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P14753

- EPOR_MOUSE

UniProt

P14753 - EPOR_MOUSE

Protein

Erythropoietin receptor

Gene

Epor

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 160 (01 Oct 2014)
      Sequence version 1 (01 Apr 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.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei116 – 1161Required for ligand bindingBy similarity
    Sitei367 – 3671Interaction with APS and STAT5, and activation
    Sitei425 – 4251Required for STAT5/PTPN11/SOCS3 binding
    Sitei453 – 4531Interaction with PTPN6

    GO - Molecular functioni

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

    GO - Biological processi

    1. brain development Source: MGI
    2. cardiac muscle tissue morphogenesis Source: DFLAT
    3. decidualization Source: MGI
    4. heart development Source: MGI
    5. heart morphogenesis Source: DFLAT
    6. signal transduction Source: MGI
    7. vasculogenesis involved in coronary vascular morphogenesis Source: DFLAT
    8. ventricular cardiac muscle tissue morphogenesis Source: DFLAT
    9. viral process Source: UniProtKB-KW
    10. visceral serous pericardium development Source: DFLAT

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Host-virus interaction

    Enzyme and pathway databases

    SABIO-RKP14753.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Erythropoietin receptor
    Short name:
    EPO-R
    Gene namesi
    Name:Epor
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 9

    Organism-specific databases

    MGIiMGI:95408. Epor.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cell membrane, Membrane, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi153 – 1531R → C: Reduced JAK2/STAT5 activation. 1 Publication
    Mutagenesisi232 – 2321W → A, C, D, E, G, H, I, K, L, M, N, P, Q, R, S, T, V or Y: Loss of EPO binding. 1 Publication
    Mutagenesisi232 – 2321W → F: Greatly reduced EPO binding. 1 Publication
    Mutagenesisi233 – 2331S → A: Not secreted and loss of EPO binding. 2 Publications
    Mutagenesisi233 – 2331S → C, D, E, F, H, I, K, L, M, N, P, Q, R, V, W or Y: Loss of EPO binding. 2 Publications
    Mutagenesisi233 – 2331S → G: 50-fold less EPO binding. 2 Publications
    Mutagenesisi233 – 2331S → T: 2-fold less EPO binding. 2 Publications
    Mutagenesisi234 – 2341A → C, D, G, H, K, N, Q, R, S or T: No change in EPO binding. 2 Publications
    Mutagenesisi234 – 2341A → E: Enhanced secretion and increased EPO binding. 2 Publications
    Mutagenesisi234 – 2341A → F, I, M, W or Y: Little EPO binding. 2 Publications
    Mutagenesisi234 – 2341A → L, P or V: Reduced EPO binding. 2 Publications
    Mutagenesisi235 – 2351W → A, C, D, E, G, H, I, K, L, M, N, P, Q, R, S, T or V: Loss of EPO binding. 1 Publication
    Mutagenesisi235 – 2351W → F: 14-fold less EPO binding. 1 Publication
    Mutagenesisi235 – 2351W → Y: 100-fold less EPO binding. 1 Publication
    Mutagenesisi236 – 2361S → A, C or G: Reduced EPO binding. 1 Publication
    Mutagenesisi236 – 2361S → D, E, F, H, I, K, L, M, N, P, Q, R, V or W: Loss of EPO binding. 1 Publication
    Mutagenesisi236 – 2361S → T: No loss of EPO binding. 1 Publication
    Mutagenesisi236 – 2361S → Y: Greatly reduced EPO binding. 1 Publication
    Mutagenesisi304 – 3041Q → L: Greatly reduced JAK2/STAT5 activation and some loss of mitogenic response. 2 Publications
    Mutagenesisi306 – 3061W → R: No JAK2 binding nor JAK2/STAT5 activation. No EPO-induced phosphorylation. Complete loss of mitogenic response. 3 Publications
    Mutagenesisi317 – 3171S → R: Slightly reduced JAK2/STAT5 activation and mitogenic response. 2 Publications
    Mutagenesisi324 – 3241E → V: No change in JAK2/STAT5 activation nor mitogenic response. 2 Publications
    Mutagenesisi330 – 3301L → R: Reduced JAK2/STAT5 activation. 2 Publications
    Mutagenesisi331 – 3311E → A: No change in JAK2/STAT5 activation nor mitogenic response. 2 Publications
    Mutagenesisi331 – 3311E → K: Reduced JAK2/STAT5 activation and mitogenic response. 2 Publications
    Mutagenesisi367 – 3671Y → F: No STAT5 activation. 2 Publications
    Mutagenesisi425 – 4251Y → F: No PTPN11 binding, reduced PTPN11 tyrosine phosphorylation and reduced cell proliferation. 1 Publication
    Mutagenesisi453 – 4553YLY → FLF: No binding to PTPN6 SH2 domains. Enhanced JAK2 activation and cell proliferation. 2 Publications
    Mutagenesisi453 – 4531Y → F: No PTPN6 binding, binds PTPN11. 2 Publications
    Mutagenesisi455 – 4551Y → F: Binds to PTPN6 and PTPN11 SH2 domains. 2 Publications
    Mutagenesisi467 – 4671Y → F: No loss of PTPN11 binding. 1 Publication
    Mutagenesisi484 – 4841Y → F: No loss of PTPN11 binding. 1 Publication
    Mutagenesisi488 – 4881Y → F: No loss of PTPN11 binding. 1 Publication
    Mutagenesisi503 – 5031Y → F: No loss of PTPN11 binding. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Add
    BLAST
    Chaini25 – 507483Erythropoietin receptorPRO_0000010869Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi52 ↔ 62By similarity
    Glycosylationi75 – 751N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi90 ↔ 106By similarity
    Glycosylationi232 – 2321C-linked (Man); in isoform EPOR-S
    Cross-linki280 – 280Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Modified residuei367 – 3671Phosphotyrosine; by JAK21 Publication
    Modified residuei425 – 4251Phosphotyrosine; by JAK21 Publication
    Cross-linki452 – 452Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Modified residuei453 – 4531Phosphotyrosine; by JAK21 Publication
    Modified residuei455 – 4551Phosphotyrosine; by JAK22 Publications
    Modified residuei467 – 4671Phosphotyrosine; by JAK2
    Modified residuei484 – 4841Phosphotyrosine; by JAK21 Publication
    Modified residuei488 – 4881Phosphotyrosine; by JAK21 Publication
    Modified residuei503 – 5031Phosphotyrosine; by JAK21 Publication

