UniProtKB - P09960 (LKHA4_HUMAN)
Protein
Leukotriene A-4 hydrolase
Gene
LTA4H
Organism
Homo sapiens (Human)
Status
Functioni
Bifunctional zinc metalloenzyme that comprises both epoxide hydrolase (EH) and aminopeptidase activities. Acts as an epoxide hydrolase to catalyze the conversion of LTA4 to the proinflammatory mediator leukotriene B4 (LTB4) (PubMed:11917124, PubMed:12207002, PubMed:15078870, PubMed:18804029, PubMed:1897988, PubMed:1975494, PubMed:2244921). Has also aminopeptidase activity, with high affinity for N-terminal arginines of various synthetic tripeptides (PubMed:20813919, PubMed:18804029). In addition to its proinflammatory EH activity, may also counteract inflammation by its aminopeptidase activity, which inactivates by cleavage another neutrophil attractant, the tripeptide Pro-Gly-Pro (PGP), a bioactive fragment of collagen generated by the action of matrix metalloproteinase-9 (MMP9) and prolylendopeptidase (PREPL) (PubMed:20813919, PubMed:24591641). Involved also in the biosynthesis of resolvin E1 and 18S-resolvin E1 from eicosapentaenoic acid, two lipid mediators that show potent anti-inflammatory and pro-resolving actions (PubMed:21206090).10 Publications
Catalytic activityi
- EC:3.3.2.610 PublicationsThis reaction proceeds in the forward1 Publication direction.
- This reaction proceeds in the forward1 Publication direction.
- (5S,6S)-epoxy-(18S)-hydroxy-(7E,9E,11Z,14Z,16E)-eicosapentaenoate + H2O = 18S-resolvin E11 PublicationThis reaction proceeds in the forward1 Publication direction.
- Release of the N-terminal residue from a tripeptide.5 Publications EC:3.4.11.4
Cofactori
Zn2+5 PublicationsNote: Binds 1 zinc ion per subunit.3 Publications
Activity regulationi
Inhibited by bestatin (PubMed:11175901). The epoxide hydrolase activity is restrained by suicide inactivation that involves binding of LTA4 to Tyr-379 (PubMed:7667299). 4-(4-benzylphenyl)thiazol-2-amine (ARM1) selectively inhibits the epoxide hydrolase activity (PubMed:24591641).3 Publications
Kineticsi
- KM=1.29 mM for Pro-Gly-Pro1 Publication
: leukotriene B4 biosynthesis Pathwayi
This protein is involved in the pathway leukotriene B4 biosynthesis, which is part of Lipid metabolism.1 PublicationView all proteins of this organism that are known to be involved in the pathway leukotriene B4 biosynthesis and in Lipid metabolism.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 272 | Pro-Gly-Pro binding1 Publication | 1 | |
Metal bindingi | 296 | Zinc; catalyticCombined sources8 Publications | 1 | |
Active sitei | 297 | Proton acceptorCombined sources2 Publications1 Publication | 1 | |
Metal bindingi | 300 | Zinc; catalyticCombined sources8 Publications | 1 | |
Metal bindingi | 319 | Zinc; catalyticCombined sources2 Publications | 1 | |
Sitei | 376 | Essential for epoxide hydrolase activity, but not for aminopeptidase activity1 Publication | 1 | |
Sitei | 379 | Covalently modified during suicide inhibition by leukotrienes1 Publication | 1 | |
Active sitei | 384 | Proton donorCombined sources2 Publications1 Publication | 1 | |
Sitei | 563 | Pro-Gly-Pro binding1 Publication | 1 |
GO - Molecular functioni
- aminopeptidase activity Source: UniProtKB
- epoxide hydrolase activity Source: UniProtKB
- leukotriene-A4 hydrolase activity Source: UniProtKB
- metalloaminopeptidase activity Source: CAFA
- peptidase activity Source: ProtInc
- RNA binding Source: UniProtKB
- tripeptide aminopeptidase activity Source: UniProtKB-EC
- zinc ion binding Source: UniProtKB
GO - Biological processi
- cellular lipid metabolic process Source: GO_Central
- cellular protein metabolic process Source: CAFA
- leukotriene biosynthetic process Source: UniProtKB
