Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P19235

- EPOR_HUMAN

UniProt

P19235 - EPOR_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Erythropoietin receptor

Gene

EPOR

Organism
Homo sapiens (Human)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Sitei117 – 1171Required for ligand binding
Sitei368 – 3681Interaction with APS and STAT5, and activationBy similarity
Sitei426 – 4261Required for STAT5/PTPN11/SOCS3 bindingBy similarity
Sitei454 – 4541Interaction with PTPN6By similarity
Sitei456 – 4561Required for STAT1/STAT3 activation
Sitei485 – 4851Required for CrkL bindingBy similarity

GO - Molecular functioni

  1. erythropoietin receptor activity Source: UniProtKB
  2. identical protein binding Source: IntAct

GO - Biological processi

  1. brain development Source: Ensembl
  2. decidualization Source: Ensembl
  3. erythropoietin-mediated signaling pathway Source: GOC
  4. heart development Source: Ensembl
  5. signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Enzyme and pathway databases

SignaLinkiP19235.

Names & Taxonomyi

Protein namesi
Recommended name:
Erythropoietin receptor
Short name:
EPO-R
Gene namesi
Name:EPOR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:3416. EPOR.

Subcellular locationi

Isoform EPOR-S : Secreted 1 Publication
Note: Secreted and located to the cell surface.

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
  2. 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) [MIM:133100]: An 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.3 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti487 – 4871N → S in ECYT1 and erythroleukemia. 1 Publication
Corresponds to variant rs62638745 [ dbSNP | Ensembl ].
VAR_027372
Natural varianti488 – 4881P → S in ECYT1. 1 Publication
Corresponds to variant rs142094773 [ dbSNP | Ensembl ].
VAR_027373

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi114 – 1141T → A: Little effect on EPO binding. 1 Publication
Mutagenesisi115 – 1151S → A: Little effect on EPO binding. 1 Publication
Mutagenesisi116 – 1161S → A: 10-fold reduction in EPO binding. 1 Publication
Mutagenesisi117 – 1171F → A or L: Greatly reduced EPO binding. 1 Publication
Mutagenesisi117 – 1171F → W: 60-fold reduction in EPO binding. 1 Publication
Mutagenesisi117 – 1171F → Y: 8-fold reduction in EPO binding. 1 Publication
Mutagenesisi118 – 1181V → A: 16-fold reduction in EPO binding. 1 Publication
Mutagenesisi120 – 1201L → A: Some reduction in EPO binding. 1 Publication
Mutagenesisi121 – 1211E → A: Little effect on EPO binding. 1 Publication
Mutagenesisi165 – 1651R → A: Little effect on EPO binding. 1 Publication
Mutagenesisi174 – 1741M → A: Little effect on EPO binding. 1 Publication
Mutagenesisi176 – 1761S → A: 16-fold reduction in EPO binding. 1 Publication
Mutagenesisi177 – 1771H → A: Little effect on EPO binding. 1 Publication
Mutagenesisi179 – 1791R → A: Little effect on EPO binding. 1 Publication
Mutagenesisi454 – 4541Y → F: Some loss of SOCS3 binding. 1 Publication
Mutagenesisi456 – 4561Y → F: Inhibition of STAT1/STAT3 activity. No effect on STAT5 activity. Some loss of SOCS3 binding. 2 Publications
Mutagenesisi468 – 4681Y → F: No effect on STAT1/STAT3 nor STAT5 activity. 1 Publication

