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P19235

- EPOR_HUMAN

UniProt

P19235 - EPOR_HUMAN

Protein

Erythropoietin receptor

Gene

EPOR

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 178 (01 Oct 2014)
      Sequence version 1 (01 Nov 1990)
      Previous versions | rss
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    Functioni

    Receptor for erythropoietin. Mediates erythropoietin-induced erythroblast proliferation and differentiation. Upon EPO stimulation, EPOR dimerizes triggering the JAK2/STAT5 signaling cascade. In some cell types, can also activate STAT1 and STAT3. May also activate the LYN tyrosine kinase.
    Isoform EPOR-T acts as a dominant-negative receptor of EPOR-mediated signaling.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei117 – 1171Required for ligand binding
    Sitei368 – 3681Interaction with APS and STAT5, and activationBy similarity
    Sitei426 – 4261Required for STAT5/PTPN11/SOCS3 bindingBy similarity
    Sitei454 – 4541Interaction with PTPN6By similarity
    Sitei456 – 4561Required for STAT1/STAT3 activation
    Sitei485 – 4851Required for CrkL bindingBy similarity

    GO - Molecular functioni

    1. erythropoietin receptor activity Source: UniProtKB
    2. identical protein binding Source: IntAct
    3. protein binding Source: IntAct

    GO - Biological processi

    1. brain development Source: Ensembl
    2. decidualization Source: Ensembl
    3. embryo development Source: Ensembl
    4. erythropoietin-mediated signaling pathway Source: GOC
    5. heart development Source: Ensembl
    6. signal transduction Source: ProtInc

    Keywords - Molecular functioni

    Receptor

    Enzyme and pathway databases

    SignaLinkiP19235.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Erythropoietin receptor
    Short name:
    EPO-R
    Gene namesi
    Name:EPOR
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:3416. EPOR.

    Subcellular locationi

    Isoform EPOR-S : Secreted 1 Publication
    Note: Secreted and located to the cell surface.

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell
    2. integral component of plasma membrane Source: ProtInc

    Keywords - Cellular componenti

    Cell membrane, Membrane, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Erythrocytosis, familial, 1 (ECYT1) [MIM:133100]: An autosomal dominant disorder characterized by increased serum red blood cell mass, elevated hemoglobin and hematocrit, hypersensitivity of erythroid progenitors to erythropoietin, erythropoietin low serum levels, and no increase in platelets nor leukocytes. It has a relatively benign course and does not progress to leukemia.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti487 – 4871N → S in ECYT1 and erythroleukemia. 1 Publication
    Corresponds to variant rs62638745 [ dbSNP | Ensembl ].
    VAR_027372
    Natural varianti488 – 4881P → S in ECYT1. 1 Publication
    Corresponds to variant rs142094773 [ dbSNP | Ensembl ].
    VAR_027373

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi114 – 1141T → A: Little effect on EPO binding. 1 Publication
    Mutagenesisi115 – 1151S → A: Little effect on EPO binding. 1 Publication
    Mutagenesisi116 – 1161S → A: 10-fold reduction in EPO binding. 1 Publication
    Mutagenesisi117 – 1171F → A or L: Greatly reduced EPO binding. 1 Publication
    Mutagenesisi117 – 1171F → W: 60-fold reduction in EPO binding. 1 Publication
    Mutagenesisi117 – 1171F → Y: 8-fold reduction in EPO binding. 1 Publication
    Mutagenesisi118 – 1181V → A: 16-fold reduction in EPO binding. 1 Publication
    Mutagenesisi120 – 1201L → A: Some reduction in EPO binding. 1 Publication
    Mutagenesisi121 – 1211E → A: Little effect on EPO binding. 1 Publication
    Mutagenesisi165 – 1651R → A: Little effect on EPO binding. 1 Publication
    Mutagenesisi174 – 1741M → A: Little effect on EPO binding. 1 Publication
    Mutagenesisi176 – 1761S → A: 16-fold reduction in EPO binding. 1 Publication
    Mutagenesisi177 – 1771H → A: Little effect on EPO binding. 1 Publication
    Mutagenesisi179 – 1791R → A: Little effect on EPO binding. 1 Publication
    Mutagenesisi454 – 4541Y → F: Some loss of SOCS3 binding. 1 Publication
    Mutagenesisi456 – 4561Y → F: Inhibition of STAT1/STAT3 activity. No effect on STAT5 activity. Some loss of SOCS3 binding. 2 Publications
    Mutagenesisi468 – 4681Y → F: No effect on STAT1/STAT3 nor STAT5 activity. 1 Publication

