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Protein

Bifunctional epoxide hydrolase 2

Gene

EPHX2

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

Functioni

Bifunctional enzyme (PubMed:12574510). The C-terminal domain has epoxide hydrolase activity and acts on epoxides (alkene oxides, oxiranes) and arene oxides (PubMed:12869654, PubMed:12574510, PubMed:22798687). Plays a role in xenobiotic metabolism by degrading potentially toxic epoxides (By similarity). Also determines steady-state levels of physiological mediators (PubMed:12869654, PubMed:12574510, PubMed:22798687). The N-terminal domain has lipid phosphatase activity, with the highest activity towards threo-9,10-phosphonooxy-hydroxy-octadecanoic acid, followed by erythro-9,10-phosphonooxy-hydroxy-octadecanoic acid, 12-phosphonooxy-octadec-9Z-enoic acid and 12-phosphonooxy-octadec-9E-enoic acid (PubMed:12574510).By similarity4 Publications

Catalytic activityi

An epoxide + H2O = a glycol.3 Publications
(9S,10S)-10-hydroxy-9-(phosphonooxy)octadecanoate + H2O = (9S,10S)-9,10-dihydroxyoctadecanoate + phosphate.3 Publications

Cofactori

Mg2+3 Publications

Enzyme regulationi

Inhibited by 1-(1-acetylpiperidin-4-yl)-3-(4-(trifl uoromethoxy)phenyl)urea (TPAU), 1-cyclohexyl-3-dodecylurea (CDU), 12-(3-adamantan-1-yl-ureido)-dodecanoic acid (AUDA), 1-((3S, 5S, 7S)-adamantan-1-yl)-3-(5-(2-(2-ethoxyethoxy) ethoxy)pentyl)urea (AEPU), N-adamantyl-N[']-cyclohexyl urea (ACU), 4-(((1S, 4S)-4-(3-((3S, 5S, 7S)-adamantan-1-yl) ureido)cyclohexyl)oxy)benzoic acid (c-AUCB), 4-(((1R, 4R)-4-(3-((3S, 5S, 7S)-adamantan-1-yl)ureido)cyclohexyl)oxy)benzoic acid (t-AUCB), 4-(((1R, 4R)-4-(3-(4(trifluoromethoxy)phenyl)ureido)cyclohexyl)oxy)benzoic acid (t-TAUCB) and to a lesser extent by 8-(3-((3S, 5S, 7S)-adamantan-1-yl)ureido) octanoic acid (AUOA).1 Publication

Kineticsi

  1. KM=21 µM for threo-9,10-phosphonooxy-hydroxy-octadecanoic acid3 Publications
  2. KM=1.7 µM for 8,9-EET1 Publication
  3. KM=3.4 µM for 11,12-EET1 Publication
  4. KM=15 µM for 14,15-EET1 Publication
  5. KM=1.5 µM for leukotoxin1 Publication
  6. KM=1.1 mM for p-nitrophenyl phosphate3 Publications
  1. Vmax=338 nmol/min/mg enzyme with threo-9,10-phosphonooxy-hydroxy-octadecanoic acid3 Publications
  2. Vmax=0.9 µmol/min/mg enzyme with 8,9-EET as substrate1 Publication
  3. Vmax=4.5 µmol/min/mg enzyme with 11,12-EET as substrate1 Publication
  4. Vmax=7 µmol/min/mg enzyme with 14,15-EET as substrate1 Publication
  5. Vmax=0.55 µmol/min/mg enzyme with leukotoxin as substrate1 Publication
  6. Vmax=5.8 nmol/min/mg enzyme with p-nitrophenyl phosphate3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi9Magnesium1 Publication1
Metal bindingi11Magnesium1 Publication1
Metal bindingi185Magnesium1 Publication1
Active sitei335Nucleophile5 Publications1
Binding sitei383Substrate5 Publications1
Active sitei466Proton donor5 Publications1
Active sitei524Proton acceptor5 Publications1

GO - Molecular functioni

  • 10-hydroxy-9-(phosphonooxy)octadecanoate phosphatase activity Source: UniProtKB-EC
  • epoxide hydrolase activity Source: UniProtKB
  • lipid phosphatase activity Source: UniProtKB
  • magnesium ion binding Source: UniProtKB
  • phosphatase activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • signaling receptor binding Source: UniProtKB
  • toxic substance binding Source: UniProtKB