    Post-translational modificationi

    The identity of the C-linked hexose on the WXXW motif has not been determined. It is probably mannose.
    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-453 is required for PTPN6 interaction, Tyr-425 for PTPN11. Tyr-425 is also required for SOCS3 binding, but Tyr-453/Tyr-455 motif is the preferred binding site By similarity.By similarity
    Ubiquitinated by NOSIP; appears to be either multi-monoubiquitinated or polyubiquitinated. Ubiquitination mediates proliferation and survival of EPO-dependent cells By similarity. Ubiquitination at Lys-280 mediates receptor internalization, whereas ubiquitination at Lys-452 promotes trafficking of activated receptors to the lysosomes for degradation.By similarity1 Publication

    Keywords - PTMi

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

    Proteomic databases

    PRIDEiP14753.

    PTM databases

    PhosphoSiteiP14753.

    Expressioni

    Tissue specificityi

    Expressed in relatively mature erythroid progenitor cells and in EPO-responsive erythroleukemia cells.

    Gene expression databases

    ArrayExpressiP14753.
    BgeeiP14753.
    CleanExiMM_EPOR.
    GenevestigatoriP14753.

    Interactioni

    Subunit structurei

    Forms homodimers on EPO stimulation. The tyrosine-phosphorylated form interacts with several SH2 domain-containing proteins including LYN, the adapter protein APS, PTPN6, PTPN11, JAK2, PI3 kinases, STAT5A/B, SOCS3 and CRKL. The N-terminal SH2 domain of PTPN6 binds Tyr-453 and inhibits signaling through dephosphorylation of JAK2. APS binding also inhibits the JAK-STAT signaling. Binding to PTPN11, preferentially through the N-terminal SH2 domain, promotes mitogenesis and phosphorylation of PTPN11. Binding of JAK2 (through its N-terminal) promotes cell-surface expression. Interaction with the ubiquitin ligase NOSIP mediates EPO-induced cell proliferation. Interacts with ATXN2L By similarity. Forms heterooligomers with friend spleen focus-forming virus (FSFFV) gp55, probably via their respective transmembrane domains. Interacts with INPP5D/SHIP1.By similarity10 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Jak2Q621204EBI-617901,EBI-646604
    Plcg1Q620774EBI-617901,EBI-300133
    Plcg2Q8CIH52EBI-617901,EBI-617954

    Protein-protein interaction databases

    BioGridi199488. 3 interactions.
    DIPiDIP-657N.
    IntActiP14753. 10 interactions.
    MINTiMINT-1348473.

