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P14753 (EPOR_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 159. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Erythropoietin receptor

Short name=EPO-R
Gene names
Name:Epor
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length507 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7 Ref.12

Subunit structure

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. Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15 Ref.17 Ref.18 Ref.20

Subcellular location

Isoform EPOR-F: Cell membrane; Single-pass type I membrane protein.

Isoform EPOR-S: Secreted.

Tissue specificity

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

Domain

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.

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.

Post-translational modification

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. Ref.8 Ref.9 Ref.10 Ref.13 Ref.15 Ref.16

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. Ref.21

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.

Sequence similarities

Belongs to the type I cytokine receptor family. Type 1 subfamily.

Contains 1 fibronectin type-III domain.

Ontologies

Keywords
   Biological processHost-virus interaction
   Cellular componentCell membrane
Membrane
Secreted
   Coding sequence diversityAlternative splicing
   DomainSignal
Transmembrane
Transmembrane helix
   Molecular functionReceptor
   PTMDisulfide bond
Glycoprotein
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbrain development

Inferred from mutant phenotype PubMed 11807041. Source: MGI

cardiac muscle tissue morphogenesis

Traceable author statement PubMed 20299672. Source: DFLAT

decidualization

Inferred from direct assay PubMed 17300687. Source: MGI

heart development

Inferred from mutant phenotype PubMed 11807041. Source: MGI

heart morphogenesis

Traceable author statement PubMed 20299672. Source: DFLAT

signal transduction

Inferred from direct assay PubMed 17300687. Source: MGI

vasculogenesis involved in coronary vascular morphogenesis

Traceable author statement PubMed 20299672. Source: DFLAT

ventricular cardiac muscle tissue morphogenesis

Traceable author statement PubMed 20299672. Source: DFLAT

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

visceral serous pericardium development

Traceable author statement PubMed 20299672. Source: DFLAT

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionerythropoietin receptor activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 15953601PubMed 17024180PubMed 21362419. Source: IntAct

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform EPOR-F (identifier: P14753-1)

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.
Isoform EPOR-S (identifier: P14753-2)

Also known as: Soluble form;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424
Chain25 – 507483Erythropoietin receptor
PRO_0000010869

Regions

Topological domain25 – 249225Extracellular Potential
Transmembrane250 – 27223Helical; Potential
Topological domain273 – 507235Cytoplasmic Potential
Domain146 – 246101Fibronectin type-III
Motif232 – 2365WSXWS motif
Motif281 – 2899Box 1 motif
Motif451 – 4566ITIM motif

Sites

Site1161Required for ligand binding By similarity
Site3671Interaction with APS and STAT5, and activation
Site4251Required for STAT5/PTPN11/SOCS3 binding
Site4531Interaction with PTPN6

Amino acid modifications

Modified residue3671Phosphotyrosine; by JAK2 Ref.13
Modified residue4251Phosphotyrosine; by JAK2 Ref.10
Modified residue4531Phosphotyrosine; by JAK2 Ref.9
Modified residue4551Phosphotyrosine; by JAK2 Probable
Modified residue4671Phosphotyrosine; by JAK2
Modified residue4841Phosphotyrosine; by JAK2 Probable
Modified residue4881Phosphotyrosine; by JAK2 Probable
Modified residue5031Phosphotyrosine; by JAK2 Probable
Glycosylation751N-linked (GlcNAc...) Potential
Glycosylation2321C-linked (Man); in isoform EPOR-S Ref.19
Disulfide bond52 ↔ 62 By similarity
Disulfide bond90 ↔ 106 By similarity
Cross-link280Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.21
Cross-link452Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.21

Natural variations

Alternative sequence246 – 26520DLDPL…ISLLL → GEALVPRGAGGAGPNTRQTP in isoform EPOR-S.
VSP_009512
Alternative sequence266 – 507242Missing in isoform EPOR-S.
VSP_009513

