G5EEU2 · SET25_CAEEL

  • Protein
    Histone-lysine N-methyltransferase set-25
  • Gene
    set-25
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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).

Catalytic activity

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site645Zn2+ (UniProtKB | ChEBI)
Binding site686S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site700Zn2+ (UniProtKB | ChEBI)
Binding site702Zn2+ (UniProtKB | ChEBI)
Binding site707Zn2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentheterochromatin
Cellular Componentnuclear lamina
Molecular Functiondouble-stranded DNA binding
Molecular Functionhistone H3K9 methyltransferase activity
Molecular Functionhistone H3K9 monomethyltransferase activity
Molecular Functionhistone methyltransferase activity
Molecular Functionmetal ion binding
Biological Processmethylation
Biological Processnegative regulation of gene expression, epigenetic

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Histone-lysine N-methyltransferase set-25
  • EC number
  • Alternative names
    • Histone H3-K9 methyltransferase set-25

Gene names

    • Name
      set-25
    • ORF names
      Y43F4B.3

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • Bristol N2
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Rhabditina > Rhabditomorpha > Rhabditoidea > Rhabditidae > Peloderinae > Caenorhabditis

Accessions

  • Primary accession
    G5EEU2

Proteomes

Organism-specific databases

Subcellular Location

Nucleus
Chromosome
Nucleus lamina
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

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis645No effect on localization to nuclear foci.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004385411-714Histone-lysine N-methyltransferase set-25

Proteomic databases

Expression

Gene expression databases

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region1-214Disordered
Compositional bias16-39Basic and acidic residues
Compositional bias41-56Polar residues
Compositional bias58-85Basic and acidic residues
Compositional bias112-127Polar residues
Compositional bias131-156Basic and acidic residues
Compositional bias169-184Polar residues
Domain547-687SET
Region586-611Disordered
Compositional bias595-611Basic and acidic residues
Domain696-712Post-SET

Domain

The SET domain is not required for localization to nuclear foci.

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    714
  • Mass (Da)
    79,618
  • Last updated
    2011-12-14 v1
  • Checksum
    9FE70D1209CA0D41
MLPAWGTSTEATASHAGWDGDDEGDIRAAYTEDEKKENIPPISLTSVSTNGAYPGQKRRRSESVRTLKPECPPEETQRLRQRRRISATDATQSSRTMNVIEDRKPRVNRARKSQDAPSTSTCGFETPVGTKRKSKAADSQKPPKQSKLRKIDEASTSKAVDNSSKDGKKTTKPAVTQSNRRRSGLSLRPVPIETIFSESSGRESSTEDEADVSHQQRVEKIAKNPIMVVVLPLGPGNYPNNERITVVSTYKSRVNKNCNEARRAQRHGSWSRKGIAFPGIPTKKFTKSDLAKYGAHASNWPAQAAFRSEEGKILIYYEGWTCLTLHRLSVEECARTAPTILEEMSIRDKFIETVKSAAAEEAKLVVEKNQENGIELTLDEALKQIFIEPVPQSSPENVFWIYQDLSYFHTMDNRDLGLAPVFYISSYTQSVRPPCYAYTAINIVDVDAYKRCLESRANMSFADLTGQKIWMPTRSKACENGTKCKCDARFMFLYDPHDVTNLECTPDGKVDFTDFKIDNARIVMECSDACGCSLDCPRRSLQRGQQHPLAVYYEGPEKGFGVRAAANIKAGELVCEYTGDVTLLPTSDPVASSSTKTDDGEEQENPEAPERVDSSYDAAFNAMDTKIIISAKKTGNISRFINHSCDPSSVFVEVYSRRFEEDPLIPRVAVYAIKDIALGEEITIAYYEPGIEWKRSSVKCRCKSTKCMGTLPAF

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias16-39Basic and acidic residues
Compositional bias41-56Polar residues
Compositional bias58-85Basic and acidic residues
Compositional bias112-127Polar residues
Compositional bias131-156Basic and acidic residues
Compositional bias169-184Polar residues
Compositional bias595-611Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BX284603
EMBL· GenBank· DDBJ
CAA16332.3
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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