| + |
JAK2 | up-regulates activity 
phosphorylation
|
EPOR |
0.812 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251348 |
Tyr368 |
SEHAQDTyLVLDKWL |
|
|
| pmid |
sentence |
| 12441334 |
JAK2 in turn phosphorylates several tyrosine residues on the EpoR-cytosolic domain and probably on JAK2 itself that serve as docking sites for SH2 or protein tyrosine binding domains of downstream signal transduction proteins such as STAT5, phosphatidylinositol 3-kinase, Shc, and tyrosine phosphatases SHP1 and SHP2 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251349 |
Tyr426 |
ASAASFEyTILDPSS |
|
|
| pmid |
sentence |
| 12441334 |
JAK2 in turn phosphorylates several tyrosine residues on the EpoR-cytosolic domain and probably on JAK2 itself that serve as docking sites for SH2 or protein tyrosine binding domains of downstream signal transduction proteins such as STAT5, phosphatidylinositol 3-kinase, Shc, and tyrosine phosphatases SHP1 and SHP2 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251350 |
Tyr454 |
PTPPHLKyLYLVVSD |
|
|
| pmid |
sentence |
| 12441334 |
JAK2 in turn phosphorylates several tyrosine residues on the EpoR-cytosolic domain and probably on JAK2 itself that serve as docking sites for SH2 or protein tyrosine binding domains of downstream signal transduction proteins such as STAT5, phosphatidylinositol 3-kinase, Shc, and tyrosine phosphatases SHP1 and SHP2 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251351 |
Tyr456 |
PPHLKYLyLVVSDSG |
|
|
| pmid |
sentence |
| 12441334 |
JAK2 in turn phosphorylates several tyrosine residues on the EpoR-cytosolic domain and probably on JAK2 itself that serve as docking sites for SH2 or protein tyrosine binding domains of downstream signal transduction proteins such as STAT5, phosphatidylinositol 3-kinase, Shc, and tyrosine phosphatases SHP1 and SHP2 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251352 |
Tyr468 |
DSGISTDySSGDSQG |
|
|
| pmid |
sentence |
| 12441334 |
JAK2 in turn phosphorylates several tyrosine residues on the EpoR-cytosolic domain and probably on JAK2 itself that serve as docking sites for SH2 or protein tyrosine binding domains of downstream signal transduction proteins such as STAT5, phosphatidylinositol 3-kinase, Shc, and tyrosine phosphatases SHP1 and SHP2 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251353 |
Tyr485 |
GGLSDGPySNPYENS |
|
|
| pmid |
sentence |
| 12441334 |
JAK2 in turn phosphorylates several tyrosine residues on the EpoR-cytosolic domain and probably on JAK2 itself that serve as docking sites for SH2 or protein tyrosine binding domains of downstream signal transduction proteins such as STAT5, phosphatidylinositol 3-kinase, Shc, and tyrosine phosphatases SHP1 and SHP2 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251354 |
Tyr489 |
DGPYSNPyENSLIPA |
|
|
| pmid |
sentence |
| 12441334 |
JAK2 in turn phosphorylates several tyrosine residues on the EpoR-cytosolic domain and probably on JAK2 itself that serve as docking sites for SH2 or protein tyrosine binding domains of downstream signal transduction proteins such as STAT5, phosphatidylinositol 3-kinase, Shc, and tyrosine phosphatases SHP1 and SHP2 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251355 |
Tyr504 |
AEPLPPSyVACS |
|
|
| pmid |
sentence |
| 12441334 |
JAK2 in turn phosphorylates several tyrosine residues on the EpoR-cytosolic domain and probably on JAK2 itself that serve as docking sites for SH2 or protein tyrosine binding domains of downstream signal transduction proteins such as STAT5, phosphatidylinositol 3-kinase, Shc, and tyrosine phosphatases SHP1 and SHP2 |
|
| Publications: |
8 |
| + |
PTPN1 | down-regulates activity 
dephosphorylation
|
EPOR |
0.462 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276994 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14527337 |
In vivo interaction between EPO-R and PTP1B suggested that PTP1B dephosphorylates the EPO-R intracellularly.|Protein tyrosine phosphatase 1B participates in the down-regulation of erythropoietin receptor signalling. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
EPO | up-regulates
binding
|
EPOR |
0.877 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-55300 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 9442088 |
Binding of erythropoietin (epo) to the epo receptor (epor) initiates a signaling cascade resulting in tyrosine phosphorylation of several proteins and induction of ap-1 transcription factor(s). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-60663 |
|
|
in vitro |
|
| pmid |
sentence |
| 9774108 |
Human erythropoietin is a haematopoietic cytokine required for the differentiation and proliferation of precursor cells into red blood cells. It activates cells by binding and orientating two cell-surface erythropoietin receptors (EPORs) which trigger an intracellular phosphorylation cascade. |
|
| Publications: |
2 |
Organism: |
Mus Musculus, In Vitro |
| + |
NOSIP | up-regulates activity
ubiquitination
|
EPOR |
0.331 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271477 |
|
|
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 12746455 |
Erythropoietin receptors associate with a ubiquitin ligase, p33RUL, and require its activity for erythropoietin-induced proliferation. This receptor-associated ubiquitin ligase, RUL, co-precipitated with EpoR from mammalian cells and mediated ubiquitination of EpoR. RUL mediates EpoR ubiquitination in COS7 cells and is inducibly ubiquitinated after Epo treatment. This observation is consistent with the lack of effects on EpoR stability by RUL-mediated ubiquitination in COS7 cells (Fig. 4). |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
3.0
EPOR
- 
- 