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P14753

- EPOR_MOUSE

UniProt

P14753 - EPOR_MOUSE

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Protein

Erythropoietin receptor

Gene
Epor
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 binding By 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
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini25 – 249225Extracellular Reviewed predictionAdd
BLAST
Transmembranei250 – 27223Helical; Reviewed predictionAdd
BLAST
Topological domaini273 – 507235Cytoplasmic Reviewed predictionAdd
BLAST

GO - Cellular componenti

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

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 ↔ 62 By similarity
Glycosylationi75 – 751N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi90 ↔ 106 By similarity
Glycosylationi232 – 2321C-linked (Man); in isoform EPOR-S1 Publication
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 JAK2 Inferred
Modified residuei467 – 4671Phosphotyrosine; by JAK2
Modified residuei484 – 4841Phosphotyrosine; by JAK2 Inferred
Modified residuei488 – 4881Phosphotyrosine; by JAK2 Inferred
Modified residuei503 – 5031Phosphotyrosine; by JAK2 Inferred

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.6 Publications
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.1 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/SHIP1.10 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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini146 – 246101Fibronectin type-IIIAdd
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

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei246 – 26520DLDPL…ISLLL → GEALVPRGAGGAGPNTRQTP in isoform EPOR-S. VSP_009512Add
BLAST
Alternative sequencei266 – 507242Missing in isoform EPOR-S. VSP_009513Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti291 – 2911E → D in AAB20029. 1 Publication

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 159 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

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