- leukotriene metabolic process Source: Reactome
- long-chain fatty acid biosynthetic process Source: Reactome
- neutrophil degranulation Source: Reactome
- peptide catabolic process Source: UniProtKB
Keywordsi
Molecular function | Hydrolase, Metalloprotease, Protease |
Biological process | Leukotriene biosynthesis, Lipid metabolism |
Ligand | Metal-binding, Zinc |
Enzyme and pathway databases
BioCyci | MetaCyc:HS03372-MONOMER |
BRENDAi | 3.3.2.6, 2681 |
PathwayCommonsi | P09960 |
Reactomei | R-HSA-2142691, Synthesis of Leukotrienes (LT) and Eoxins (EX) R-HSA-6798695, Neutrophil degranulation R-HSA-9018676, Biosynthesis of D-series resolvins R-HSA-9018681, Biosynthesis of protectins R-HSA-9018896, Biosynthesis of E-series 18(S)-resolvins R-HSA-9020265, Biosynthesis of aspirin-triggered D-series resolvins R-HSA-9023661, Biosynthesis of E-series 18(R)-resolvins |
SABIO-RKi | P09960 |
UniPathwayi | UPA00878 |
Protein family/group databases
MEROPSi | M01.004 |
MoonProti | P09960 |
Chemistry databases
SwissLipidsi | SLP:000001118 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:LTA4H Synonyms:LTA4 |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:6710, LTA4H |
MIMi | 151570, gene |
neXtProti | NX_P09960 |
VEuPathDBi | HostDB:ENSG00000111144.9 |
Subcellular locationi
Other locations
- Cytoplasm 1 Publication
Cytosol
- cytosol Source: HPA
Extracellular region or secreted
- extracellular exosome Source: UniProtKB
- extracellular region Source: Reactome
Nucleus
- nucleoplasm Source: HPA
- nucleus Source: GO_Central
Other locations
- ficolin-1-rich granule lumen Source: Reactome
- tertiary granule lumen Source: Reactome
Keywords - Cellular componenti
CytoplasmPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 135 | Q → A or L: Srongly increased epoxide hydrolase activity. 1 Publication | 1 | |
Mutagenesisi | 135 | Q → A: Strongly reduced aminopeptidase activity. Strongly decreased affinity for leukotriene. Abolishes epoxide hydrolase activity. 1 Publication | 1 | |
Mutagenesisi | 137 | Q → A: No loss of activity. 1 Publication | 1 | |
Mutagenesisi | 137 | Q → L: Aminopeptidase activity strongly impaired, but keeps LTA4 activity. 1 Publication | 1 | |
Mutagenesisi | 137 | Q → N: Aminopeptidase activity almost absent, but keeps LTA4 activity. 1 Publication | 1 | |
Mutagenesisi | 140 | H → Q: Aminopeptidase activity almost absent, but keeps LTA4 activity. 1 Publication | 1 | |
Mutagenesisi | 269 | G → A: No loss of activity. 1 Publication | 1 | |
Mutagenesisi | 270 | G → A: No loss of activity. 1 Publication | 1 | |
Mutagenesisi | 271 | M → L: No loss of activity. 1 Publication | 1 | |
Mutagenesisi | 272 | E → A or D: Complete loss of epoxide hydrolase activity and aminopeptidase activity. 1 Publication | 1 | |
Mutagenesisi | 272 | E → Q: Loss of LTA4 hydrolase activity, and aminopeptidase activity strongly impaired. 1 Publication | 1 | |
Mutagenesisi | 273 | N → A: No loss of epoxide hydrolase activity and aminopeptidase activity. 1 Publication | 1 | |
Mutagenesisi | 296 | H → Y: Complete loss of LTA4 hydrolase and peptidase enzyme activities. 1 Publication | 1 | |
Mutagenesisi | 297 | E → A: Loss of epoxide hydrolase and aminopeptidase activities. 3 Publications | 1 | |
Mutagenesisi | 297 | E → K: Loss of epoxide hydrolase and aminopeptidase activities. 3 Publications | 1 | |
Mutagenesisi | 297 | E → Q: Loss of aminopeptidase activity, but keeps LTA4 hydrolase activity. 3 Publications | 1 | |
Mutagenesisi | 300 | H → L: Complete loss of LTA4 hydrolase and peptidase enzyme activities. 1 Publication | 1 | |
Mutagenesisi | 319 | E → A: Complete loss of LTA4 hydrolase and peptidase enzyme activities. 1 Publication | 1 | |