Keywords - Diseasei

Congenital erythrocytosis, Disease mutation

Organism-specific databases

MIMi133100. phenotype.
Orphaneti90042. Primary familial polycythemia.
PharmGKBiPA27834.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Add
BLAST
Chaini25 – 508484Erythropoietin receptorPRO_0000010868Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi52 ↔ 62
Glycosylationi76 – 761N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi91 ↔ 107
Cross-linki281 – 281Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei368 – 3681Phosphotyrosine; by JAK2By similarity
Modified residuei426 – 4261Phosphotyrosine; by JAK2By similarity
Cross-linki453 – 453Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei454 – 4541Phosphotyrosine; by JAK2By similarity
Modified residuei456 – 4561Phosphotyrosine; by JAK2By similarity
Modified residuei468 – 4681Phosphotyrosine; by JAK2By similarity
Modified residuei485 – 4851Phosphotyrosine; by JAK2By similarity
Modified residuei489 – 4891Phosphotyrosine; by JAK2By similarity
Modified residuei504 – 5041Phosphotyrosine; by JAK2By similarity

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.
PRIDEiP19235.

PTM databases

PhosphoSiteiP19235.

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

BgeeiP19235.
CleanExiHS_EPOR.
ExpressionAtlasiP19235. baseline and differential.
GenevestigatoriP19235.

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

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. 30 interactions.
DIPiDIP-5732N.
IntActiP19235. 21 interactions.
MINTiMINT-273225.
STRINGi9606.ENSP00000222139.

Structurei

Secondary structure

1
508
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi33 – 4513
Beta strandi51 – 588
Beta strandi61 – 677
Beta strandi76 – 838
Beta strandi84 – 863
Beta strandi89 – 913
Beta strandi93 – 986
Turni99 – 1013
Beta strandi102 – 1087
Helixi111 – 1133
Beta strandi116 – 1183
Beta strandi120 – 1267
Turni127 – 1293
Beta strandi131 – 1377
Helixi139 – 1413
Beta strandi142 – 1443
Beta strandi149 – 1557
Turni157 – 1593
Beta strandi162 – 1676
Beta strandi169 – 1713
Helixi175 – 1773
Beta strandi178 – 1858
Beta strandi188 – 1903
Beta strandi195 – 1984
Beta strandi204 – 2074
Beta strandi212 – 22413
Turni226 – 2283
Beta strandi240 – 2445

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP19235.
SMRiP19235. Positions 32-247.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19235.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini25 – 250226ExtracellularSequence AnalysisAdd
BLAST
Topological domaini274 – 508235CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei251 – 27323HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini147 – 247101Fibronectin type-IIIPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni454 – 4563Required for high-affinity SOCS3 binding

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi233 – 2375WSXWS motif
Motifi282 – 2909Box 1 motif
Motifi452 – 4576ITIM motif

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

eggNOGiNOG46583.
GeneTreeiENSGT00730000111300.
HOGENOMiHOG000059639.
HOVERGENiHBG005595.
InParanoidiP19235.
KOiK05079.
OMAiFMVRARM.
OrthoDBiEOG74BJS6.
PhylomeDBiP19235.
TreeFamiTF336573.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
InterProiIPR009167. Erythropoietin_rcpt.
IPR003961. Fibronectin_type3.
IPR015152. Growth/epo_recpt_lig-bind.
IPR013783. Ig-like_fold.
IPR003528. Long_hematopoietin_rcpt_CS.
[Graphical view]
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. Align

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti102 – 1021A → R no nucleotide entry (PubMed:2163695)Curated
Sequence conflicti189 – 1902GA → RP no nucleotide entry (PubMed:2163695)Curated
Sequence conflicti244 – 2441T → E no nucleotide entry (PubMed:2163695)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti380 – 3801P → A.
Corresponds to variant rs35423344 [ dbSNP | Ensembl ].
VAR_033919
Natural varianti487 – 4871N → S in ECYT1 and erythroleukemia. 1 Publication
Corresponds to variant rs62638745 [ dbSNP | Ensembl ].
VAR_027372
Natural varianti488 – 4881P → S in ECYT1. 1 Publication
Corresponds to variant rs142094773 [ dbSNP | Ensembl ].
VAR_027373

