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Protein

Erythropoietin receptor

Gene

Epor

Organism
Mus musculus (Mouse)
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.2 Publications

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.

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>Sitei116Required for ligand bindingBy similarity1
Sitei425Required for STAT5/PTPN11/SOCS3 binding1

<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

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
Biological processHost-virus interaction

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-9027276 Erythropoietin activates Phosphoinositide-3-kinase (PI3K)
R-MMU-9027284 Erythropoietin activates RAS

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P14753

<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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 9

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:95408 Epor

<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 – 249ExtracellularSequence analysisAdd BLAST225
<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>Transmembranei250 – 272HelicalSequence analysisAdd BLAST23
Topological domaini273 – 507CytoplasmicSequence 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

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>Mutagenesisi153R → C: Reduced JAK2/STAT5 activation. 1 Publication1
Mutagenesisi232W → A, C, D, E, G, H, I, K, L, M, N, P, Q, R, S, T, V or Y: Loss of EPO binding. 1 Publication1
Mutagenesisi232W → F: Greatly reduced EPO binding. 1 Publication1
Mutagenesisi233S → A: Not secreted and loss of EPO binding. 2 Publications1
Mutagenesisi233S → C, D, E, F, H, I, K, L, M, N, P, Q, R, V, W or Y: Loss of EPO binding. 2 Publications1
Mutagenesisi233S → G: 50-fold less EPO binding. 2 Publications1
Mutagenesisi233S → T: 2-fold less EPO binding. 2 Publications1
Mutagenesisi234A → C, D, G, H, K, N, Q, R, S or T: No change in EPO binding. 2 Publications1
Mutagenesisi234A → E: Enhanced secretion and increased EPO binding. 2 Publications1
Mutagenesisi234A → F, I, M, W or Y: Little EPO binding. 2 Publications1
Mutagenesisi234A → L, P or V: Reduced EPO binding. 2 Publications1
Mutagenesisi235W → A, C, D, E, G, H, I, K, L, M, N, P, Q, R, S, T or V: Loss of EPO binding. 1 Publication1
Mutagenesisi235W → F: 14-fold less EPO binding. 1 Publication1
Mutagenesisi235W → Y: 100-fold less EPO binding. 1 Publication1
Mutagenesisi236S → A, C or G: Reduced EPO binding. 1 Publication1
Mutagenesisi236S → D, E, F, H, I, K, L, M, N, P, Q, R, V or W: Loss of EPO binding. 1 Publication1
Mutagenesisi236S → T: No loss of EPO binding. 1 Publication1
Mutagenesisi236S → Y: Greatly reduced EPO binding. 1 Publication1
Mutagenesisi304Q → L: Greatly reduced JAK2/STAT5 activation and some loss of mitogenic response. 2 Publications1
Mutagenesisi306W → R: No JAK2 binding nor JAK2/STAT5 activation. No EPO-induced phosphorylation. Complete loss of mitogenic response. 3 Publications1
Mutagenesisi317S → R: Slightly reduced JAK2/STAT5 activation and mitogenic response. 2 Publications1
Mutagenesisi324E → V: No change in JAK2/STAT5 activation nor mitogenic response. 2 Publications1
Mutagenesisi330L → R: Reduced JAK2/STAT5 activation. 2 Publications1
Mutagenesisi331E → A: No change in JAK2/STAT5 activation nor mitogenic response. 2 Publications1
Mutagenesisi331E → K: Reduced JAK2/STAT5 activation and mitogenic response. 2 Publications1
Mutagenesisi367Y → F: No STAT5 activation. 2 Publications1
Mutagenesisi425Y → F: No PTPN11 binding, reduced PTPN11 tyrosine phosphorylation and reduced cell proliferation. 1 Publication1
Mutagenesisi453 – 455YLY → FLF: No binding to PTPN6 SH2 domains. Enhanced JAK2 activation and cell proliferation. 1 Publication3
Mutagenesisi453Y → F: No PTPN6 binding, binds PTPN11. 2 Publications1
Mutagenesisi455Y → F: Binds to PTPN6 and PTPN11 SH2 domains. 2 Publications1
Mutagenesisi467Y → F: No loss of PTPN11 binding. 1 Publication1
Mutagenesisi484Y → F: No loss of PTPN11 binding. 1 Publication1
Mutagenesisi488Y → F: No loss of PTPN11 binding. 1 Publication1
Mutagenesisi503Y → F: No loss of PTPN11 binding. 1 Publication1