    Keywords - Diseasei

    Congenital erythrocytosis, Disease mutation

    Organism-specific databases

    MIMi133100. phenotype.
    Orphaneti90042. Primary familial polycythemia.
    PharmGKBiPA27834.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Add
    BLAST
    Chaini25 – 508484Erythropoietin receptorPRO_0000010868Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi52 ↔ 62
    Glycosylationi76 – 761N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi91 ↔ 107
    Cross-linki281 – 281Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei368 – 3681Phosphotyrosine; by JAK2By similarity
    Modified residuei426 – 4261Phosphotyrosine; by JAK2By similarity
    Cross-linki453 – 453Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei454 – 4541Phosphotyrosine; by JAK2By similarity
    Modified residuei456 – 4561Phosphotyrosine; by JAK2By similarity
    Modified residuei468 – 4681Phosphotyrosine; by JAK2By similarity
    Modified residuei485 – 4851Phosphotyrosine; by JAK2By similarity
    Modified residuei489 – 4891Phosphotyrosine; by JAK2By similarity
    Modified residuei504 – 5041Phosphotyrosine; by JAK2By similarity

    Post-translational modificationi

    On EPO stimulation, phosphorylated on C-terminal tyrosine residues by JAK2. The phosphotyrosine motifs are also recruitment sites for several SH2-containing proteins and adapter proteins which mediate cell proliferation. Phosphorylation on Tyr-454 is required for PTPN6 interaction, Tyr-426 for PTPN11. Tyr-426 is also required for SOCS3 binding, but Tyr-454/Tyr-456 motif is the preferred binding site.1 Publication
    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. Ubiquitination mediates proliferation and survival of EPO-dependent cells.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiP19235.
    PRIDEiP19235.

    PTM databases

    PhosphoSiteiP19235.

    Expressioni

    Tissue specificityi

    Erythroid cells and erythroid progenitor cells. Isoform EPOR-F is the most abundant form in EPO-dependent erythroleukemia cells and in late-stage erythroid progenitors. Isoform EPOR-S and isoform EPOR-T are the predominant forms in bone marrow. Isoform EPOR-T is the most abundant from in early-stage erythroid progenitor cells.

    Gene expression databases

    ArrayExpressiP19235.
    BgeeiP19235.
    CleanExiHS_EPOR.
    GenevestigatoriP19235.

    Interactioni

    Subunit structurei

    Forms homodimers on EPO stimulation. The tyrosine-phosphorylated form interacts with several SH2 domain-containing proteins including LYN By similarity, the adapter protein APS, PTPN6 By similarity, PTPN11, JAK2, PI3 kinases, STAT5A/B, SOCS3, CRKL By similarity. Interacts with INPP5D/SHIP1 By similarity. The N-terminal SH2 domain of PTPN6 binds Tyr-454 and inhibits signaling through dephosphorylation of JAK2 By similarity. APS binding also inhibits the JAK-STAT signaling. Binding to PTPN11, preferentially through the N-terminal SH2 domain, promotes mitogenesis and phosphorylation of PTPN11 By similarity. Binding of JAK2 (through its N-terminal) promotes cell-surface expression By similarity. Interaction with the ubiquitin ligase NOSIP mediates EPO-induced cell proliferation. Interacts with ATXN2L.By similarity7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-617321,EBI-617321
    ATXN2LQ8WWM72EBI-617321,EBI-948363
    CishQ622254EBI-617321,EBI-617489From a different organism.
    EPOP015882EBI-617321,EBI-1027362
    PLCG2P168853EBI-617321,EBI-617403
    PTPN1P180313EBI-617321,EBI-968788
    PTPN6P2935011EBI-617321,EBI-78260
    SOCS2O145083EBI-617321,EBI-617737

    Protein-protein interaction databases

    BioGridi108371. 30 interactions.
    DIPiDIP-5732N.
    IntActiP19235. 21 interactions.
    MINTiMINT-273225.
    STRINGi9606.ENSP00000222139.

