| + |
INPP5D | down-regulates activity 
dephosphorylation
|
SYK |
0.429 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268456 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32323266 |
An adaptor protein Dok-3 mediates the suppressive function of LYN. The Dok-3 phosphorylated by LYN upon BCR stimulation forms a complex with GRB2, which allows it to enter into the signalosome and associate with activation of SHIP protein. This translocation facilitates the efficient inhibition of PLCc2 and SYK from activation, subsequently resulting in the suppression of downstream Ca2+ signaling. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | B-cell activation |
| + |
INPP5D | down-regulates activity
binding
|
TRAF6 |
0.341 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261429 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 24817116 |
Of note, SHIP1 was associated with TRAF6 in co-transfected HEK293T cells (Fig. 6A). Moreover, SHIP1 overexpression suppressed TRAF6 autoubiquitination in a dose-dependent manner |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
INPP5D | down-regulates activity
dephosphorylation
|
PLCG2 |
0.319 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268455 |
|
|
Homo sapiens |
B-lymphocyte |
| pmid |
sentence |
| 32323266 |
An adaptor protein Dok-3 mediates the suppressive function of LYN. The Dok-3 phosphorylated by LYN upon BCR stimulation forms a complex with GRB2, which allows it to enter into the signalosome and associate with activation of SHIP protein. This translocation facilitates the efficient inhibition of PLCc2 and SYK from activation, subsequently resulting in the suppression of downstream Ca2+ signaling. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | B-cell activation |
| + |
SHC1 | up-regulates 
binding
|
INPP5D |
0.68 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-66949 |
|
|
Homo sapiens |
B-lymphocyte |
| pmid |
sentence |
| 10207047 |
The results indicate that ship, shc, and grb2 form a ternary complex in stimulated b cells, with grb2 stabilizing the interaction between shc and ship. The interactions between shc, grb2, and ship are therefore analogous to the interactions between shc, grb2, and sos. Shc and grb2 may help to localize ship to the cell membrane, regulating ship's inhibitory function following bcr stimulation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, miRNA in AML |
| + |
ARRB2 | up-regulates activity
binding
|
INPP5D |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261428 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24817116 |
We identified a new adaptor beta-arrestin 2 that associates with phosphorylated TIGIT and mediates recruitment of inositol phosphatase SHIP1 through the ITT-like motif (Fig. 7). Finally, SHIP1 impairs TRAF6 autoubiquitination to abolish NF-kappaB activation, leading to inhibition of IFN- gamma production in NK cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GRB2 | up-regulates activity
binding
|
INPP5D |
0.558 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268449 |
|
|
Homo sapiens |
B-lymphocyte |
| pmid |
sentence |
| 32323266 |
An adaptor protein Dok-3 mediates the suppressive function of LYN. The Dok-3 phosphorylated by LYN upon BCR stimulation forms a complex with GRB2, which allows it to enter into the signalosome and associate with activation of SHIP protein. This translocation facilitates the efficient inhibition of PLCc2 and SYK from activation, subsequently resulting in the suppression of downstream Ca2+ signaling. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, B-cell activation |
| + |
INPP5D | up-regulates quantity
chemical modification
|
phosphatidylinositol bisphosphate |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252427 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23650141 |
PtdIns(3,4)P2 is commonly reported as a product of the SH2 domain-containing inositol 5-phosphatases 1/2 (SHIP1 and SHIP2) that dephosphorylate PtdIns(3,4,5)P3 at the 5-position |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
miR-155 | down-regulates quantity by repression
post transcriptional regulation
|
INPP5D |
0.4 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255764 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24708856 |
We found overexpression of miR-155 led to increase in cJUN, FOS and TRIB2, and decrease in MEIS1, GFI1, cMYC and JARID2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, miRNA in AML |
| + |
INPP5D | down-regulates quantity
chemical modification
|
PIP3 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252428 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12421919 |
Two inositol phosphatases implicated in the degradation of PI(3, 4, 5)P3, namely the 5_ phosphatase Src homology 2 domain containing inositol polyphosphate phosphatase (SHIP) and the 3_ phosphatase and tensin homolog deleted on chromosome ten |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, miRNA in AML, B-cell activation |
3.0
INPP5D
- 
- 