| + |
SHMT1 | up-regulates quantity 
chemical modification
|
glycine |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268223 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32439610 |
Serine catabolism initiated by serine hydroxymethyltransferase (SHMT) transfers thegamma-carbon amino acid side chain to THF, forming glycine and 5,10-methylene-THF (me-THF) (Fig. 1). The cytosolic (SHMT1) and mitochondrial (SHMT2) isoforms perform the same reactions. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | One-carbon Metabolism |
| + |
SHMT1 | up-regulates quantity
chemical modification
|
glycine zwitterion |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269689 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11802770 |
HTMLA might be identical to serine hydroxymethyltransferase (SHMT; EC 2.1.2.1), since it has been shown that SHMT purified from rabbit liver acts upon HTML, yielding TMABA and glycine. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Carnitine biosynthesis |
| + |
SHMT1 | up-regulates quantity
chemical modification
|
4-trimethylammoniobutanal |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269688 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11802770 |
HTMLA might be identical to serine hydroxymethyltransferase (SHMT; EC 2.1.2.1), since it has been shown that SHMT purified from rabbit liver acts upon HTML, yielding TMABA and glycine. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Carnitine biosynthesis |
| + |
SHMT1 | up-regulates quantity
chemical modification
|
(6R)-5,10-methylenetetrahydrofolate(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268226 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32439610 |
Serine catabolism initiated by serine hydroxymethyltransferase (SHMT) transfers thegamma-carbon amino acid side chain to THF, forming glycine and 5,10-methylene-THF (me-THF) (Fig. 1). The cytosolic (SHMT1) and mitochondrial (SHMT2) isoforms perform the same reactions. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | One-carbon Metabolism |
| + |
SHMT1 | down-regulates quantity 
chemical modification
|
3-hydroxy-N(6),N(6),N(6)-trimethyl-L-lysine |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269687 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11802770 |
HTMLA might be identical to serine hydroxymethyltransferase (SHMT; EC 2.1.2.1), since it has been shown that SHMT purified from rabbit liver acts upon HTML, yielding TMABA and glycine. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Carnitine biosynthesis |
| + |
MYC | up-regulates quantity by expression
transcriptional regulation
|
SHMT1 |
0.28 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267379 |
|
|
Homo sapiens |
P493-6 Cell |
| pmid |
sentence |
| 18628958 |
Myc regulates the de novo purine and pyrimidine synthetic genes in multiple biological systems. Intriguingly, MYC was found to directly activate the expression of SHMT1, and SHMT2, which are enzymes involved in single carbon metabolism and are essential for dNTP synthesis |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
SHMT1
- 
- 