Epor
entrez
13857
canonical
uniprot
P14753
canonical
ensembl
ENSMUSG00000006235
resolver
ensp
ENSMUSP00000006397
resolver
genesymbol
Epor
resolver
uniprot
Q3UTV9
resolver
uniprot
Q63852
resolver
uniprot_entry
EPOR_MOUSE
resolver
uniprot_entry
Q3UTV9_MOUSE
resolver
uniprot_sec
Q63852
resolver
amino_acid_sequence
MDKLRVPLWPRVGPLCLLLAGAAWAPSPSLPDPKFESKAALLASRGSEELLCFTQRLEDLVCFWEEAASSGMDFNYSFSYQLEGESRKSCSLHQAPTVRGSVRFWCSLPTADTSSFVPLELQVTEASGSPRYHRIIHINEVVLLDAPAGLLARRAEEGSHVVLRWLPPPGAPMTTHIRYEVDVSAGNRAGGTQRVEVLEGRTECVLSNLRGGTRYTFAVRARMAEPSFSGFWSAWSEPASLLTASDLDPLILTLSLILVLISLLLTVLALLSHRRTLQQKIWPGIPSPESEFEGLFTTHKGNFQLWLLQRDGCLWWSPGSSFPEDPPAHLEVLSEPRWAVTQAGDPGADDEGPLLEPVGSEHAQDTYLVLDKWLLPRTPCSENLSGPGGSVDPVTMDEASETSSCPSDLASKPRPEGTSPSSFEYTILDPSSQLLCPRALPPELPPTPPHLKYLYLVVSDSGISTDYSSGGSQGVHGDSSDGPYSHPYENSLVPDSEPLHPGYVACS
uniprot
proteins
function
FUNCTION: Receptor for erythropoietin, which mediates erythropoietin-induced erythroblast proliferation and differentiation (PubMed:2539263, PubMed:8341708, PubMed:8382775, PubMed:8617735). Upon EPO stimulation, EPOR dimerizes triggering the JAK2/STAT5 signaling cascade (PubMed:2539263, PubMed:8382775, PubMed:8617735). In some cell types, can also activate STAT1 and STAT3. May also activate the LYN tyrosine kinase (PubMed:9573010). {ECO:0000269|PubMed:2539263, ECO:0000269|PubMed:8341708, ECO:0000269|PubMed:8382775, ECO:0000269|PubMed:8617735, ECO:0000269|PubMed:9573010}.
uniprot
proteins
mass_dalton
55194
uniprot
proteins
mutagenesis
MUTAGEN 153; /note="R->C: Reduced JAK2/STAT5 activation."; /evidence="ECO:0000269|PubMed:8657137"; MUTAGEN 232; /note="W->A,C,D,E,G,H,I,K,L,M,N,P,Q,R,S,T,V,Y: Loss of EPO binding."; /evidence="ECO:0000269|PubMed:8617735"; MUTAGEN 232; /note="W->F: Greatly reduced EPO binding."; /evidence="ECO:0000269|PubMed:8617735"; MUTAGEN 233; /note="S->A: Not secreted and loss of EPO binding."; /evidence="ECO:0000269|PubMed:12859190, ECO:0000269|PubMed:8617735"; MUTAGEN 233; /note="S->C,D,E,F,H,I,K,L,M,N,P,Q,R,V,W,Y: Loss of EPO binding."; /evidence="ECO:0000269|PubMed:12859190, ECO:0000269|PubMed:8617735"; MUTAGEN 233; /note="S->G: 50-fold less EPO binding."; /evidence="ECO:0000269|PubMed:12859190, ECO:0000269|PubMed:8617735"; MUTAGEN 233; /note="S->T: 2-fold less EPO binding."; /evidence="ECO:0000269|PubMed:12859190, ECO:0000269|PubMed:8617735"; MUTAGEN 234; /note="A->C,D,G,H,K,N,Q,R,S,T: No change in EPO binding."; /evidence="ECO:0000269|PubMed:12859190, ECO:0000269|PubMed:8617735"; MUTAGEN 234; /note="A->E: Enhanced secretion and increased EPO binding."; /evidence="ECO:0000269|PubMed:12859190, ECO:0000269|PubMed:8617735"; MUTAGEN 234; /note="A->F,I,M,W,Y: Little EPO binding."; /evidence="ECO:0000269|PubMed:12859190, ECO:0000269|PubMed:8617735"; MUTAGEN 234; /note="A->L,P,V: Reduced EPO binding."; /evidence="ECO:0000269|PubMed:12859190, ECO:0000269|PubMed:8617735"; MUTAGEN 235; /note="W->A,C,D,E,G,H,I,K,L,M,N,P,Q,R,S,T,V: Loss of EPO binding."; /evidence="ECO:0000269|PubMed:8617735"; MUTAGEN 235; /note="W->F: 14-fold less EPO binding."; /evidence="ECO:0000269|PubMed:8617735"; MUTAGEN 235; /note="W->Y: 100-fold less EPO binding."; /evidence="ECO:0000269|PubMed:8617735"; MUTAGEN 236; /note="S->A,C,G: Reduced EPO binding."; /evidence="ECO:0000269|PubMed:8617735"; MUTAGEN 236; /note="S->D,E,F,H,I,K,L,M,N,P,Q,R,V,W: Loss of EPO binding."; /evidence="ECO:0000269|PubMed:8617735"; MUTAGEN 236; /note="S->T: No loss of EPO binding."; /evidence="ECO:0000269|PubMed:8617735"; MUTAGEN 236; /note="S->Y: Greatly reduced EPO binding."; /evidence="ECO:0000269|PubMed:8617735"; MUTAGEN 304; /note="Q->L: Greatly reduced JAK2/STAT5 activation and some loss of mitogenic response."; /evidence="ECO:0000269|PubMed:8382775, ECO:0000269|PubMed:8657137"; MUTAGEN 306; /note="W->R: No JAK2 binding nor JAK2/STAT5 activation. No EPO-induced phosphorylation. Complete loss of mitogenic response."; /evidence="ECO:0000269|PubMed:8068943, ECO:0000269|PubMed:8382775, ECO:0000269|PubMed:8657137"; MUTAGEN 317; /note="S->R: Slightly reduced JAK2/STAT5 activation and mitogenic response."; /evidence="ECO:0000269|PubMed:8382775, ECO:0000269|PubMed:8657137"; MUTAGEN 324; /note="E->V: No change in JAK2/STAT5 activation nor mitogenic response."; /evidence="ECO:0000269|PubMed:8382775, ECO:0000269|PubMed:8657137"; MUTAGEN 330; /note="L->R: Reduced JAK2/STAT5 activation."; /evidence="ECO:0000269|PubMed:8382775, ECO:0000269|PubMed:8657137"; MUTAGEN 331; /note="E->A: No change in JAK2/STAT5 activation nor mitogenic response."; /evidence="ECO:0000269|PubMed:8382775, ECO:0000269|PubMed:8657137"; MUTAGEN 331; /note="E->K: Reduced JAK2/STAT5 activation and mitogenic response."; /evidence="ECO:0000269|PubMed:8382775, ECO:0000269|PubMed:8657137"; MUTAGEN 367; /note="Y->F: No STAT5 activation."; /evidence="ECO:0000269|PubMed:8639815, ECO:0000269|PubMed:8657137"; MUTAGEN 425; /note="Y->F: No PTPN11 binding, reduced PTPN11 tyrosine phosphorylation and reduced cell proliferation."; /evidence="ECO:0000269|PubMed:8639815"; MUTAGEN 453..455; /note="YLY->FLF: No binding to PTPN6 SH2 domains. Enhanced JAK2 activation and cell proliferation."; /evidence="ECO:0000269|PubMed:7889566"; MUTAGEN 453; /note="Y->F: No PTPN6 binding, binds PTPN11."; /evidence="ECO:0000269|PubMed:7889566, ECO:0000269|PubMed:8639815"; MUTAGEN 455; /note="Y->F: Binds to PTPN6 and PTPN11 SH2 domains."; /evidence="ECO:0000269|PubMed:7889566, ECO:0000269|PubMed:8639815"; MUTAGEN 467; /note="Y->F: No loss of PTPN11 binding."; /evidence="ECO:0000269|PubMed:8639815"; MUTAGEN 484; /note="Y->F: No loss of PTPN11 binding."; /evidence="ECO:0000269|PubMed:8639815"; MUTAGEN 488; /note="Y->F: No loss of PTPN11 binding."; /evidence="ECO:0000269|PubMed:8639815"; MUTAGEN 503; /note="Y->F: No loss of PTPN11 binding."; /evidence="ECO:0000269|PubMed:8639815
uniprot
proteins
post_translational_modification
PTM: The identity of the C-linked hexose on the WXXW motif has not been determined (PubMed:12859190). It is probably mannose (PubMed:12859190). {ECO:0000269|PubMed:12859190}.; PTM: On EPO stimulation, phosphorylated on C-terminal tyrosine residues by JAK2 (PubMed:7889566, PubMed:8639815, PubMed:8665851). The phosphotyrosine motifs are also recruitment sites for several SH2-containing proteins and adapter proteins which mediate cell proliferation (PubMed:7889566, PubMed:8639815, PubMed:8665851). Phosphorylation on Tyr-453 is required for PTPN6 interaction, Tyr-425 for PTPN11 (PubMed:7889566, PubMed:8639815). Tyr-425 is also required for SOCS3 binding, but Tyr-453/Tyr-455 motif is the preferred binding site (By similarity). {ECO:0000250|UniProtKB:P19235, ECO:0000269|PubMed:7889566, ECO:0000269|PubMed:8639815, ECO:0000269|PubMed:8665851}.; PTM: Ubiquitinated by the ECS(SOCS2) complex following ligand-binding and phosphorylation by JAK2, leading to its degradation by the proteasome (By similarity). Regulation by the ECS(SOCS2) complex acts as a negative feedback loop of erythropoietin-mediated signaling pathway (By similarity). Ubiquitination at Lys-280 mediates receptor internalization, whereas ubiquitination at Lys-452 promotes trafficking of activated receptors to the lysosomes for degradation (PubMed:21183685). Ubiquitinated by NOSIP; appears to be either multi-monoubiquitinated or polyubiquitinated (By similarity). Ubiquitination mediates proliferation and survival of EPO-dependent cells (By similarity). {ECO:0000250|UniProtKB:P19235, ECO:0000269|PubMed:21183685}.
uniprot
proteins
protein_family
Type 1 subfamily
uniprot
proteins
protein_family
Type I cytokine receptor family
uniprot
proteins
pubmed
10660611
uniprot
proteins
pubmed
11290583
uniprot
proteins
pubmed
11443118
uniprot
proteins
pubmed
12444928
uniprot
proteins
pubmed
12859190
uniprot
proteins
pubmed
12930840
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1656233
uniprot
proteins
pubmed
1849897
uniprot
proteins
pubmed
21183685
uniprot
proteins
pubmed
2162479
uniprot
proteins
pubmed
2175360
uniprot
proteins
pubmed
2539263
uniprot
proteins
pubmed
7889566
uniprot
proteins
pubmed
8068943
uniprot
proteins
pubmed
8341708
uniprot
proteins
pubmed
8382775
uniprot
proteins
pubmed
8617735
uniprot
proteins
pubmed
8639815
uniprot
proteins
pubmed
8657137
uniprot
proteins
pubmed
8665851
uniprot
proteins
pubmed
9573010
uniprot
proteins
sequence_length
507
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8341708}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform EPOR-F]: Cell membrane {ECO:0000269|PubMed:2175360}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform EPOR-S]: Secreted {ECO:0000269|PubMed:2175360}.
uniprot
proteins
transmembrane_region
TRANSMEM 250..272; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins