| + |
PAS complex | up-regulates quantity 
chemical modification
|
1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate)(5-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253531 |
|
|
in vitro |
|
| pmid |
sentence |
| 17556371 |
Here we have identified and characterized Sac3, a Sac domain phosphatase, as the Fig4 mammalian counterpart. Endogenous Sac3, a widespread 97-kDa protein, formed a stable ternary complex with ArPIKfyve and PIKfyve. Sac3 assembles with PIKfyve and ArPIKfyve in a stable ternary complex and controls PtdIns(3,5)P2 levels. we demonstrate a central function for each component of the core protein machinery for PtdIns(3,5)P2 synthesis and turnover in the formation/detachment (or maturation) of transport vesicle intermediates from early endosomes. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PAS complex | up-regulates 
|
Multivesicular_body_assembly |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253532 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17556371 |
Sac3 assembles with PIKfyve and ArPIKfyve in a stable ternary complex and controls PtdIns(3,5)P2 levels. We further demonstrate a key function for each of the three proteins in the biogenesis of ECV/MVB transport intermediates from early endosomes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PAS complex | down-regulates quantity 
chemical modification
|
1-phosphatidyl-1D-myo-inositol 3-phosphate |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253533 |
|
|
in vitro |
|
| pmid |
sentence |
| 18950639 |
PtdIns(3,5)P2 is synthesized from PtdIns(3)P through the action of mammalian PIKfyve or the yeast counterpart Fab1, both sole enzymes for PtdIns(3,5)P2 synthesis. PIKfyve and Fab1, in turn, are activated by the orthologous proteins, mammalian ArPIKfyve and yeast Vac14, to upregulate intracellular PtdIns(3,5)P2 production. PtdIns(3,5)P2 turnover is catalyzed, at least in part, by mammalian Sac3 or its yeast counterpart Fig4 |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PIKFYVE | form complex 
binding
|
PAS complex |
0.932 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253529 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 17556371 |
Here we have identified and characterized Sac3, a Sac domain phosphatase, as the Fig4 mammalian counterpart. Endogenous Sac3, a widespread 97-kDa protein, formed a stable ternary complex with ArPIKfyve and PIKfyve. Sac3 assembles with PIKfyve and ArPIKfyve in a stable ternary complex and controls PtdIns(3,5)P2 levels. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FIG4 | form complex
binding
|
PAS complex |
0.929 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253528 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 17556371 |
Here we have identified and characterized Sac3, a Sac domain phosphatase, as the Fig4 mammalian counterpart. Endogenous Sac3, a widespread 97-kDa protein, formed a stable ternary complex with ArPIKfyve and PIKfyve. Sac3 assembles with PIKfyve and ArPIKfyve in a stable ternary complex and controls PtdIns(3,5)P2 levels. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
VAC14 | form complex
binding
|
PAS complex |
0.923 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253530 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 17556371 |
Here we have identified and characterized Sac3, a Sac domain phosphatase, as the Fig4 mammalian counterpart. Endogenous Sac3, a widespread 97-kDa protein, formed a stable ternary complex with ArPIKfyve and PIKfyve. Sac3 assembles with PIKfyve and ArPIKfyve in a stable ternary complex and controls PtdIns(3,5)P2 levels. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
PAS complex