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Entry version 218 (13 Feb 2019)
Sequence version 1 (01 Nov 1990)
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Protein

Erythropoietin receptor

Gene

EPOR

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei117Required for ligand binding1
Sitei426Required for STAT5/PTPN11/SOCS3 bindingBy similarity1
Sitei456Required for STAT1/STAT3 activation1
Sitei485Required for CrkL bindingBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • erythropoietin receptor activity Source: UniProtKB
  • identical protein binding Source: IntAct

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionReceptor

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-9006335 Signaling by Erythropoietin
R-HSA-9027276 Erythropoietin activates Phosphoinositide-3-kinase (PI3K)
R-HSA-9027277 Erythropoietin activates Phospholipase C gamma (PLCG)
R-HSA-9027283 Erythropoietin activates STAT5
R-HSA-9027284 Erythropoietin activates RAS

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
P19235

SIGNOR Signaling Network Open Resource

More...
SIGNORi
P19235

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Erythropoietin receptor
Short name:
EPO-R
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:EPOR
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 19

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000187266.13

Human Gene Nomenclature Database

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HGNCi
HGNC:3416 EPOR

Online Mendelian Inheritance in Man (OMIM)

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MIMi
133171 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P19235

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini25 – 250ExtracellularSequence analysisAdd BLAST226
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei251 – 273HelicalSequence analysisAdd BLAST23
Topological domaini274 – 508CytoplasmicSequence analysisAdd BLAST235

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>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
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_027372487N → S in ECYT1 and erythroleukemia. 1 PublicationCorresponds to variant dbSNP:rs62638745EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

DisGeNET

More...
DisGeNETi
2057

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

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GeneReviewsi
EPOR

MalaCards human disease database

More...
MalaCardsi
EPOR
MIMi133100 phenotype

Open Targets

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OpenTargetsi
ENSG00000187266

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
90042 Primary familial polycythemia

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA27834

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL1817

Drug and drug target database

More...
DrugBanki
DB00012 Darbepoetin alfa
DB08923 Epoetin Zeta
DB00016 Erythropoietin
DB09107 Methoxy polyethylene glycol-epoetin beta
DB08894 Peginesatide

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
1718

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
EPOR

Domain mapping of disease mutations (DMDM)

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DMDMi
119524

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 24Add BLAST24
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001086825 – 508Erythropoietin receptorAdd BLAST484

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi52 ↔ 62
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi76N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi91 ↔ 107
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki281Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P19235

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P19235

PeptideAtlas

More...
PeptideAtlasi
P19235

PRoteomics IDEntifications database

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PRIDEi
P19235

ProteomicsDB human proteome resource

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ProteomicsDBi
53638
53639 [P19235-2]
53640 [P19235-3]

Consortium for Top Down Proteomics

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TopDownProteomicsi
P19235-3 [P19235-3]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P19235

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P19235

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>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

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000187266 Expressed in 226 organ(s), highest expression level in type B pancreatic cell

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P19235 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P19235 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA077613

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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). Interacts with RHEX; this interaction occurs in a erythropoietin (EPO)-dependent manner (PubMed:25092874). Interaction with the ubiquitin ligase NOSIP mediates EPO-induced cell proliferation. Interacts with ATXN2L.By similarity8 Publications

Sites

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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
108371, 34 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P19235

Database of interacting proteins

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DIPi
DIP-5732N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
P19235

Protein interaction database and analysis system

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IntActi
P19235, 21 interactors

Molecular INTeraction database

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MINTi
P19235

STRING: functional protein association networks

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STRINGi
9606.ENSP00000222139

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P19235

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1508
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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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[»]
6E2QX-ray2.65M/N/O/P273-338[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P19235

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P19235

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P19235

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini147 – 247Fibronectin type-IIIPROSITE-ProRule annotationAdd BLAST101

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni454 – 456Required for high-affinity SOCS3 binding3

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi233 – 237WSXWS motif5
Motifi282 – 290Box 1 motif9
Motifi452 – 457ITIM motif6

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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.

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
ENOG410IFGH Eukaryota
ENOG4111PGS LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000160315

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000059639

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG005595

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P19235

KEGG Orthology (KO)

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KOi
K05079

Identification of Orthologs from Complete Genome Data

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OMAi
VGSEHAQ

Database of Orthologous Groups

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OrthoDBi
1442632at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P19235

TreeFam database of animal gene trees

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TreeFami
TF336573

Family and domain databases

Conserved Domains Database

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CDDi
cd00063 FN3, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.60.40.10, 2 hits

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR009167 Erythropoietin_rcpt
IPR003961 FN3_dom
IPR036116 FN3_sf
IPR015152 Growth/epo_recpt_lig-bind
IPR013783 Ig-like_fold
IPR003528 Long_hematopoietin_rcpt_CS

The PANTHER Classification System

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PANTHERi
PTHR23037:SF28 PTHR23037:SF28, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF09067 EpoR_lig-bind, 1 hit
PF00041 fn3, 1 hit