    Structurei

    Secondary structure

    1
    508
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi33 – 4513
    Beta strandi51 – 588
    Beta strandi61 – 677
    Beta strandi76 – 838
    Beta strandi84 – 863
    Beta strandi89 – 913
    Beta strandi93 – 986
    Turni99 – 1013
    Beta strandi102 – 1087
    Helixi111 – 1133
    Beta strandi116 – 1183
    Beta strandi120 – 1267
    Turni127 – 1293
    Beta strandi131 – 1377
    Helixi139 – 1413
    Beta strandi142 – 1443
    Beta strandi149 – 1557
    Turni157 – 1593
    Beta strandi162 – 1676
    Beta strandi169 – 1713
    Helixi175 – 1773
    Beta strandi178 – 1858
    Beta strandi188 – 1903
    Beta strandi195 – 1984
    Beta strandi204 – 2074
    Beta strandi212 – 22413
    Turni226 – 2283
    Beta strandi240 – 2445

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CN4X-ray2.80A/B25-249[»]
    1EBAX-ray2.70A/B34-248[»]
    1EBPX-ray2.80A/B34-244[»]
    1EERX-ray1.90B/C27-250[»]
    1ERNX-ray2.40A/B34-246[»]
    2JIXX-ray3.20B/C/E25-249[»]
    ProteinModelPortaliP19235.
    SMRiP19235. Positions 32-247.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP19235.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini25 – 250226ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini274 – 508235CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei251 – 27323HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini147 – 247101Fibronectin type-IIIPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni454 – 4563Required for high-affinity SOCS3 binding

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi233 – 2375WSXWS motif
    Motifi282 – 2909Box 1 motif
    Motifi452 – 4576ITIM motif

    Domaini

    The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding.
    The box 1 motif is required for JAK interaction and/or activation.

    Sequence similaritiesi

    Contains 1 fibronectin type-III domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG46583.
    HOGENOMiHOG000059639.
    HOVERGENiHBG005595.
    InParanoidiP19235.
    KOiK05079.
    OMAiFMVRARM.
    OrthoDBiEOG74BJS6.
    PhylomeDBiP19235.
    TreeFamiTF336573.

    Family and domain databases

    Gene3Di2.60.40.10. 2 hits.
    InterProiIPR009167. Erythropoietin_rcpt.
    IPR003961. Fibronectin_type3.
    IPR015152. Growth/epo_recpt_lig-bind.
    IPR013783. Ig-like_fold.
    IPR003528. Long_hematopoietin_rcpt_CS.
    [Graphical view]
    PfamiPF09067. EpoR_lig-bind. 1 hit.
    PF00041. fn3. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001959. EPO_receptor. 1 hit.
    SMARTiSM00060. FN3. 1 hit.
    [Graphical view]
    SUPFAMiSSF49265. SSF49265. 2 hits.
    PROSITEiPS50853. FN3. 1 hit.
    PS01352. HEMATOPO_REC_L_F1. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform EPOR-F (identifier: P19235-1) [UniParc]FASTAAdd to Basket

