Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific
mouse protein (annotated by UniProtKB/Swiss-Prot O88491)
Press Enter · cited answer in seconds
0 sources
Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific
Summary
Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific is a protein[1].
Key Facts
- Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific's instance of is recorded as protein[2].
- Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific's UniProt protein ID is recorded as O88491[3].
- Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific's part of is recorded as Zinc finger, FYVE/PHD-type[4].
- Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific's part of is recorded as Zinc finger, RING/FYVE/PHD-type[5].
- Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific's part of is recorded as Zinc finger, PHD-finger, protein family[6].
- Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific's part of is recorded as Zinc finger, PHD-type, protein family[7].
- Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific's part of is recorded as Post-SET domain, protein family[8].
- Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific's part of is recorded as Zinc finger, RING-type, protein family[9].
- Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific's part of is recorded as SET domain, protein family[10].
- Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific's part of is recorded as PWWP domain, protein family[11].
- Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific's part of is recorded as AWS domain, protein family[12].
- Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific's part of is recorded as Zinc finger, PHD-type, conserved site, protein family[13].
- Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific's has part is recorded as Zinc finger, PHD-type, conserved site[14].
- Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific's has part is recorded as Post-SET domain[15].
- Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific's has part is recorded as SET domain[16].
- Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific's has part is recorded as AWS domain[17].
- Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific's has part is recorded as Zinc finger, RING-type[18].
- Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific's has part is recorded as Zinc finger, PHD-finger[19].
- Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific's has part is recorded as Zinc finger, PHD-type[20].
- Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific's has part is recorded as PWWP domain[21].
- Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific's PDB structure ID is recorded as 2NAA[22].
- Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific's molecular function is recorded as metal ion binding[23].
- Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific's molecular function is recorded as transcription corepressor activity[24].
- Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific's molecular function is recorded as transferase activity[25].
- Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific's molecular function is recorded as histone methyltransferase activity (H4-K20 specific)[26].