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei196 – 24146VEILE…SEPVS → GTVFLSPDWLSSTRARPHVI YFCLLRVPRPDSAPRWRSWR AAPSVC in isoform EPOR-S. 1 PublicationVSP_009508Add
BLAST
Alternative sequencei242 – 508267Missing in isoform EPOR-S. 1 PublicationVSP_009509Add
BLAST
Alternative sequencei306 – 32823LWLYQ…TEDPP → VGGLVVPSVPGLPCFLQPNC RPL in isoform EPOR-T. 1 PublicationVSP_009510Add
BLAST
Alternative sequencei329 – 508180Missing in isoform EPOR-T. 1 PublicationVSP_009511Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.2. human. [P19235-1]

Polymorphism databases

DMDMi119524.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS12260.1. [P19235-1 ]
PIRi A43799. ZUHUR.
I38208.
RefSeqi NP_000112.1. NM_000121.3. [P19235-1 ]
UniGenei Hs.631624.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CN4 X-ray 2.80 A/B 25-249 [» ]
1EBA X-ray 2.70 A/B 34-248 [» ]
1EBP X-ray 2.80 A/B 34-244 [» ]
1EER X-ray 1.90 B/C 27-250 [» ]
1ERN X-ray 2.40 A/B 34-246 [» ]
2JIX X-ray 3.20 B/C/E 25-249 [» ]
ProteinModelPortali P19235.
SMRi P19235. Positions 32-247.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108371. 30 interactions.
DIPi DIP-5732N.
IntActi P19235. 21 interactions.
MINTi MINT-273225.
STRINGi 9606.ENSP00000222139.

Chemistry

BindingDBi P19235.
ChEMBLi CHEMBL1817.
DrugBanki DB00012. Darbepoetin alfa.
DB00016. Epoetin alfa.
DB08923. Epoetin Zeta.
DB08894. Peginesatide.
GuidetoPHARMACOLOGYi 1718.

PTM databases

PhosphoSitei P19235.

Polymorphism databases

DMDMi 119524.

Proteomic databases

PaxDbi P19235.
PRIDEi P19235.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000222139 ; ENSP00000222139 ; ENSG00000187266 . [P19235-1 ]
ENST00000592375 ; ENSP00000467809 ; ENSG00000187266 . [P19235-3 ]
GeneIDi 2057.
KEGGi hsa:2057.
UCSCi uc002mrj.2. human. [P19235-1 ]

Organism-specific databases

CTDi 2057.
GeneCardsi GC19M011489.
H-InvDB HIX0080119.
HGNCi HGNC:3416. EPOR.
MIMi 133100. phenotype.
133171. gene.
neXtProti NX_P19235.
Orphaneti 90042. Primary familial polycythemia.
PharmGKBi PA27834.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG46583.
GeneTreei ENSGT00730000111300.
HOGENOMi HOG000059639.
HOVERGENi HBG005595.
InParanoidi P19235.
KOi K05079.
OMAi FMVRARM.
OrthoDBi EOG74BJS6.
PhylomeDBi P19235.
TreeFami TF336573.

Enzyme and pathway databases

SignaLinki P19235.

Miscellaneous databases

ChiTaRSi EPOR. human.
EvolutionaryTracei P19235.
GeneWikii Erythropoietin_receptor.
GenomeRNAii 2057.
NextBioi 8365.
PROi P19235.
SOURCEi Search...

Gene expression databases

Bgeei P19235.
CleanExi HS_EPOR.
ExpressionAtlasi P19235. baseline and differential.
Genevestigatori P19235.