Mutagenesisi | 372 | D → N: No loss of activity. 1 Publication | 1 | |
Mutagenesisi | 374 | D → N: No loss of activity. 1 Publication | 1 | |
Mutagenesisi | 376 | D → A: Strongly reduced hydrolysis of peptides starting with Arg. Small effect on hydrolysis of peptides starting with Ala. Abolishes epoxide hydrolase activity. 2 Publications | 1 | |
Mutagenesisi | 376 | D → E: Strongly reduced aminopeptidase activity. Abolishes epoxide hydrolase activity. 2 Publications | 1 | |
Mutagenesisi | 376 | D → N: Abolishes aminopeptidase activity. Decreased epoxide hydrolase activity. 2 Publications | 1 | |
Mutagenesisi | 385 | E → Q: Reduced aminopeptidase activity. Minor effect on epoxide hydrolase activity. 1 Publication | 1 | |
Mutagenesisi | 564 | R → A, K or M: Abolishes epoxide hydrolase activity. Reduced aminopeptidase activity. 1 Publication | 1 | |
Mutagenesisi | 566 | K → A or M: Strongly reduced affinity for peptide substrates. Reduced epoxide hydrolase and aminopeptidase activity. 1 Publication | 1 | |
Mutagenesisi | 566 | K → R: No effect on epoxide hydrolase and aminopeptidase activity. 1 Publication | 1 |
Organism-specific databases
DisGeNETi | 4048 |
OpenTargetsi | ENSG00000111144 |
PharmGKBi | PA24345 |
Miscellaneous databases
Pharosi | P09960, Tchem |
Chemistry databases
ChEMBLi | CHEMBL4618 |
DrugBanki | DB07102, (2S)-2-amino-5-oxo-5-[(4-phenylmethoxyphenyl)amino]pentanoic acid DB06917, (4-fluorophenyl)(pyridin-4-yl)methanone DB07258, (R)-pyridin-4-yl[4-(2-pyrrolidin-1-ylethoxy)phenyl]methanol DB07094, 1-(2,2'-bithiophen-5-yl)methanamine DB07259, 1-(4-thiophen-2-ylphenyl)methanamine DB02352, 3-(Benzyloxy)Pyridin-2-Amine DB07292, 4-(2-amino-1,3-thiazol-4-yl)phenol DB07104, 4-amino-N-[4-(benzyloxy)phenyl]butanamide DB06828, 5-[2-(1H-pyrrol-1-yl)ethoxy]-1H-indole DB08466, 5-[2-(4-hydroxyphenyl)ethyl]benzene-1,3-diol DB01197, Captopril DB05177, DG051 DB03366, Imidazole DB08040, Kelatorphan DB06851, N-(pyridin-3-ylmethyl)aniline DB02062, N-[3-[(1-Aminoethyl)(Hydroxy)Phosphoryl]-2-(1,1'-Biphenyl-4-Ylmethyl)Propanoyl]Alanine DB07099, N-[4-(benzyloxy)phenyl]glycinamide DB07260, N-benzyl-4-[(2R)-pyrrolidin-2-ylmethoxy]aniline DB07196, N-methyl-1-(2-thiophen-2-ylphenyl)methanamine DB11781, Tosedostat DB03424, Ubenimex DB07237, {4-[(2R)-pyrrolidin-2-ylmethoxy]phenyl}(4-thiophen-3-ylphenyl)methanone |
DrugCentrali | P09960 |
GuidetoPHARMACOLOGYi | 1395 |
Genetic variation databases
BioMutai | LTA4H |
DMDMi | 126353 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | RemovedCombined sources2 Publications | |||
ChainiPRO_0000095124 | 2 – 611 | Leukotriene A-4 hydrolaseAdd BLAST | 610 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 73 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 337 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 414 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 416 | Phosphoserine1 Publication | 1 | |
Modified residuei | 573 | N6-acetyllysineCombined sources | 1 |
Post-translational modificationi
Phosphorylation at Ser-416 inhibits leukotriene-A4 hydrolase activity.1 Publication
Keywords - PTMi
Acetylation, PhosphoproteinProteomic databases
CPTACi | CPTAC-92 CPTAC-93 |
EPDi | P09960 |
jPOSTi | P09960 |
MassIVEi | P09960 |
MaxQBi | P09960 |
PaxDbi | P09960 |
PeptideAtlasi | P09960 |
PRIDEi | P09960 |
ProteomicsDBi | 28779 52284 [P09960-1] 52285 [P09960-2] 52286 [P09960-3] |
2D gel databases
REPRODUCTION-2DPAGEi | IPI00219077 |
PTM databases
iPTMneti | P09960 |
MetOSitei | P09960 |
PhosphoSitePlusi | P09960 |
SwissPalmi | P09960 |
Expressioni
Tissue specificityi
Isoform 1 and isoform 2 are expressed in monocytes, lymphocytes, neutrophils, reticulocytes, platelets and fibroblasts.
