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Protein

Erythropoietin receptor

Gene

EPOR

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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.
Isoform EPOR-T acts as a dominant-negative receptor of EPOR-mediated signaling.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei117Required for ligand binding1
Sitei426Required for STAT5/PTPN11/SOCS3 bindingBy similarity1
Sitei456Required for STAT1/STAT3 activation1
Sitei485Required for CrkL bindingBy similarity1

GO - Molecular functioni

  • erythropoietin receptor activity Source: UniProtKB

GO - Biological processi

  • brain development Source: Ensembl
  • decidualization Source: Ensembl
  • heart development Source: Ensembl
  • signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Enzyme and pathway databases

BioCyciZFISH:ENSG00000105532-MONOMER.
SignaLinkiP19235.
SIGNORiP19235.

Names & Taxonomyi

Protein namesi
Recommended name:
Erythropoietin receptor
Short name:
EPO-R
Gene namesi
Name:EPOR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:3416. EPOR.

Subcellular locationi

Isoform EPOR-S :

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini25 – 250ExtracellularSequence analysisAdd BLAST226
Transmembranei251 – 273HelicalSequence analysisAdd BLAST23
Topological domaini274 – 508CytoplasmicSequence analysisAdd BLAST235

GO - Cellular componenti

  • extracellular region Source: UniProtKB-SubCell
  • integral component of plasma membrane Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Involvement in diseasei

Erythrocytosis, familial, 1 (ECYT1)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant disorder characterized by increased serum red blood cell mass, elevated hemoglobin and hematocrit, hypersensitivity of erythroid progenitors to erythropoietin, erythropoietin low serum levels, and no increase in platelets nor leukocytes. It has a relatively benign course and does not progress to leukemia.
See also OMIM:133100
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_027372487N → S in ECYT1 and erythroleukemia. 1 PublicationCorresponds to variant rs62638745dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi114T → A: Little effect on EPO binding. 1 Publication1
Mutagenesisi115S → A: Little effect on EPO binding. 1 Publication1
Mutagenesisi116S → A: 10-fold reduction in EPO binding. 1 Publication1
Mutagenesisi117F → A or L: Greatly reduced EPO binding. 1 Publication1
Mutagenesisi117F → W: 60-fold reduction in EPO binding. 1 Publication1
Mutagenesisi117F → Y: 8-fold reduction in EPO binding. 1 Publication1
Mutagenesisi118V → A: 16-fold reduction in EPO binding. 1 Publication1
Mutagenesisi120L → A: Some reduction in EPO binding. 1 Publication1
Mutagenesisi121E → A: Little effect on EPO binding. 1 Publication1
Mutagenesisi165R → A: Little effect on EPO binding. 1 Publication1
Mutagenesisi174M → A: Little effect on EPO binding. 1 Publication1
Mutagenesisi176S → A: 16-fold reduction in EPO binding. 1 Publication1
Mutagenesisi177H → A: Little effect on EPO binding. 1 Publication1
Mutagenesisi179R → A: Little effect on EPO binding. 1 Publication1
Mutagenesisi454Y → F: Some loss of SOCS3 binding. 1 Publication1
Mutagenesisi456Y → F: Inhibition of STAT1/STAT3 activity. No effect on STAT5 activity. Some loss of SOCS3 binding. 2 Publications1
Mutagenesisi468Y → F: No effect on STAT1/STAT3 nor STAT5 activity. 1 Publication1

Keywords - Diseasei

Congenital erythrocytosis, Disease mutation

Organism-specific databases

DisGeNETi2057.
MalaCardsiEPOR.
MIMi133100. phenotype.
OpenTargetsiENSG00000187266.
Orphaneti90042. Primary familial polycythemia.
PharmGKBiPA27834.

Chemistry databases

ChEMBLiCHEMBL1817.
DrugBankiDB00012. Darbepoetin alfa.
DB00016. Epoetin alfa.
DB08923. Epoetin Zeta.
DB08894. Peginesatide.
GuidetoPHARMACOLOGYi1718.

Polymorphism and mutation databases

BioMutaiEPOR.
DMDMi119524.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 24Add BLAST24
ChainiPRO_000001086825 – 508Erythropoietin receptorAdd BLAST484

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi52 ↔ 62
Glycosylationi76N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi91 ↔ 107
Cross-linki281Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei368Phosphotyrosine; by JAK2By similarity1
Modified residuei426Phosphotyrosine; by JAK2By similarity1
Cross-linki453Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei454Phosphotyrosine; by JAK2By similarity1
Modified residuei456Phosphotyrosine; by JAK2By similarity1
Modified residuei468Phosphotyrosine; by JAK2By similarity1
Modified residuei485Phosphotyrosine; by JAK2By similarity1
Modified residuei489Phosphotyrosine; by JAK2By similarity1
Modified residuei504Phosphotyrosine; by JAK2By similarity1

Post-translational modificationi

On EPO stimulation, phosphorylated on C-terminal tyrosine residues by JAK2. The phosphotyrosine motifs are also recruitment sites for several SH2-containing proteins and adapter proteins which mediate cell proliferation. Phosphorylation on Tyr-454 is required for PTPN6 interaction, Tyr-426 for PTPN11. Tyr-426 is also required for SOCS3 binding, but Tyr-454/Tyr-456 motif is the preferred binding site.1 Publication
Ubiquitination at Lys-281 mediates receptor internalization, whereas ubiquitination at Lys-453 promotes trafficking of activated receptors to the lysosomes for degradation (By similarity). Ubiquitinated by NOSIP; appears to be either multi-monoubiquitinated or polyubiquitinated. Ubiquitination mediates proliferation and survival of EPO-dependent cells.By similarity

Keywords - PTMi

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

Proteomic databases

PaxDbiP19235.
PeptideAtlasiP19235.
PRIDEiP19235.
TopDownProteomicsiP19235-3. [P19235-3]

PTM databases

iPTMnetiP19235.
PhosphoSitePlusiP19235.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSG00000187266.
CleanExiHS_EPOR.
ExpressionAtlasiP19235. baseline and differential.
GenevisibleiP19235. HS.

Interactioni

Subunit structurei

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei368Interaction with APS and STAT5, and activationBy similarity1
Sitei454Interaction with PTPN6By similarity1

Binary interactionsi

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

Protein-protein interaction databases

BioGridi108371. 34 interactors.
DIPiDIP-5732N.
IntActiP19235. 21 interactors.
MINTiMINT-273225.
STRINGi9606.ENSP00000222139.

Chemistry databases

BindingDBiP19235.

Structurei

Secondary structure

1508
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi33 – 45Combined sources13
Beta strandi47 – 49Combined sources3
Beta strandi51 – 58Combined sources8
Beta strandi61 – 67Combined sources7
Beta strandi76 – 83Combined sources8
Beta strandi84 – 86Combined sources3
Beta strandi89 – 91Combined sources3
Beta strandi93 – 98Combined sources6
Turni99 – 101Combined sources3
Beta strandi102 – 108Combined sources7
Helixi111 – 113Combined sources3
Beta strandi116 – 118Combined sources3
Beta strandi120 – 126Combined sources7
Turni127 – 129Combined sources3
Beta strandi131 – 137Combined sources7
Helixi139 – 141Combined sources3
Beta strandi142 – 144Combined sources3
Beta strandi149 – 155Combined sources7
Beta strandi157 – 159Combined sources3
Beta strandi162 – 167Combined sources6
Beta strandi169 – 171Combined sources3
Helixi175 – 177Combined sources3
Beta strandi178 – 185Combined sources8
Beta strandi188 – 190Combined sources3
Beta strandi195 – 198Combined sources4
Beta strandi204 – 207Combined sources4
Beta strandi212 – 224Combined sources13
Turni226 – 228Combined sources3
Beta strandi240 – 244Combined sources5
Turni245 – 247Combined sources3
Helixi250 – 282Combined sources33

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CN4X-ray2.80A/B25-249[»]
1EBAX-ray2.70A/B34-248[»]
1EBPX-ray2.80A/B34-244[»]
1EERX-ray1.90B/C27-250[»]
1ERNX-ray2.40A/B34-246[»]
2JIXX-ray3.20B/C/E25-249[»]
2MV6NMR-A237-284[»]
4Y5VX-ray2.60C/F/I32-249[»]
4Y5XX-ray3.15C/F/I/L32-249[»]
4Y5YX-ray2.85C/F32-249[»]
ProteinModelPortaliP19235.
SMRiP19235.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19235.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini147 – 247Fibronectin type-IIIPROSITE-ProRule annotationAdd BLAST101

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni454 – 456Required for high-affinity SOCS3 binding3

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi233 – 237WSXWS motif5
Motifi282 – 290Box 1 motif9
Motifi452 – 457ITIM motif6

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

eggNOGiENOG410IFGH. Eukaryota.
ENOG4111PGS. LUCA.
GeneTreeiENSGT00840000129885.
HOGENOMiHOG000059639.
HOVERGENiHBG005595.
InParanoidiP19235.
KOiK05079.
OMAiFMVRARM.
OrthoDBiEOG091G0AK8.
PhylomeDBiP19235.
TreeFamiTF336573.

Family and domain databases

CDDicd00063. FN3. 1 hit.
Gene3Di2.60.40.10. 2 hits.
InterProiIPR009167. Erythropoietin_rcpt.
IPR003961. FN3_dom.
IPR015152. Growth/epo_recpt_lig-bind.
IPR013783. Ig-like_fold.
IPR003528. Long_hematopoietin_rcpt_CS.
[Graphical view]
PANTHERiPTHR23037:SF28. PTHR23037:SF28. 1 hit.
PfamiPF09067. EpoR_lig-bind. 1 hit.
PF00041. fn3. 1 hit.
[Graphical view]
PIRSFiPIRSF001959. EPO_receptor. 1 hit.
SMARTiSM00060. FN3. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 2 hits.
PROSITEiPS50853. FN3. 1 hit.
PS01352. HEMATOPO_REC_L_F1. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform EPOR-F (identifier: P19235-1) [UniParc]FASTAAdd to basket
Also known as: Full-length form

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

« Hide

        10         20         30         40         50
MDHLGASLWP QVGSLCLLLA GAAWAPPPNL PDPKFESKAA LLAARGPEEL
60 70 80 90 100
LCFTERLEDL VCFWEEAASA GVGPGNYSFS YQLEDEPWKL CRLHQAPTAR
110 120 130 140 150
GAVRFWCSLP TADTSSFVPL ELRVTAASGA PRYHRVIHIN EVVLLDAPVG
160 170 180 190 200
LVARLADESG HVVLRWLPPP ETPMTSHIRY EVDVSAGNGA GSVQRVEILE
210 220 230 240 250
GRTECVLSNL RGRTRYTFAV RARMAEPSFG GFWSAWSEPV SLLTPSDLDP
260 270 280 290 300
LILTLSLILV VILVLLTVLA LLSHRRALKQ KIWPGIPSPE SEFEGLFTTH
310 320 330 340 350
KGNFQLWLYQ NDGCLWWSPC TPFTEDPPAS LEVLSERCWG TMQAVEPGTD
360 370 380 390 400
DEGPLLEPVG SEHAQDTYLV LDKWLLPRNP PSEDLPGPGG SVDIVAMDEG
410 420 430 440 450
SEASSCSSAL ASKPSPEGAS AASFEYTILD PSSQLLRPWT LCPELPPTPP
460 470 480 490 500
HLKYLYLVVS DSGISTDYSS GDSQGAQGGL SDGPYSNPYE NSLIPAAEPL

PPSYVACS
Length:508
Mass (Da):55,065
Last modified:November 1, 1990 - v1
Checksum:iF9F326E162E9512A
GO
Isoform EPOR-S (identifier: P19235-2) [UniParc]FASTAAdd to basket
Also known as: Soluble form

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

Show »
Length:241
Mass (Da):26,456
Checksum:i0E74BF60CCFB694D
GO
Isoform EPOR-T (identifier: P19235-3) [UniParc]FASTAAdd to basket
Also known as: Truncated form

