P14753 (EPOR_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Erythropoietin receptor
Short name=EPO-R

Gene names

Name:

Epor

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	507 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.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 process	Host-virus interaction
Cellular component	Cell membrane Membrane Secreted
Coding sequence diversity	Alternative splicing
Domain	Signal Transmembrane Transmembrane helix
Molecular function	Receptor
PTM	Disulfide bond Glycoprotein Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	brain development Inferred from mutant phenotype PubMed 11807041. Source: MGI decidualization Inferred from direct assay PubMed 17300687. Source: MGI embryo development 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 virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW visceral serous pericardium development Traceable author statement PubMed 20299672. Source: DFLAT
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	erythropoietin receptor activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Plcg1	Q62077	4	EBI-617901,EBI-300133
Plcg2	Q8CIH5	2	EBI-617901,EBI-617954

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 24	24
	Chain	25 – 507	483	Erythropoietin receptor		PRO_0000010869
Regions
	Topological domain	25 – 249	225	Extracellular Potential
	Transmembrane	250 – 272	23	Helical; Potential
	Topological domain	273 – 507	235	Cytoplasmic Potential
	Domain	143 – 239	97	Fibronectin type-III
	Motif	232 – 236	5	WSXWS motif
	Motif	281 – 289	9	Box 1 motif
	Motif	451 – 456	6	ITIM motif
Sites
	Site	116	1	Required for ligand binding By similarity
	Site	367	1	Interaction with APS and STAT5, and activation
	Site	425	1	Required for STAT5/PTPN11/SOCS3 binding
	Site	453	1	Interaction with PTPN6
Amino acid modifications
	Modified residue	367	1	Phosphotyrosine; by JAK2
	Modified residue	425	1	Phosphotyrosine; by JAK2
	Modified residue	453	1	Phosphotyrosine; by JAK2
	Modified residue	455	1	Phosphotyrosine; by JAK2
	Modified residue	467	1	Phosphotyrosine; by JAK2
	Modified residue	484	1	Phosphotyrosine; by JAK2
	Modified residue	488	1	Phosphotyrosine; by JAK2
	Modified residue	503	1	Phosphotyrosine; by JAK2
	Glycosylation	75	1	N-linked (GlcNAc...) Potential
	Glycosylation	232	1	C-linked (Man); in isoform EPOR-S Ref.19
	Disulfide bond	52 ↔ 62		By similarity
	Disulfide bond	90 ↔ 106		By similarity
	Cross-link	280		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.21
	Cross-link	452		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.21
Natural variations
	Alternative sequence	246 – 265	20	DLDPL…ISLLL → GEALVPRGAGGAGPNTRQTP in isoform EPOR-S.		VSP_009512
	Alternative sequence	266 – 507	242	Missing in isoform EPOR-S.		VSP_009513
Experimental info
	Mutagenesis	153	1	R → C: Reduced JAK2/STAT5 activation. Ref.13
	Mutagenesis	232	1	W → 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
	Mutagenesis	232	1	W → F: Greatly reduced EPO binding. Ref.12
	Mutagenesis	233	1	S → A: Not secreted and loss of EPO binding. Ref.12 Ref.19
	Mutagenesis	233	1	S → 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
	Mutagenesis	233	1	S → G: 50-fold less EPO binding. Ref.12 Ref.19
	Mutagenesis	233	1	S → T: 2-fold less EPO binding. Ref.12 Ref.19
	Mutagenesis	234	1	A → C, D, G, H, K, N, Q, R, S or T: No change in EPO binding. Ref.12 Ref.19
	Mutagenesis	234	1	A → E: Enhanced secretion and increased EPO binding. Ref.12 Ref.19
	Mutagenesis	234	1	A → F, I, M, W or Y: Little EPO binding. Ref.12 Ref.19
	Mutagenesis	234	1	A → L, P or V: Reduced EPO binding. Ref.12 Ref.19
	Mutagenesis	235	1	W → A, C, D, E, G, H, I, K, L, M, N, P, Q, R, S, T or V: Loss of EPO binding. Ref.12
	Mutagenesis	235	1	W → F: 14-fold less EPO binding. Ref.12
	Mutagenesis	235	1	W → Y: 100-fold less EPO binding. Ref.12
	Mutagenesis	236	1	S → A, C or G: Reduced EPO binding. Ref.12
	Mutagenesis	236	1	S → D, E, F, H, I, K, L, M, N, P, Q, R, V or W: Loss of EPO binding. Ref.12
	Mutagenesis	236	1	S → T: No loss of EPO binding. Ref.12
	Mutagenesis	236	1	S → Y: Greatly reduced EPO binding. Ref.12
	Mutagenesis	304	1	Q → L: Greatly reduced JAK2/STAT5 activation and some loss of mitogenic response. Ref.7 Ref.13
	Mutagenesis	306	1	W → R: No JAK2 binding nor JAK2/STAT5 activation. No EPO-induced phosphorylation. Complete loss of mitogenic response. Ref.7 Ref.8 Ref.13
	Mutagenesis	317	1	S → R: Slightly reduced JAK2/STAT5 activation and mitogenic response. Ref.7 Ref.13
	Mutagenesis	324	1	E → V: No change in JAK2/STAT5 activation nor mitogenic response. Ref.7 Ref.13
	Mutagenesis	330	1	L → R: Reduced JAK2/STAT5 activation. Ref.7 Ref.13
	Mutagenesis	331	1	E → A: No change in JAK2/STAT5 activation nor mitogenic response. Ref.7 Ref.13
	Mutagenesis	331	1	E → K: Reduced JAK2/STAT5 activation and mitogenic response. Ref.7 Ref.13
	Mutagenesis	367	1	Y → F: No STAT5 activation. Ref.10 Ref.13
	Mutagenesis	425	1	Y → F: No PTPN11 binding, reduced PTPN11 tyrosine phosphorylation and reduced cell proliferation. Ref.10
	Mutagenesis	453 – 455	3	YLY → FLF: No binding to PTPN6 SH2 domains. Enhanced JAK2 activation and cell proliferation. Ref.9 Ref.10
	Mutagenesis	453	1	Y → F: No PTPN6 binding, binds PTPN11. Ref.9 Ref.10
	Mutagenesis	455	1	Y → F: Binds to PTPN6 and PTPN11 SH2 domains. Ref.9 Ref.10
	Mutagenesis	467	1	Y → F: No loss of PTPN11 binding. Ref.10
	Mutagenesis	484	1	Y → F: No loss of PTPN11 binding. Ref.10
	Mutagenesis	488	1	Y → F: No loss of PTPN11 binding. Ref.10
	Mutagenesis	503	1	Y → F: No loss of PTPN11 binding. Ref.10
	Sequence conflict	291	1	E → D in AAB20029. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform EPOR-F (Membrane-bound form) [UniParc]. Last modified April 1, 1990. Version 1. Checksum: 067657A2E26451CA	FASTA	507	55,194
	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
	Isoform EPOR-S (Soluble form) [UniParc]. Checksum: 3368CF30E673F5CC	FASTA	265	28,798
	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 LLTASGEALV PRGAGGAGPN TRQTP

