EPHX2

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

Activity 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

Sites

Feature key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	9	Magnesium1 Publication	1
Metal bindingⁱ	11	Magnesium1 Publication	1
Metal bindingⁱ	185	Magnesium1 Publication	1
Active siteⁱ	335	Nucleophile5 Publications	1
Binding siteⁱ	383	Substrate5 Publications	1
Active siteⁱ	466	Proton donor5 Publications	1
Active siteⁱ	524	Proton acceptor5 Publications	1

GO - Molecular functionⁱ

10-hydroxy-9-(phosphonooxy)octadecanoate phosphatase activity Source: UniProtKB-EC
epoxide hydrolase activity
Source: UniProtKB
Inferred from direct assayⁱ
lipid phosphatase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 12574510
magnesium ion binding
Source: UniProtKB
Inferred from direct assayⁱ
- 12574510
phosphatase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 12574508
- 15196990
protein homodimerization activity
Source: UniProtKB
Inferred from direct assayⁱ
- 15096040
- 18513744
signaling receptor binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 20178365
toxic substance binding
Source: UniProtKB
Inferred from direct assayⁱ
- 15096040

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

cellular calcium ion homeostasis
Source: UniProtKB
Non-traceable author statementⁱ
- 10862610
cholesterol homeostasis
Source: UniProtKB
Inferred from direct assayⁱ
- 18974052
dephosphorylation
Source: UniProtKB
Inferred from direct assayⁱ
- 12574508
drug metabolic process
Source: UniProtKB
Non-traceable author statementⁱ
- 10862610
epoxide metabolic process
Source: UniProtKB
Inferred from direct assayⁱ
- 22798687
epoxygenase P450 pathway Source: Reactome
inflammatory response
Source: UniProtKB
Non-traceable author statementⁱ
- 10862610
long-chain fatty acid biosynthetic process Source: Reactome
phospholipid dephosphorylation
Source: UniProtKB
Inferred from direct assayⁱ
- 12574510
positive regulation of blood vessel diameter
Source: UniProtKB
Non-traceable author statementⁱ
- 10862610
positive regulation of gene expression
Source: UniProtKB
Inferred from direct assayⁱ
- 18974052
protein targeting to peroxisome Source: Reactome
reactive oxygen species metabolic process
Source: UniProtKB
Non-traceable author statementⁱ
- 10862610
regulation of blood pressure
Source: UniProtKB
Non-traceable author statementⁱ
- 10862610
regulation of cholesterol metabolic process
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 18974052
response to toxic substance
Source: UniProtKB
Non-traceable author statementⁱ
- 10862610
stilbene catabolic process
Source: UniProtKB
Inferred from direct assayⁱ
- 8342951
xenobiotic metabolic process
Source: UniProtKB
Non-traceable author statementⁱ
- 10862610

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Hydrolase, Multifunctional enzyme
Biological process	Aromatic hydrocarbons catabolism, Detoxification, Lipid metabolism
Ligand	Magnesium, Metal-binding

Enzyme and pathway databases

BRENDAⁱ	3.3.2.10 2681
Reactomeⁱ	R-HSA-2142670 Synthesis of epoxy (EET) and dihydroxyeicosatrienoic acids (DHET) R-HSA-9018682 Biosynthesis of maresins R-HSA-9033241 Peroxisomal protein import
SABIO-RKⁱ	P34913

Protein family/group databases

ESTHERⁱ	human-EPHX2 Epoxide_hydrolase
MEROPS protease database More...MEROPSⁱ	S33.973

Chemistry databases

SwissLipidsⁱ	SLP:000001105

SwissLipidsⁱ

SLP: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
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 8

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000120915.13
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:3402 EPHX2
MIMⁱ	132811 gene
neXtProtⁱ	NX_P34913

Keywords - Cellular componentⁱ

Cytoplasm, Peroxisome

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Mutagenesisⁱ	9	D → A: Loss of phosphatase activity. 1 Publication		1
Mutagenesisⁱ	522	C → S: Loss of S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine-induced inhibition of epoxide hydrolase activity. 1 Publication		1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	2053
MalaCards human disease database More...MalaCardsⁱ	EPHX2
Open Targets More...OpenTargetsⁱ	ENSG00000120915
PharmGKBⁱ	PA27830

