+ |
TM9SF4 | up-regulates activity
binding
|
ATP6V1H |
0.275 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266885 |
|
|
Homo sapiens |
HCT-116 Cell, SW-480 Cell |
pmid |
sentence |
25659576 |
Here, we demonstrate that TM9SF4 represents a novel V-ATPase-associated protein involved in V-ATPase activation. We have observed in HCT116 and SW480 colon cancer cell lines that TM9SF4 interacts with the ATP6V1H subunit of the V-ATPase V1 sector. Suppression of TM9SF4 with small interfering RNAs strongly reduces assembly of V-ATPase V0/V1 sectors, thus reversing tumor pH gradient with a decrease of cytosolic pH, alkalization of intracellular vesicles and a reduction of extracellular acidity. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
TFEB | up-regulates quantity by expression
transcriptional regulation
|
ATP6V1H |
0.31 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276535 |
|
|
|
|
pmid |
sentence |
19556463 |
Under aberrant lysosomal storage conditions, TFEB translocated from the cytoplasm to the nucleus, resulting in the activation of its target genes.|Expression analysis of lysosomal genes after TFEB overexpression and silencing. Blue bars show the fold change of the mRNA levels of lysosomal genes in TFEB- versus pcDNA3-transfected cells. |
|
Publications: |
1 |
+ |
ATP6V1H | up-regulates activity
binding
|
AP-2 complex |
0.228 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266887 |
|
|
Mus musculus |
Bone Marrow Stromal Cell |
pmid |
sentence |
29782852 |
ATP6V1H interacts with TGF-β receptor I and AP-2 complex to regulate the proliferation and differentiation of BMSCs. Lack of ATP6V1H function decreases bone formation in vivo |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
ATP6V1H | up-regulates activity
binding
|
TGFBR1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266886 |
|
|
Mus musculus |
Bone Marrow Stromal Cell |
pmid |
sentence |
29782852 |
ATP6V1H interacts with TGF-β receptor I and AP-2 complex to regulate the proliferation and differentiation of BMSCs. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
ATP6V1H | form complex
binding
|
V-ATPase |
0.791 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277749 |
|
|
Homo sapiens |
|
pmid |
sentence |
33065002 |
Vesicular- or vacuolar-type adenosine triphosphatases (V-ATPases) are ATP-driven proton pumps comprised of a cytoplasmic V1 complex for ATP hydrolysis and a membrane-embedded Vo complex for proton transfer. They play important roles in acidification of intracellular vesicles, organelles, and the extracellular milieu in eukaryotes. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |