G5EEU2 · SET25_CAEEL
- ProteinHistone-lysine N-methyltransferase set-25
- Geneset-25
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids714 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 using mono- and dimethylated H3 'Lys-9' as substrate (PubMed:22939621, PubMed:28428426).
Acts redundantly with the methyltransferase met-2 to position chromosome arms at the nuclear lamina (PubMed:22939621).
Required for small-RNA-induced H3K9 methylation (PubMed:26365259).
Together with met-2, protects and stabilizes repeat-rich genomic regions by suppressing transcription-induced replication stress through methylation of H3K9 (PubMed:27668659).
Suppresses transcription from various repetitive genomic elements through methylation of H3K9; exposure to moderately raised temperature reduces methylation by set-25 leading to de-repression of transcription of repetitive elements lasting at least 3 subsequent generations, despite culture at lower temperatures (PubMed:28428426).
May play a role in transgenerational transmission of environmental information (PubMed:28428426).
Acts redundantly with the methyltransferase met-2 to position chromosome arms at the nuclear lamina (PubMed:22939621).
Required for small-RNA-induced H3K9 methylation (PubMed:26365259).
Together with met-2, protects and stabilizes repeat-rich genomic regions by suppressing transcription-induced replication stress through methylation of H3K9 (PubMed:27668659).
Suppresses transcription from various repetitive genomic elements through methylation of H3K9; exposure to moderately raised temperature reduces methylation by set-25 leading to de-repression of transcription of repetitive elements lasting at least 3 subsequent generations, despite culture at lower temperatures (PubMed:28428426).
May play a role in transgenerational transmission of environmental information (PubMed:28428426).
Catalytic activity
- N6-methyl-L-lysyl9-[histone H3] + S-adenosyl-L-methionine = H+ + N6,N6-dimethyl-L-lysyl9-[histone H3] + S-adenosyl-L-homocysteine
RHEA-COMP:15542 CHEBI:61929 Position: 9+ CHEBI:59789 = CHEBI:15378 + RHEA-COMP:15541 CHEBI:61976 Position: 9+ CHEBI:57856
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | heterochromatin | |
Cellular Component | nuclear lamina | |
Molecular Function | double-stranded DNA binding | |
Molecular Function | histone H3K9 methyltransferase activity | |
Molecular Function | histone H3K9 monomethyltransferase activity | |
Molecular Function | histone methyltransferase activity | |
Molecular Function | metal ion binding | |
Biological Process | methylation | |
Biological Process | negative regulation of gene expression, epigenetic |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameHistone-lysine N-methyltransferase set-25
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Rhabditina > Rhabditomorpha > Rhabditoidea > Rhabditidae > Peloderinae > Caenorhabditis
Accessions
- Primary accessionG5EEU2
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Colocalizes with its own product and hpl-1 in foci in the peripheral region of the nucleus, in a manner dependent on H3K9me3.
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 645 | No effect on localization to nuclear foci. | ||||