Chemistry databases

ChEMBLⁱ	CHEMBL2409
Drug and drug target database More...DrugBankⁱ	DB08257 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
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYⁱ	2970

Polymorphism and mutation databases

BioMutaⁱ	EPHX2
DMDMⁱ	67476665

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000084111	1 – 555	Bifunctional epoxide hydrolase 2Add BLAST		555

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	43	N6-acetyllysineCombined sources	1
Modified residueⁱ	55	N6-succinyllysineBy similarity	1
Modified residueⁱ	191	N6-acetyllysineBy similarity	1
Modified residueⁱ	215	N6-acetyllysineBy similarity	1
Modified residueⁱ	370	PhosphoserineBy similarity	1
Modified residueⁱ	421	N6-succinyllysineBy similarity	1
Modified residueⁱ	455	N6-succinyllysineBy similarity	1
Lipidationⁱ	522	S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine1 Publication	1
Modified residueⁱ	554	N6-succinyllysineBy similarity	1

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

EPDⁱ	P34913
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P34913
PaxDbⁱ	P34913
PeptideAtlas More...PeptideAtlasⁱ	P34913
PRIDEⁱ	P34913
ProteomicsDBⁱ	54953

PTM databases

DEPODⁱ	P34913
iPTMnetⁱ	P34913
PhosphoSitePlusⁱ	P34913

Expressionⁱ

Inductionⁱ

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

Gene expression databases

Bgeeⁱ	ENSG00000120915 Expressed in 162 organ(s), highest expression level in right lobe of liver
CleanExⁱ	HS_EPHX2
ExpressionAtlasⁱ	P34913 baseline and differential
Genevisibleⁱ	P34913 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	HPA023094 HPA023660

HPAⁱ

HPA023094
HPA023660

Interactionⁱ

Subunit structureⁱ

Homodimer.3 Publications

GO - Molecular functionⁱ

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	108367, 5 interactors
IntActⁱ	P34913, 5 interactors
STRINGⁱ	9606.ENSP00000430269