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

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti102A → R no nucleotide entry (PubMed:2163695).Curated1
Sequence conflicti189 – 190GA → RP no nucleotide entry (PubMed:2163695).Curated2
Sequence conflicti244T → E no nucleotide entry (PubMed:2163695).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_033919380P → A.Corresponds to variant rs35423344dbSNPEnsembl.1
Natural variantiVAR_027372487N → S in ECYT1 and erythroleukemia. 1 PublicationCorresponds to variant rs62638745dbSNPEnsembl.1
Natural variantiVAR_027373488P → S.2 PublicationsCorresponds to variant rs142094773dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_009508196 – 241VEILE…SEPVS → GTVFLSPDWLSSTRARPHVI YFCLLRVPRPDSAPRWRSWR AAPSVC in isoform EPOR-S. 1 PublicationAdd BLAST46
Alternative sequenceiVSP_009509242 – 508Missing in isoform EPOR-S. 1 PublicationAdd BLAST267
Alternative sequenceiVSP_009510306 – 328LWLYQ…TEDPP → VGGLVVPSVPGLPCFLQPNC RPL in isoform EPOR-T. 1 PublicationAdd BLAST23
Alternative sequenceiVSP_009511329 – 508Missing in isoform EPOR-T. 1 PublicationAdd BLAST180

Sequence databases

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

Genome annotation databases

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

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CN4X-ray2.80A/B25-249[»]
1EBAX-ray2.70A/B34-248[»]
1EBPX-ray2.80A/B34-244[»]
1EERX-ray1.90B/C27-250[»]
1ERNX-ray2.40A/B34-246[»]
2JIXX-ray3.20B/C/E25-249[»]
2MV6NMR-A237-284[»]
4Y5VX-ray2.60C/F/I32-249[»]
4Y5XX-ray3.15C/F/I/L32-249[»]
4Y5YX-ray2.85C/F32-249[»]
ProteinModelPortaliP19235.
SMRiP19235.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108371. 34 interactors.
DIPiDIP-5732N.
IntActiP19235. 21 interactors.
MINTiMINT-273225.
STRINGi9606.ENSP00000222139.

Chemistry databases

BindingDBiP19235.
ChEMBLiCHEMBL1817.
DrugBankiDB00012. Darbepoetin alfa.
DB00016. Epoetin alfa.
DB08923. Epoetin Zeta.
DB08894. Peginesatide.
GuidetoPHARMACOLOGYi1718.

PTM databases

iPTMnetiP19235.
PhosphoSitePlusiP19235.

Polymorphism and mutation databases

BioMutaiEPOR.
DMDMi119524.

Proteomic databases

PaxDbiP19235.
PeptideAtlasiP19235.
PRIDEiP19235.
TopDownProteomicsiP19235-3. [P19235-3]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi2057.
DisGeNETi2057.
GeneCardsiEPOR.
H-InvDBHIX0080119.
HGNCiHGNC:3416. EPOR.
MalaCardsiEPOR.
MIMi133100. phenotype.
133171. gene.
neXtProtiNX_P19235.
OpenTargetsiENSG00000187266.
Orphaneti90042. Primary familial polycythemia.
PharmGKBiPA27834.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IFGH. Eukaryota.
ENOG4111PGS. LUCA.
GeneTreeiENSGT00840000129885.
HOGENOMiHOG000059639.
HOVERGENiHBG005595.
InParanoidiP19235.
KOiK05079.
OMAiFMVRARM.
OrthoDBiEOG091G0AK8.
PhylomeDBiP19235.
TreeFamiTF336573.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000105532-MONOMER.
SignaLinkiP19235.
SIGNORiP19235.

Miscellaneous databases

ChiTaRSiEPOR. human.
EvolutionaryTraceiP19235.
GeneWikiiErythropoietin_receptor.
GenomeRNAii2057.
PROiP19235.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000187266.
CleanExiHS_EPOR.
ExpressionAtlasiP19235. baseline and differential.
GenevisibleiP19235. HS.

Family and domain databases

CDDicd00063. FN3. 1 hit.
Gene3Di2.60.40.10. 2 hits.
InterProiIPR009167. Erythropoietin_rcpt.
IPR003961. FN3_dom.
IPR015152. Growth/epo_recpt_lig-bind.
IPR013783. Ig-like_fold.
IPR003528. Long_hematopoietin_rcpt_CS.
[Graphical view]
PANTHERiPTHR23037:SF28. PTHR23037:SF28. 1 hit.
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]
ProtoNetiSearch...

Entry informationi

Entry nameiEPOR_HUMAN
AccessioniPrimary (citable) accession number: P19235
Secondary accession number(s): B2RCG4, Q15443, Q2M205
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: November 30, 2016
This is version 202 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.