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Protein Page:
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: Receptor, cytokine; Membrane protein, integral
Chromosomal Location of Human Ortholog: 19p13.3-p13.2
Cellular Component: integral to plasma membrane
Molecular Function: erythropoietin receptor activity; identical protein binding; protein binding
Disease: Erythrocytosis, Familial, 1
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

Protein Structure Not Found.
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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
activity, inhibited: 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  
 

Show Multiple Sequence Alignment



 LTP 

LTP: 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.


 HTP 

HTP: 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 2 S115‑p sLPTADTssFVPLEL
0 1 S116‑p LPTADTssFVPLELR
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
7 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
S115 LPTADTSSFVPLELQ
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
S115 LPTADTSSFVPLELQ
Y179‑p PMTTHIRyEVDVSAG
S184 IRyEVDVSAGNRAGG
G191 SAGNRAGGTQRVEVL
L308 GNFQLWLLQRDGCLW
Y367 SERAQDTYLVLDEWL
Y425 TSPSSFEYTILDPSS
Y453 PTPPHLKYLyLVVSD
Y455‑p PPHLKYLyLVVSDSG
Y467 DSGISTDYSSGGSQG
Y484 GDSSDGPYSHPYENS
Y488 DGPYSHPYENSLVPD
Y503 TEPLRPSYVACS___
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