Family and domain databases

Gene3Di 2.60.40.10. 2 hits.
InterProi IPR009167. Erythropoietin_rcpt.
IPR003961. Fibronectin_type3.
IPR015152. Growth/epo_recpt_lig-bind.
IPR013783. Ig-like_fold.
IPR003528. Long_hematopoietin_rcpt_CS.
[Graphical view ]
Pfami PF09067. EpoR_lig-bind. 1 hit.
PF00041. fn3. 1 hit.
[Graphical view ]
PIRSFi PIRSF001959. EPO_receptor. 1 hit.
SMARTi SM00060. FN3. 1 hit.
[Graphical view ]
SUPFAMi SSF49265. SSF49265. 2 hits.
PROSITEi PS50853. FN3. 1 hit.
PS01352. HEMATOPO_REC_L_F1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The gene for the human erythropoietin receptor: analysis of the coding sequence and assignment to chromosome 19p."
    Winkelmann J.C., Penny L.A., Deaven L.L., Forget B.G., Jenkins R.B.
    Blood 76:24-30(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Human erythropoietin receptor: cloning, expression, and biologic characterization."
    Jones S.S., D'Andrea A.D., Haines L.L., Wong G.G.
    Blood 76:31-35(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM EPOR-F).
    Tissue: Erythroleukemia and Fetal liver.
  3. "Cloning of the human erythropoietin receptor gene."
    Noguchi C.T., Bae K.S., Chin K., Wada Y., Schechter A.N., Hankins W.D.
    Blood 78:2548-2556(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Placenta.
  4. "The erythropoietin receptor gene: cloning and identification of multiple transcripts in an erythroid cell line OCIM1."
    Ehrenman K., St John T.
    Exp. Hematol. 19:973-977(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM EPOR-F).
    Tissue: Erythroleukemia.
  5. "A truncated erythropoietin receptor that fails to prevent programmed cell death of erythroid cells."
    Nakamura Y., Komatsu N., Nakauchi H.
    Science 257:1138-1141(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS EPOR-F; EPOR-S AND EPOR-T).
    Tissue: Bone marrow and Megakaryoblast.
  6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM EPOR-F).
    Tissue: Caudate nucleus.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM EPOR-F).
    Tissue: Brain.
  9. "Cloning of the gene encoding the human erythropoietin receptor."
    Maouche L., Tournamille C., Hattab C., Boffa G., Cartron J.-P., Chretien S.
    Blood 78:2557-2563(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-96.
    Tissue: Placenta.
  10. "Genomic organization of the human erythropoietin receptor gene."
    Penny L.A., Forget B.G.
    Genomics 11:974-980(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17.
  11. "Isolation of a cDNA encoding a potential soluble receptor for human erythropoietin."
    Todokoro K., Kuramochi S., Nagasawa T., Abe T., Ikawa Y.
    Gene 106:283-284(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (EPOR-S).
    Tissue: Erythroid cell.
  12. "Identification of the human erythropoietin receptor region required for Stat1 and Stat3 activation."
    Kirito K., Nakajima K., Watanabe T., Uchida M., Tanaka M., Ozawa K., Komatsu N.
    Blood 99:102-110(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: STAT1/STAT3 ACTIVATION, MUTAGENESIS OF TYR-456 AND TYR-468.
  13. "Involvement of SH2-containing phosphotyrosine phosphatase Syp in erythropoietin receptor signal transduction pathways."
    Tauchi T., Feng G.-S., Shen R., Hoatlin M., Bagby G.C. Jr., Kabat D., Lu L., Broxmeyer H.E.
    J. Biol. Chem. 270:5631-5635(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PTPN11.
  14. "Identification of a critical ligand binding determinant of the human erythropoietin receptor. Evidence for common ligand binding motifs in the cytokine receptor family."
    Middleton S.A., Johnson D.L., Jin R., McMahon F.J., Collins A., Tullai J., Gruninger R.H., Jolliffe L.K., Mulcahy L.S.
    J. Biol. Chem. 271:14045-14054(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: LIGAND-BINDING SITE, MUTAGENESIS OF THR-114; SER-115; SER-116; PHE-117; VAL-118; LEU-120; GLU-121; ARG-165; MET-174; SER-176; HIS-177 AND ARG-179.
  15. "Increased cell surface expression of C-terminal truncated erythropoietin receptors in polycythemia."