Chemistry databases

BindingDBⁱ

P34913

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	5 – 8	Combined sources	4
Turnⁱ	12 – 14	Combined sources	3
Beta strandⁱ	15 – 17	Combined sources	3
Helixⁱ	19 – 29	Combined sources	11
Helixⁱ	36 – 42	Combined sources	7
Helixⁱ	45 – 47	Combined sources	3
Helixⁱ	49 – 54	Combined sources	6
Beta strandⁱ	57 – 59	Combined sources	3
Helixⁱ	60 – 72	Combined sources	13
Turnⁱ	77 – 79	Combined sources	3
Helixⁱ	88 – 97	Combined sources	10
Helixⁱ	103 – 114	Combined sources	12
Beta strandⁱ	118 – 123	Combined sources	6
Turnⁱ	131 – 133	Combined sources	3
Helixⁱ	140 – 145	Combined sources	6
Beta strandⁱ	147 – 152	Combined sources	6
Helixⁱ	153 – 156	Combined sources	4
Beta strandⁱ	160 – 162	Combined sources	3
Helixⁱ	163 – 173	Combined sources	11
Helixⁱ	177 – 179	Combined sources	3
Beta strandⁱ	180 – 185	Combined sources	6
Helixⁱ	187 – 195	Combined sources	9
Beta strandⁱ	199 – 202	Combined sources	4
Helixⁱ	206 – 217	Combined sources	12
Helixⁱ	234 – 236	Combined sources	3
Beta strandⁱ	237 – 245	Combined sources	9
Beta strandⁱ	248 – 255	Combined sources	8
Beta strandⁱ	257 – 264	Combined sources	8
Helixⁱ	271 – 274	Combined sources	4
Turnⁱ	275 – 277	Combined sources	3
Helixⁱ	278 – 283	Combined sources	6
Beta strandⁱ	287 – 291	Combined sources	5
Helixⁱ	305 – 308	Combined sources	4
Helixⁱ	310 – 324	Combined sources	15
Beta strandⁱ	329 – 334	Combined sources	6
Helixⁱ	336 – 347	Combined sources	12
Helixⁱ	349 – 351	Combined sources	3
Beta strandⁱ	352 – 359	Combined sources	8
Beta strandⁱ	367 – 369	Combined sources	3
Helixⁱ	371 – 376	Combined sources	6
Helixⁱ	379 – 382	Combined sources	4
Helixⁱ	383 – 386	Combined sources	4
Helixⁱ	392 – 398	Combined sources	7
Helixⁱ	401 – 408	Combined sources	8
Helixⁱ	412 – 414	Combined sources	3
Helixⁱ	419 – 421	Combined sources	3
Turnⁱ	424 – 426	Combined sources	3
Turnⁱ	428 – 431	Combined sources	4
Beta strandⁱ	440 – 442	Combined sources	3
Helixⁱ	444 – 455	Combined sources	12
Turnⁱ	456 – 459	Combined sources	4
Helixⁱ	460 – 464	Combined sources	5
Turnⁱ	465 – 468	Combined sources	4
Helixⁱ	469 – 477	Combined sources	9
Turnⁱ	478 – 481	Combined sources	4
Beta strandⁱ	488 – 493	Combined sources	6
Beta strandⁱ	497 – 499	Combined sources	3
Helixⁱ	501 – 504	Combined sources	4
Helixⁱ	507 – 509	Combined sources	3
Beta strandⁱ	515 – 519	Combined sources	5
Helixⁱ	526 – 529	Combined sources	4
Helixⁱ	531 – 545	Combined sources	15

Show more details

3D structure databases

ProteinModelPortalⁱ	P34913
SMRⁱ	P34913
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P34913

EvolutionaryTraceⁱ

P34913

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	259 – 531	AB hydrolase-1Sequence analysisAdd BLAST		273

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	1 – 224	PhosphataseAdd BLAST	224
Regionⁱ	123 – 124	Phosphate binding1 Publication	2
Regionⁱ	235 – 555	Epoxide hydrolaseAdd BLAST	321

Motif

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Motifⁱ	553 – 555	Microbody targeting signalSequence analysis		3

Domainⁱ

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

Sequence similaritiesⁱ

Belongs to the AB hydrolase superfamily. Epoxide hydrolase family.Curated

Phylogenomic databases

eggNOGⁱ	KOG3085 Eukaryota KOG4178 Eukaryota COG1011 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00530000063213
HOGENOMⁱ	HOG000028073
HOVERGENⁱ	HBG006095
InParanoidⁱ	P34913
KEGG Orthology (KO) More...KOⁱ	K08726
OMAⁱ	LTNNWLD
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G078G
PhylomeDBⁱ	P34913
TreeFamⁱ	TF315395

Family and domain databases

Gene3Dⁱ	1.10.150.240, 1 hit 3.40.50.1000, 1 hit 3.40.50.1820, 1 hit
InterProⁱ	View 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
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00561 Abhydrolase_1, 1 hit
PRINTSⁱ	PR00111 ABHYDROLASE PR00412 EPOXHYDRLASE
SUPFAMⁱ	SSF53474 SSF53474, 1 hit SSF56784 SSF56784, 1 hit
TIGRFAMsⁱ	TIGR02247 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. Align Add to basket

This entry has 3 described isoforms and 4 potential isoforms that are computationally mapped.Show all Align All

