+ |
MAPK1 | up-regulates
phosphorylation
|
PFAS |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267306 |
Thr619 |
GQGDAPPtPLPTPVD |
Homo sapiens |
|
pmid |
sentence |
32485148 |
T619 in PFAS is required to mediate ERK2-dependent purine synthesis stimulation. We demonstrate that ERK2, but not ERK1, phosphorylates the purine synthesis enzyme PFAS (phosphoribosylformylglycinamidine synthase) at T619 in cells to stimulate de novo purine synthesis. The expression of nonphosphorylatable PFAS (T619A) decreases purine synthesis, RAS-dependent cancer cell-colony formation, and tumor growth. Thus, ERK2-mediated PFAS phosphorylation facilitates the increase in nucleic acid synthesis required for anabolic cell growth and proliferation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Nucleotide Biosynthesis |
+ |
PFAS | down-regulates quantity
chemical modification
|
N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide(2-) |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267309 |
|
|
Homo sapiens |
|
pmid |
sentence |
33179964 |
The first two reactions catalyzed by TGART are sequential and produce FGAR, which is then acted upon by the third enzyme in the pathway, formylglycinamidine synthase (PFAS/FGAMS).The transferred ammonia is then used to convert FGAR to FGAM. The FGAMS protein exhibits interesting biophys ical properties and will be covered later in this review. The FGAM produced by FGAMS is then converted into AIR by the AIRS domain of TGART, resulting in a five membered ring closure. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Nucleotide Biosynthesis |
+ |
PFAS | up-regulates quantity
chemical modification
|
glutamic acid |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267312 |
|
|
Homo sapiens |
|
pmid |
sentence |
33179964 |
The first two reactions catalyzed by TGART are sequential and produce FGAR, which is then acted upon by the third enzyme in the pathway, formylglycinamidine synthase (PFAS/FGAMS).The transferred ammonia is then used to convert FGAR to FGAM. The FGAMS protein exhibits interesting biophys ical properties and will be covered later in this review. The FGAM produced by FGAMS is then converted into AIR by the AIRS domain of TGART, resulting in a five membered ring closure. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PFAS | down-regulates quantity
chemical modification
|
L-glutamine zwitterion |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267310 |
|
|
Homo sapiens |
|
pmid |
sentence |
33179964 |
The first two reactions catalyzed by TGART are sequential and produce FGAR, which is then acted upon by the third enzyme in the pathway, formylglycinamidine synthase (PFAS/FGAMS).The transferred ammonia is then used to convert FGAR to FGAM. The FGAMS protein exhibits interesting biophys ical properties and will be covered later in this review. The FGAM produced by FGAMS is then converted into AIR by the AIRS domain of TGART, resulting in a five membered ring closure. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Nucleotide Biosynthesis |
+ |
PFAS | up-regulates quantity
chemical modification
|
2-formamido-N(1)-(5-O-phosphonato-beta-D-ribosyl)acetamidine |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267311 |
|
|
Homo sapiens |
|
pmid |
sentence |
33179964 |
The first two reactions catalyzed by TGART are sequential and produce FGAR, which is then acted upon by the third enzyme in the pathway, formylglycinamidine synthase (PFAS/FGAMS).The transferred ammonia is then used to convert FGAR to FGAM. The FGAMS protein exhibits interesting biophys ical properties and will be covered later in this review. The FGAM produced by FGAMS is then converted into AIR by the AIRS domain of TGART, resulting in a five membered ring closure. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Nucleotide Biosynthesis |