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EpoR (human)

Overview EpoR erythropoietin receptor: a member of the cytokine receptor family. Mediates erythropoietin-induced erythroblast proliferation, differentiation and survival. Upon EPO stimulation, EPOR dimerizes triggering the JAK2/STAT5 signaling cascade. In some cell types, can also activate STAT1 and STAT3. Forms homodimers on EPO stimulation. Tyrosine-phosphorylated EpoR may bind several SH2 domain-containing proteins including LYN, the adapter protein APS, SHP-1, SHP-2, JAK2, PI3 kinases, STAT5A/B, SOCS3, and CRKL. Defects in the erythropoietin receptor may produce erythroleukemia and familial erythrocytosis. Three alternatively-spliced isoforms have been described. Isoform EPOR-T, missing the cytoplasmic tail, acts as a dominant-negative receptor of EPOR-mediated signaling. Note: This description may include information from UniProtKB. Protein type: Membrane protein, integral; Receptor, cytokine; EC 2.7.10.2 Cellular Component: integral to plasma membrane; extracellular region Molecular Function: identical protein binding; protein binding; erythropoietin receptor activity Biological Process: elevation of cytosolic calcium ion concentration; embryonic development; heart development; brain development; decidualization; signal transduction Reference #:  P19235 (UniProtKB) Alt. Names/Synonyms: EPO-R; EPOR; Erythropoietin receptor; MGC138358 Gene Symbols: EPOR Molecular weight: 55,065 Da Basal Isoelectric point: 4.64  Predict pI for various phosphorylation states

Select Structure to View Below EpoR 1CN4 - A/B=25-249 (human) 1EBA - A/B=34-248 (human) 1EBP - A/B=34-244 (human) 1EER - B/C=31-250 (human) 1ERN - A/B=34-246 (human) 2JIX - B/C/E=25-249 (human)

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB 1CN4 1EBA 1EBP 1EER 1ERN 2JIX  |  ENZYME  |  Phospho3D  |  DISEASE 133100 133171  |  Source  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene

	Sites Implicated In
apoptosis, induced: Y426‑p apoptosis, inhibited: Y368‑p, Y426‑p, Y454‑p, Y456‑p, Y468‑p, Y485‑p, Y489‑p, Y504‑p cell cycle regulation: Y368‑p, Y426‑p cell growth, altered: Y309‑p, Y368‑p, Y426‑p transcription, altered: Y368‑p inhibition: Y426‑p molecular association, regulation: Y368‑p, Y426‑p, Y454‑p, Y456‑p phosphorylation: Y309‑p, Y368‑p, Y426‑p

	Modification Sites and Domains

	Modification Sites in Parent Protein, Orthologs, and Isoforms

SS  SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.	MS  MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.			human
0	1		S69	CFWEEAASAGVGPGN
0	1		A70	FWEEAASAGVGPGNY
0	1		S108-p	GAVRFWCsLPTADTs
0	1		S115-p	sLPTADTsSFVPLEL
0	1		Y180	PMTSHIRYEVDVsAG
0	1		S185-p	IRYEVDVsAGNGAGs
0	1		S192-p	sAGNGAGsVQRVEIL
1	0		Y309-p	GNFQLWLyQNDGCLW
16	0		Y368-p	SEHAQDTyLVLDKWL
8	0		Y426-p	ASAASFEyTILDPSS
5	0		Y454-p	PTPPHLKyLyLVVSD
6	0		Y456-p	PPHLKyLyLVVSDSG
2	0		Y468-p	DSGISTDySSGDSQG
2	0		Y485-p	GGLSDGPySNPyENS
3	0		Y489-p	DGPySNPyENSLIPA
8	0		Y504-p	AEPLPPSyVACS___

	mouse
S69-p	CFWEEAAssGMDFNY
S70-p	FWEEAAssGMDFNYS
S107	GSVRFWCSLPTADTS
S114	SLPTADTSSFVPLEL
Y179	PMTTHIRYEVDVSAG
S184	IRYEVDVSAGNRAGG
G191	SAGNRAGGTQRVEVL
L308	GNFQLWLLQRDGCLW
Y367-p	SEHAQDTyLVLDKWL
Y425-p	TSPSSFEyTILDPSS
Y453-p	PTPPHLKyLyLVVSD
Y455-p	PPHLKyLyLVVSDSG
Y467-p	DSGISTDySSGGSQG
Y484-p	GDSSDGPySHPyENS
Y488-p	DGPySHPyENSLVPD
Y503-p	SEPLHPGyVACS___

	rat
N69	CFWEEAANSGMGFNY
S70	FWEEAANSGMGFNYS
S107	GSMRFWCSLPTADTS
S114	SLPTADTSSFVPLEL
Y179-p	PMTTHIRyEVDVSAG
S184	IRyEVDVSAGNRAGG
G191	SAGNRAGGTQRVEVL
L308	GNFQLWLLQRDGCLW
Y367	SERAQDTYLVLDEWL
Y425	TSPSSFEYTILDPSS
Y453	PTPPHLKYLYLVVSD
Y455	PPHLKYLYLVVSDSG
Y467	DSGISTDYSSGGSQG
Y484	GDSSDGPYSHPYENS
Y488	DGPYSHPYENSLVPD
Y503	TEPLRPSYVACS___

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