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF001959 EPO_receptor, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00060 FN3, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF49265 SSF49265, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50853 FN3, 1 hit
PS01352 HEMATOPO_REC_L_F1, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 3 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
K7ERB5K7ERB5_HUMAN
Erythropoietin receptor
EPOR
276Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
K7EP50K7EP50_HUMAN
Erythropoietin receptor
EPOR
130Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
K7EN47K7EN47_HUMAN
Erythropoietin receptor
EPOR
119Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>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 dbSNP:rs35423344EnsemblClinVar.1
Natural variantiVAR_027372487N → S in ECYT1 and erythroleukemia. 1 PublicationCorresponds to variant dbSNP:rs62638745EnsemblClinVar.1
Natural variantiVAR_027373488P → S2 PublicationsCorresponds to variant dbSNP:rs142094773EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>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:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS12260.1 [P19235-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
A43799 ZUHUR
I38208

NCBI Reference Sequences

More...
RefSeqi
NP_000112.1, NM_000121.3 [P19235-1]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.631624

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000222139; ENSP00000222139; ENSG00000187266 [P19235-1]
ENST00000592375; ENSP00000467809; ENSG00000187266 [P19235-3]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
2057

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:2057

UCSC genome browser

More...
UCSCi
uc002mrj.3 human [P19235-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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[»]
6E2QX-ray2.65M/N/O/P273-338[»]
ProteinModelPortaliP19235
SMRiP19235
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108371, 34 interactors
CORUMiP19235
DIPiDIP-5732N
ELMiP19235
IntActiP19235, 21 interactors
MINTiP19235
STRINGi9606.ENSP00000222139

Chemistry databases

BindingDBiP19235
ChEMBLiCHEMBL1817
DrugBankiDB00012 Darbepoetin alfa
DB08923 Epoetin Zeta
DB00016 Erythropoietin
DB09107 Methoxy polyethylene glycol-epoetin beta
DB08894 Peginesatide
GuidetoPHARMACOLOGYi1718

PTM databases

iPTMnetiP19235
PhosphoSitePlusiP19235

Polymorphism and mutation databases

BioMutaiEPOR
DMDMi119524

Proteomic databases

jPOSTiP19235
PaxDbiP19235
PeptideAtlasiP19235
PRIDEiP19235
ProteomicsDBi53638
53639 [P19235-2]
53640 [P19235-3]
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

Comparative Toxicogenomics Database

More...
CTDi
2057
DisGeNETi2057
EuPathDBiHostDB:ENSG00000187266.13

GeneCards: human genes, protein and diseases

More...
GeneCardsi
EPOR
GeneReviewsiEPOR

H-Invitational Database, human transcriptome db

More...
H-InvDBi
HIX0080119
HGNCiHGNC:3416 EPOR
HPAiHPA077613
MalaCardsiEPOR
MIMi133100 phenotype
133171 gene
neXtProtiNX_P19235
OpenTargetsiENSG00000187266
Orphaneti90042 Primary familial polycythemia
PharmGKBiPA27834

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiENOG410IFGH Eukaryota
ENOG4111PGS LUCA
GeneTreeiENSGT00940000160315
HOGENOMiHOG000059639
HOVERGENiHBG005595
InParanoidiP19235
KOiK05079
OMAiVGSEHAQ
OrthoDBi1442632at2759
PhylomeDBiP19235
TreeFamiTF336573

Enzyme and pathway databases

ReactomeiR-HSA-9006335 Signaling by Erythropoietin
R-HSA-9027276 Erythropoietin activates Phosphoinositide-3-kinase (PI3K)
R-HSA-9027277 Erythropoietin activates Phospholipase C gamma (PLCG)
R-HSA-9027283 Erythropoietin activates STAT5
R-HSA-9027284 Erythropoietin activates RAS
SignaLinkiP19235
SIGNORiP19235

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
EPOR human
EvolutionaryTraceiP19235

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
Erythropoietin_receptor

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
2057

Protein Ontology

More...
PROi
PR:P19235

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000187266 Expressed in 226 organ(s), highest expression level in type B pancreatic cell
ExpressionAtlasiP19235 baseline and differential
GenevisibleiP19235 HS

Family and domain databases

CDDicd00063 FN3, 1 hit
Gene3Di2.60.40.10, 2 hits
InterProiView protein in InterPro
IPR009167 Erythropoietin_rcpt
IPR003961 FN3_dom
IPR036116 FN3_sf
IPR015152 Growth/epo_recpt_lig-bind
IPR013783 Ig-like_fold
IPR003528 Long_hematopoietin_rcpt_CS
PANTHERiPTHR23037:SF28 PTHR23037:SF28, 1 hit
PfamiView protein in Pfam
PF09067 EpoR_lig-bind, 1 hit
PF00041 fn3, 1 hit
PIRSFiPIRSF001959 EPO_receptor, 1 hit
SMARTiView protein in SMART
SM00060 FN3, 1 hit
SUPFAMiSSF49265 SSF49265, 2 hits
PROSITEiView protein in PROSITE
PS50853 FN3, 1 hit
PS01352 HEMATOPO_REC_L_F1, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiEPOR_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P19235
Secondary accession number(s): B2RCG4, Q15443, Q2M205
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: February 13, 2019
This is version 218 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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