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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: EC 2.7.10.2; Receptor, cytokine; Membrane protein, integral
Cellular Component: integral to plasma membrane; extracellular region
Molecular Function: identical protein binding; protein binding; erythropoietin receptor activity
Biological Process: 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

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


 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 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
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
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 PPHLKYLYLVVSDSG
Y467 DSGISTDYSSGGSQG
Y484 GDSSDGPYSHPYENS
Y488 DGPYSHPYENSLVPD
Y503 TEPLRPSYVACS___
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