GO - Biological processi

  • cellular calcium ion homeostasis Source: UniProtKB
  • cholesterol homeostasis Source: UniProtKB
  • dephosphorylation Source: UniProtKB
  • drug metabolic process Source: UniProtKB
  • epoxide metabolic process Source: UniProtKB
  • epoxygenase P450 pathway Source: Reactome
  • inflammatory response Source: UniProtKB
  • long-chain fatty acid biosynthetic process Source: Reactome
  • phospholipid dephosphorylation Source: UniProtKB
  • positive regulation of blood vessel diameter Source: UniProtKB
  • positive regulation of gene expression Source: UniProtKB
  • protein targeting to peroxisome Source: Reactome
  • reactive oxygen species metabolic process Source: UniProtKB
  • regulation of blood pressure Source: UniProtKB
  • regulation of cholesterol metabolic process Source: UniProtKB
  • response to toxic substance Source: UniProtKB
  • stilbene catabolic process Source: UniProtKB
  • xenobiotic metabolic process Source: UniProtKB

Keywordsi

Molecular functionHydrolase, Multifunctional enzyme
Biological processAromatic hydrocarbons catabolism, Detoxification, Lipid metabolism
LigandMagnesium, Metal-binding

Enzyme and pathway databases

BRENDAi3.3.2.10 2681
ReactomeiR-HSA-2142670 Synthesis of epoxy (EET) and dihydroxyeicosatrienoic acids (DHET)
R-HSA-9018682 Biosynthesis of maresins
R-HSA-9033241 Peroxisomal protein import
SABIO-RKiP34913

Protein family/group databases

ESTHERihuman-EPHX2 Epoxide_hydrolase
MEROPSiS33.973

Chemistry databases

SwissLipidsiSLP:000001105

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional epoxide hydrolase 2
Including the following 2 domains:
Cytosolic epoxide hydrolase 2 (EC:3.3.2.104 Publications)
Short name:
CEH
Alternative name(s):
Epoxide hydratase
Soluble epoxide hydrolase
Short name:
SEH
Lipid-phosphate phosphatase (EC:3.1.3.762 Publications)
Gene namesi
Name:EPHX2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

EuPathDBiHostDB:ENSG00000120915.13
HGNCiHGNC:3402 EPHX2
MIMi132811 gene
neXtProtiNX_P34913

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

Keywords - Cellular componenti

Cytoplasm, Peroxisome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi9D → A: Loss of phosphatase activity. 1 Publication1
Mutagenesisi522C → S: Loss of S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine-induced inhibition of epoxide hydrolase activity. 1 Publication1

Organism-specific databases

DisGeNETi2053
MalaCardsiEPHX2
OpenTargetsiENSG00000120915
PharmGKBiPA27830

Chemistry databases

ChEMBLiCHEMBL2409
DrugBankiDB08257 4-{[(CYCLOHEXYLAMINO)CARBONYL]AMINO}BUTANOIC ACID
DB08258 6-{[(CYCLOHEXYLAMINO)CARBONYL]AMINO}HEXANOIC ACID
DB08259 7-{[(CYCLOHEXYLAMINO)CARBONYL]AMINO}HEPTANOIC ACID
DB08256 N-[(CYCLOHEXYLAMINO)CARBONYL]GLYCINE
DB02029 N-Cyclohexyl-N'-(4-Iodophenyl)Urea
DB04213 N-Cyclohexyl-N'-(Propyl)Phenyl Urea
DB03677 N-Cyclohexyl-N'-Decylurea
GuidetoPHARMACOLOGYi2970

Polymorphism and mutation databases

BioMutaiEPHX2
DMDMi67476665

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000841111 – 555Bifunctional epoxide hydrolase 2Add BLAST555

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei43N6-acetyllysineCombined sources1
Modified residuei55N6-succinyllysineBy similarity1
Modified residuei191N6-acetyllysineBy similarity1
Modified residuei215N6-acetyllysineBy similarity1
Modified residuei370PhosphoserineBy similarity1
Modified residuei421N6-succinyllysineBy similarity1
Modified residuei455N6-succinyllysineBy similarity1
Lipidationi522S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine1 Publication1
Modified residuei554N6-succinyllysineBy similarity1

