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Q9EQQ0

- SUV92_MOUSE

UniProt

Q9EQQ0 - SUV92_MOUSE

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Protein

Histone-lysine N-methyltransferase SUV39H2

Gene

Suv39h2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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. Recruited by the large PER complex to the E-box elements of the circadian target genes such as PER2 itself or PER1, contributes to the conversion of local chromatin to a heterochromatin-like repressive state through H3 'Lys-9' trimethylation.5 Publications

Catalytic activityi

S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi258 – 2581Zinc 1By similarity
Metal bindingi258 – 2581Zinc 2By similarity
Metal bindingi260 – 2601Zinc 1By similarity
Metal bindingi263 – 2631Zinc 1By similarity
Metal bindingi263 – 2631Zinc 3By similarity
Metal bindingi268 – 2681Zinc 1By similarity
Metal bindingi269 – 2691Zinc 1By similarity
Metal bindingi269 – 2691Zinc 2By similarity
Metal bindingi296 – 2961Zinc 2By similarity
Metal bindingi296 – 2961Zinc 3By similarity
Metal bindingi300 – 3001Zinc 2By similarity
Metal bindingi302 – 3021Zinc 3By similarity
Metal bindingi306 – 3061Zinc 3By similarity
Binding sitei371 – 3711S-adenosyl-L-methioninePROSITE-ProRule annotation
Metal bindingi400 – 4001Zinc 4By similarity
Metal bindingi465 – 4651Zinc 4By similarity
Metal bindingi467 – 4671Zinc 4By similarity
Metal bindingi472 – 4721Zinc 4By similarity

GO - Molecular functioni

  1. chromatin binding Source: UniProtKB
  2. histone-lysine N-methyltransferase activity Source: UniProtKB
  3. histone methyltransferase activity (H3-K9 specific) Source: UniProtKB
  4. methyltransferase activity Source: UniProtKB
  5. protein methyltransferase activity Source: MGI
  6. transcription regulatory region sequence-specific DNA binding Source: UniProtKB
  7. zinc ion binding Source: InterPro

GO - Biological processi

  1. cell differentiation Source: UniProtKB-KW
  2. chromatin assembly or disassembly Source: UniProtKB
  3. chromatin remodeling Source: UniProtKB
  4. histone H3-K9 dimethylation Source: UniProtKB
  5. histone H3-K9 methylation Source: MGI
  6. histone H3-K9 trimethylation Source: UniProtKB
  7. histone lysine methylation Source: MGI
  8. male meiosis Source: UniProtKB
  9. negative regulation of circadian rhythm Source: UniProtKB
  10. negative regulation of transcription, DNA-templated Source: UniProtKB
  11. rhythmic process Source: UniProtKB-KW
  12. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Methyltransferase, Repressor, Transferase

Keywords - Biological processi

Biological rhythms, Cell cycle, Differentiation, Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, S-adenosyl-L-methionine, Zinc

Names & Taxonomyi

Protein namesi
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 namesi
Name:Suv39h2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:1890396. Suv39h2.

Subcellular locationi

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.

GO - Cellular componenti

  1. chromatin Source: UniProtKB
  2. chromosome, centromeric region Source: UniProtKB-KW
  3. nuclear heterochromatin Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Nucleus

Pathology & Biotechi

Disruption phenotypei

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.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 477477Histone-lysine N-methyltransferase SUV39H2PRO_0000186060Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei448 – 4481PhosphoserineBy similarity
Modified residuei451 – 4511PhosphoserineBy similarity
Modified residuei455 – 4551PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9EQQ0.
PRIDEiQ9EQQ0.

PTM databases

PhosphoSiteiQ9EQQ0.

Expressioni

Tissue specificityi

Testis specific; predominant expression in type B spermatogonia and preleptotene spermatocytes.

Developmental stagei

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.

Gene expression databases

BgeeiQ9EQQ0.
ExpressionAtlasiQ9EQQ0. baseline and differential.
GenevestigatoriQ9EQQ0.

Interactioni

Subunit structurei

Interacts with SMAD5. The large PER complex involved in the histone methylation is composed of at least PER2, CBX3, TRIM28, SUV39H1 and/or SUV39H2; CBX3 mediates the formation of the complex.

Protein-protein interaction databases

BioGridi211103. 2 interactions.
DIPiDIP-32586N.
IntActiQ9EQQ0. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ9EQQ0.
SMRiQ9EQQ0. Positions 119-167, 191-477.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini118 – 17659ChromoPROSITE-ProRule annotationAdd
BLAST
Domaini256 – 31459Pre-SETPROSITE-ProRule annotationAdd
BLAST
Domaini317 – 440124SETPROSITE-ProRule annotationAdd
BLAST
Domaini461 – 47717Post-SETPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni328 – 3303S-adenosyl-L-methionine bindingBy similarity
Regioni397 – 3982S-adenosyl-L-methionine bindingBy similarity

Domaini

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).By similarity
In the pre-SET domain, Cys residues bind 3 zinc ions that are arranged in a triangular cluster; some of these Cys residues contribute to the binding of two zinc ions within the cluster.By similarity

Sequence similaritiesi

Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. Suvar3-9 subfamily.PROSITE-ProRule annotation
Contains 1 chromo domain.PROSITE-ProRule annotation
Contains 1 post-SET domain.PROSITE-ProRule annotation
Contains 1 pre-SET domain.PROSITE-ProRule annotation
Contains 1 SET domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG2940.
GeneTreeiENSGT00760000118855.
HOGENOMiHOG000231244.
HOVERGENiHBG055621.
InParanoidiQ9EQQ0.
KOiK11419.
OrthoDBiEOG7RJPR0.
PhylomeDBiQ9EQQ0.
TreeFamiTF106452.