    Also known as: Full-length form

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MDHLGASLWP QVGSLCLLLA GAAWAPPPNL PDPKFESKAA LLAARGPEEL    50
    LCFTERLEDL VCFWEEAASA GVGPGNYSFS YQLEDEPWKL CRLHQAPTAR 100
    GAVRFWCSLP TADTSSFVPL ELRVTAASGA PRYHRVIHIN EVVLLDAPVG 150
    LVARLADESG HVVLRWLPPP ETPMTSHIRY EVDVSAGNGA GSVQRVEILE 200
    GRTECVLSNL RGRTRYTFAV RARMAEPSFG GFWSAWSEPV SLLTPSDLDP 250
    LILTLSLILV VILVLLTVLA LLSHRRALKQ KIWPGIPSPE SEFEGLFTTH 300
    KGNFQLWLYQ NDGCLWWSPC TPFTEDPPAS LEVLSERCWG TMQAVEPGTD 350
    DEGPLLEPVG SEHAQDTYLV LDKWLLPRNP PSEDLPGPGG SVDIVAMDEG 400
    SEASSCSSAL ASKPSPEGAS AASFEYTILD PSSQLLRPWT LCPELPPTPP 450
    HLKYLYLVVS DSGISTDYSS GDSQGAQGGL SDGPYSNPYE NSLIPAAEPL 500
    PPSYVACS 508
    Length:508
    Mass (Da):55,065
    Last modified:November 1, 1990 - v1
    Checksum:iF9F326E162E9512A
    GO
    Isoform EPOR-S (identifier: P19235-2) [UniParc]FASTAAdd to Basket

    Also known as: Soluble form

    The sequence of this isoform differs from the canonical sequence as follows:
         196-241: VEILEGRTEC...FWSAWSEPVS → GTVFLSPDWL...RSWRAAPSVC
         242-508: Missing.

    Show »
    Length:241
    Mass (Da):26,456
    Checksum:i0E74BF60CCFB694D
    GO
    Isoform EPOR-T (identifier: P19235-3) [UniParc]FASTAAdd to Basket

    Also known as: Truncated form

    The sequence of this isoform differs from the canonical sequence as follows:
         306-328: LWLYQNDGCLWWSPCTPFTEDPP → VGGLVVPSVPGLPCFLQPNCRPL
         329-508: Missing.

    Show »
    Length:328
    Mass (Da):35,809
    Checksum:i7A22EFEBA11A430F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti102 – 1021A → R no nucleotide entry (PubMed:2163695)Curated
    Sequence conflicti189 – 1902GA → RP no nucleotide entry (PubMed:2163695)Curated
    Sequence conflicti244 – 2441T → E no nucleotide entry (PubMed:2163695)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti380 – 3801P → A.
    Corresponds to variant rs35423344 [ dbSNP | Ensembl ].
    VAR_033919
    Natural varianti487 – 4871N → S in ECYT1 and erythroleukemia. 1 Publication
    Corresponds to variant rs62638745 [ dbSNP | Ensembl ].
    VAR_027372
    Natural varianti488 – 4881P → S in ECYT1. 1 Publication
    Corresponds to variant rs142094773 [ dbSNP | Ensembl ].
    VAR_027373

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei196 – 24146VEILE…SEPVS → GTVFLSPDWLSSTRARPHVI YFCLLRVPRPDSAPRWRSWR AAPSVC in isoform EPOR-S. 1 PublicationVSP_009508Add
    BLAST
    Alternative sequencei242 – 508267Missing in isoform EPOR-S. 1 PublicationVSP_009509Add
    BLAST
    Alternative sequencei306 – 32823LWLYQ…TEDPP → VGGLVVPSVPGLPCFLQPNC RPL in isoform EPOR-T. 1 PublicationVSP_009510Add
    BLAST
    Alternative sequencei329 – 508180Missing in isoform EPOR-T. 1 PublicationVSP_009511Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M60459 mRNA. Translation: AAA52403.1.
    S45332 Genomic DNA. Translation: AAB23271.1.
    M34986 mRNA. Translation: AAA52401.1.
    AK315097 mRNA. Translation: BAG37561.1.
    CH471106 Genomic DNA. Translation: EAW84205.1.
    BC112153 mRNA. Translation: AAI12154.1.
    M76595 Genomic DNA. Translation: AAA52393.1.
    M77244 Genomic DNA. Translation: AAA52392.1.
    X57282 mRNA. Translation: CAA40550.1.
    CCDSiCCDS12260.1. [P19235-1]
    PIRiA43799. ZUHUR.
    I38208.
    RefSeqiNP_000112.1. NM_000121.3. [P19235-1]
    UniGeneiHs.631624.