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

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

« Hide

        10         20         30         40         50
MKGEITLSQW IPLMEENCRK CSETAKVCLP KNFSIKEIFD KAISARKINR 
        60         70         80         90        100
PMLQAALMLR KKGFTTAILT NTWLDDRAER DGLAQLMCEL KMHFDFLIES 
       110        120        130        140        150
CQVGMVKPEP QIYKFLLDTL KASPSEVVFL DDIGANLKPA RDLGMVTILV 
       160        170        180        190        200
QDTDTALKEL EKVTGIQLLN TPAPLPTSCN PSDMSHGYVT VKPRVRLHFV 
       210        220        230        240        250
ELGSGPAVCL CHGFPESWYS WRYQIPALAQ AGYRVLAMDM KGYGESSAPP 
       260        270        280        290        300
EIEEYCMEVL CKEMVTFLDK LGLSQAVFIG HDWGGMLVWY MALFYPERVR 
       310        320        330        340        350
AVASLNTPFI PANPNMSPLE SIKANPVFDY QLYFQEPGVA EAELEQNLSR 
       360        370        380        390        400
TFKSLFRASD ESVLSMHKVC EAGGLFVNSP EEPSLSRMVT EEEIQFYVQQ 
       410        420        430        440        450
FKKSGFRGPL NWYRNMERNW KWACKSLGRK ILIPALMVTA EKDFVLVPQM 
       460        470        480        490        500
SQHMEDWIPH LKRGHIEDCG HWTQMDKPTE VNQILIKWLD SDARNPPVVS 

KM

Note: No experimental confirmation available.

Show »

Length:502

Mass (Da):57,123

Checksum:ⁱCB56A36CDF4F2FFF

GO

Isoform 3 (identifier: P34913-3) [UniParc]FASTA Add to basket

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

« Hide

        10         20         30         40         50
MEENCRKCSE TAKVCLPKNF SIKEIFDKAI SARKINRPML QAALMLRKKG 
        60         70         80         90        100
FTTAILTNTW LDDRAERDGL AQLMCELKMH FDFLIESCQV GMVKPEPQIY 
       110        120        130        140        150
KFLLDTLKAS PSEVVFLDDI GANLKPARDL GMVTILVQDT DTALKELEKV 
       160        170        180        190        200
TGIQLLNTPA PLPTSCNPSD MSHGYVTVKP RVRLHFVELG SGPAVCLCHG 
       210        220        230        240        250
FPESWYSWRY QIPALAQAGY RVLAMDMKGY GESSAPPEIE EYCMEVLCKE 
       260        270        280        290        300
MVTFLDKLGL SQAVFIGHDW GGMLVWYMAL FYPERVRAVA SLNTPFIPAN 
       310        320        330        340        350
PNMSPLESIK ANPVFDYQLY FQEPGVAEAE LEQNLSRTFK SLFRASDESV 
       360        370        380        390        400
LSMHKVCEAG GLFVNSPEEP SLSRMVTEEE IQFYVQQFKK SGFRGPLNWY 
       410        420        430        440        450
RNMERNWKWA CKSLGRKILI PALMVTAEKD FVLVPQMSQH MEDWIPHLKR 
       460        470        480 
GHIEDCGHWT QMDKPTEVNQ ILIKWLDSDA RNPPVVSKM

Note: No experimental confirmation available.

Show »

Length:489

Mass (Da):55,626

Checksum:ⁱ7188F0A08408CD29

GO

Computationally mapped potential isoform sequencesⁱ

There are 4 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

E5RFH6	E5RFH6_HUMAN	Bifunctional epoxide hydrolase 2 Bifunctional epoxide hydrolase 2	EPHX2	372	Annotation score:
E5RFU2	E5RFU2_HUMAN	Bifunctional epoxide hydrolase 2 Bifunctional epoxide hydrolase 2	EPHX2	523	Annotation score:
E5RI53	E5RI53_HUMAN	Bifunctional epoxide hydrolase 2 Bifunctional epoxide hydrolase 2	EPHX2	158	Annotation score:
H0YAW7	H0YAW7_HUMAN	Bifunctional epoxide hydrolase 2 Bifunctional epoxide hydrolase 2	EPHX2	312	Annotation score:

