HUMAN:LKHA4

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	LTA4H (synonyms: LTA4)
Protein Name(s)	Leukotriene A-4 hydrolase LTA-4 hydrolase Leukotriene A(4) hydrolase
External Links
UniProt	P09960
EMBL	J03459 J02959 U27293 U27275 U27276 U27277 U27278 U27279 U27280 U27281 U27282 U27283 U27284 U27285 U27286 U27287 U27288 U27289 U27290 U27291 U27292 AK298017 CR457068 BX647158 AC007298 CH471054 BC032528 U43410 U43411
CCDS	CCDS58266.1 CCDS58267.1 CCDS9059.1
PIR	S65947
RefSeq	NP_000886.1 NP_001243572.1 NP_001243573.1 XP_005268928.1
UniGene	Hs.524648
PDB	1GW6 1H19 1HS6 1SQM 2R59 2VJ8 3B7R 3B7S 3B7T 3B7U 3CHO 3CHP 3CHQ 3CHR 3CHS 3FH5 3FH7 3FH8 3FHE 3FTS 3FTU 3FTV 3FTW 3FTX 3FTY 3FTZ 3FU0 3FU3 3FU5 3FU6 3FUD 3FUE 3FUF 3FUH 3FUI 3FUJ 3FUK 3FUL 3FUM 3FUN 3U9W 4DPR 4L2L 4MKT 4MS6 4R7L 4RSY 4RVB 5AEN
PDBsum	1GW6 1H19 1HS6 1SQM 2R59 2VJ8 3B7R 3B7S 3B7T 3B7U 3CHO 3CHP 3CHQ 3CHR 3CHS 3FH5 3FH7 3FH8 3FHE 3FTS 3FTU 3FTV 3FTW 3FTX 3FTY 3FTZ 3FU0 3FU3 3FU5 3FU6 3FUD 3FUE 3FUF 3FUH 3FUI 3FUJ 3FUK 3FUL 3FUM 3FUN 3U9W 4DPR 4L2L 4MKT 4MS6 4R7L 4RSY 4RVB 5AEN
ProteinModelPortal	P09960
SMR	P09960
BioGrid	110226
IntAct	P09960
MINT	MINT-1388946
STRING	9606.ENSP00000228740
BindingDB	P09960
ChEMBL	CHEMBL4618
DrugBank	DB01197
GuidetoPHARMACOLOGY	1395
SwissLipids	SLP:000001118
MEROPS	M01.004
iPTMnet	P09960
PhosphoSite	P09960
SwissPalm	P09960
BioMuta	LTA4H
DMDM	126353
REPRODUCTION-2DPAGE	IPI00219077
EPD	P09960
MaxQB	P09960
PaxDb	P09960
PRIDE	P09960
DNASU	4048
Ensembl	ENST00000228740 ENST00000413268 ENST00000552789
GeneID	4048
KEGG	hsa:4048
UCSC	uc001ten.3
CTD	4048
GeneCards	LTA4H
HGNC	HGNC:6710
HPA	CAB015221 HPA008399 HPA017017
MIM	151570
neXtProt	NX_P09960
PharmGKB	PA24345
eggNOG	KOG1047 COG0308
GeneTree	ENSGT00530000063003
HOGENOM	HOG000293296
HOVERGEN	HBG001274
InParanoid	P09960
KO	K01254
OMA	FANSNFR
OrthoDB	EOG7SJD42
PhylomeDB	P09960
TreeFam	TF300758
BioCyc	MetaCyc:HS03372-MONOMER
BRENDA	3.3.2.6
Reactome	R-HSA-2142691
UniPathway	UPA00878
ChiTaRS	LTA4H
EvolutionaryTrace	P09960
GenomeRNAi	4048
NextBio	15856
PRO	PR:P09960
Proteomes	UP000005640
Bgee	P09960
CleanEx	HS_LTA4H
ExpressionAtlas	P09960
Genevisible	P09960
GO	GO:0005737 GO:0005829 GO:0070062 GO:0005654 GO:0005634 GO:0005886 GO:0004177 GO:0004301 GO:0004463 GO:0070006 GO:0008233 GO:0042277 GO:0044822 GO:0008270 GO:0019369 GO:0006954 GO:0019370 GO:0006691 GO:0043171 GO:0043434 GO:0010043 GO:0044281 GO:0060509
InterPro	IPR016024 IPR012777 IPR001930 IPR015211 IPR014782
PANTHER	PTHR11533
Pfam	PF09127 PF01433
PRINTS	PR00756
SUPFAM	SSF48371
TIGRFAMs	TIGR02411
PROSITE	PS00142

