| + |
PRKACA |
phosphorylation
|
IGF2R |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-37839 |
Ser2347 |
TTCCRRSsNVSYKYS |
Homo sapiens |
|
| pmid |
sentence |
| 8318012 |
Pka phosphorylates the cytoplasmic mpr 300 domain at ser20 and at a non-identified site, |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CSNK2A1 |
phosphorylation
|
IGF2R |
0.485 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-37831 |
Ser2409 |
LHGDDQDsEDEVLTI |
Homo sapiens |
|
| pmid |
sentence |
| 8318012 |
The two sites phosphorylated by ck ii in vivo and in vitro are ser82 and ser157. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-37835 |
Ser2484 |
LVSFHDDsDEDLLHI |
Homo sapiens |
|
| pmid |
sentence |
| 8318012 |
The two sites phosphorylated by ck ii in vivo and in vitro are ser82 and ser157. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
GZMB | up-regulates 
binding
|
IGF2R |
0.417 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-84314 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11081635 |
The serine proteinase granzyme b is crucial for the rapid induction of target cell apoptosis by cytotoxic t cells. We now present evidence that this receptor is the cation-independent mannose 6-phosphate/insulin-like growth factor receptor (ci-mpr). Inhibition of the granzyme b ci-mpr interaction prevented granzyme b cell surface binding, uptake, and the induction of apoptosis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PLIN3 | up-regulates activity
relocalization
|
IGF2R |
0.714 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253092 |
|
|
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 9590177 |
TIP47 is present in cytosol and on endosomes and is required for MPR transport from endosomes to the trans-Golgi network in vitro and in vivo. TIP47 recognizes a phenylalanine/tryptophan signal in the tail of the cation-dependent MPR that is essential for its proper sorting within the endosomal pathway. These data suggest that TIP47 binds MPR cytoplasmic domains and facilitates their collection into transport vesicles destined for the Golgi. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
IGF2 | up-regulates
binding
|
IGF2R |
0.751 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-115250 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11867533 |
Insulin-like growth factor ii receptor (igf2r) is a multifunctional cell surface receptor implicated in tumour suppression. Its growth inhibitory activity has been associated with an ability to bind igf-ii. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GCC2 | up-regulates activity
relocalization
|
IGF2R |
0.509 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253085 |
|
|
|
|
| pmid |
sentence |
| 18195106 |
Rab9-dependent transport from late endosomes to the Golgi requires the Rab9 effectors p40 (Diaz et al., 1997) and TIP47 (Diaz and Pfeffer, 1998), a protein that recognizes the cytoplasmic domains of the two types of MPRs and packages them into nascent transport vesicles (Carroll et al., 2001). MPR recycling also utilizes a TGN-localized coiled-coil protein named GCC185 that is also a Rab9 effector |
|
| Publications: |
1 |
| + |
RABEPK | up-regulates activity
relocalization
|
IGF2R |
0.358 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253090 |
|
|
|
|
| pmid |
sentence |
| 9230071 |
P40 is a very potent transport factor in that the pure, recombinant protein can stimulate, significantly, an in vitro transport assay that measures transport of mannose 6-phosphate receptors from endosomes to the trans-Golgi network. The functional importance of p40 is confirmed by the finding that anti-p40 antibodies inhibit in vitro transport. Finally, p40 shows synergy with Rab9 in terms of its ability to stimulate mannose 6-phosphate receptor transport. These data are consistent with a model in which p40 and Rab9 act together to drive the process of transport vesicle docking. |
|
| Publications: |
1 |
| + |
LE-TGN SNARE | up-regulates activity
relocalization
|
IGF2R |
0.465 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253083 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18195106 |
These findings place the retromer complex upstream of both STX10 function and the GCC185 tethering complex in MPR transport. Together, our data suggest that STX10, STX16, Vti1a, and VAMP3 are important for the trafficking of both CD- and CI-MPRs.|Thus, MPRs must pass through a compartment of pH ≤ 5.5 before returning to the Golgi to carry out their biological function. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SNX6 | down-regulates quantity 
binding
|
IGF2R |
0.371 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269443 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 32150533 |
Here, we discovered that the binding between SNX-BARs and CI-MPR or IGF1R is mediated by the phox-homology (PX) domain of SNX5 or SNX6 and a bipartite motif, termed SNX-BAR-binding motif (SBM), in the cargoes. our studies establish that SNX-BARs function as a direct cargo-selecting module for a large set of transmembrane proteins transiting the endosome, in addition to their roles in phospholipid recognition and biogenesis of tubular structures. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SNX5 | down-regulates quantity
binding
|
IGF2R |
0.551 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269442 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 32150533 |
Here, we discovered that the binding between SNX-BARs and CI-MPR or IGF1R is mediated by the phox-homology (PX) domain of SNX5 or SNX6 and a bipartite motif, termed SNX-BAR-binding motif (SBM), in the cargoes. our studies establish that SNX-BARs function as a direct cargo-selecting module for a large set of transmembrane proteins transiting the endosome, in addition to their roles in phospholipid recognition and biogenesis of tubular structures. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
IGF2R
- 
- 