Sequence: C → A |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000438541 | 1-714 | Histone-lysine N-methyltransferase set-25 | |||
Sequence: MLPAWGTSTEATASHAGWDGDDEGDIRAAYTEDEKKENIPPISLTSVSTNGAYPGQKRRRSESVRTLKPECPPEETQRLRQRRRISATDATQSSRTMNVIEDRKPRVNRARKSQDAPSTSTCGFETPVGTKRKSKAADSQKPPKQSKLRKIDEASTSKAVDNSSKDGKKTTKPAVTQSNRRRSGLSLRPVPIETIFSESSGRESSTEDEADVSHQQRVEKIAKNPIMVVVLPLGPGNYPNNERITVVSTYKSRVNKNCNEARRAQRHGSWSRKGIAFPGIPTKKFTKSDLAKYGAHASNWPAQAAFRSEEGKILIYYEGWTCLTLHRLSVEECARTAPTILEEMSIRDKFIETVKSAAAEEAKLVVEKNQENGIELTLDEALKQIFIEPVPQSSPENVFWIYQDLSYFHTMDNRDLGLAPVFYISSYTQSVRPPCYAYTAINIVDVDAYKRCLESRANMSFADLTGQKIWMPTRSKACENGTKCKCDARFMFLYDPHDVTNLECTPDGKVDFTDFKIDNARIVMECSDACGCSLDCPRRSLQRGQQHPLAVYYEGPEKGFGVRAAANIKAGELVCEYTGDVTLLPTSDPVASSSTKTDDGEEQENPEAPERVDSSYDAAFNAMDTKIIISAKKTGNISRFINHSCDPSSVFVEVYSRRFEEDPLIPRVAVYAIKDIALGEEITIAYYEPGIEWKRSSVKCRCKSTKCMGTLPAF |
Proteomic databases
Expression
Gene expression databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-214 | Disordered | ||||
Sequence: MLPAWGTSTEATASHAGWDGDDEGDIRAAYTEDEKKENIPPISLTSVSTNGAYPGQKRRRSESVRTLKPECPPEETQRLRQRRRISATDATQSSRTMNVIEDRKPRVNRARKSQDAPSTSTCGFETPVGTKRKSKAADSQKPPKQSKLRKIDEASTSKAVDNSSKDGKKTTKPAVTQSNRRRSGLSLRPVPIETIFSESSGRESSTEDEADVSH | ||||||
Compositional bias | 16-39 | Basic and acidic residues | ||||
Sequence: AGWDGDDEGDIRAAYTEDEKKENI | ||||||
Compositional bias | 41-56 | Polar residues | ||||
Sequence: PISLTSVSTNGAYPGQ | ||||||
Compositional bias | 58-85 | Basic and acidic residues | ||||
Sequence: RRRSESVRTLKPECPPEETQRLRQRRRI | ||||||
Compositional bias | 112-127 | Polar residues | ||||
Sequence: KSQDAPSTSTCGFETP | ||||||
Compositional bias | 131-156 | Basic and acidic residues | ||||
Sequence: KRKSKAADSQKPPKQSKLRKIDEAST | ||||||
Compositional bias | 169-184 | Polar residues | ||||
Sequence: KTTKPAVTQSNRRRSG | ||||||
Domain | 547-687 | SET | ||||
Sequence: HPLAVYYEGPEKGFGVRAAANIKAGELVCEYTGDVTLLPTSDPVASSSTKTDDGEEQENPEAPERVDSSYDAAFNAMDTKIIISAKKTGNISRFINHSCDPSSVFVEVYSRRFEEDPLIPRVAVYAIKDIALGEEITIAYY | ||||||
Region | 586-611 | Disordered | ||||
Sequence: TSDPVASSSTKTDDGEEQENPEAPER | ||||||
Compositional bias | 595-611 | Basic and acidic residues | ||||
Sequence: TKTDDGEEQENPEAPER | ||||||
Domain | 696-712 | Post-SET | ||||
Sequence: SSVKCRCKSTKCMGTLP |
Domain
The SET domain is not required for localization to nuclear foci.
Sequence similarities
Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length714
- Mass (Da)79,618
- Last updated2011-12-14 v1
- Checksum9FE70D1209CA0D41
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 16-39 | Basic and acidic residues | ||||
Sequence: AGWDGDDEGDIRAAYTEDEKKENI | ||||||
Compositional bias | 41-56 | Polar residues | ||||
Sequence: PISLTSVSTNGAYPGQ | ||||||
Compositional bias | 58-85 | Basic and acidic residues | ||||
Sequence: RRRSESVRTLKPECPPEETQRLRQRRRI | ||||||
Compositional bias | 112-127 | Polar residues | ||||
Sequence: KSQDAPSTSTCGFETP | ||||||
Compositional bias | 131-156 | Basic and acidic residues | ||||
Sequence: KRKSKAADSQKPPKQSKLRKIDEAST | ||||||
Compositional bias | 169-184 | Polar residues | ||||
Sequence: KTTKPAVTQSNRRRSG | ||||||
Compositional bias | 595-611 | Basic and acidic residues | ||||
Sequence: TKTDDGEEQENPEAPER |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BX284603 EMBL· GenBank· DDBJ | CAA16332.3 EMBL· GenBank· DDBJ | Genomic DNA |