Experimental info

Mutagenesis1531R → C: Reduced JAK2/STAT5 activation. Ref.13
Mutagenesis2321W → A, C, D, E, G, H, I, K, L, M, N, P, Q, R, S, T, V or Y: Loss of EPO binding. Ref.12
Mutagenesis2321W → F: Greatly reduced EPO binding. Ref.12
Mutagenesis2331S → A: Not secreted and loss of EPO binding. Ref.12 Ref.19
Mutagenesis2331S → C, D, E, F, H, I, K, L, M, N, P, Q, R, V, W or Y: Loss of EPO binding. Ref.12 Ref.19
Mutagenesis2331S → G: 50-fold less EPO binding. Ref.12 Ref.19
Mutagenesis2331S → T: 2-fold less EPO binding. Ref.12 Ref.19
Mutagenesis2341A → C, D, G, H, K, N, Q, R, S or T: No change in EPO binding. Ref.12 Ref.19
Mutagenesis2341A → E: Enhanced secretion and increased EPO binding. Ref.12 Ref.19
Mutagenesis2341A → F, I, M, W or Y: Little EPO binding. Ref.12 Ref.19
Mutagenesis2341A → L, P or V: Reduced EPO binding. Ref.12 Ref.19
Mutagenesis2351W → A, C, D, E, G, H, I, K, L, M, N, P, Q, R, S, T or V: Loss of EPO binding. Ref.12
Mutagenesis2351W → F: 14-fold less EPO binding. Ref.12
Mutagenesis2351W → Y: 100-fold less EPO binding. Ref.12
Mutagenesis2361S → A, C or G: Reduced EPO binding. Ref.12
Mutagenesis2361S → D, E, F, H, I, K, L, M, N, P, Q, R, V or W: Loss of EPO binding. Ref.12
Mutagenesis2361S → T: No loss of EPO binding. Ref.12
Mutagenesis2361S → Y: Greatly reduced EPO binding. Ref.12
Mutagenesis3041Q → L: Greatly reduced JAK2/STAT5 activation and some loss of mitogenic response. Ref.7 Ref.13
Mutagenesis3061W → R: No JAK2 binding nor JAK2/STAT5 activation. No EPO-induced phosphorylation. Complete loss of mitogenic response. Ref.7 Ref.8 Ref.13
Mutagenesis3171S → R: Slightly reduced JAK2/STAT5 activation and mitogenic response. Ref.7 Ref.13
Mutagenesis3241E → V: No change in JAK2/STAT5 activation nor mitogenic response. Ref.7 Ref.13
Mutagenesis3301L → R: Reduced JAK2/STAT5 activation. Ref.7 Ref.13
Mutagenesis3311E → A: No change in JAK2/STAT5 activation nor mitogenic response. Ref.7 Ref.13
Mutagenesis3311E → K: Reduced JAK2/STAT5 activation and mitogenic response. Ref.7 Ref.13
Mutagenesis3671Y → F: No STAT5 activation. Ref.10 Ref.13
Mutagenesis4251Y → F: No PTPN11 binding, reduced PTPN11 tyrosine phosphorylation and reduced cell proliferation. Ref.10
Mutagenesis453 – 4553YLY → FLF: No binding to PTPN6 SH2 domains. Enhanced JAK2 activation and cell proliferation. Ref.9 Ref.10
Mutagenesis4531Y → F: No PTPN6 binding, binds PTPN11. Ref.9 Ref.10
Mutagenesis4551Y → F: Binds to PTPN6 and PTPN11 SH2 domains. Ref.9 Ref.10
Mutagenesis4671Y → F: No loss of PTPN11 binding. Ref.10
Mutagenesis4841Y → F: No loss of PTPN11 binding. Ref.10
Mutagenesis4881Y → F: No loss of PTPN11 binding. Ref.10
Mutagenesis5031Y → F: No loss of PTPN11 binding. Ref.10
Sequence conflict2911E → D in AAB20029. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform EPOR-F (Membrane-bound form) [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 067657A2E26451CA