    Motohashi T., Nakamura Y., Osawa M., Hiroyama T., Iwama A., Shibuya A., Nakauchi H.
    Eur. J. Haematol. 67:88-93(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION (ISOFORM EPOR-S).
  16. "A new high affinity binding site for suppressor of cytokine signaling-3 on the erythropoietin receptor."
    Hoertner M., Nielsch U., Mayr L.M., Heinrich P.C., Haan S.
    Eur. J. Biochem. 269:2516-2526(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SOCS3, MUTAGENESIS OF TYR-454 AND TYR-456.
  17. "Erythropoietin receptors associate with a ubiquitin ligase, p33RUL, and require its activity for erythropoietin-induced proliferation."
    Friedman A.D., Nimbalkar D., Quelle F.W.
    J. Biol. Chem. 278:26851-26861(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NOSIP.
  18. "APS, an adaptor protein containing pleckstrin homology (PH) and Src homology-2 (SH2) domains inhibits the JAK-STAT pathway in collaboration with c-Cbl."
    Wakioka T., Sasaki A., Mitsui K., Yokouchi M., Inoue A., Komiya S., Yoshimura A.
    Leukemia 13:760-767(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, INTERACTION WITH APS.
  19. "Cloning and characterization of a family of proteins associated with Mpl."
    Meunier C.F., Bordereaux D., Porteu F., Gisselbrecht S., Chretien S., Courtois G.
    J. Biol. Chem. 277:9139-9147(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ATXN2L.
  20. "Functional mimicry of a protein hormone by a peptide agonist: the EPO receptor complex at 2.8 A."
    Livnah O., Stura E.A., Johnson D.L., Middleton S.A., Mulcahy L.S., Wrighton N.C., Dower W.J., Jolliffe L.K., Wilson I.A.
    Science 273:464-471(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 34-244.
  21. "An antagonist peptide-EPO receptor complex suggests that receptor dimerization is not sufficient for activation."
    Livnah O., Johnson D.L., Stura E.A., Farrell F.X., Barbone F.P., You Y., Liu K.D., Goldsmith M.A., He W., Krause C.D., Pestka S., Jolliffe L.K., Wilson I.A.
    Nat. Struct. Biol. 5:993-1004(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 34-244.
  22. Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 32-244 IN COMPLEX WITH EPO.
  23. "Engineering a soluble extracellular erythropoietin receptor (EPObp) in Pichia pastoris to eliminate microheterogeneity, and its complex with erythropoietin."
    Zhan H., Liu B., Reid S.W., Aoki K.H., Li C., Syed R.S., Karkaria C., Koe G., Sitney K., Hayenga K., Mistry F., Savel L., Dreyer M., Katz B.A., Schreurs J., Matthews D.J., Cheetham J.C., Egrie J., Giebel L.B., Stroud R.M.
    Protein Eng. 12:505-513(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 22-249 IN COMPLEX WITH EPO.
  24. "Crystallographic evidence for preformed dimers of erythropoietin receptor before ligand activation."
    Livnah O., Stura E.A., Middleton S.A., Johnson D.L., Jolliffe L.K., Wilson I.A.
    Science 283:987-990(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 34-246.
  25. "Truncated erythropoietin receptor causes dominantly inherited benign human erythrocytosis."
    de la Chapelle A., Traskelin A.-L., Juvonen E.
    Proc. Natl. Acad. Sci. U.S.A. 90:4495-4499(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN ECYT1.
  26. "Mutation in the negative regulatory element of the erythropoietin receptor gene in a case of sporadic primary polycythemia."
    Sokol L., Prchal J.F., D'Andrea A., Rado T.A., Prchal J.T.
    Exp. Hematol. 22:447-453(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ECYT1 SER-488.
  27. "Missense mutation of the erythropoietin receptor is a rare event in human erythroid malignancies."
    Le Couedic J.-P., Mitjavila M.-T., Villeval J.-L., Feger F., Gobert S., Mayeux P., Casadevall N., Vainchenker W.
    Blood 87:1502-1511(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ECYT1 SER-487, VARIANT ERYTHROLEUKEMIA SER-487.

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: October 29, 2014
This is version 179 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

External Data

Dasty 3