<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_000001086925 – 507Erythropoietin receptorAdd BLAST483

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 ↔ 62By similarity
<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>Glycosylationi75N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi90 ↔ 106By similarity
<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-linki280Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
<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 residuei367Phosphotyrosine; by JAK21 Publication2 Publications1
Modified residuei425Phosphotyrosine; by JAK22 Publications1
Cross-linki452Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei453Phosphotyrosine; by JAK21 Publication1 Publication1
Modified residuei455Phosphotyrosine; by JAK22 Publications1
Modified residuei467Phosphotyrosine; by JAK21 Publication1
Modified residuei484Phosphotyrosine; by JAK21 Publication1
Modified residuei488Phosphotyrosine; by JAK21 Publication1
Modified residuei503Phosphotyrosine; by JAK21 Publication1
Isoform EPOR-S (identifier: P14753-2)
Glycosylationi232C-linked (Man) tryptophan1 Publication1

<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

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).By similarity
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.By similarity1 Publication

Keywords - PTMi

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

Proteomic databases

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

More...
PaxDbi
P14753

PRoteomics IDEntifications database

More...
PRIDEi
P14753

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P14753

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

More...
PhosphoSitePlusi
P14753

<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

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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000006235 Expressed in 124 organ(s), highest expression level in blood

CleanEx database of gene expression profiles

More...
CleanExi
MM_EPOR

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P14753 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P14753 MM

<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, 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.By similarity10 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei367Interaction with APS and STAT5, and activation1
Sitei453Interaction with PTPN61

<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
199488, 4 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P14753

Database of interacting proteins

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DIPi
DIP-657N

Protein interaction database and analysis system

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IntActi
P14753, 10 interactors

Molecular INTeraction database

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MINTi
P14753

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000006397

<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

1507
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P14753

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

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SMRi
P14753

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...

<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>Domaini146 – 246Fibronectin type-IIIPROSITE-ProRule annotationAdd BLAST101

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>Motifi232 – 236WSXWS motif5
Motifi281 – 289Box 1 motif9
Motifi451 – 456ITIM 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

More...
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
P14753

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

More...
OrthoDBi
EOG091G0AK8

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P14753

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

More...
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 (2+)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 2 <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
Note: Additional isoforms seem to exist.

This entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform EPOR-F (identifier: P14753-1) [UniParc]FASTAAdd to basket
Also known as: Membrane-bound form

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

« Hide
        10         20         30         40         50
MDKLRVPLWP RVGPLCLLLA GAAWAPSPSL PDPKFESKAA LLASRGSEEL
60 70 80 90 100
LCFTQRLEDL VCFWEEAASS GMDFNYSFSY QLEGESRKSC SLHQAPTVRG
110 120 130 140 150
SVRFWCSLPT ADTSSFVPLE LQVTEASGSP RYHRIIHINE VVLLDAPAGL
160 170 180 190 200
LARRAEEGSH VVLRWLPPPG APMTTHIRYE VDVSAGNRAG GTQRVEVLEG
210 220 230 240 250
RTECVLSNLR GGTRYTFAVR ARMAEPSFSG FWSAWSEPAS LLTASDLDPL
260 270 280 290 300
ILTLSLILVL ISLLLTVLAL LSHRRTLQQK IWPGIPSPES EFEGLFTTHK
310 320 330 340 350
GNFQLWLLQR DGCLWWSPGS SFPEDPPAHL EVLSEPRWAV TQAGDPGADD
360 370 380 390 400
EGPLLEPVGS EHAQDTYLVL DKWLLPRTPC SENLSGPGGS VDPVTMDEAS
410 420 430 440 450
ETSSCPSDLA SKPRPEGTSP SSFEYTILDP SSQLLCPRAL PPELPPTPPH
460 470 480 490 500
LKYLYLVVSD SGISTDYSSG GSQGVHGDSS DGPYSHPYEN SLVPDSEPLH