FASTA50755,194
        10         20         30         40         50         60 
MDKLRVPLWP RVGPLCLLLA GAAWAPSPSL PDPKFESKAA LLASRGSEEL LCFTQRLEDL 

        70         80         90        100        110        120 
VCFWEEAASS GMDFNYSFSY QLEGESRKSC SLHQAPTVRG SVRFWCSLPT ADTSSFVPLE 

       130        140        150        160        170        180 
LQVTEASGSP RYHRIIHINE VVLLDAPAGL LARRAEEGSH VVLRWLPPPG APMTTHIRYE 

       190        200        210        220        230        240 
VDVSAGNRAG GTQRVEVLEG RTECVLSNLR GGTRYTFAVR ARMAEPSFSG FWSAWSEPAS 

       250        260        270        280        290        300 
LLTASDLDPL ILTLSLILVL ISLLLTVLAL LSHRRTLQQK IWPGIPSPES EFEGLFTTHK 

       310        320        330        340        350        360 
GNFQLWLLQR DGCLWWSPGS SFPEDPPAHL EVLSEPRWAV TQAGDPGADD EGPLLEPVGS 

       370        380        390        400        410        420 
EHAQDTYLVL DKWLLPRTPC SENLSGPGGS VDPVTMDEAS ETSSCPSDLA SKPRPEGTSP 

       430        440        450        460        470        480 
SSFEYTILDP SSQLLCPRAL PPELPPTPPH LKYLYLVVSD SGISTDYSSG GSQGVHGDSS 

       490        500 
DGPYSHPYEN SLVPDSEPLH PGYVACS 

« Hide

Isoform EPOR-S (Soluble form) [UniParc].

Checksum: 3368CF30E673F5CC
Show »

FASTA26528,798

References

« Hide 'large scale' references
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS22915.1. [P14753-1]
PIRA32385. A41686.
S14081.
RefSeqNP_034279.3. NM_010149.3. [P14753-1]
UniGeneMm.2653.

3D structure databases

ProteinModelPortalP14753.
SMRP14753. Positions 32-246.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199488. 3 interactions.
DIPDIP-657N.
IntActP14753. 10 interactions.
MINTMINT-1348473.

PTM databases

PhosphoSiteP14753.

Proteomic databases

PRIDEP14753.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000006397; ENSMUSP00000006397; ENSMUSG00000006235. [P14753-1]
GeneID13857.
KEGGmmu:13857.
UCSCuc009ond.1. mouse. [P14753-1]
uc009one.1. mouse. [P14753-2]

Organism-specific databases

CTD2057.
MGIMGI:95408. Epor.

Phylogenomic databases

eggNOGNOG46583.
HOGENOMHOG000059639.
HOVERGENHBG005595.
InParanoidP14753.
KOK05079.
OMAFMVRARM.
OrthoDBEOG74BJS6.
PhylomeDBP14753.
TreeFamTF336573.

Enzyme and pathway databases

SABIO-RKP14753.

Gene expression databases

ArrayExpressP14753.
BgeeP14753.
CleanExMM_EPOR.
GenevestigatorP14753.

Family and domain databases

Gene3D2.60.40.10. 2 hits.
InterProIPR009167. Erythropoietin_rcpt.
IPR003961. Fibronectin_type3.
IPR015152. Growth/epo_recpt_lig-bind.
IPR013783. Ig-like_fold.
IPR003528. Long_hematopoietin_rcpt_CS.
[Graphical view]
PfamPF09067. EpoR_lig-bind. 1 hit.
PF00041. fn3. 1 hit.
[Graphical view]
PIRSFPIRSF001959. EPO_receptor. 1 hit.
SMARTSM00060. FN3. 1 hit.
[Graphical view]
SUPFAMSSF49265. SSF49265. 2 hits.
PROSITEPS50853. FN3. 1 hit.
PS01352. HEMATOPO_REC_L_F1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio284730.
PROP14753.
SOURCESearch...

Entry information

Entry nameEPOR_MOUSE
AccessionPrimary (citable) accession number: P14753
Secondary accession number(s): Q63852
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot