| + |
SIRT2 | up-regulates activity 
deacetylation
|
PGAM1 |
0.279 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266517 |
Lys100 |
GGLTGLNkAETAAKH |
Homo sapiens |
|
| pmid |
sentence |
| 24786789 |
Here we report that PGAM is acetylated at lysine 100 (K100), an active site residue that is invariably conserved from bacteria, to yeast, plant, and mammals. K100 acetylation is detected in fly, mouse, and human cells and in multiple tissues and decreases PGAM2 activity. The cytosolic protein deacetylase sirtuin 2 (SIRT2) deacetylates and activates PGAM2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glycolysis and Gluconeogenesis |
| + |
PAK1 | down-regulates 
phosphorylation
|
PGAM1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-91594 |
Ser118 |
QVKIWRRsYDVPPPP |
Homo sapiens |
Neutrophil |
| pmid |
sentence |
| 12189148 |
Activated pak1 inhibits glycolysis by association of its catalytic domain with pgam-b and subsequent phosphorylation of the enzyme on serine residues 23 and 118, thereby abolishing pgam activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-91598 |
Ser23 |
WNLENRFsGWYDADL |
Homo sapiens |
Neutrophil |
| pmid |
sentence |
| 12189148 |
Activated pak1 inhibits glycolysis by association of its catalytic domain with pgam-b and subsequent phosphorylation of the enzyme on serine residues 23 and 118, thereby abolishing pgam activity. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PKN1 | down-regulates
phosphorylation
|
PGAM1 |
0.254 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-91602 |
Ser118 |
QVKIWRRsYDVPPPP |
Homo sapiens |
Neutrophil |
| pmid |
sentence |
| 12189148 |
Activated pak1 inhibits glycolysis by association of its catalytic domain with pgam-b and subsequent phosphorylation of the enzyme on serine residues 23 and 118, thereby abolishing pgam activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-91606 |
Ser23 |
WNLENRFsGWYDADL |
Homo sapiens |
Neutrophil |
| pmid |
sentence |
| 12189148 |
Activated pak1 inhibits glycolysis by association of its catalytic domain with pgam-b and subsequent phosphorylation of the enzyme on serine residues 23 and 118, thereby abolishing pgam activity. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PGAM1 | up-regulates quantity
chemical modification
|
2-phosphonato-D-glycerate(3-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266514 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24786789 |
Phosphoglycerate mutase (PGAM) is a glycolytic enzyme that catalyzes the reversible conversion of 3-phosphoglycerate (3-PG) to 2-phosphoglycerate (2-PG; ref. 4). Human genome contains two PGAM genes, PGAM1 (also known as PGAM-B), which is expressed in brain and most other tissues, and PGAM2 (also known as PGAM-M), which is highly expressed in muscle. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glycolysis and Gluconeogenesis |
| + |
PGAM1 | down-regulates quantity
chemical modification
|
3-phosphonato-D-glycerate(3-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266511 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24786789 |
Phosphoglycerate mutase (PGAM) is a glycolytic enzyme that catalyzes the reversible conversion of 3-phosphoglycerate (3-PG) to 2-phosphoglycerate (2-PG; ref. 4). Human genome contains two PGAM genes, PGAM1 (also known as PGAM-B), which is expressed in brain and most other tissues, and PGAM2 (also known as PGAM-M), which is highly expressed in muscle. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glycolysis and Gluconeogenesis |
| + |
FGFR1 | up-regulates activity
phosphorylation
|
PGAM1 |
0.329 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279175 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23653202 |
Nevertheless, these data suggest that FGFR1 dependent tyrosine phosphorylation " further " enhances PGAM1 activation.|Phosphorylation of PGAM1 WT by FGFR1 resulted in a significant increase in the amount of bound 2,3-BPG analogue, whereas substitution of PGAM1 Y26 abolished enhanced binding of cofactor in the presence of rFGFR1 (XREF_FIG). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
PGAM1
- 
- 