Family and domain databases

InterProiIPR023780. 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]
PfamiPF00385. Chromo. 1 hit.
PF05033. Pre-SET. 1 hit.
PF00856. SET. 1 hit.
[Graphical view]
PIRSFiPIRSF009343. SUV39_SET. 1 hit.
SMARTiSM00298. CHROMO. 1 hit.
SM00508. PostSET. 1 hit.
SM00317. SET. 1 hit.
[Graphical view]
SUPFAMiSSF54160. SSF54160. 1 hit.
PROSITEiPS00598. 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]

Sequencei

Sequence statusi: Complete.

Q9EQQ0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MATARAKARG SEAGARCHRA PGPPPRPKAR RTARRRRAET LTARRSRPSA
60 70 80 90 100
GERRAGSQRA WSGAPRAAVF GDECARGALF KAWCVPCLVS LDTLQELCRK
110 120 130 140 150
EKLTCKSIGI TKRNLNNYEV EYLCDYKVAK GVEYYLVKWK GWPDSTNTWE
160 170 180 190 200
PLRNLRCPQL LRQFSDDKKT YLAQERKCKA VNSKSLQPAI AEYIVQKAKQ
210 220 230 240 250
RIALQRWQDY LNRRKNHKGM IFVENTVDLE GPPLDFYYIN EYRPAPGISI
260 270 280 290 300
NSEATFGCSC TDCFFDKCCP AEAGVVLAYN KKQQIKIQPG TPIYECNSRC
310 320 330 340 350
RCGPECPNRI VQKGTQYSLC IFKTSNGCGW GVKTLVKIKR MSFVMEYVGE
360 370 380 390 400
VITSEEAERR GQFYDNKGIT YLFDLDYESD EFTVDAARYG NVSHFVNHSC
410 420 430 440 450
DPNLQVFSVF IDNLDTRLPR IALFSTRTIN AGEELTFDYQ MKGSGEASSD
460 470
SIDHSPAKKR VRTQCKCGAE TCRGYLN
Length:477
Mass (Da):54,098
Last modified:March 1, 2001 - v1
Checksum:i4008D46CF0F07006
GO

Sequence cautioni

The sequence AAF73152.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31T → A in BAC38921. (PubMed:16141072)Curated
Sequence conflicti131 – 1311Missing in AAF73152. (PubMed:11094092)Curated
Sequence conflicti323 – 3231K → R in BAB29948. (PubMed:16141072)Curated
Sequence conflicti323 – 3231K → R in BAC38921. (PubMed:16141072)Curated
Sequence conflicti325 – 3251S → N in AAF73152. (PubMed:11094092)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS15652.1.
RefSeqiNP_073561.2. NM_022724.4.
UniGeneiMm.128273.
Mm.23483.

Genome annotation databases

EnsembliENSMUST00000027956; ENSMUSP00000027956; ENSMUSG00000026646.
GeneIDi64707.
KEGGimmu:64707.
UCSCiuc008ied.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS15652.1.
RefSeqi NP_073561.2. NM_022724.4.
UniGenei Mm.128273.
Mm.23483.

3D structure databases

ProteinModelPortali Q9EQQ0.
SMRi Q9EQQ0. Positions 119-167, 191-477.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 211103. 2 interactions.
DIPi DIP-32586N.
IntActi Q9EQQ0. 1 interaction.

PTM databases

PhosphoSitei Q9EQQ0.

Proteomic databases

MaxQBi Q9EQQ0.
PRIDEi Q9EQQ0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000027956 ; ENSMUSP00000027956 ; ENSMUSG00000026646 .
GeneIDi 64707.
KEGGi mmu:64707.
UCSCi uc008ied.2. mouse.

Organism-specific databases

CTDi 79723.
MGIi MGI:1890396. Suv39h2.

Phylogenomic databases

eggNOGi COG2940.
GeneTreei ENSGT00760000118855.
HOGENOMi HOG000231244.
HOVERGENi HBG055621.
InParanoidi Q9EQQ0.
KOi K11419.
OrthoDBi EOG7RJPR0.
PhylomeDBi Q9EQQ0.
TreeFami TF106452.

Miscellaneous databases

NextBioi 320183.
PROi Q9EQQ0.
SOURCEi Search...

Gene expression databases

Bgeei Q9EQQ0.
ExpressionAtlasi Q9EQQ0. baseline and differential.
Genevestigatori Q9EQQ0.

Family and domain databases

InterProi 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 ]
Pfami PF00385. Chromo. 1 hit.
PF05033. Pre-SET. 1 hit.
PF00856. SET. 1 hit.
[Graphical view ]
PIRSFi PIRSF009343. SUV39_SET. 1 hit.
SMARTi SM00298. CHROMO. 1 hit.
SM00508. PostSET. 1 hit.
SM00317. SET. 1 hit.
[Graphical view ]
SUPFAMi SSF54160. SSF54160. 1 hit.
PROSITEi PS00598. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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.
  8. "Temporal orchestration of repressive chromatin modifiers by circadian clock Period complexes."
    Duong H.A., Weitz C.J.
    Nat. Struct. Mol. Biol. 21:126-132(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CIRCADIAN RHYTHMS, IDENTIFIACTION IN A LARGE PER COMPLEX.

Entry informationi

Entry nameiSUV92_MOUSE
AccessioniPrimary (citable) accession number: Q9EQQ0
Secondary accession number(s): Q8BNK2, Q9CUK3, Q9JLP7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: March 1, 2001
Last modified: October 29, 2014
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3