    Structurei

    3D structure databases

    ProteinModelPortaliP14753.
    SMRiP14753. Positions 32-246.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini25 – 249225ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini273 – 507235CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei250 – 27223HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini146 – 246101Fibronectin type-IIIPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi232 – 2365WSXWS motif
    Motifi281 – 2899Box 1 motif
    Motifi451 – 4566ITIM 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.
    InParanoidiP14753.
    KOiK05079.
    OMAiFMVRARM.
    OrthoDBiEOG74BJS6.
    PhylomeDBiP14753.
    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 (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform EPOR-F (identifier: P14753-1) [UniParc]FASTAAdd to Basket

    Also known as: Membrane-bound 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

    MDKLRVPLWP RVGPLCLLLA GAAWAPSPSL PDPKFESKAA LLASRGSEEL    50
    LCFTQRLEDL VCFWEEAASS GMDFNYSFSY QLEGESRKSC SLHQAPTVRG 100
    SVRFWCSLPT ADTSSFVPLE LQVTEASGSP RYHRIIHINE VVLLDAPAGL 150
    LARRAEEGSH VVLRWLPPPG APMTTHIRYE VDVSAGNRAG GTQRVEVLEG 200
    RTECVLSNLR GGTRYTFAVR ARMAEPSFSG FWSAWSEPAS LLTASDLDPL 250
    ILTLSLILVL ISLLLTVLAL LSHRRTLQQK IWPGIPSPES EFEGLFTTHK 300
    GNFQLWLLQR DGCLWWSPGS SFPEDPPAHL EVLSEPRWAV TQAGDPGADD 350
    EGPLLEPVGS EHAQDTYLVL DKWLLPRTPC SENLSGPGGS VDPVTMDEAS 400
    ETSSCPSDLA SKPRPEGTSP SSFEYTILDP SSQLLCPRAL PPELPPTPPH 450
    LKYLYLVVSD SGISTDYSSG GSQGVHGDSS DGPYSHPYEN SLVPDSEPLH 500
    PGYVACS 507
    Length:507
    Mass (Da):55,194
    Last modified:April 1, 1990 - v1
    Checksum:i067657A2E26451CA
    GO
    Isoform EPOR-S (identifier: P14753-2) [UniParc]FASTAAdd to Basket

    Also known as: Soluble form

    The sequence of this isoform differs from the canonical sequence as follows:
         246-265: DLDPLILTLSLILVLISLLL → GEALVPRGAGGAGPNTRQTP
         266-507: Missing.

    Show »
    Length:265
    Mass (Da):28,798
    Checksum:i3368CF30E673F5CC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti291 – 2911E → D in AAB20029. (PubMed:1656233)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei246 – 26520DLDPL…ISLLL → GEALVPRGAGGAGPNTRQTP in isoform EPOR-S. CuratedVSP_009512Add
    BLAST
    Alternative sequencei266 – 507242Missing in isoform EPOR-S. CuratedVSP_009513Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04843 mRNA. Translation: AAA37571.1.
    X53081 Genomic DNA. Translation: CAA37248.1.
    S59388 mRNA. Translation: AAB20029.2.
    BC003953 mRNA. Translation: AAH03953.1.
    BC046282 mRNA. Translation: AAH46282.1.
    M38133 Genomic DNA. Translation: AAA37572.1.
    M62360 Genomic DNA. Translation: AAA37582.1.
    CCDSiCCDS22915.1. [P14753-1]
    PIRiA41686. A32385.
    S14081.
    RefSeqiNP_034279.3. NM_010149.3. [P14753-1]
    UniGeneiMm.2653.

    Genome annotation databases

    EnsembliENSMUST00000006397; ENSMUSP00000006397; ENSMUSG00000006235. [P14753-1]
    GeneIDi13857.
    KEGGimmu:13857.
    UCSCiuc009ond.1. mouse. [P14753-1]
    uc009one.1. mouse. [P14753-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04843 mRNA. Translation: AAA37571.1 .
    X53081 Genomic DNA. Translation: CAA37248.1 .
    S59388 mRNA. Translation: AAB20029.2 .
    BC003953 mRNA. Translation: AAH03953.1 .
    BC046282 mRNA. Translation: AAH46282.1 .
    M38133 Genomic DNA. Translation: AAA37572.1 .
    M62360 Genomic DNA. Translation: AAA37582.1 .
    CCDSi CCDS22915.1. [P14753-1 ]
    PIRi A41686. A32385.
    S14081.
    RefSeqi NP_034279.3. NM_010149.3. [P14753-1 ]
    UniGenei Mm.2653.

    3D structure databases

    ProteinModelPortali P14753.
    SMRi P14753. Positions 32-246.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199488. 3 interactions.
    DIPi DIP-657N.
    IntActi P14753. 10 interactions.
    MINTi MINT-1348473.

