| + |
TRMT112 | form complex 
binding
|
TRMT11-TRM112 methyltransferase complex |
0.896 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281119 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 34948388 |
Methylation is an essential epigenetic modification mainly catalysed by S-Adenosyl methionine-dependent methyltransferases (MTases). Several MTases require a cofactor for their metabolic stability and enzymatic activity. TRMT112 is a small evolutionary conserved protein that acts as a co-factor and activator for different MTases involved in rRNA, tRNA and protein methylation. Using a SILAC screen, we pulled down seven methyltransferases-N6AMT1, WBSCR22, METTL5, ALKBH8, THUMPD2, THUMPD3 and TRMT11-as interaction partners of TRMT112. We showed that TRMT112 stabilises all seven MTases in cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TRMT112 | form complex
binding
|
METTL5-TRM112 methyltransferase complex |
0.356 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281122 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 31328227 |
Here, we identify METTL5 as the enzyme responsible for 18S rRNA m6A modification and confirm ZCCHC4 as the 28S rRNA modification enzyme. We show that METTL5 must form a heterodimeric complex with TRMT112, a known methyltransferase activator, to gain metabolic stability in cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TRMT112 | form complex
binding
|
THUMPD2-TRM112 methyltransferase complex |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281125 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 34948388 |
Methylation is an essential epigenetic modification mainly catalysed by S-Adenosyl methionine-dependent methyltransferases (MTases). Several MTases require a cofactor for their metabolic stability and enzymatic activity. TRMT112 is a small evolutionary conserved protein that acts as a co-factor and activator for different MTases involved in rRNA, tRNA and protein methylation. Using a SILAC screen, we pulled down seven methyltransferases-N6AMT1, WBSCR22, METTL5, ALKBH8, THUMPD2, THUMPD3 and TRMT11-as interaction partners of TRMT112. We showed that TRMT112 stabilises all seven MTases in cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TRMT112 | form complex
binding
|
ALKBH8-TRM112 methyltransferase complex |
0.735 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281128 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 34948388 |
Methylation is an essential epigenetic modification mainly catalysed by S-Adenosyl methionine-dependent methyltransferases (MTases). Several MTases require a cofactor for their metabolic stability and enzymatic activity. TRMT112 is a small evolutionary conserved protein that acts as a co-factor and activator for different MTases involved in rRNA, tRNA and protein methylation. Using a SILAC screen, we pulled down seven methyltransferases-N6AMT1, WBSCR22, METTL5, ALKBH8, THUMPD2, THUMPD3 and TRMT11-as interaction partners of TRMT112. We showed that TRMT112 stabilises all seven MTases in cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TRMT112 | form complex
binding
|
N6AMT1-TRM112 methyltransferase complex |
0.922 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281130 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 34948388 |
Methylation is an essential epigenetic modification mainly catalysed by S-Adenosyl methionine-dependent methyltransferases (MTases). Several MTases require a cofactor for their metabolic stability and enzymatic activity. TRMT112 is a small evolutionary conserved protein that acts as a co-factor and activator for different MTases involved in rRNA, tRNA and protein methylation. Using a SILAC screen, we pulled down seven methyltransferases-N6AMT1, WBSCR22, METTL5, ALKBH8, THUMPD2, THUMPD3 and TRMT11-as interaction partners of TRMT112. We showed that TRMT112 stabilises all seven MTases in cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TRMT112 | form complex
binding
|
BUD23-TRM112 methyltransferase complex |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281134 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 34948388 |
Methylation is an essential epigenetic modification mainly catalysed by S-Adenosyl methionine-dependent methyltransferases (MTases). Several MTases require a cofactor for their metabolic stability and enzymatic activity. TRMT112 is a small evolutionary conserved protein that acts as a co-factor and activator for different MTases involved in rRNA, tRNA and protein methylation. Using a SILAC screen, we pulled down seven methyltransferases-N6AMT1, WBSCR22, METTL5, ALKBH8, THUMPD2, THUMPD3 and TRMT11-as interaction partners of TRMT112. We showed that TRMT112 stabilises all seven MTases in cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TRMT112 | form complex
binding
|
THUMPD3-TRM112 methyltransferase complex |
0.352 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281137 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 34948388 |
Methylation is an essential epigenetic modification mainly catalysed by S-Adenosyl methionine-dependent methyltransferases (MTases). Several MTases require a cofactor for their metabolic stability and enzymatic activity. TRMT112 is a small evolutionary conserved protein that acts as a co-factor and activator for different MTases involved in rRNA, tRNA and protein methylation. Using a SILAC screen, we pulled down seven methyltransferases-N6AMT1, WBSCR22, METTL5, ALKBH8, THUMPD2, THUMPD3 and TRMT11-as interaction partners of TRMT112. We showed that TRMT112 stabilises all seven MTases in cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
TRMT112
- 
- 