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	5	A → G in AAA02756 (PubMed:8342951).Curated	1
Sequence conflictⁱ	257 – 258	SG → W in AAA02756 (PubMed:8342951).Curated	2
Sequence conflictⁱ	409	F → L in BAG53362 (PubMed:14702039).Curated	1
Sequence conflictⁱ	473	W → R in BAG53362 (PubMed:14702039).Curated	1
Sequence conflictⁱ	494	E → G in BAG53362 (PubMed:14702039).Curated	1

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_055392	21	G → A1 PublicationCorresponds to variant dbSNP:rs72473930Ensembl.	1
Natural variantⁱVAR_055393	52	R → Q1 PublicationCorresponds to variant dbSNP:rs72475803Ensembl.	1
Natural variantⁱVAR_051059	55	K → R Decreased phosphatase activity; no effect on epoxyde hydrolase activity. 3 PublicationsCorresponds to variant dbSNP:rs41507953Ensembl.	1
Natural variantⁱVAR_033991	103	R → C Decreased phosphatase activity; no effect on epoxyde hydrolase activity. 3 PublicationsCorresponds to variant dbSNP:rs17057255Ensembl.	1
Natural variantⁱVAR_055394	154	C → Y Decreased phosphatase activity; no effect on epoxyde hydrolase activity. 3 PublicationsCorresponds to variant dbSNP:rs57699806Ensembl.	1
Natural variantⁱVAR_055395	225	P → L1 PublicationCorresponds to variant dbSNP:rs72475821Ensembl.	1
Natural variantⁱVAR_014852	287	R → Q No effect on phosphatase activity; decreased epoxyde hydrolase activity. 5 PublicationsCorresponds to variant dbSNP:rs751141EnsemblClinVar.	1
Natural variantⁱVAR_055396	369	M → V1 PublicationCorresponds to variant dbSNP:rs72475894Ensembl.	1
Natural variantⁱVAR_022613	403	R → RR2 Publications	1
Natural variantⁱVAR_055397	470	E → G No effect on phosphatase activity and epoxyde hydrolase activity. 3 PublicationsCorresponds to variant dbSNP:rs68053459Ensembl.	1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_045597	1 – 66	Missing in isoform 3. 1 PublicationAdd BLAST		66
Alternative sequenceⁱVSP_045598	1 – 53	Missing in isoform 2. 1 PublicationAdd BLAST		53

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	L05779 mRNA Translation: AAA02756.1 X97024 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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS59097.1 [P34913-2] CCDS59098.1 [P34913-3] CCDS6060.1 [P34913-1]
PIRⁱ	JC4711
NCBI Reference Sequences More...RefSeqⁱ	NP_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]
UniGeneⁱ	Hs.212088

Genome annotation databases

Ensemblⁱ	ENST00000380476; ENSP00000369843; ENSG00000120915 [P34913-2] ENST00000521400; ENSP00000430269; ENSG00000120915 [P34913-1] ENST00000521780; ENSP00000430302; ENSG00000120915 [P34913-3]
GeneIDⁱ	2053
KEGGⁱ	hsa:2053
UCSC genome browser More...UCSCⁱ	uc003xfu.5 human [P34913-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Polymorphism

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P34913	Bifunctional epoxide hydrolase 2 (Fragment)		HUMAN		158	UniRef100_P34913
Isoform 2 of Bifunctional epoxide hydrolase 2		HUMAN		502
Isoform 3 of Bifunctional epoxide hydrolase 2		HUMAN		489
UPI0004437F02		HUMAN		561
UPI0005092ACE		HUMAN		326

Protein	Similar proteins		Species	Score	Length	Source
P34913	Bifunctional epoxide hydrolase 2 (Fragment)		HUMAN		158	UniRef90_P34913
EPHX2 isoform 1		PANTR		555
EPHX2 isoform 1		PONAB		555
Epoxide hydrolase 2		MACMU		555
Uncharacterized protein		CERAT		555
+42

Protein	Similar proteins		Species	Score	Length	Source
P34913	Bifunctional epoxide hydrolase 2		PIG		555	UniRef50_P34913
Bifunctional epoxide hydrolase 2	)	MOUSE		554
Bifunctional epoxide hydrolase 2		RAT		554
Bifunctional epoxide hydrolase 2 (Fragment)		HUMAN		158
Epoxide hydrolase 2		MACMU		555
+132

