKT YLAQERKCKA 190 200 210 220 230 240 VNSKSLQPAI AEYIVQKAKQ RIALQRWQDY LNRRKNHKGM IFVENTVDLE GPPLDFYYIN 250 260 270 280 290 300 EYRPAPGISI NSEATFGCSC TDCFFDKCCP AEAGVVLAYN KKQQIKIQPG TPIYECNSRC 310 320 330 340 350 360 RCGPECPNRI VQKGTQYSLC IFKTSNGCGW GVKTLVKIKR MSFVMEYVGE VITSEEAERR 370 380 390 400 410 420 GQFYDNKGIT YLFDLDYESD EFTVDAARYG NVSHFVNHSC DPNLQVFSVF IDNLDTRLPR 430 440 450 460 470 IALFSTRTIN AGEELTFDYQ MKGSGEASSD SIDHSPAKKR VRTQCKCGAE TCRGYLN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of Suv39h2, a second histone H3 methyltransferase gene that displays testis-specific expression." O'Carroll D., Scherthan H., Peters A.H.F.M., Opravil S., Haynes A.R., Laible G., Rea S., Schmid M., Lebersorger A., Jerratsch M., Sattler L., Mattei M.-G., Denny P., Brown S.D.M., Schweizer D., Jenuwein T. Mol. Cell. Biol. 20:9423-9433(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], CHARACTERIZATION. Strain: C57BL/6J.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Testis.
[3]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[4]	"Loss of the Suv39h histone methyltransferases impairs mammalian heterochromatin and genome stability." Peters A.H.F.M., O'Carroll D., Scherthan H., Mechtler K., Sauer S., Schofer C., Weipoltshammer K., Pagani M., Lachner M., Kohlmaier A., Opravil S., Doyle M., Sibilia M., Jenuwein T. Cell 107:323-337(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[5]	"Partitioning and plasticity of repressive histone methylation states in mammalian chromatin." Peters A.H.F.M., Kubicek S., Mechtler K., O'Sullivan R.J., Derijck A.A., Perez-Burgos L., Kohlmaier A., Opravil S., Tachibana M., Shinkai Y., Martens J.H.A., Jenuwein T. Mol. Cell 12:1577-1589(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[6]	"Histone methyltransferases direct different degrees of methylation to define distinct chromatin domains." Rice J.C., Briggs S.D., Ueberheide B., Barber C.M., Shabanowitz J., Hunt D.F., Shinkai Y., Allis C.D. Mol. Cell 12:1591-1598(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[7]	"Epigenetic regulation of telomere length in mammalian cells by the Suv39h1 and Suv39h2 histone methyltransferases." Garcia-Cao M., O'Sullivan R., Peters A.H.F.M., Jenuwein T., Blasco M.A. Nat. Genet. 36:94-99(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF149204 Genomic DNA. Translation: AAF73152.1. Sequence problems. AF149205 mRNA. Translation: AAG09134.1. AK015728 mRNA. Translation: BAB29948.1. AK083457 mRNA. Translation: BAC38921.1. AL732620 Genomic DNA. Translation: CAM16043.1.
IPI	IPI00111417.
RefSeq	NP_073561.2. NM_022724.4.
UniGene	Mm.128273. Mm.23483.
3D structure databases
ProteinModelPortal	Q9EQQ0.
SMR	Q9EQQ0. Positions 119-167, 191-477.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9EQQ0. 1 interaction.
PTM databases
PhosphoSite	Q9EQQ0.
Proteomic databases
PRIDE	Q9EQQ0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000027956; ENSMUSP00000027956; ENSMUSG00000026646.
GeneID	64707.
KEGG	mmu:64707.
UCSC	uc008ied.2. mouse.
Organism-specific databases
CTD	79723.
MGI	MGI:1890396. Suv39h2.
Phylogenomic databases
eggNOG	COG2940.
GeneTree	ENSGT00690000101898.
HOGENOM	HOG000231244.
HOVERGEN	HBG055621.
InParanoid	Q9EQQ0.
KO	K11419.
OrthoDB	EOG4RFKSJ.
Gene expression databases
ArrayExpress	Q9EQQ0.
Bgee	Q9EQQ0.
Genevestigator	Q9EQQ0.
GermOnline	ENSMUSG00000026646. Mus musculus.
Family and domain databases
InterPro	IPR023780. Chromo_domain. IPR000953. Chromo_domain/shadow. IPR016197. Chromodomain-like. IPR023779. Chromodomain_CS. IPR011381. Histone_H3-K9_MeTrfase. IPR003616. Post-SET_dom. IPR007728. Pre-SET_dom. IPR001214. SET_dom. [Graphical view]
Pfam	PF00385. Chromo. 1 hit. PF05033. Pre-SET. 1 hit. PF00856. SET. 1 hit. [Graphical view]
PIRSF	PIRSF009343. SUV39_SET. 1 hit.
SMART	SM00298. CHROMO. 1 hit. SM00508. PostSET. 1 hit. SM00317. SET. 1 hit. [Graphical view]
SUPFAM	SSF54160. Chromodomain-like. 1 hit.
PROSITE	PS00598. CHROMO_1. 1 hit. PS50013. CHROMO_2. 1 hit. PS50868. POST_SET. 1 hit. PS50867. PRE_SET. 1 hit. PS50280. SET. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	320183.
SOURCE	Search...

Entry information

Entry name

SUV92_MOUSE

Accession

Primary (citable) accession number: Q9EQQ0
Secondary accession number(s): Q8BNK2, Q9CUK3, Q9JLP7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 15, 2002
Last sequence update:	March 1, 2001
Last modified:	April 3, 2013
This is version 114 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program