Post-translational modificationi

The N-terminus is blocked.
The covalent modification of cysteine by 15-deoxy-Delta12,14-prostaglandin-J2 is autocatalytic and reversible. It may occur as an alternative to other cysteine modifications, such as S-nitrosylation and S-palmitoylation (Probable).Curated

Keywords - PTMi

Acetylation, Lipoprotein, Phosphoprotein

Proteomic databases

EPDiP34913
MaxQBiP34913
PaxDbiP34913
PeptideAtlasiP34913
PRIDEiP34913
ProteomicsDBi54953

PTM databases

DEPODiP34913
iPTMnetiP34913
PhosphoSitePlusiP34913

Expressioni

Inductioni

By compounds that cause peroxisome proliferation such as clofibrate, tiadenol and fenofibrate.

Gene expression databases

BgeeiENSG00000120915
CleanExiHS_EPHX2
ExpressionAtlasiP34913 baseline and differential
GenevisibleiP34913 HS

Organism-specific databases

HPAiHPA023094
HPA023660

Interactioni

Subunit structurei

Homodimer.3 Publications

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB
  • signaling receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi108367, 5 interactors
IntActiP34913, 5 interactors
STRINGi9606.ENSP00000430269

Chemistry databases

BindingDBiP34913

Structurei

Secondary structure

1555
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 8Combined sources4
Turni12 – 14Combined sources3
Beta strandi15 – 17Combined sources3
Helixi19 – 29Combined sources11
Helixi36 – 42Combined sources7
Helixi45 – 47Combined sources3
Helixi49 – 54Combined sources6
Beta strandi57 – 59Combined sources3
Helixi60 – 72Combined sources13
Turni77 – 79Combined sources3
Helixi88 – 97Combined sources10
Helixi103 – 114Combined sources12
Beta strandi118 – 123Combined sources6
Turni131 – 133Combined sources3
Helixi140 – 145Combined sources6
Beta strandi147 – 152Combined sources6
Helixi153 – 156Combined sources4
Beta strandi160 – 162Combined sources3
Helixi163 – 173Combined sources11
Helixi177 – 179Combined sources3
Beta strandi180 – 185Combined sources6
Helixi187 – 195Combined sources9
Beta strandi199 – 202Combined sources4
Helixi206 – 217Combined sources12
Helixi234 – 236Combined sources3
Beta strandi237 – 245Combined sources9
Beta strandi248 – 255Combined sources8
Beta strandi257 – 264Combined sources8
Helixi271 – 274Combined sources4
Turni275 – 277Combined sources3
Helixi278 – 283Combined sources6
Beta strandi287 – 291Combined sources5
Helixi305 – 308Combined sources4
Helixi310 – 324Combined sources15
Beta strandi329 – 334Combined sources6
Helixi336 – 347Combined sources12
Helixi349 – 351Combined sources3
Beta strandi352 – 359Combined sources8
Beta strandi367 – 369Combined sources3
Helixi371 – 376Combined sources6
Helixi379 – 382Combined sources4
Helixi383 – 386Combined sources4
Helixi392 – 398Combined sources7
Helixi401 – 408Combined sources8
Helixi412 – 414Combined sources3
Helixi419 – 421Combined sources3
Turni424 – 426Combined sources3
Turni428 – 431Combined sources4
Beta strandi440 – 442Combined sources3
Helixi444 – 455Combined sources12
Turni456 – 459Combined sources4
Helixi460 – 464Combined sources5
Turni465 – 468Combined sources4
Helixi469 – 477Combined sources9
Turni478 – 481Combined sources4
Beta strandi488 – 493Combined sources6
Beta strandi497 – 499Combined sources3
Helixi501 – 504Combined sources4
Helixi507 – 509Combined sources3
Beta strandi515 – 519Combined sources5
Helixi526 – 529Combined sources4
Helixi531 – 545Combined sources15

3D structure databases

ProteinModelPortaliP34913
SMRiP34913
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP34913

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini259 – 531AB hydrolase-1Sequence analysisAdd BLAST273

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 224PhosphataseAdd BLAST224
Regioni123 – 124Phosphate binding1 Publication2
Regioni235 – 555Epoxide hydrolaseAdd BLAST321

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi553 – 555Microbody targeting signalSequence analysis3

Domaini

The N-terminal domain has phosphatase activity. The C-terminal domain has epoxide hydrolase activity.

