Gene interactions and pathways from curated databases and text-mining

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EPOR — JAK2

Pathways - manually collected, often from reviews:

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

Text-mined interactions from Literome

Digicaylioglu et al., Nature 2001 : We show that EPOR mediated activation of Jak2 leads to phosphorylation of the inhibitor of NF-kappaB ( IkappaB ), subsequent nuclear translocation of the transcription factor NF-kappaB, and NF-kappaB dependent transcription of neuroprotective genes
Royer et al., DNA Cell Biol 2004 : Epo dependent proliferation assays and analysis of Jak2 dependent EpoR cell-surface expression showed that these vectors were able to function indistinguishable from the original pMX-EpoR-IRES-GFP
Kakihana et al., Biochem Biophys Res Commun 2005 : Binding studies using various EpoR mutants in hematopoietic cells showed that CaM binds the membrane-proximal 65-amino-acid cytoplasmic region ( amino acids 258-312 ) of EpoR that is critical for activation of Jak2 mediated EpoR signaling ... Together, these results indicate that CaM binds to the membrane-proximal EpoR cytoplasmic region and plays an essential role in activation of Jak2 mediated EpoR signaling
Lu et al., J Biol Chem 2008 (Cell Transformation, Neoplastic) : We further showed that disruption of EpoR dimerization by coexpressing a truncated EpoR disrupted JAK2V617F mediated transformation, indicating that EpoR dimerization plays an essential role in the activation of JAK2V617F
Funakoshi-Tago et al., Mol Cell Biol 2008 : Jak2 FERM domain interaction with the erythropoietin receptor regulates Jak2 kinase activity
Funakoshi-Tago et al., J Biol Chem 2010 (Cell Transformation, Neoplastic...) : Although it remains unclear why the presence of EpoR is required to activate oncogenic signaling via the JAK2 mutant and STAT5, its interacting ability is a target for the treatment of these hematopoietic diseases
Griner et al., Br J Haematol 2013 (Leukemia, Erythroblastic, Acute...) : Recent work has suggested a potential role for cellular cholesterol in the activation of JAK2 by the erythropoietin receptor and in the development of an MPN-like disorder in mice
Klingmüller et al., Cell 1995 : The binding of erythropoietin (EPO) to its receptor ( EPO-R ) activates the protein tyrosine kinase JAK2
Klingmüller et al., Proc Natl Acad Sci U S A 1997 : Homodimerization of the erythropoietin (EPO) receptor ( EPO-R ) in response to EPO binding transiently activates the receptor associated protein tyrosine kinase JAK2
Cohen et al., Biochem J 1997 : Both EPO-R and JAK2 were phosphorylated with similar kinetics by PV treatment, suggesting that JAK2 , as well as protein Tyr kinases different from JAK2, might mediate PV-dependent EPO-R phosphorylation
Chin et al., Blood 1998 : These results suggest that Lyn may play a role in activation of the Jak2/Stat5 and other signaling pathways by the EpoR