+ |
DHCR7 | up-regulates quantity
chemical modification
|
cholesterol |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267252 |
|
|
Homo sapiens |
|
pmid |
sentence |
9634533 |
In cholesterol biosynthesis, 7-DHC is converted to cholesterol by the enzyme sterol D7 -reductase. This NADPH-dependent enzyme catalyzes the reduction of the D7 -diene bond in 7-DHC, to form cholesterol. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
cholesta-5,7-dien-3beta-ol | up-regulates quantity
precursor of
|
cholesterol |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267250 |
|
|
Homo sapiens |
|
pmid |
sentence |
9634533 |
In cholesterol biosynthesis, 7-DHC is converted to cholesterol by the enzyme sterol D7 -reductase. This NADPH-dependent enzyme catalyzes the reduction of the D7 -diene bond in 7-DHC, to form cholesterol. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
cholesterol | up-regulates quantity
precursor of
|
pregnenolone |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-268629 |
|
|
Homo sapiens |
|
pmid |
sentence |
33117906 |
The steroidogenic acute regulatory protein (StAR) assists in the transport of cholesterol from the cytosol to the inner mitochondria membrane to be converted into pregnenolone using the P450 side-chain cleavage (P450scc) enzyme. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Zona Glomerulosa |
Pathways: | Sex Hormone Biosynthesis |
+ |
ABCA13 | up-regulates quantity
relocalization
|
cholesterol |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265158 |
|
|
Homo sapiens |
|
pmid |
sentence |
33478937 |
ATP-binding cassette subfamily A member 13 (ABCA13) is predicted to be the largest ABC protein, consisting of 5058 amino acids and a long N-terminal region. Mutations in the ABCA13 gene were reported to increase the susceptibility to schizophrenia, bipolar disorder, and major depression.Here, we examined the biochemical activity of ABCA13 using HEK293 cells transfected with mouse ABCA13. The expression of ABCA13 induced the internalization of cholesterol and gangliosides from the plasma membrane to intracellular vesicles. These findings suggest that ABCA13 accelerates cholesterol internalization by endocytic retrograde transport in neurons and that loss of this function is associated with the pathophysiology of psychiatric disorders. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
cholesterol | up-regulates activity
chemical activation
|
SOAT1 |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265159 |
|
|
Homo sapiens |
|
pmid |
sentence |
31848472 |
Excess cholesterol is esterified by acyl coenzyme A:cholesterol acyltransferase (ACAT; also known as SOAT) to cholesteryl esters |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Liver |
+ |
APOA1 | up-regulates
|
cholesterol |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-252104 |
|
|
Homo sapiens |
|
pmid |
sentence |
20642861 |
ApoA-I increases cholesterol release in mature human adipocytes. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
cholesterol | up-regulates quantity
relocalization
|
RAC1 |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277761 |
|
|
Homo sapiens |
Pancreatic Cancer Cell |
pmid |
sentence |
31827278 |
Accumulation of V-ATPase at the plasma membrane is necessary for the cholesterol-dependent plasma-membrane association of RAC1, a prerequisite for the stimulation of membrane ruffling and macropinocytosis. In line with these observations, immunohistochemical staining of V-ATPase in human pancreatic ductal adenocarcinoma (PDAC) specimens revealed prominent staining at the cell periphery in neoplastic lesions, in con- trast to the predominantly cytoplasmic staining observed in adjacent normal tissues (Fig. 2e). Thus, mutant RAS-dependent plasma mem- brane V-ATPase displayed preferential accumulation in membrane ruffles, consistent with patterns observed in invasive breast, melanoma and pancreatic cancer cells |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CYP11A1 | down-regulates quantity
chemical modification
|
cholesterol |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-268633 |
|
|
Homo sapiens |
|
pmid |
sentence |
33117906 |
The steroidogenic acute regulatory protein (StAR) assists in the transport of cholesterol from the cytosol to the inner mitochondria membrane to be converted into pregnenolone using the P450 side-chain cleavage (P450scc) enzyme. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Zona Glomerulosa |
Pathways: | Sex Hormone Biosynthesis |
+ |
V-ATPase | up-regulates quantity
relocalization
|
cholesterol |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277760 |
|
|
Homo sapiens |
Pancreatic Cancer Cell |
pmid |
sentence |
31827278 |
Accumulation of V-ATPase at the plasma membrane is necessary for the cholesterol-dependent plasma-membrane association of RAC1, a prerequisite for the stimulation of membrane ruffling and macropinocytosis. In line with these observations, immunohistochemical staining of V-ATPase in human pancreatic ductal adenocarcinoma (PDAC) specimens revealed prominent staining at the cell periphery in neoplastic lesions, in con- trast to the predominantly cytoplasmic staining observed in adjacent normal tissues (Fig. 2e). Thus, mutant RAS-dependent plasma mem- brane V-ATPase displayed preferential accumulation in membrane ruffles, consistent with patterns observed in invasive breast, melanoma and pancreatic cancer cells |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
STAR | up-regulates quantity
relocalization
|
cholesterol |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265727 |
|
|
|
|
pmid |
sentence |
17579211 |
StAR transfers cholesterol from the outer to the inner mitochondrial membranes, where the enzyme complex of cholesterol side chain cleavage cytochrome P450 (P450scc) converts it to the first steroid, pregnenolone |
|
Publications: |
1 |
Pathways: | Sex Hormone Biosynthesis |
+ |
OSBP2 | up-regulates quantity
relocalization
|
cholesterol |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264879 |
|
|
|
|
pmid |
sentence |
30925160 |
CK1a1, JNK1 and CDK1 had the highest site-specific activity for ORP4L, while CDK1, GSK3a, CK1a1 and GSK3b showed the highest specificity for the site when corrected for background activity with ORP4L-S4A. Because of the complexity of the serine/proline-rich site, we did not determine which serine(s) in ORP4L were phosphorylated by candidate kinases.|We conclude that phosphorylation of a unique serine/proline motif in the ORD induces a conformation change in ORP4L that enhances interaction with vimentin and cholesterol extraction from membranes. |
|
Publications: |
1 |