Gene expression databases
Bgeei | ENSG00000111144, Expressed in visceral pleura and 246 other tissues |
ExpressionAtlasi | P09960, baseline and differential |
Genevisiblei | P09960, HS |
Organism-specific databases
HPAi | ENSG00000111144, Low tissue specificity |
Interactioni
Subunit structurei
Monomer.
3 PublicationsBinary interactionsi
P09960
With | #Exp. | IntAct |
---|---|---|
TINF2 [Q9BSI4] | 2 | EBI-721089,EBI-717399 |
Protein-protein interaction databases
BioGRIDi | 110226, 34 interactors |
IntActi | P09960, 11 interactors |
STRINGi | 9606.ENSP00000228740 |
Chemistry databases
BindingDBi | P09960 |
Miscellaneous databases
RNActi | P09960, protein |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P09960 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P09960 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 135 – 137 | Substrate binding1 Publication | 3 | |
Regioni | 267 – 272 | Substrate binding1 Publication | 6 | |
Regioni | 362 – 365 | Inhibitor ARM1 binding1 Publication | 4 | |
Regioni | 564 – 566 | Substrate binding1 Publication | 3 |
Sequence similaritiesi
Belongs to the peptidase M1 family.Curated
Phylogenomic databases
eggNOGi | KOG1047, Eukaryota |
GeneTreei | ENSGT00940000156375 |
HOGENOMi | CLU_014505_0_0_1 |
InParanoidi | P09960 |
OMAi | NSNFRMK |
PhylomeDBi | P09960 |
TreeFami | TF300758 |
Family and domain databases
CDDi | cd09599, M1_LTA4H, 1 hit |
Gene3Di | 1.10.390.10, 1 hit 1.25.40.320, 1 hit 2.60.40.1730, 1 hit |
InterProi | View protein in InterPro IPR042097, Aminopeptidase_N-like_N IPR016024, ARM-type_fold IPR012777, LTA4H IPR038502, M1_LTA-4_hydro/amino_C_sf IPR034015, M1_LTA4H IPR001930, Peptidase_M1 IPR015211, Peptidase_M1_C IPR014782, Peptidase_M1_dom IPR027268, Peptidase_M4/M1_CTD_sf |
PANTHERi | PTHR45726, PTHR45726, 1 hit |
Pfami | View protein in Pfam PF09127, Leuk-A4-hydro_C, 1 hit PF01433, Peptidase_M1, 1 hit |
PRINTSi | PR00756, ALADIPTASE |
SMARTi | View protein in SMART SM01263, Leuk-A4-hydro_C, 1 hit |
SUPFAMi | SSF48371, SSF48371, 1 hit SSF63737, SSF63737, 1 hit |
TIGRFAMsi | TIGR02411, leuko_A4_hydro, 1 hit |
PROSITEi | View protein in PROSITE PS00142, ZINC_PROTEASE, 1 hit |
s (4+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry describes 4 produced by isoformsialternative splicing. AlignAdd to basketThis entry has 4 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All
Isoform 1 (identifier: P09960-1) [UniParc]FASTAAdd to basket
Also known as: L-LTA4
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MPEIVDTCSL ASPASVCRTK HLHLRCSVDF TRRTLTGTAA LTVQSQEDNL
60 70 80 90 100
RSLVLDTKDL TIEKVVINGQ EVKYALGERQ SYKGSPMEIS LPIALSKNQE
110 120 130 140 150
IVIEISFETS PKSSALQWLT PEQTSGKEHP YLFSQCQAIH CRAILPCQDT
