| + |
AURKA | up-regulates activity 
phosphorylation
|
ALDH1A1 |
0.381 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276750 |
Thr267 |
KSNLKRVtLELGGKS |
in vitro |
|
| pmid |
sentence |
| 28193222 |
AURKA phosphorylates ALDH1A1 at three critical residues which exert a multifaceted regulation over its level, enzymatic activity, and quaternary structure. While all three phosphorylation sites contribute to its increased stability, T267 phosphorylation primarily regulates ALDH1A1 activity. AURKA-mediated phosphorylation rapidly dissociates tetrameric ALDH1A1 into a highly active monomeric species. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276748 |
Thr442 |
KDIDKAItISSALQA |
in vitro |
|
| pmid |
sentence |
| 28193222 |
AURKA phosphorylates ALDH1A1 at three critical residues which exert a multifaceted regulation over its level, enzymatic activity, and quaternary structure. While all three phosphorylation sites contribute to its increased stability, T267 phosphorylation primarily regulates ALDH1A1 activity. AURKA-mediated phosphorylation rapidly dissociates tetrameric ALDH1A1 into a highly active monomeric species. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276749 |
Thr493 |
YTEVKTVtVKISQKN |
in vitro |
|
| pmid |
sentence |
| 28193222 |
AURKA phosphorylates ALDH1A1 at three critical residues which exert a multifaceted regulation over its level, enzymatic activity, and quaternary structure. While all three phosphorylation sites contribute to its increased stability, T267 phosphorylation primarily regulates ALDH1A1 activity. AURKA-mediated phosphorylation rapidly dissociates tetrameric ALDH1A1 into a highly active monomeric species. |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
ALDH1A1 | up-regulates quantity
chemical modification
|
all-trans-retinoic acid |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265123 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21621639 |
All-trans-retinoic acid (atRA) provides essential support to diverse biological systems and physiological processes.| An accrual of biochemical, physiological and genetic data have identified specific functional outcomes for the retinol dehydrogenases, RDH1, RDH10, and DHRS9, as physiological catalysts of the first step in atRA biosynthesis, and for the retinal dehydrogenases RALDH1, RALDH2, and RALDH3, as catalysts of the second and irreversible step. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Retinoic Acid Metabolism |
| + |
PRMT3 | down-regulates activity 
binding
|
ALDH1A1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276751 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 33495566 |
We identified the specific residues in the catalytic domain of PRMT3 that facilitate interaction with the C-terminal region of ALDH1A1. PRMT3 inhibits the enzymatic activity of ALDH1A1 and negatively regulates the expression of retinoic acid responsive genes in a methyltransferase activity independent manner. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ALDH1A1 | down-regulates quantity
chemical modification
|
retinal |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265122 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21621639 |
All-trans-retinoic acid (atRA) provides essential support to diverse biological systems and physiological processes.| An accrual of biochemical, physiological and genetic data have identified specific functional outcomes for the retinol dehydrogenases, RDH1, RDH10, and DHRS9, as physiological catalysts of the first step in atRA biosynthesis, and for the retinal dehydrogenases RALDH1, RALDH2, and RALDH3, as catalysts of the second and irreversible step. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Retinoic Acid Metabolism |
| + |
EZH2 | down-regulates quantity by repression 
transcriptional regulation
|
ALDH1A1 |
0.401 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254141 |
|
|
Homo sapiens |
Epithelial Ovarian Cancer Cell |
| pmid |
sentence |
| 22144423 |
For three selected genes (ALDH1A1, SSTR1, and DACT3), we validated their upregulation upon EZH2 knockdown and confirmed the binding of EZH2/H3K27Me3 to their genomic loci. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
ALDH1A1
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- 