E3JU34 · E3JU34_PUCGT

Function

function

Histone methyltransferase that specifically trimethylates histone H3 to form H3K79me3. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histone.

Miscellaneous

In contrast to other lysine histone methyltransferases, it does not contain a SET domain, suggesting the existence of another mechanism for methylation of lysine residues of histones.

Catalytic activity

Activity regulation

Ubiquitination of histone H2B to form H2BK123ub1 is required for efficient DOT1 methyltransferase activity on histone H3.

GO annotations

AspectTerm
Cellular Componentnucleus
Molecular Functionhistone H3K79 methyltransferase activity
Molecular Functionhistone H3K79 trimethyltransferase activity
Biological ProcessDNA damage checkpoint signaling
Biological ProcessDNA repair
Biological Processmethylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Histone-lysine N-methyltransferase, H3 lysine-79 specific
  • EC number
  • Alternative names
    • Histone H3-K79 methyltransferase

Gene names

    • ORF names
      PGTG_00890

Organism names

Accessions

  • Primary accession
    E3JU34

Proteomes

Organism-specific databases

Subcellular Location

Keywords

  • Cellular component

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, compositional bias, domain.

Type
IDPosition(s)Description
Region1-22Disordered
Compositional bias7-22Basic and acidic residues
Region33-52Disordered
Compositional bias66-113Polar residues
Region66-139Disordered
Compositional bias152-190Polar residues
Region152-191Disordered
Domain321-657DOT1
Compositional bias334-355Polar residues
Region334-356Disordered

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    658
  • Mass (Da)
    74,721
  • Last updated
    2012-04-18 v2
  • Checksum
    BFA10E8A98747FA9
MDLPPFEVPVDQKHTHNHPRRMDCFFKDPRLLKQQQQQKQTTTQQQQQQQQIRIKTLQSNQQPLPKRIKLNHQQQTATGTNQTTTTTKKSIHSKPQLNNTQQSDQLSKTRETKPLVNQTEDNHHKTQEINNNNTTQDINQTQDINKTQDIKKNQNNNTTQNNFNTQDKQPQDDQNQTNKNPTTNHQDYQLHPIIPRSVDKTITAYSSNHPLNVEPAERKLTSSAKLVNANRNQFKPWFTNQDPQRWPFKKNQDPKIRVGYPTGAHELFRLLVPKNDLDEYRPLDDLLNVITTTLTYYLTPDQSLHFFSEPHPITSPSASVPHSQLNDFSFLNRRSQERSSPEPGRSTTPKIPLSDASLDLSSKPLLKELVKTIRRKNGPEFLGLVGWYNRVIKYLVEGKEIGRQIGSFVGMPQGVWETILGQAYDRQVGPQLELLQGYETWSSNVYGELKPRFVSEIIRLVGLRPGMVFLDLGSGIGNIVLQVALEVGCVAVGFEIMDGCAKLANLQRSELVGRAHSLWGVNLGAPLLFQADFTKDPRVGQWLQQADVVLVNNQVFTPSLNESLSLLFLELKDTAQIVSLKPFISSSFKLNQRNLDSPLAILSRPALRPTPPSTLVANSPGVFSYPSNSVSWTDNPGDFFVSVVNRDKLIRFQESFQA

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias7-22Basic and acidic residues
Compositional bias66-113Polar residues
Compositional bias152-190Polar residues
Compositional bias334-355Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DS178264
EMBL· GenBank· DDBJ
EFP75559.2
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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