Q9EQQ0 (SUV92_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified July 9, 2014. Version 123. History...
Names and origin
|Protein names||Recommended name:|
Histone-lysine N-methyltransferase SUV39H2
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
|Organism||Mus musculus (Mouse) [Reference proteome]|
|Taxonomic identifier||10090 [NCBI]|
|Taxonomic lineage||Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus|
|Sequence length||477 AA.|
|Protein existence||Evidence at protein level|
General annotation (Comments)
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. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8
S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
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.
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.
Testis specific; predominant expression in type B spermatogonia and preleptotene spermatocytes.
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.
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.
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.
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
Contains 1 chromo domain.
Contains 1 post-SET domain.
Contains 1 pre-SET domain.
Contains 1 SET domain.
The sequence AAF73152.1 differs from that shown. Reason: Erroneous gene model prediction.
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Chain||1 – 477||477||Histone-lysine N-methyltransferase SUV39H2||PRO_0000186060|
|Domain||118 – 176||59||Chromo|
|Domain||256 – 314||59||Pre-SET|
|Domain||317 – 440||124||SET|
|Domain||461 – 477||17||Post-SET|
|Region||328 – 330||3||S-adenosyl-L-methionine binding By similarity|
|Region||397 – 398||2||S-adenosyl-L-methionine binding By similarity|
|Metal binding||258||1||Zinc 1 By similarity|
|Metal binding||258||1||Zinc 2 By similarity|
|Metal binding||260||1||Zinc 1 By similarity|
|Metal binding||263||1||Zinc 1 By similarity|
|Metal binding||263||1||Zinc 3 By similarity|
|Metal binding||268||1||Zinc 1 By similarity|
|Metal binding||269||1||Zinc 1 By similarity|
|Metal binding||269||1||Zinc 2 By similarity|
|Metal binding||296||1||Zinc 2 By similarity|
|Metal binding||296||1||Zinc 3 By similarity|
|Metal binding||300||1||Zinc 2 By similarity|
|Metal binding||302||1||Zinc 3 By similarity|
|Metal binding||306||1||Zinc 3 By similarity|
|Metal binding||400||1||Zinc 4 By similarity|
|Metal binding||465||1||Zinc 4 By similarity|
|Metal binding||467||1||Zinc 4 By similarity|
|Metal binding||472||1||Zinc 4 By similarity|
|Binding site||371||1||S-adenosyl-L-methionine By similarity|
Amino acid modifications
|Modified residue||448||1||Phosphoserine By similarity|
|Modified residue||451||1||Phosphoserine By similarity|
|Modified residue||455||1||Phosphoserine By similarity|
|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|
|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.
|RefSeq||NP_073561.2. NM_022724.4. |
3D structure databases
|SMR||Q9EQQ0. Positions 119-167, 191-477. |
Protein-protein interaction databases
|BioGrid||211103. 2 interactions.|
|IntAct||Q9EQQ0. 1 interaction.|
Protocols and materials databases
Genome annotation databases
|Ensembl||ENSMUST00000027956; ENSMUSP00000027956; ENSMUSG00000026646. |
|UCSC||uc008ied.2. mouse. |
|MGI||MGI:1890396. Suv39h2. |
Gene expression databases
Family and domain databases
|InterPro||IPR023780. Chromo_domain. |
|Pfam||PF00385. Chromo. 1 hit. |
PF05033. Pre-SET. 1 hit.
PF00856. SET. 1 hit.
|PIRSF||PIRSF009343. SUV39_SET. 1 hit. |
|SMART||SM00298. CHROMO. 1 hit. |
SM00508. PostSET. 1 hit.
SM00317. SET. 1 hit.
|SUPFAM||SSF54160. SSF54160. 1 hit. |
|PROSITE||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.
|Accession||Primary (citable) accession number: Q9EQQ0|
Secondary accession number(s): Q8BNK2, Q9CUK3, Q9JLP7
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Chordata Protein Annotation Program|