positive regulation of phosphatidylinositol 3-kinase signaling
positive regulation of Ras protein signal transduction
Sources:Amigo / QuickGO
Orthologs
Species
Human
Mouse
Entrez
2057
13857
Ensembl
ENSG00000187266
ENSMUSG00000006235
UniProt
P19235
P14753
RefSeq (mRNA)
NM_000121
NM_010149
RefSeq (protein)
NP_000112
NP_034279
Location (UCSC)
Chr 19: 11.38 – 11.38 Mb
Chr 9: 21.87 – 21.87 Mb
PubMed search
[3]
[4]
Wikidata
View/Edit Human
View/Edit Mouse
The erythropoietin receptor (EpoR) is a protein that in humans is encoded by the EPOR gene.[5] EpoR is a 52kDa peptide with a single carbohydrate chain resulting in an approximately 56-57 kDa protein found on the surface of EPO responding cells. It is a member of the cytokine receptor family. EpoR pre-exists as dimers. These dimers were originally thought to be formed by extracellular domain interactions,[6] however, it is now assumed that it is formed by interactions of the transmembrane domain[7][8] and that the original structure of the extracellular interaction site was due to crystallisation conditions and does not depict the native conformation.[9] Binding of a 30 kDa ligand erythropoietin (Epo), changes the receptor's conformational change, resulting in the autophosphorylation of Jak2 kinases that are pre-associated with the receptor (i.e., EpoR does not possess intrinsic kinase activity and depends on Jak2 activity).[10][11] At present, the best-established function of EpoR is to promote proliferation and rescue of erythroid (red blood cell) progenitors from apoptosis.[5]
^ abcGRCh38: Ensembl release 89: ENSG00000187266 – Ensembl, May 2017
^ abcGRCm38: Ensembl release 89: ENSMUSG00000006235 – Ensembl, May 2017
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ ab"Entrez Gene: EPOR erythropoietin receptor".
^Livnah O, Stura EA, Middleton SA, Johnson DL, Jolliffe LK, Wilson IA (Feb 1999). "Crystallographic evidence for preformed dimers of erythropoietin receptor before ligand activation". Science. 283 (5404): 987–90. Bibcode:1999Sci...283..987L. doi:10.1126/science.283.5404.987. PMID 9974392.
^Ebie, Alexandra Z.; Fleming, Karen G. (February 2007). "Dimerization of the Erythropoietin Receptor Transmembrane Domain in Micelles". Journal of Molecular Biology. 366 (2): 517–524. doi:10.1016/j.jmb.2006.11.035. PMID 17173930.
^Li, Qingxin; Wong, Ying Lei; Huang, Qiwei; Kang, CongBao (November 2014). "Structural Insight into the Transmembrane Domain and the Juxtamembrane Region of the Erythropoietin Receptor in Micelles". Biophysical Journal. 107 (10): 2325–2336. Bibcode:2014BpJ...107.2325L. doi:10.1016/j.bpj.2014.10.013. PMC 4241451. PMID 25418301.
^Pang, Xiaodong; Zhou, Huan-Xiang (2012-03-08). "A Common Model for Cytokine Receptor Activation: Combined Scissor-Like Rotation and Self-Rotation of Receptor Dimer Induced by Class I Cytokine". PLOS Computational Biology. 8 (3): e1002427. Bibcode:2012PLSCB...8E2427P. doi:10.1371/journal.pcbi.1002427. ISSN 1553-7358. PMC 3297564. PMID 22412367.
^Youssoufian H, Longmore G, Neumann D, Yoshimura A, Lodish HF (May 1993). "Structure, function, and activation of the erythropoietin receptor". Blood. 81 (9): 2223–36. doi:10.1182/blood.V81.9.2223.2223. PMID 8481505.
^Wilson IA, Jolliffe LK (Dec 1999). "The structure, organization, activation and plasticity of the erythropoietin receptor". Current Opinion in Structural Biology. 9 (6): 696–704. doi:10.1016/S0959-440X(99)00032-9. PMID 10607675.
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