Relation Results

Summary

Name EPOR
Full Name Erythropoietin receptor
Synonyms EPO-R
Primary ID P19235
Links - -
Type protein
Relations 12
Function Receptor for erythropoietin. Mediates erythropoietin-induced erythroblast proliferation and differentiation. Upon EPO stimulation, EPOR dimerizes trig ...
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Type: Score: Layout: SPV 
0.8110.3320.4630.876JAK2EPORNOSIPPTPN1EPO

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▶Modifications Tables

Relations
Regulator
Mechanism
target
score ℹ
+ JAK2up-regulates activity img/direct-activation.png phosphorylation EPOR 0.811
Identifier Residue Sequence Organism Cell Line
SIGNOR-251348 Tyr368 SEHAQDTyLVLDKWL
pmid sentence
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
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
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
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
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
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
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
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
+ NOSIPup-regulates activity img/direct-activation.png ubiquitination EPOR 0.332
Identifier Residue Sequence Organism Cell Line
SIGNOR-271477 Chlorocebus aethiops COS-7 Cell
pmid sentence
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
+ PTPN1down-regulates activity img/direct_inhibition.png dephosphorylation EPOR 0.463
Identifier Residue Sequence Organism Cell Line
SIGNOR-276994 Homo sapiens
pmid sentence
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
+ EPOup-regulates img/direct-activation.png binding EPOR 0.876
Identifier Residue Sequence Organism Cell Line
SIGNOR-55300 Mus musculus
pmid sentence
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
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
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