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3085 Eukaryota
KOG4178 Eukaryota
COG1011 LUCA
GeneTreeiENSGT00530000063213
HOGENOMiHOG000028073
HOVERGENiHBG006095
InParanoidiP34913
KOiK08726
OMAiGHWTQMD
OrthoDBiEOG091G078G
PhylomeDBiP34913
TreeFamiTF315395

Family and domain databases

Gene3Di1.10.150.240, 1 hit
3.40.50.1000, 2 hits
3.40.50.1820, 1 hit
InterProiView protein in InterPro
IPR029058 AB_hydrolase
IPR000073 AB_hydrolase_1
IPR000639 Epox_hydrolase-like
IPR036412 HAD-like_sf
IPR006439 HAD-SF_hydro_IA
IPR011945 HAD-SF_ppase_IA/epoxid_hydro_N
IPR023214 HAD_sf
IPR023198 PGP-like_dom2
PfamiView protein in Pfam
PF00561 Abhydrolase_1, 1 hit
PRINTSiPR00111 ABHYDROLASE
PR00412 EPOXHYDRLASE
SUPFAMiSSF53474 SSF53474, 1 hit
SSF56784 SSF56784, 1 hit
TIGRFAMsiTIGR02247 HAD-1A3-hyp, 1 hit
TIGR01509 HAD-SF-IA-v3, 1 hit

Sequences (3)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: P34913-1) [UniParc]FASTAAdd to basket

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
MTLRAAVFDL DGVLALPAVF GVLGRTEEAL ALPRGLLNDA FQKGGPEGAT
60 70 80 90 100
TRLMKGEITL SQWIPLMEEN CRKCSETAKV CLPKNFSIKE IFDKAISARK
110 120 130 140 150
INRPMLQAAL MLRKKGFTTA ILTNTWLDDR AERDGLAQLM CELKMHFDFL
160 170 180 190 200
IESCQVGMVK PEPQIYKFLL DTLKASPSEV VFLDDIGANL KPARDLGMVT
210 220 230 240 250
ILVQDTDTAL KELEKVTGIQ LLNTPAPLPT SCNPSDMSHG YVTVKPRVRL
260 270 280 290 300
HFVELGSGPA VCLCHGFPES WYSWRYQIPA LAQAGYRVLA MDMKGYGESS
310 320 330 340 350
APPEIEEYCM EVLCKEMVTF LDKLGLSQAV FIGHDWGGML VWYMALFYPE
360 370 380 390 400
RVRAVASLNT PFIPANPNMS PLESIKANPV FDYQLYFQEP GVAEAELEQN
410 420 430 440 450
LSRTFKSLFR ASDESVLSMH KVCEAGGLFV NSPEEPSLSR MVTEEEIQFY
460 470 480 490 500
VQQFKKSGFR GPLNWYRNME RNWKWACKSL GRKILIPALM VTAEKDFVLV
510 520 530 540 550
PQMSQHMEDW IPHLKRGHIE DCGHWTQMDK PTEVNQILIK WLDSDARNPP

VVSKM
Length:555
Mass (Da):62,616
Last modified:June 7, 2005 - v2
Checksum:i1B5ACE7F80F9A26C
GO
Isoform 2 (identifier: P34913-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-53: Missing.

Note: No experimental confirmation available.
Show »
Length:502
Mass (Da):57,123
Checksum:iCB56A36CDF4F2FFF
GO
Isoform 3 (identifier: P34913-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-66: Missing.