    Genome annotation databases

    EnsembliENST00000222139; ENSP00000222139; ENSG00000187266. [P19235-1]
    ENST00000592375; ENSP00000467809; ENSG00000187266. [P19235-3]
    GeneIDi2057.
    KEGGihsa:2057.
    UCSCiuc002mrj.2. human. [P19235-1]

    Polymorphism databases

    DMDMi119524.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M60459 mRNA. Translation: AAA52403.1 .
    S45332 Genomic DNA. Translation: AAB23271.1 .
    M34986 mRNA. Translation: AAA52401.1 .
    AK315097 mRNA. Translation: BAG37561.1 .
    CH471106 Genomic DNA. Translation: EAW84205.1 .
    BC112153 mRNA. Translation: AAI12154.1 .
    M76595 Genomic DNA. Translation: AAA52393.1 .
    M77244 Genomic DNA. Translation: AAA52392.1 .
    X57282 mRNA. Translation: CAA40550.1 .
    CCDSi CCDS12260.1. [P19235-1 ]
    PIRi A43799. ZUHUR.
    I38208.
    RefSeqi NP_000112.1. NM_000121.3. [P19235-1 ]
    UniGenei Hs.631624.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CN4 X-ray 2.80 A/B 25-249 [» ]
    1EBA X-ray 2.70 A/B 34-248 [» ]
    1EBP X-ray 2.80 A/B 34-244 [» ]
    1EER X-ray 1.90 B/C 27-250 [» ]
    1ERN X-ray 2.40 A/B 34-246 [» ]
    2JIX X-ray 3.20 B/C/E 25-249 [» ]
    ProteinModelPortali P19235.
    SMRi P19235. Positions 32-247.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108371. 30 interactions.
    DIPi DIP-5732N.
    IntActi P19235. 21 interactions.
    MINTi MINT-273225.
    STRINGi 9606.ENSP00000222139.

    Chemistry

    BindingDBi P19235.
    ChEMBLi CHEMBL1817.
    DrugBanki DB00012. Darbepoetin alfa.
    DB00016. Epoetin alfa.
    GuidetoPHARMACOLOGYi 1718.

    PTM databases

    PhosphoSitei P19235.

    Polymorphism databases

    DMDMi 119524.

    Proteomic databases

    PaxDbi P19235.
    PRIDEi P19235.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000222139 ; ENSP00000222139 ; ENSG00000187266 . [P19235-1 ]
    ENST00000592375 ; ENSP00000467809 ; ENSG00000187266 . [P19235-3 ]
    GeneIDi 2057.
    KEGGi hsa:2057.
    UCSCi uc002mrj.2. human. [P19235-1 ]

    Organism-specific databases

    CTDi 2057.
    GeneCardsi GC19M011489.
    H-InvDB HIX0080119.
    HGNCi HGNC:3416. EPOR.
    MIMi 133100. phenotype.
    133171. gene.
    neXtProti NX_P19235.
    Orphaneti 90042. Primary familial polycythemia.
    PharmGKBi PA27834.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG46583.
    HOGENOMi HOG000059639.
    HOVERGENi HBG005595.
    InParanoidi P19235.
    KOi K05079.
    OMAi FMVRARM.
    OrthoDBi EOG74BJS6.
    PhylomeDBi P19235.
    TreeFami TF336573.

    Enzyme and pathway databases

    SignaLinki P19235.

    Miscellaneous databases

    ChiTaRSi EPOR. human.
    EvolutionaryTracei P19235.
    GeneWikii Erythropoietin_receptor.
    GenomeRNAii 2057.
    NextBioi 8365.
    PROi P19235.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P19235.
    Bgeei P19235.
    CleanExi HS_EPOR.
    Genevestigatori P19235.

    Family and domain databases

    Gene3Di 2.60.40.10. 2 hits.
    InterProi IPR009167. Erythropoietin_rcpt.
    IPR003961. Fibronectin_type3.
    IPR015152. Growth/epo_recpt_lig-bind.
    IPR013783. Ig-like_fold.
    IPR003528. Long_hematopoietin_rcpt_CS.
    [Graphical view ]
    Pfami PF09067. EpoR_lig-bind. 1 hit.
    PF00041. fn3. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001959. EPO_receptor. 1 hit.
    SMARTi SM00060. FN3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49265. SSF49265. 2 hits.
    PROSITEi PS50853. FN3. 1 hit.
    PS01352. HEMATOPO_REC_L_F1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The gene for the human erythropoietin receptor: analysis of the coding sequence and assignment to chromosome 19p."
      Winkelmann J.C., Penny L.A., Deaven L.L., Forget B.G., Jenkins R.B.
      Blood 76:24-30(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Human erythropoietin receptor: cloning, expression, and biologic characterization."
      Jones S.S., D'Andrea A.D., Haines L.L., Wong G.G.
      Blood 76:31-35(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM EPOR-F).
      Tissue: Erythroleukemia and Fetal liver.
    3. "Cloning of the human erythropoietin receptor gene."
      Noguchi C.T., Bae K.S., Chin K., Wada Y., Schechter A.N., Hankins W.D.
      Blood 78:2548-2556(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Placenta.
    4. "The erythropoietin receptor gene: cloning and identification of multiple transcripts in an erythroid cell line OCIM1."
      Ehrenman K., St John T.
      Exp. Hematol. 19:973-977(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM EPOR-F).
      Tissue: Erythroleukemia.
    5. "A truncated erythropoietin receptor that fails to prevent programmed cell death of erythroid cells."
      Nakamura Y., Komatsu N., Nakauchi H.
      Science 257:1138-1141(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS EPOR-F; EPOR-S AND EPOR-T).
      Tissue: Bone marrow and Megakaryoblast.
    6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM EPOR-F).
      Tissue: Caudate nucleus.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM EPOR-F).
      Tissue: Brain.
    9. "Cloning of the gene encoding the human erythropoietin receptor."
      Maouche L., Tournamille C., Hattab C., Boffa G., Cartron J.-P., Chretien S.
      Blood 78:2557-2563(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-96.
      Tissue: Placenta.
    10. "Genomic organization of the human erythropoietin receptor gene."
      Penny L.A., Forget B.G.
      Genomics 11:974-980(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17.
    11. "Isolation of a cDNA encoding a potential soluble receptor for human erythropoietin."
      Todokoro K., Kuramochi S., Nagasawa T., Abe T., Ikawa Y.
      Gene 106:283-284(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (EPOR-S).
      Tissue: Erythroid cell.
    12. "Identification of the human erythropoietin receptor region required for Stat1 and Stat3 activation."
      Kirito K., Nakajima K., Watanabe T., Uchida M., Tanaka M., Ozawa K., Komatsu N.
      Blood 99:102-110(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: STAT1/STAT3 ACTIVATION, MUTAGENESIS OF TYR-456 AND TYR-468.
    13. "Involvement of SH2-containing phosphotyrosine phosphatase Syp in erythropoietin receptor signal transduction pathways."
      Tauchi T., Feng G.-S., Shen R., Hoatlin M., Bagby G.C. Jr., Kabat D., Lu L., Broxmeyer H.E.
      J. Biol. Chem. 270:5631-5635(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PTPN11.
    14. "Identification of a critical ligand binding determinant of the human erythropoietin receptor. Evidence for common ligand binding motifs in the cytokine receptor family."
      Middleton S.A., Johnson D.L., Jin R., McMahon F.J., Collins A., Tullai J., Gruninger R.H., Jolliffe L.K., Mulcahy L.S.
      J. Biol. Chem. 271:14045-14054(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: LIGAND-BINDING SITE, MUTAGENESIS OF THR-114; SER-115; SER-116; PHE-117; VAL-118; LEU-120; GLU-121; ARG-165; MET-174; SER-176; HIS-177 AND ARG-179.
    15. "Increased cell surface expression of C-terminal truncated erythropoietin receptors in polycythemia."