PGYVACS
Length:507
Mass (Da):55,194
Last modified:April 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:i067657A2E26451CA
GO
Isoform EPOR-S (identifier: P14753-2) [UniParc]FASTAAdd to basket
Also known as: Soluble form

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

Show »
Length:265
Mass (Da):28,798
Checksum:i3368CF30E673F5CC
GO

<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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A1L1SRC0A0A1L1SRC0_MOUSE
Erythropoietin receptor
Epor
111Annotation 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 conflicti291E → D in AAB20029 (PubMed:1656233).Curated1

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. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_009512246 – 265DLDPL…ISLLL → GEALVPRGAGGAGPNTRQTP in isoform EPOR-S. CuratedAdd BLAST20
Alternative sequenceiVSP_009513266 – 507Missing in isoform EPOR-S. CuratedAdd BLAST242

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
J04843 mRNA Translation: AAA37571.1
X53081 Genomic DNA Translation: CAA37248.1
S59388 mRNA Translation: AAB20029.2
BC003953 mRNA Translation: AAH03953.1
BC046282 mRNA Translation: AAH46282.1
M38133 Genomic DNA Translation: AAA37572.1
M62360 Genomic DNA Translation: AAA37582.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS22915.1 [P14753-1]

Protein sequence database of the Protein Information Resource

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PIRi
A41686 A32385
S14081

NCBI Reference Sequences

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RefSeqi
NP_034279.3, NM_010149.3 [P14753-1]

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Mm.2653

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000006397; ENSMUSP00000006397; ENSMUSG00000006235 [P14753-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
13857

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:13857

UCSC genome browser

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UCSCi
uc009ond.1 mouse [P14753-1]
uc009one.1 mouse [P14753-2]

Keywords - Coding sequence diversityi

Alternative splicing

<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
J04843 mRNA Translation: AAA37571.1
X53081 Genomic DNA Translation: CAA37248.1
S59388 mRNA Translation: AAB20029.2
BC003953 mRNA Translation: AAH03953.1
BC046282 mRNA Translation: AAH46282.1
M38133 Genomic DNA Translation: AAA37572.1
M62360 Genomic DNA Translation: AAA37582.1
CCDSiCCDS22915.1 [P14753-1]
PIRiA41686 A32385
S14081
RefSeqiNP_034279.3, NM_010149.3 [P14753-1]
UniGeneiMm.2653

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
2MXBNMR-A236-283[»]
ProteinModelPortaliP14753
SMRiP14753
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199488, 4 interactors
CORUMiP14753
DIPiDIP-657N
IntActiP14753, 10 interactors
MINTiP14753
STRINGi10090.ENSMUSP00000006397

PTM databases

iPTMnetiP14753
PhosphoSitePlusiP14753

Proteomic databases

PaxDbiP14753
PRIDEiP14753

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000006397; ENSMUSP00000006397; ENSMUSG00000006235 [P14753-1]
GeneIDi13857
KEGGimmu:13857
UCSCiuc009ond.1 mouse [P14753-1]
uc009one.1 mouse [P14753-2]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
2057
MGIiMGI:95408 Epor

Phylogenomic databases

eggNOGiENOG410IFGH Eukaryota
ENOG4111PGS LUCA
GeneTreeiENSGT00940000160315
HOGENOMiHOG000059639
HOVERGENiHBG005595
InParanoidiP14753
KOiK05079
OMAiVGSEHAQ
OrthoDBiEOG091G0AK8
PhylomeDBiP14753
TreeFamiTF336573

Enzyme and pathway databases

ReactomeiR-MMU-9027276 Erythropoietin activates Phosphoinositide-3-kinase (PI3K)
R-MMU-9027284 Erythropoietin activates RAS
SABIO-RKiP14753

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P14753

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000006235 Expressed in 124 organ(s), highest expression level in blood
CleanExiMM_EPOR
ExpressionAtlasiP14753 baseline and differential
GenevisibleiP14753 MM

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_MOUSE
<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: P14753
Secondary accession number(s): Q63852
<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: April 1, 1990
Last sequence update: April 1, 1990
Last modified: December 5, 2018
This is version 191 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

<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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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