Note: No experimental confirmation available.
Show »
Length:489
Mass (Da):55,626
Checksum:i7188F0A08408CD29
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti5A → G in AAA02756 (PubMed:8342951).Curated1
Sequence conflicti257 – 258SG → W in AAA02756 (PubMed:8342951).Curated2
Sequence conflicti409F → L in BAG53362 (PubMed:14702039).Curated1
Sequence conflicti473W → R in BAG53362 (PubMed:14702039).Curated1
Sequence conflicti494E → G in BAG53362 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05539221G → A1 PublicationCorresponds to variant dbSNP:rs72473930Ensembl.1
Natural variantiVAR_05539352R → Q1 PublicationCorresponds to variant dbSNP:rs72475803Ensembl.1
Natural variantiVAR_05105955K → R Decreased phosphatase activity; no effect on epoxyde hydrolase activity. 3 PublicationsCorresponds to variant dbSNP:rs41507953Ensembl.1
Natural variantiVAR_033991103R → C Decreased phosphatase activity; no effect on epoxyde hydrolase activity. 3 PublicationsCorresponds to variant dbSNP:rs17057255Ensembl.1
Natural variantiVAR_055394154C → Y Decreased phosphatase activity; no effect on epoxyde hydrolase activity. 3 PublicationsCorresponds to variant dbSNP:rs57699806Ensembl.1
Natural variantiVAR_055395225P → L1 PublicationCorresponds to variant dbSNP:rs72475821Ensembl.1
Natural variantiVAR_014852287R → Q No effect on phosphatase activity; decreased epoxyde hydrolase activity. 5 PublicationsCorresponds to variant dbSNP:rs751141EnsemblClinVar.1
Natural variantiVAR_055396369M → V1 PublicationCorresponds to variant dbSNP:rs72475894Ensembl.1
Natural variantiVAR_022613403R → RR2 Publications1
Natural variantiVAR_055397470E → G No effect on phosphatase activity and epoxyde hydrolase activity. 3 PublicationsCorresponds to variant dbSNP:rs68053459Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0455971 – 66Missing in isoform 3. 1 PublicationAdd BLAST66
Alternative sequenceiVSP_0455981 – 53Missing in isoform 2. 1 PublicationAdd BLAST53

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L05779 mRNA Translation: AAA02756.1
X97024
, X97025, X97026, X97027, X97028, X97029, X97030, X97031, X97032, X97033, X97034, X97035, X97036, X97037, X97038 Genomic DNA Translation: CAA65751.1
AF233334 mRNA Translation: AAG14966.1
AF233335 mRNA Translation: AAG14967.1
AF233336 mRNA Translation: AAG14968.1
BT006885 mRNA Translation: AAP35531.1
AK096089 mRNA Translation: BAG53210.1
AK096770 mRNA Translation: BAG53362.1
EU584434 Genomic DNA Translation: ACD11487.1
AF311103 Genomic DNA No translation available.
CH471080 Genomic DNA Translation: EAW63548.1
CH471080 Genomic DNA Translation: EAW63549.1
CH471080 Genomic DNA Translation: EAW63551.1
BC007708 mRNA Translation: AAH07708.1
BC011628 mRNA Translation: AAH11628.1
BC013874 mRNA Translation: AAH13874.1
CCDSiCCDS59097.1 [P34913-2]
CCDS59098.1 [P34913-3]
CCDS6060.1 [P34913-1]
PIRiJC4711
RefSeqiNP_001243411.1, NM_001256482.1 [P34913-2]
NP_001243412.1, NM_001256483.1 [P34913-3]
NP_001243413.1, NM_001256484.1 [P34913-2]
NP_001970.2, NM_001979.5 [P34913-1]
UniGeneiHs.212088

Genome annotation databases

EnsembliENST00000380476; ENSP00000369843; ENSG00000120915 [P34913-2]
ENST00000521400; ENSP00000430269; ENSG00000120915 [P34913-1]
ENST00000521780; ENSP00000430302; ENSG00000120915 [P34913-3]
GeneIDi2053
KEGGihsa:2053
UCSCiuc003xfu.5 human [P34913-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiHYES_HUMAN
AccessioniPrimary (citable) accession number: P34913
Secondary accession number(s): B2Z3B1
, B3KTU8, B3KUA0, G3V134, J3KPH7, Q16764, Q9HBJ1, Q9HBJ2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: June 7, 2005
Last modified: June 20, 2018
This is version 183 of the entry and version 2 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: 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

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