References

	« Hide 'large scale' referencesShow '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, 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, 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, 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.
[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.
IPI	IPI00129864. IPI00408736.
PIR	A32385. A41686. S14081.
RefSeq	NP_034279.3. NM_010149.3.
UniGene	Mm.2653.
3D structure databases
ProteinModelPortal	P14753.
SMR	P14753. Positions 32-246.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-657N.
IntAct	P14753. 5 interactions.
MINT	MINT-1348473.
PTM databases
PhosphoSite	P14753.
Proteomic databases
PRIDE	P14753.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000006397; ENSMUSP00000006397; ENSMUSG00000006235.
GeneID	13857.
KEGG	mmu:13857.
UCSC	uc009ond.1. mouse. uc009one.1. mouse.
Organism-specific databases
CTD	2057.
MGI	MGI:95408. Epor.
Phylogenomic databases
eggNOG	NOG46583.
HOGENOM	HOG000059639.
HOVERGEN	HBG005595.
InParanoid	P14753.
KO	K05079.
OMA	SERCWGV.
OrthoDB	EOG46HG9M.
Gene expression databases
ArrayExpress	P14753.
Bgee	P14753.
CleanEx	MM_EPOR.
Genevestigator	P14753.
GermOnline	ENSMUSG00000006235. Mus musculus.
Family and domain databases
Gene3D	2.60.40.10. 2 hits.
InterPro	IPR009167. Erythropoietin_rcpt. IPR003961. Fibronectin_type3. IPR015152. Growth/epo_recpt_lig-bind. IPR013783. Ig-like_fold. IPR003528. Long_hematopoietin_rcpt_CS. [Graphical view]
PANTHER	PTHR23037:SF10. PTHR23037:SF10. 1 hit.
Pfam	PF09067. EpoR_lig-bind. 1 hit. PF00041. fn3. 1 hit. [Graphical view]
PIRSF	PIRSF001959. EPO_receptor. 1 hit.
SMART	SM00060. FN3. 1 hit. [Graphical view]
SUPFAM	SSF49265. FN_III-like. 2 hits.
PROSITE	PS50853. FN3. 1 hit. PS01352. HEMATOPO_REC_L_F1. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	284730.
SOURCE	Search...

Entry information

Entry name

EPOR_MOUSE

Accession

Primary (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:	May 29, 2013
This is version 148 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program