    PTM databases

    PhosphoSitei P14753.

    Proteomic databases

    PRIDEi P14753.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000006397 ; ENSMUSP00000006397 ; ENSMUSG00000006235 . [P14753-1 ]
    GeneIDi 13857.
    KEGGi mmu:13857.
    UCSCi uc009ond.1. mouse. [P14753-1 ]
    uc009one.1. mouse. [P14753-2 ]

    Organism-specific databases

    CTDi 2057.
    MGIi MGI:95408. Epor.

    Phylogenomic databases

    eggNOGi NOG46583.
    HOGENOMi HOG000059639.
    HOVERGENi HBG005595.
    InParanoidi P14753.
    KOi K05079.
    OMAi FMVRARM.
    OrthoDBi EOG74BJS6.
    PhylomeDBi P14753.
    TreeFami TF336573.

    Enzyme and pathway databases

    SABIO-RK P14753.

    Miscellaneous databases

    NextBioi 284730.
    PROi P14753.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P14753.
    Bgeei P14753.
    CleanExi MM_EPOR.
    Genevestigatori P14753.

    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. "Expression cloning of the murine erythropoietin receptor."
      D'Andrea A.D., Lodish H.F., Wong G.G.
      Cell 57:277-285(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM EPOR-F).
      Tissue: Erythroleukemia.
    2. "Characterization of murine erythropoietin receptor genes."
      Kuramochi S., Ikawa Y., Todokoro K.
      J. Mol. Biol. 216:567-575(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS EPOR-F AND EPOR-S).
      Strain: BALB/c.
      Tissue: Erythroleukemia and Liver.
    3. "Unregulated expression of the erythropoietin receptor gene caused by insertion of spleen focus-forming virus long terminal repeat in a murine erythroleukemia cell line."
      Hino M., Tojo A., Misawa Y., Morii H., Takaku F., Shibuya M.
      Mol. Cell. Biol. 11:5527-5533(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM EPOR-F), ALTERNATIVE SPLICING DUE TO FRIEND SPLEEN FOCUS-FORMING VIRUS.
      Tissue: Erythroleukemia.
    4. "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).
      Strain: C57BL/6J and FVB/N-3.
      Tissue: Mammary tumor.
    5. "Structure and transcription of the mouse erythropoietin receptor gene."
      Youssoufian H., Zon L.I., Orkin S.H., D'Andrea A.D., Lodish H.F.
      Mol. Cell. Biol. 10:3675-3682(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27.
    6. "Spleen focus-forming virus long terminal repeat insertional activation of the murine erythropoietin receptor gene in the T3Cl-2 friend leukemia cell line."
      Lacombe C., Chretien S., Lemarchandel V., Mayeux P., Romeo P.-H., Gisselbrecht S., Cartron J.-P.
      J. Biol. Chem. 266:6952-6956(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24.
    7. "Inactivation of erythropoietin receptor function by point mutations in a region having homology with other cytokine receptors."
      Miura O., Cleveland J.L., Ihle J.N.
      Mol. Cell. Biol. 13:1788-1795(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ERYTHROPOIETIN-INDUCED MITOGENESIS, MUTAGENESIS OF GLN-304; TRP-306; SER-317; GLU-324; LEU-330 AND GLU-331.
    8. "Erythropoietin induces association of the JAK2 protein tyrosine kinase with the erythropoietin receptor in vivo."
      Miura O., Nakamura N., Quelle F.W., Witthuhn B.A., Ihle J.N., Aoki N.
      Blood 84:1501-1507(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH JAK2, PHOSPHORYLATION, MUTAGENESIS OF TRP-306.
    9. "Specific recruitment of SH-PTP1 to the erythropoietin receptor causes inactivation of JAK2 and termination of proliferative signals."
      Klingmueller U., Lorenz U., Cantley L.C., Neel B.G., Lodish H.F.
      Cell 80:729-738(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PTPN6, PHOSPHORYLATION AT TYR-453, MUTAGENESIS OF TYR-453; 453-TYR--TYR-455 AND TYR-455.
    10. "Tyrosine 425 within the activated erythropoietin receptor binds Syp, reduces the erythropoietin required for Syp tyrosine phosphorylation, and promotes mitogenesis."
      Tauchi T., Damen J.E., Toyama K., Feng G.-S., Broxmeyer H.E., Krystal G.
      Blood 87:4495-4501(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PTPN11, PHOSPHORYLATION AT TYR-425; TYR-455; TYR-484; TYR-488 AND TYR-503, MUTAGENESIS OF TYR-367; TYR-425; TYR-453; TYR-455; TYR-467; TYR-484; TYR-488 AND TYR-503.
    11. "Identification of tyrosine residues within the intracellular domain of the erythropoietin receptor crucial for STAT5 activation."
      Gobert S., Chretien S., Gouilleux F., Muller O., Pallard C., Dusanter-Fourt I., Groner B., Lacombe C., Gisselbrecht S., Mayeux P.
      EMBO J. 15:2434-2441(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH STAT5.
    12. "Saturation mutagenesis of the WSXWS motif of the erythropoietin receptor."
      Hilton D.J., Watowich S.S., Katz L., Lodish H.F.
      J. Biol. Chem. 271:4699-4708(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE WSXWS MOTIF, MUTAGENESIS OF TRP-232; SER-233; ALA-234; TRP-235 AND SER-236.
    13. "Erythropoietin induces activation of Stat5 through association with specific tyrosines on the receptor that are not required for a mitogenic response."
      Quelle F.W., Wang D., Nosaka T., Thierfelder W.E., Stravopodis D., Weinstein Y., Ihle J.N.
      Mol. Cell. Biol. 16:1622-1631(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH STAT5, PHOSPHORYLATION AT TYR-367, MUTAGENESIS OF ARG-153; GLN-304; TRP-306; SER-317; GLU-324; LEU-330; GLU-331 AND TYR-367.
    14. "Lyn physically associates with the erythropoietin receptor and may play a role in activation of the Stat5 pathway."
      Chin H., Arai A., Wakao H., Kamiyama R., Miyasaka N., Miura O.
      Blood 91:3734-3745(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH WITH LYN.
    15. "The SH2 inositol 5-phosphatase Ship1 is recruited in an SH2-dependent manner to the erythropoietin receptor."
      Mason J.M., Beattie B.K., Liu Q., Dumont D.J., Barber D.L.
      J. Biol. Chem. 275:4398-4406(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH INPP5D, PHOSPHORYLATION AT TYR-455.
    16. "A common epitope is shared by activated signal transducer and activator of transcription-5 (STAT5) and the phosphorylated erythropoietin receptor: implications for the docking model of STAT activation."
      Barber D.L., Beattie B.K., Mason J.M., Nguyen M.H.-H., Yoakim M., Neel B.G., D'Andrea A.D., Frank D.A.
      Blood 97:2230-2237(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, STAT5 ACTIVATION.
    17. "CrkL is recruited through its SH2 domain to the erythropoietin receptor and plays a role in Lyn-mediated receptor signaling."
      Arai A., Kanda E., Nosaka Y., Miyasaka N., Miura O.
      J. Biol. Chem. 276:33282-33290(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CRKL AND LYN.
    18. "The adapter protein APS associates with the multifunctional docking sites Tyr-568 and Tyr-936 in c-Kit."
      Wollberg P., Lennartsson J., Gottfridsson E., Yoshimura A., Ronnstrand L.
      Biochem. J. 370:1033-1038(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH APS.
    19. "The WSAWS motif is C-hexosylated in a soluble form of the erythropoietin receptor."
      Furmanek A., Hess D., Rogniaux H., Hofsteenge J.
      Biochemistry 42:8452-8458(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF SER-233 AND ALA-234, GLYCOSYLATION AT TRP-232.
    20. "The erythropoietin receptor transmembrane domain mediates complex formation with viral anemic and polycythemic gp55 proteins."
      Constantinescu S.N., Keren T., Russ W.P., Ubarretxena-Belandia I., Malka Y., Kubatzky K.F., Engelman D.M., Lodish H.F., Henis Y.I.
      J. Biol. Chem. 278:43755-43763(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FRIEND SPLEEN FOCUS-FORMING VIRUS GP55.
    21. "Ubiquitination regulates the internalization, endolysosomal sorting, and signaling of the erythropoietin receptor."
      Bulut G.B., Sulahian R., Ma Y., Chi N.W., Huang L.J.
      J. Biol. Chem. 286:6449-6457(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION AT LYS-280 AND LYS-452.

    Entry informationi

    Entry nameiEPOR_MOUSE
    AccessioniPrimary (citable) accession number: P14753
    Secondary accession number(s): Q63852
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 1, 1990
    Last modified: October 1, 2014
    This is version 160 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Interaction with FSFFV envelope-like membrane glycoprotein gp55 leads to ligand-independent activation of EPOR and to the abnormally rapid proliferation of erythroid precursor cells.
    Viral promoter integration by Friend spleen focus-forming virus (F-SFFVP) in the murine erythroleukemia cell line F5-5, results in aberrant EPOR sequences and EPOR overexpression in erythroid progenitor cells.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3