      Motohashi T., Nakamura Y., Osawa M., Hiroyama T., Iwama A., Shibuya A., Nakauchi H.
      Eur. J. Haematol. 67:88-93(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION (ISOFORM EPOR-S).
    16. "A new high affinity binding site for suppressor of cytokine signaling-3 on the erythropoietin receptor."
      Hoertner M., Nielsch U., Mayr L.M., Heinrich P.C., Haan S.
      Eur. J. Biochem. 269:2516-2526(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SOCS3, MUTAGENESIS OF TYR-454 AND TYR-456.
    17. "Erythropoietin receptors associate with a ubiquitin ligase, p33RUL, and require its activity for erythropoietin-induced proliferation."
      Friedman A.D., Nimbalkar D., Quelle F.W.
      J. Biol. Chem. 278:26851-26861(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NOSIP.
    18. "APS, an adaptor protein containing pleckstrin homology (PH) and Src homology-2 (SH2) domains inhibits the JAK-STAT pathway in collaboration with c-Cbl."
      Wakioka T., Sasaki A., Mitsui K., Yokouchi M., Inoue A., Komiya S., Yoshimura A.
      Leukemia 13:760-767(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, INTERACTION WITH APS.
    19. "Cloning and characterization of a family of proteins associated with Mpl."
      Meunier C.F., Bordereaux D., Porteu F., Gisselbrecht S., Chretien S., Courtois G.
      J. Biol. Chem. 277:9139-9147(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ATXN2L.
    20. "Functional mimicry of a protein hormone by a peptide agonist: the EPO receptor complex at 2.8 A."
      Livnah O., Stura E.A., Johnson D.L., Middleton S.A., Mulcahy L.S., Wrighton N.C., Dower W.J., Jolliffe L.K., Wilson I.A.
      Science 273:464-471(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 34-244.
    21. "An antagonist peptide-EPO receptor complex suggests that receptor dimerization is not sufficient for activation."
      Livnah O., Johnson D.L., Stura E.A., Farrell F.X., Barbone F.P., You Y., Liu K.D., Goldsmith M.A., He W., Krause C.D., Pestka S., Jolliffe L.K., Wilson I.A.
      Nat. Struct. Biol. 5:993-1004(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 34-244.
    22. Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 32-244 IN COMPLEX WITH EPO.
    23. "Engineering a soluble extracellular erythropoietin receptor (EPObp) in Pichia pastoris to eliminate microheterogeneity, and its complex with erythropoietin."
      Zhan H., Liu B., Reid S.W., Aoki K.H., Li C., Syed R.S., Karkaria C., Koe G., Sitney K., Hayenga K., Mistry F., Savel L., Dreyer M., Katz B.A., Schreurs J., Matthews D.J., Cheetham J.C., Egrie J., Giebel L.B., Stroud R.M.
      Protein Eng. 12:505-513(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 22-249 IN COMPLEX WITH EPO.
    24. "Crystallographic evidence for preformed dimers of erythropoietin receptor before ligand activation."
      Livnah O., Stura E.A., Middleton S.A., Johnson D.L., Jolliffe L.K., Wilson I.A.
      Science 283:987-990(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 34-246.
    25. "Truncated erythropoietin receptor causes dominantly inherited benign human erythrocytosis."
      de la Chapelle A., Traskelin A.-L., Juvonen E.
      Proc. Natl. Acad. Sci. U.S.A. 90:4495-4499(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN ECYT1.
    26. "Mutation in the negative regulatory element of the erythropoietin receptor gene in a case of sporadic primary polycythemia."
      Sokol L., Prchal J.F., D'Andrea A., Rado T.A., Prchal J.T.
      Exp. Hematol. 22:447-453(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ECYT1 SER-488.
    27. "Missense mutation of the erythropoietin receptor is a rare event in human erythroid malignancies."
      Le Couedic J.-P., Mitjavila M.-T., Villeval J.-L., Feger F., Gobert S., Mayeux P., Casadevall N., Vainchenker W.
      Blood 87:1502-1511(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ECYT1 SER-487, VARIANT ERYTHROLEUKEMIA SER-487.

    Entry informationi

    Entry nameiEPOR_HUMAN
    AccessioniPrimary (citable) accession number: P19235
    Secondary accession number(s): B2RCG4, Q15443, Q2M205
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: November 1, 1990
    Last modified: October 1, 2014
    This is version 178 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3