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0000175	3'-5'-exoribonuclease activity	PMID:24558481^[1]	ECO:0000250		UniProtKB:Q57X81	F		HHPRED shows an e value of 1.4E-13. Figure two from the article shows sequence similarity between the two proteins. Along with a gel electrophoresis comparing the bands between of dna between the two proteins	complete CACAO 11915
involved_in	GO:0043171	peptide catabolic process	PMID:9774412^[2]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0019370	leukotriene biosynthetic process	PMID:9774412^[2]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0004177	aminopeptidase activity	PMID:9774412^[2]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004463	leukotriene-A4 hydrolase activity	PMID:9774412^[2]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0044267	cellular protein metabolic process	PMID:11675384^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	PMID:11675384^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004301	epoxide hydrolase activity	PMID:11675384^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0070006	metalloaminopeptidase activity	PMID:11675384^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0019370	leukotriene biosynthetic process	PMID:11675384^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:23533145^[4]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:19056867^[5]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001088)	Seeded From UniProt	complete
enables	GO:0003723	RNA binding	PMID:22658674^[6]	ECO:0007005	high throughput direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0043171	peptide catabolic process	PMID:15078870^[7]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043171	peptide catabolic process	PMID:18804029^[8]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0019370	leukotriene biosynthetic process	PMID:15078870^[7]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	PMID:15078870^[7]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	PMID:18804029^[8]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004463	leukotriene-A4 hydrolase activity	PMID:15078870^[7]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004301	epoxide hydrolase activity	PMID:15078870^[7]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004177	aminopeptidase activity	PMID:15078870^[7]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004177	aminopeptidase activity	PMID:18804029^[8]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0044255	cellular lipid metabolic process	PMID:21873635^[9]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000164255 SGD:S000004990	P		Seeded From UniProt	complete
involved_in	GO:0019370	leukotriene biosynthetic process	PMID:21873635^[9]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000164329 UniProtKB:P09960	P		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:21873635^[9]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000164329 RGD:1311333 UniProtKB:P09960	C		Seeded From UniProt	complete
enables	GO:0004463	leukotriene-A4 hydrolase activity	PMID:21873635^[9]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000164329 RGD:1311333 UniProtKB:P09960	F		Seeded From UniProt	complete
enables	GO:0004301	epoxide hydrolase activity	PMID:21873635^[9]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000164255 SGD:S000004990 UniProtKB:P09960	F		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0006508	proteolysis	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001930	P		Seeded From UniProt	complete
enables	GO:0008237	metallopeptidase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR014782 InterPro:IPR015211	F		Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR012777 InterPro:IPR014782 InterPro:IPR015211	F		Seeded From UniProt	complete
enables	GO:0004463	leukotriene-A4 hydrolase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:3.3.2.6	F		Seeded From UniProt	complete
involved_in	GO:0019370	leukotriene biosynthetic process	PMID:1881903^[10]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	PMID:1881903^[10]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0008233	peptidase activity	PMID:1881903^[10]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004463	leukotriene-A4 hydrolase activity	PMID:1881903^[10]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004301	epoxide hydrolase activity	PMID:11154734^[11]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:1904813	ficolin-1-rich granule lumen	Reactome:R-HSA-6800434	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:1904724	tertiary granule lumen	Reactome:R-HSA-6798745	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0043312	neutrophil degranulation	Reactome:R-HSA-6798695	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0042759	long-chain fatty acid biosynthetic process	Reactome:R-HSA-9023661 Reactome:R-HSA-9020265 Reactome:R-HSA-9018896 Reactome:R-HSA-9018681 Reactome:R-HSA-9018676	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006691	leukotriene metabolic process	Reactome:R-HSA-2142691	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	Reactome:R-HSA-9024890 Reactome:R-HSA-9020270 Reactome:R-HSA-9020258 Reactome:R-HSA-9020257 Reactome:R-HSA-9020253 Reactome:R-HSA-9020252 Reactome:R-HSA-9018877 Reactome:R-HSA-9018862 Reactome:R-HSA-266072	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	Reactome:R-HSA-6800434 Reactome:R-HSA-6798745	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0008233	peptidase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0645	F		Seeded From UniProt	complete
enables	GO:0008237	metallopeptidase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0482	F		Seeded From UniProt	complete
involved_in	GO:0006508	proteolysis	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0645	P		Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C		Seeded From UniProt	complete
involved_in	GO:0019370	leukotriene biosynthetic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0434	P		Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F		Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ Barbosa, RL et al. (2014) RRP6 from Trypanosoma brucei: crystal structure of the catalytic domain, association with EAP3 and activity towards structured and non-structured RNA substrates. PLoS ONE 9 e89138 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 Baset, HA et al. (1998) Molecular cloning and functional expression of a Caenorhabditis elegans aminopeptidase structurally related to mammalian leukotriene A4 hydrolases. J. Biol. Chem. 273 27978-87 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 ^3.4 Rudberg, PC et al. (2002) Leukotriene A4 hydrolase/aminopeptidase. Glutamate 271 is a catalytic residue with specific roles in two distinct enzyme mechanisms. J. Biol. Chem. 277 1398-404 PubMed GONUTS page
↑ Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page
↑ Gonzales, PA et al. (2009) Large-scale proteomics and phosphoproteomics of urinary exosomes. J. Am. Soc. Nephrol. 20 363-79 PubMed GONUTS page
↑ Castello, A et al. (2012) Insights into RNA biology from an atlas of mammalian mRNA-binding proteins. Cell 149 1393-406 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 ^7.3 ^7.4 ^7.5 Rudberg, PC et al. (2004) Leukotriene A4 hydrolase: identification of a common carboxylate recognition site for the epoxide hydrolase and aminopeptidase substrates. J. Biol. Chem. 279 27376-82 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 Tholander, F et al. (2008) Structure-based dissection of the active site chemistry of leukotriene A4 hydrolase: implications for M1 aminopeptidases and inhibitor design. Chem. Biol. 15 920-9 PubMed GONUTS page
↑ ^9.0 ^9.1 ^9.2 ^9.3 ^9.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ ^10.0 ^10.1 ^10.2 ^10.3 Medina, JF et al. (1991) Leukotriene A4 hydrolase: determination of the three zinc-binding ligands by site-directed mutagenesis and zinc analysis. Proc. Natl. Acad. Sci. U.S.A. 88 7620-4 PubMed GONUTS page
↑ Fretland, AJ & Omiecinski, CJ (2000) Epoxide hydrolases: biochemistry and molecular biology. Chem. Biol. Interact. 129 41-59 PubMed GONUTS page

[PMID:24558481-1] Barbosa, RL et al. (2014) RRP6 from Trypanosoma brucei: crystal structure of the catalytic domain, association with EAP3 and activity towards structured and non-structured RNA substrates. PLoS ONE 9 e89138 PubMed GONUTS page

[PMID:9774412-2] 2.0 ^2.1 ^2.2 ^2.3 Baset, HA et al. (1998) Molecular cloning and functional expression of a Caenorhabditis elegans aminopeptidase structurally related to mammalian leukotriene A4 hydrolases. J. Biol. Chem. 273 27978-87 PubMed GONUTS page

[PMID:11675384-3] 3.0 ^3.1 ^3.2 ^3.3 ^3.4 Rudberg, PC et al. (2002) Leukotriene A4 hydrolase/aminopeptidase. Glutamate 271 is a catalytic residue with specific roles in two distinct enzyme mechanisms. J. Biol. Chem. 277 1398-404 PubMed GONUTS page

[PMID:23533145-4] Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page

[PMID:19056867-5] Gonzales, PA et al. (2009) Large-scale proteomics and phosphoproteomics of urinary exosomes. J. Am. Soc. Nephrol. 20 363-79 PubMed GONUTS page

[PMID:22658674-6] Castello, A et al. (2012) Insights into RNA biology from an atlas of mammalian mRNA-binding proteins. Cell 149 1393-406 PubMed GONUTS page

[PMID:15078870-7] 7.0 ^7.1 ^7.2 ^7.3 ^7.4 ^7.5 Rudberg, PC et al. (2004) Leukotriene A4 hydrolase: identification of a common carboxylate recognition site for the epoxide hydrolase and aminopeptidase substrates. J. Biol. Chem. 279 27376-82 PubMed GONUTS page

[PMID:18804029-8] 8.0 ^8.1 ^8.2 Tholander, F et al. (2008) Structure-based dissection of the active site chemistry of leukotriene A4 hydrolase: implications for M1 aminopeptidases and inhibitor design. Chem. Biol. 15 920-9 PubMed GONUTS page

[PMID:21873635-9] 9.0 ^9.1 ^9.2 ^9.3 ^9.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:1881903-10] 10.0 ^10.1 ^10.2 ^10.3 Medina, JF et al. (1991) Leukotriene A4 hydrolase: determination of the three zinc-binding ligands by site-directed mutagenesis and zinc analysis. Proc. Natl. Acad. Sci. U.S.A. 88 7620-4 PubMed GONUTS page

[PMID:11154734-11] Fretland, AJ & Omiecinski, CJ (2000) Epoxide hydrolases: biochemistry and molecular biology. Chem. Biol. Interact. 129 41-59 PubMed GONUTS page

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HUMAN:LKHA4

Contents

Annotations

Notes

References

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