160 170 180 190 200
PSVKLTYTAE VSVPKELVAL MSAIRDGETP DPEDPSRKIY KFIQKVPIPC
210 220 230 240 250
YLIALVVGAL ESRQIGPRTL VWSEKEQVEK SAYEFSETES MLKIAEDLGG
260 270 280 290 300
PYVWGQYDLL VLPPSFPYGG MENPCLTFVT PTLLAGDKSL SNVIAHEISH
310 320 330 340 350
SWTGNLVTNK TWDHFWLNEG HTVYLERHIC GRLFGEKFRH FNALGGWGEL
360 370 380 390 400
QNSVKTFGET HPFTKLVVDL TDIDPDVAYS SVPYEKGFAL LFYLEQLLGG
410 420 430 440 450
PEIFLGFLKA YVEKFSYKSI TTDDWKDFLY SYFKDKVDVL NQVDWNAWLY
460 470 480 490 500
SPGLPPIKPN YDMTLTNACI ALSQRWITAK EDDLNSFNAT DLKDLSSHQL
510 520 530 540 550
NEFLAQTLQR APLPLGHIKR MQEVYNFNAI NNSEIRFRWL RLCIQSKWED
560 570 580 590 600
AIPLALKMAT EQGRMKFTRP LFKDLAAFDK SHDQAVRTYQ EHKASMHPVT
610
AMLVGKDLKV D
Computationally mapped potential isoform sequencesi
There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basketB4DEH5 | B4DEH5_HUMAN | Leukotriene A-4 hydrolase | LTA4H | 132 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 115 | A → T in BX647158 (PubMed:17974005).Curated | 1 | |
Sequence conflicti | 123 | Q → R in BX647158 (PubMed:17974005).Curated | 1 | |
Sequence conflicti | 297 | E → G in BAG60321 (PubMed:14702039).Curated | 1 | |
Sequence conflicti | 309 | N → S in BX647158 (PubMed:17974005).Curated | 1 | |
Sequence conflicti | 378 | A → V in BX647158 (PubMed:17974005).Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_051570 | 131 | Y → H. Corresponds to variant dbSNP:rs45630737Ensembl. | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_041107 | 1 – 53 | MPEIV…NLRSL → MLPQRNLSKRQVPTMHIPVK TRRLLAALK in isoform 3 and isoform 4. 2 PublicationsAdd BLAST | 53 | |
Alternative sequenceiVSP_041108 | 511 – 532 | APLPL…NAINN → MAAALHSIQVGGRNSFGAKD GN in isoform 2 and isoform 3. 1 PublicationAdd BLAST | 22 | |
Alternative sequenceiVSP_041109 | 533 – 611 | Missing in isoform 2 and isoform 3. 1 PublicationAdd BLAST | 79 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | J03459 mRNA Translation: AAA36176.1 J02959 mRNA Translation: AAA36177.1 U27293 , U27275, U27276, U27277, U27278, U27279, U27280, U27281, U27282, U27283, U27284, U27285, U27286, U27287, U27288, U27289, U27290, U27291, U27292 Genomic DNA Translation: AAA89077.1 AK298017 mRNA Translation: BAG60321.1 CR457068 mRNA Translation: CAG33349.1 BX647158 mRNA No translation available. AC007298 Genomic DNA No translation available. CH471054 Genomic DNA Translation: EAW97559.1 BC032528 mRNA Translation: AAH32528.1 U43410 Genomic DNA No translation available. U43411 Genomic DNA No translation available. |
CCDSi | CCDS58266.1 [P09960-3] CCDS58267.1 [P09960-4] CCDS9059.1 [P09960-1] |
PIRi | S65947 |
RefSeqi | NP_000886.1, NM_000895.2 [P09960-1] NP_001243572.1, NM_001256643.1 [P09960-4] NP_001243573.1, NM_001256644.1 [P09960-3] XP_005268928.1, XM_005268871.1 [P09960-2] |
Genome annotation databases
Ensembli | ENST00000228740; ENSP00000228740; ENSG00000111144 [P09960-1] ENST00000413268; ENSP00000395051; ENSG00000111144 [P09960-3] ENST00000552789; ENSP00000449958; ENSG00000111144 [P09960-4] |
GeneIDi | 4048 |
KEGGi | hsa:4048 |
UCSCi | uc001ten.3, human [P09960-1] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | J03459 mRNA Translation: AAA36176.1 J02959 mRNA Translation: AAA36177.1 U27293 , U27275, U27276, U27277, U27278, U27279, U27280, U27281, U27282, U27283, U27284, U27285, U27286, U27287, U27288, U27289, U27290, U27291, U27292 Genomic DNA Translation: AAA89077.1 AK298017 mRNA Translation: BAG60321.1 CR457068 mRNA Translation: CAG33349.1 BX647158 mRNA No translation available. AC007298 Genomic DNA No translation available. CH471054 Genomic DNA Translation: EAW97559.1 BC032528 mRNA Translation: AAH32528.1 U43410 Genomic DNA No translation available. U43411 Genomic DNA No translation available. |
CCDSi | CCDS58266.1 [P09960-3] CCDS58267.1 [P09960-4] CCDS9059.1 [P09960-1] |
PIRi | S65947 |
RefSeqi | NP_000886.1, NM_000895.2 [P09960-1] NP_001243572.1, NM_001256643.1 [P09960-4] NP_001243573.1, NM_001256644.1 [P09960-3] XP_005268928.1, XM_005268871.1 [P09960-2] |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1GW6 | X-ray | 2.20 | A | 2-611 | [»] | |
1H19 | X-ray | 2.10 | A | 2-611 | [»] | |
1HS6 | X-ray | 1.95 | A | 1-611 | [»] | |
1SQM | X-ray | 2.30 | A | 2-611 | [»] | |
2R59 | X-ray | 1.89 | A | 2-611 | [»] | |
2VJ8 | X-ray | 1.80 | A | 1-611 | [»] | |
3B7R | X-ray | 1.81 | L | 2-611 | [»] | |
3B7S | X-ray | 1.47 | A | 2-611 | [»] | |
3B7T | X-ray | 2.30 | A | 2-611 | [»] | |
3B7U | X-ray | 1.90 | X | 2-611 | [»] | |
3CHO | X-ray | 1.80 | A | 2-611 | [»] | |
3CHP | X-ray | 2.10 | A | 2-611 | [»] | |
3CHQ | X-ray | 2.09 | A | 2-611 | [»] | |
3CHR | X-ray | 2.20 | A | 2-611 | [»] | |
3CHS | X-ray | 2.55 | A | 2-611 | [»] | |
3FH5 | X-ray | 1.63 | A | 1-611 | [»] | |
3FH7 | X-ray | 2.05 | A | 1-611 | [»] | |
3FH8 | X-ray | 1.67 | A | 1-611 | [»] | |
3FHE | X-ray | 2.16 | A | 1-611 | [»] | |
3FTS | X-ray | 2.33 | A | 1-611 | [»] | |
3FTU | X-ray | 1.90 | A | 1-611 | [»] | |
3FTV | X-ray | 1.70 | A | 1-611 | [»] | |
3FTW | X-ray | 1.85 | A | 1-611 | [»] | |
3FTX | X-ray | 1.96 | A | 1-611 | [»] | |
3FTY | X-ray | 2.15 | A | 1-611 | [»] | |
3FTZ | X-ray | 2.00 | A | 1-611 | [»] | |
3FU0 | X-ray | 1.80 | A | 1-611 | [»] | |
3FU3 | X-ray | 2.00 | A | 1-611 | [»] | |
3FU5 | X-ray | 2.30 | A | 1-611 | [»] | |
3FU6 | X-ray | 2.05 | A | 1-611 | [»] | |
3FUD | X-ray | 2.20 | A | 1-611 | [»] | |
3FUE | X-ray | 2.38 | A | 1-611 | [»] | |
3FUF | X-ray | 2.60 | A | 1-611 | [»] | |