Cross-referencesⁱ

Web resourcesⁱ

NIEHS-SNPs

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	L05779 mRNA Translation: AAA02756.1 X97024 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
CCDSⁱ	CCDS59097.1 [P34913-2] CCDS59098.1 [P34913-3] CCDS6060.1 [P34913-1]
PIRⁱ	JC4711
RefSeqⁱ	NP_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]
UniGeneⁱ	Hs.212088

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1S8O	X-ray	2.60	A	1-555	[»]
	1VJ5	X-ray	2.35	A	1-555	[»]
	1ZD2	X-ray	3.00	P	1-555	[»]
	1ZD3	X-ray	2.30	A	1-555	[»]
	1ZD4	X-ray	2.70	A	1-555	[»]
	1ZD5	X-ray	2.60	A	1-555	[»]
	3ANS	X-ray	1.98	A/B	230-555	[»]
	3ANT	X-ray	2.40	A/B	230-555	[»]
	3I1Y	X-ray	2.47	A	1-555	[»]
	3I28	X-ray	1.95	A	1-555	[»]
	3KOO	X-ray	2.79	A	1-555	[»]
	3OTQ	X-ray	3.00	A	1-555	[»]
	3PDC	X-ray	2.60	A/B	226-548	[»]
	3WK4	X-ray	2.11	A	1-555	[»]
	3WK5	X-ray	2.77	A	1-555	[»]
	3WK6	X-ray	2.10	A	1-555	[»]
	3WK7	X-ray	2.20	A	1-555	[»]
	3WK8	X-ray	2.20	A	1-555	[»]
	3WK9	X-ray	2.20	A	1-555	[»]
	3WKA	X-ray	2.01	A	1-555	[»]
	3WKB	X-ray	2.20	A	1-555	[»]
	3WKC	X-ray	2.20	A	1-555	[»]
	3WKD	X-ray	2.48	A	1-555	[»]
	3WKE	X-ray	2.75	A	1-555	[»]
	4C4X	X-ray	2.17	A/B	230-555	[»]
	4C4Y	X-ray	2.41	A	230-555	[»]
	4C4Z	X-ray	2.06	A/B	230-555	[»]
	4HAI	X-ray	2.55	A	1-555	[»]
	4J03	X-ray	2.92	A	1-555	[»]
	4JNC	X-ray	1.96	A	238-549	[»]
	4OCZ	X-ray	2.94	A	1-555	[»]
	4OD0	X-ray	2.92	A	1-555	[»]
	4X6X	X-ray	1.80	A/B	230-555	[»]
	4X6Y	X-ray	2.10	A/B	230-555	[»]
	4Y2J	X-ray	2.15	A	1-555	[»]
	4Y2P	X-ray	2.05	A	1-555	[»]
	4Y2Q	X-ray	2.40	A	1-555	[»]
	4Y2R	X-ray	2.45	A	1-555	[»]
	4Y2S	X-ray	2.30	A	1-555	[»]
	4Y2T	X-ray	2.40	A	1-555	[»]
	4Y2U	X-ray	2.75	A	1-555	[»]
	4Y2V	X-ray	2.40	A	1-555	[»]
	4Y2X	X-ray	2.50	A	1-555	[»]
	4Y2Y	X-ray	2.30	A	1-555	[»]
	5AHX	X-ray	2.00	A	1-548	[»]
	5AI0	X-ray	1.75	A	1-548	[»]
	5AI4	X-ray	1.93	A	1-548	[»]
	5AI5	X-ray	2.28	A	1-548	[»]
	5AI6	X-ray	2.30	A	1-548	[»]
	5AI8	X-ray	1.85	A	1-548	[»]
	5AI9	X-ray	1.80	A	1-548	[»]
	5AIA	X-ray	2.26	A	1-548	[»]
	5AIB	X-ray	1.95	A	1-548	[»]
	5AIC	X-ray	1.89	A	1-548	[»]
	5AK3	X-ray	2.28	A	1-548	[»]
	5AK4	X-ray	1.79	A	1-548	[»]
	5AK5	X-ray	2.22	A	1-548	[»]
	5AK6	X-ray	2.15	A	1-548	[»]
	5AKE	X-ray	2.26	A	1-548	[»]
	5AKG	X-ray	2.51	A	1-548	[»]
	5AKH	X-ray	2.10	A	1-548	[»]
	5AKI	X-ray	1.81	A	1-548	[»]
	5AKJ	X-ray	2.03	A	1-548	[»]
5AKK	X-ray	1.90	A	1-548	[»]
5AKL	X-ray	2.00	A	1-548	[»]
5AKX	X-ray	2.09	A	1-548	[»]
5AKY	X-ray	2.18	A	1-548	[»]
5AKZ	X-ray	2.18	A	1-548	[»]
5ALD	X-ray	2.26	A	1-548	[»]
5ALE	X-ray	1.95	A	1-548	[»]
5ALF	X-ray	2.32	A	1-548	[»]
5ALG	X-ray	2.40	A	1-548	[»]
5ALH	X-ray	1.90	A	1-548	[»]
5ALI	X-ray	1.85	A	1-548	[»]
5ALJ	X-ray	2.10	A	1-548	[»]
5ALK	X-ray	2.33	A	1-548	[»]
5ALL	X-ray	2.20	A	1-548	[»]
5ALM	X-ray	2.00	A	1-548	[»]
5ALN	X-ray	2.00	A	1-548	[»]
5ALO	X-ray	2.00	A	1-548	[»]
5ALP	X-ray	2.06	A	1-548	[»]
5ALQ	X-ray	2.78	A	1-548	[»]
5ALR	X-ray	2.60	A	1-548	[»]
5ALS	X-ray	2.57	A	1-548	[»]
5ALT	X-ray	2.15	A	1-548	[»]
5ALU	X-ray	1.87	A	1-548	[»]
5ALV	X-ray	1.80	A	1-548	[»]
5ALW	X-ray	2.20	A	1-548	[»]
5ALX	X-ray	2.23	A	1-548	[»]
5ALY	X-ray	1.90	A	1-548	[»]
5ALZ	X-ray	2.30	A	1-548	[»]
5AM0	X-ray	1.88	A	1-548	[»]
5AM1	X-ray	2.15	A	1-548	[»]
5AM2	X-ray	1.70	A	1-548	[»]
5AM3	X-ray	2.20	A	1-548	[»]
5AM4	X-ray	1.87	A	1-548	[»]
5AM5	X-ray	2.26	A	1-548	[»]
5FP0	X-ray	2.35	A	1-548	[»]
5MWA	X-ray	1.55	A	2-224	[»]
6AUM	X-ray	2.95	A	1-555	[»]
ProteinModelPortalⁱ	P34913
SMRⁱ	P34913
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	108367, 5 interactors
IntActⁱ	P34913, 5 interactors
STRINGⁱ	9606.ENSP00000430269

