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Protein

Erythropoietin receptor

Gene

EPOR

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Receptor for erythropoietin. Mediates erythropoietin-induced erythroblast proliferation and differentiation. Upon EPO stimulation, EPOR dimerizes triggering the JAK2/STAT5 signaling cascade. In some cell types, can also activate STAT1 and STAT3. May also activate the LYN tyrosine kinase.
Isoform EPOR-T acts as a dominant-negative receptor of EPOR-mediated signaling.

Sites

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

GO - Molecular functioni

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

GO - Biological processi

  • brain development Source: Ensembl
  • decidualization Source: Ensembl
  • heart development Source: Ensembl
  • signal transduction Source: ProtInc

Keywordsi

Molecular functionReceptor

Enzyme and pathway databases

SignaLinkiP19235
SIGNORiP19235

Names & Taxonomyi

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

Organism-specific databases

EuPathDBiHostDB:ENSG00000187266.13
HGNCiHGNC:3416 EPOR
MIMi133171 gene
neXtProtiNX_P19235

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
Topological domaini25 – 250ExtracellularSequence analysisAdd BLAST226
Transmembranei251 – 273HelicalSequence analysisAdd BLAST23
Topological domaini274 – 508CytoplasmicSequence analysisAdd BLAST235

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Involvement in diseasei

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

Mutagenesis

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

Keywords - Diseasei

Congenital erythrocytosis, Disease mutation

Organism-specific databases

DisGeNETi2057
MalaCardsiEPOR
MIMi133100 phenotype
OpenTargetsiENSG00000187266
Orphaneti90042 Primary familial polycythemia
PharmGKBiPA27834

Chemistry databases

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

Polymorphism and mutation databases

BioMutaiEPOR
DMDMi119524

PTM / Processingi

Molecule processing

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

Amino acid modifications

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

Post-translational modificationi

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

Keywords - PTMi

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

Proteomic databases

PaxDbiP19235
PeptideAtlasiP19235
PRIDEiP19235
ProteomicsDBi53638
53639 [P19235-2]
53640 [P19235-3]
TopDownProteomicsiP19235-3 [P19235-3]

PTM databases

iPTMnetiP19235
PhosphoSitePlusiP19235

Expressioni

Tissue specificityi

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

Gene expression databases

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

Organism-specific databases

HPAiHPA077613

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). 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

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

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

Chemistry databases

BindingDBiP19235

Structurei

Secondary structure

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

3D structure databases

ProteinModelPortaliP19235
SMRiP19235
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19235

Family & Domainsi

Domains and Repeats

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

Region

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

Motif

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

Domaini

The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding.
The box 1 motif is required for JAK interaction and/or activation.

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IFGH Eukaryota
ENOG4111PGS LUCA
GeneTreeiENSGT00920000149107
HOGENOMiHOG000059639
HOVERGENiHBG005595
InParanoidiP19235
KOiK05079
OMAiVGSEHAQ
OrthoDBiEOG091G0AK8
PhylomeDBiP19235
TreeFamiTF336573

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

Sequences (3+)i

Sequence statusi: Complete.

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

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

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
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

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:
K7EP50K7EP50_HUMAN
Erythropoietin receptor
EPOR
130Annotation score:
K7EN47K7EN47_HUMAN
Erythropoietin receptor
EPOR
119Annotation score:

Experimental Info

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

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_033919380P → A. Corresponds to variant 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
Alternative sequenceiVSP_009508196 – 241VEILE…SEPVS → GTVFLSPDWLSSTRARPHVI YFCLLRVPRPDSAPRWRSWR AAPSVC in isoform EPOR-S. 1 PublicationAdd BLAST46
Alternative sequenceiVSP_009509242 – 508Missing in isoform EPOR-S. 1 PublicationAdd BLAST267
Alternative sequenceiVSP_009510306 – 328LWLYQ…TEDPP → VGGLVVPSVPGLPCFLQPNC RPL in isoform EPOR-T. 1 PublicationAdd BLAST23
Alternative sequenceiVSP_009511329 – 508Missing in isoform EPOR-T. 1 PublicationAdd BLAST180

Sequence databases

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

Genome annotation databases

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

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

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

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

CTDi2057
DisGeNETi2057
EuPathDBiHostDB:ENSG00000187266.13
GeneCardsiEPOR
H-InvDBiHIX0080119
HGNCiHGNC:3416 EPOR
HPAiHPA077613
MalaCardsiEPOR
MIMi133100 phenotype
133171 gene
neXtProtiNX_P19235
OpenTargetsiENSG00000187266
Orphaneti90042 Primary familial polycythemia
PharmGKBiPA27834
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IFGH Eukaryota
ENOG4111PGS LUCA
GeneTreeiENSGT00920000149107
HOGENOMiHOG000059639
HOVERGENiHBG005595
InParanoidiP19235
KOiK05079
OMAiVGSEHAQ
OrthoDBiEOG091G0AK8
PhylomeDBiP19235
TreeFamiTF336573

Enzyme and pathway databases

SignaLinkiP19235
SIGNORiP19235

Miscellaneous databases

ChiTaRSiEPOR human
EvolutionaryTraceiP19235
GeneWikiiErythropoietin_receptor
GenomeRNAii2057
PROiPR:P19235
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000187266 Expressed in 226 organ(s), highest expression level in type B pancreatic cell
CleanExiHS_EPOR
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
ProtoNetiSearch...

Entry informationi

Entry nameiEPOR_HUMAN
AccessioniPrimary (citable) accession number: P19235
Secondary accession number(s): B2RCG4, Q15443, Q2M205
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: October 10, 2018
This is version 214 of the entry and version 1 of the sequence. See 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 entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  2. SIMILARITY comments
    Index of protein domains and families
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  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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