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Q9EQQ0 (SUV92_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length477 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Chromosomecentromere. 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 class V-like SAM-binding methyltransferase superfamily. 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 processCell cycle
Differentiation
Transcription
Transcription regulation
   Cellular componentCentromere
Chromosome
Nucleus
   LigandS-adenosyl-L-methionine
   Molecular functionChromatin regulator
Methyltransferase
Repressor
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell 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

histone H3-K9 methylation

Inferred from genetic interaction PubMed 15788566. Source: MGI

histone lysine methylation

Inferred from genetic interaction PubMed 23451023. Source: MGI

male meiosis

Inferred from expression pattern Ref.1. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentchromatin

Inferred from sequence or structural similarity. Source: UniProtKB

chromosome, centromeric region

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear heterochromatin

Inferred from direct assay Ref.1. Source: MGI

   Molecular_functionchromatin binding

Inferred from direct assay Ref.1. Source: UniProtKB

histone methyltransferase activity (H3-K9 specific)

Inferred from sequence or structural similarity. Source: UniProtKB

histone-lysine N-methyltransferase activity

Inferred from direct assay PubMed 10949293. Source: UniProtKB

methyltransferase activity

Inferred from direct assay PubMed 10949293. Source: UniProtKB

protein methyltransferase activity

Inferred from direct assay Ref.1. Source: MGI

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 477477Histone-lysine N-methyltransferase SUV39H2
PRO_0000186060

Regions

Domain118 – 17659Chromo
Domain256 – 31459Pre-SET
Domain317 – 440124SET
Domain461 – 47717Post-SET

Amino acid modifications

Modified residue4481Phosphoserine By similarity
Modified residue4511Phosphoserine By similarity
Modified residue4551Phosphoserine By similarity

Experimental info

Sequence conflict31T → A in BAC38921. Ref.2
Sequence conflict1311Missing in AAF73152. Ref.1
Sequence conflict3231K → R in BAB29948. Ref.2
Sequence conflict3231K → R in BAC38921. Ref.2
Sequence conflict3251S → N in AAF73152. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9EQQ0 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 4008D46CF0F07006

FASTA47754,098
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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.
RefSeqNP_073561.2. NM_022724.4.
UniGeneMm.128273.
Mm.23483.

3D structure databases

ProteinModelPortalQ9EQQ0.
SMRQ9EQQ0. Positions 119-167, 191-477.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid211103. 2 interactions.
IntActQ9EQQ0. 1 interaction.

PTM databases

PhosphoSiteQ9EQQ0.

Proteomic databases

PRIDEQ9EQQ0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000027956; ENSMUSP00000027956; ENSMUSG00000026646.
GeneID64707.
KEGGmmu:64707.
UCSCuc008ied.2. mouse.

Organism-specific databases

CTD79723.
MGIMGI:1890396. Suv39h2.

Phylogenomic databases

eggNOGCOG2940.
GeneTreeENSGT00750000117355.
HOGENOMHOG000231244.
HOVERGENHBG055621.
InParanoidQ9EQQ0.
KOK11419.
OrthoDBEOG7RJPR0.
PhylomeDBQ9EQQ0.
TreeFamTF106452.

Gene expression databases

ArrayExpressQ9EQQ0.
BgeeQ9EQQ0.
GenevestigatorQ9EQQ0.

Family and domain databases

InterProIPR023780. 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]
PfamPF00385. Chromo. 1 hit.
PF05033. Pre-SET. 1 hit.
PF00856. SET. 1 hit.
[Graphical view]
PIRSFPIRSF009343. SUV39_SET. 1 hit.
SMARTSM00298. CHROMO. 1 hit.
SM00508. PostSET. 1 hit.
SM00317. SET. 1 hit.
[Graphical view]
SUPFAMSSF54160. SSF54160. 1 hit.
PROSITEPS00598. CHROMO_1. 1 hit.
PS50013. CHROMO_2. 1 hit.
PS50868. POST_SET. 1 hit.
PS50867. PRE_SET. 1 hit.
PS51579. SAM_MT43_SUVAR39_3. 1 hit.
PS50280. SET. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio320183.
PROQ9EQQ0.
SOURCESearch...

Entry information

Entry nameSUV92_MOUSE
AccessionPrimary (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 16, 2014
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot