{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P19235","secondaryAccessions":["B2RCG4","Q15443","Q2M205"],"uniProtkbId":"EPOR_HUMAN","entryAudit":{"firstPublicDate":"1990-11-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1990-11-01","entryVersion":255,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"2163695"}],"value":"Erythropoietin receptor"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"2163695"}],"value":"EPO-R"}]},"flag":"Precursor"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"2163695"},{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:3416"}],"value":"EPOR"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P14753"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10388848"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11756159"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2163695"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2163696"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8662939"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9774108"}],"value":"Receptor for erythropoietin, which mediates erythropoietin-induced erythroblast proliferation and differentiation (PubMed:10388848, PubMed:2163695, PubMed:2163696, PubMed:8662939, PubMed:9774108). Upon EPO stimulation, EPOR dimerizes triggering the JAK2/STAT5 signaling cascade (By similarity). In some cell types, can also activate STAT1 and STAT3 (PubMed:11756159). May also activate the LYN tyrosine kinase (By similarity)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1324524"}],"value":"Acts as a dominant-negative receptor of EPOR-mediated signaling"}],"commentType":"FUNCTION","molecule":"Isoform EPOR-T"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P14753"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10374881"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10388848"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11784712"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12027890"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25092874"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7534299"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9774108"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9974392"}],"value":"Forms homodimers on EPO stimulation (PubMed:10388848, PubMed:9774108, PubMed:9974392). The tyrosine-phosphorylated form interacts with several SH2 domain-containing proteins including LYN, the adapter protein SH2B2, PTPN6, PTPN11, JAK2, PI3 kinases, STAT5A/B, SOCS3, CRKL (PubMed:12027890, PubMed:7534299). Interacts with INPP5D/SHIP1 (By similarity). SH2B2 binding inhibits the JAK-STAT signaling (PubMed:10374881). Interacts with RHEX; this interaction occurs in a erythropoietin (EPO)-dependent manner (PubMed:25092874). Interacts with ATXN2L (PubMed:11784712)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"P19235","intActId":"EBI-617321"},"interactantTwo":{"uniProtKBAccession":"Q8WWM7","geneName":"ATXN2L","intActId":"EBI-948363"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P19235","intActId":"EBI-617321"},"interactantTwo":{"uniProtKBAccession":"P01588","geneName":"EPO","intActId":"EBI-1027362"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P19235","intActId":"EBI-617321"},"interactantTwo":{"uniProtKBAccession":"P01588","geneName":"EPO","chainId":"PRO_0000008401","intActId":"EBI-11508463"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P19235","intActId":"EBI-617321"},"interactantTwo":{"uniProtKBAccession":"P19235","geneName":"EPOR","intActId":"EBI-617321"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P19235","intActId":"EBI-617321"},"interactantTwo":{"uniProtKBAccession":"P16885","geneName":"PLCG2","intActId":"EBI-617403"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P19235","intActId":"EBI-617321"},"interactantTwo":{"uniProtKBAccession":"P18031","geneName":"PTPN1","intActId":"EBI-968788"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P19235","intActId":"EBI-617321"},"interactantTwo":{"uniProtKBAccession":"P29350","geneName":"PTPN6","intActId":"EBI-78260"},"numberOfExperiments":11,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P19235","intActId":"EBI-617321"},"interactantTwo":{"uniProtKBAccession":"O14508","geneName":"SOCS2","intActId":"EBI-617737"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P19235","intActId":"EBI-617321"},"interactantTwo":{"uniProtKBAccession":"Q62225","geneName":"Cish","intActId":"EBI-617489"},"numberOfExperiments":4,"organismDiffer":true}]},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P14753"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000255"}],"value":"Single-pass type I membrane protein","id":"SL-9905"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Isoform EPOR-S","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11722595"}],"value":"Secreted and located to the cell surface"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11722595"}],"value":"Secreted","id":"SL-0243"}}]},{"commentType":"ALTERNATIVE PRODUCTS","events":["Alternative splicing"],"isoforms":[{"name":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"1324524"}],"value":"EPOR-F"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"1324524"}],"value":"Full-length form"}],"isoformIds":["P19235-1"],"isoformSequenceStatus":"Displayed"},{"name":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"1324524"}],"value":"EPOR-S"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"1324524"}],"value":"Soluble form"}],"isoformIds":["P19235-2"],"sequenceIds":["VSP_009508","VSP_009509"],"isoformSequenceStatus":"Described"},{"name":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"1324524"}],"value":"EPOR-T"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"1324524"}],"value":"Truncated form"}],"isoformIds":["P19235-3"],"sequenceIds":["VSP_009510","VSP_009511"],"isoformSequenceStatus":"Described"}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2163696"}],"value":"Erythroid cells and erythroid progenitor cells"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1324524"}],"value":"Isoform EPOR-F is the most abundant form in EPO-dependent erythroleukemia cells and in late-stage erythroid progenitors"}],"commentType":"TISSUE SPECIFICITY","molecule":"Isoform EPOR-F"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1324524"}],"value":"Isoform EPOR-S and isoform EPOR-T are the predominant forms in bone marrow"}],"commentType":"TISSUE SPECIFICITY","molecule":"Isoform EPOR-S"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1324524"}],"value":"Isoform EPOR-S and isoform EPOR-T are the predominant forms in bone marrow (PubMed:1324524). Isoform EPOR-T is the most abundant from in early-stage erythroid progenitor cells (PubMed:1324524)"}],"commentType":"TISSUE SPECIFICITY","molecule":"Isoform EPOR-T"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9774108"}],"value":"The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P16310"}],"value":"The box 1 motif is required for JAK interaction and/or activation"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P14753"}],"value":"Contains 1 copy of a cytoplasmic motif that is referred to as the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is involved in modulation of cellular responses. The phosphorylated ITIM motif can bind the SH2 domain of several SH2-containing phosphatases"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P14753"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10374881"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11781573"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12027890"}],"value":"On EPO stimulation, phosphorylated on C-terminal tyrosine residues by JAK2 (PubMed:11781573). The phosphotyrosine motifs are also recruitment sites for several SH2-containing proteins and adapter proteins which mediate cell proliferation (PubMed:10374881). Phosphorylation on Tyr-454 is required for PTPN6 interaction, Tyr-426 for PTPN11 (By similarity). Tyr-426 is also required for SOCS3 binding, but Tyr-454/Tyr-456 motif is the preferred binding site (PubMed:12027890)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P14753"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11781573"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12746455"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31182716"}],"value":"Ubiquitinated by the ECS(SOCS2) complex following ligand-binding and phosphorylation by JAK2, leading to its degradation by the proteasome (PubMed:11781573, PubMed:31182716). Regulation by the ECS(SOCS2) complex acts as a negative feedback loop of erythropoietin-mediated signaling pathway (PubMed:11781573). Ubiquitination at Lys-281 mediates receptor internalization, whereas ubiquitination at Lys-453 promotes trafficking of activated receptors to the lysosomes for degradation (By similarity). Ubiquitinated by NOSIP; appears to be either multi-monoubiquitinated or polyubiquitinated (PubMed:12746455). Ubiquitination mediates proliferation and survival of EPO-dependent cells (By similarity)"}],"commentType":"PTM"},{"commentType":"DISEASE","disease":{"diseaseId":"Erythrocytosis, familial, 1","diseaseAccession":"DI-00479","acronym":"ECYT1","description":"An autosomal dominant disorder characterized by elevated hemoglobin and hematocrit, hypersensitivity of erythroid progenitors to erythropoietin, erythropoietin low serum levels, and no increase in platelets nor leukocytes. 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Type 1 subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Signal","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":24,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Chain","location":{"start":{"value":25,"modifier":"EXACT"},"end":{"value":508,"modifier":"EXACT"}},"description":"Erythropoietin receptor","featureId":"PRO_0000010868"},{"type":"Topological domain","location":{"start":{"value":25,"modifier":"EXACT"},"end":{"value":250,"modifier":"EXACT"}},"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Transmembrane","location":{"start":{"value":251,"modifier":"EXACT"},"end":{"value":273,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Topological 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