Chemistry databases

BindingDBⁱ	P34913
ChEMBLⁱ	CHEMBL2409
DrugBankⁱ	DB08257 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
GuidetoPHARMACOLOGYⁱ	2970
SwissLipidsⁱ	SLP:000001105

Protein family/group databases

ESTHERⁱ	human-EPHX2 Epoxide_hydrolase
MEROPSⁱ	S33.973

PTM databases

DEPODⁱ	P34913
iPTMnetⁱ	P34913
PhosphoSitePlusⁱ	P34913

Polymorphism and mutation databases

BioMutaⁱ	EPHX2
DMDMⁱ	67476665

Proteomic databases

EPDⁱ	P34913
MaxQBⁱ	P34913
PaxDbⁱ	P34913
PeptideAtlasⁱ	P34913
PRIDEⁱ	P34913
ProteomicsDBⁱ	54953

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	2053
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000380476; ENSP00000369843; ENSG00000120915 [P34913-2] ENST00000521400; ENSP00000430269; ENSG00000120915 [P34913-1] ENST00000521780; ENSP00000430302; ENSG00000120915 [P34913-3]
GeneIDⁱ	2053
KEGGⁱ	hsa:2053
UCSCⁱ	uc003xfu.5 human [P34913-1]

Organism-specific databases

CTDⁱ	2053
DisGeNETⁱ	2053
EuPathDBⁱ	HostDB:ENSG00000120915.13
GeneCardsⁱ	EPHX2
HGNCⁱ	HGNC:3402 EPHX2
HPAⁱ	HPA023094 HPA023660
MalaCardsⁱ	EPHX2
MIMⁱ	132811 gene
neXtProtⁱ	NX_P34913
OpenTargetsⁱ	ENSG00000120915
PharmGKBⁱ	PA27830
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG3085 Eukaryota KOG4178 Eukaryota COG1011 LUCA
GeneTreeⁱ	ENSGT00530000063213
HOGENOMⁱ	HOG000028073
HOVERGENⁱ	HBG006095
InParanoidⁱ	P34913
KOⁱ	K08726
OMAⁱ	LTNNWLD
OrthoDBⁱ	EOG091G078G
PhylomeDBⁱ	P34913
TreeFamⁱ	TF315395

Enzyme and pathway databases

BRENDAⁱ	3.3.2.10 2681
Reactomeⁱ	R-HSA-2142670 Synthesis of epoxy (EET) and dihydroxyeicosatrienoic acids (DHET) R-HSA-9018682 Biosynthesis of maresins R-HSA-9033241 Peroxisomal protein import
SABIO-RKⁱ	P34913

Miscellaneous databases

ChiTaRSⁱ	EPHX2 human
EvolutionaryTraceⁱ	P34913
GeneWikiⁱ	Epoxide_hydrolase_2
GenomeRNAiⁱ	2053
Protein Ontology More...PROⁱ	PR:P34913
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000120915 Expressed in 162 organ(s), highest expression level in right lobe of liver
CleanExⁱ	HS_EPHX2
ExpressionAtlasⁱ	P34913 baseline and differential
Genevisibleⁱ	P34913 HS

Family and domain databases

Gene3Dⁱ	1.10.150.240, 1 hit 3.40.50.1000, 1 hit 3.40.50.1820, 1 hit
InterProⁱ	View 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
Pfamⁱ	View protein in Pfam PF00561 Abhydrolase_1, 1 hit
PRINTSⁱ	PR00111 ABHYDROLASE PR00412 EPOXHYDRLASE
SUPFAMⁱ	SSF53474 SSF53474, 1 hit SSF56784 SSF56784, 1 hit
TIGRFAMsⁱ	TIGR02247 HAD-1A3-hyp, 1 hit TIGR01509 HAD-SF-IA-v3, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	HYES_HUMAN
Accessionⁱ	P34913Primary (citable) accession number: P34913 Secondary accession number(s): B2Z3B1 Q9HBJ2
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
	Last sequence update:	June 7, 2005
	Last modified:	November 7, 2018
	This is version 185 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any 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

SIMILARITY comments
Index of protein domains and families
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Human chromosome 8
Human chromosome 8: entries, gene names and cross-references to MIM

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Help

UniRef

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Supporting data

UniProtKB - P34913 (HYES_HUMAN)

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Bifunctional epoxide hydrolase 2

Select a section on the left to see content.

<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

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

Sites

<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

Enzyme and pathway databases

Protein family/group databases

Chemistry databases

<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

Organism-specific databases

<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

Peroxisome

Other locations

Cytosol

Extracellular region or secreted

Peroxisome

Keywords - Cellular componenti

<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

Organism-specific databases

Chemistry databases

Polymorphism and mutation databases

<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

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<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

Gene expression databases

Organism-specific databases

<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

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

<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

3D structure databases

Miscellaneous databases

<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

Region

Motif

<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

Phylogenomic databases

Family and domain databases

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

Protein family/group databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

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Functionⁱ

Kineticsⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