3FUH | X-ray | 1.80 | A | 1-611 | [»] | |
3FUI | X-ray | 2.20 | A | 1-611 | [»] | |
3FUJ | X-ray | 1.90 | A | 1-611 | [»] | |
3FUK | X-ray | 1.95 | A | 1-611 | [»] | |
3FUL | X-ray | 2.39 | A | 1-611 | [»] | |
3FUM | X-ray | 2.15 | A | 1-611 | [»] | |
3FUN | X-ray | 1.58 | A | 1-611 | [»] | |
3U9W | X-ray | 1.25 | A | 4-611 | [»] | |
4DPR | X-ray | 2.02 | A | 1-611 | [»] | |
4L2L | X-ray | 1.65 | A | 1-611 | [»] | |
4MKT | X-ray | 1.62 | A | 1-611 | [»] | |
4MS6 | X-ray | 1.72 | A | 1-611 | [»] | |
4R7L | X-ray | 1.66 | A | 1-611 | [»] | |
4RSY | X-ray | 1.93 | A | 1-611 | [»] | |
4RVB | X-ray | 1.93 | A | 1-611 | [»] | |
5AEN | X-ray | 1.86 | A | 4-611 | [»] | |
5BPP | X-ray | 2.03 | A | 1-611 | [»] | |
5FWQ | X-ray | 2.05 | A | 1-611 | [»] | |
5N3W | X-ray | 2.30 | A | 1-611 | [»] | |
5NI2 | X-ray | 1.50 | A | 2-611 | [»] | |
5NI4 | X-ray | 1.90 | A/B/C | 2-611 | [»] | |
5NI6 | X-ray | 1.54 | A | 2-611 | [»] | |
5NIA | X-ray | 1.76 | A | 2-611 | [»] | |
5NID | X-ray | 1.57 | A | 2-611 | [»] | |
5NIE | X-ray | 2.60 | A/B/C | 2-611 | [»] | |
6ENB | X-ray | 1.84 | A | 2-611 | [»] | |
6ENC | X-ray | 1.95 | A | 2-611 | [»] | |
6END | X-ray | 2.24 | A | 2-611 | [»] | |
6O5H | X-ray | 2.84 | A/B/C | 4-611 | [»] | |
SMRi | P09960 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 110226, 34 interactors |
IntActi | P09960, 11 interactors |
STRINGi | 9606.ENSP00000228740 |
Chemistry databases
BindingDBi | P09960 |
ChEMBLi | CHEMBL4618 |
DrugBanki | DB07102, (2S)-2-amino-5-oxo-5-[(4-phenylmethoxyphenyl)amino]pentanoic acid DB06917, (4-fluorophenyl)(pyridin-4-yl)methanone DB07258, (R)-pyridin-4-yl[4-(2-pyrrolidin-1-ylethoxy)phenyl]methanol DB07094, 1-(2,2'-bithiophen-5-yl)methanamine DB07259, 1-(4-thiophen-2-ylphenyl)methanamine DB02352, 3-(Benzyloxy)Pyridin-2-Amine DB07292, 4-(2-amino-1,3-thiazol-4-yl)phenol DB07104, 4-amino-N-[4-(benzyloxy)phenyl]butanamide DB06828, 5-[2-(1H-pyrrol-1-yl)ethoxy]-1H-indole DB08466, 5-[2-(4-hydroxyphenyl)ethyl]benzene-1,3-diol DB01197, Captopril DB05177, DG051 DB03366, Imidazole DB08040, Kelatorphan DB06851, N-(pyridin-3-ylmethyl)aniline DB02062, N-[3-[(1-Aminoethyl)(Hydroxy)Phosphoryl]-2-(1,1'-Biphenyl-4-Ylmethyl)Propanoyl]Alanine DB07099, N-[4-(benzyloxy)phenyl]glycinamide DB07260, N-benzyl-4-[(2R)-pyrrolidin-2-ylmethoxy]aniline DB07196, N-methyl-1-(2-thiophen-2-ylphenyl)methanamine DB11781, Tosedostat DB03424, Ubenimex DB07237, {4-[(2R)-pyrrolidin-2-ylmethoxy]phenyl}(4-thiophen-3-ylphenyl)methanone |
DrugCentrali | P09960 |
GuidetoPHARMACOLOGYi | 1395 |
SwissLipidsi | SLP:000001118 |
Protein family/group databases
MEROPSi | M01.004 |
MoonProti | P09960 |
PTM databases
iPTMneti | P09960 |
MetOSitei | P09960 |
PhosphoSitePlusi | P09960 |
SwissPalmi | P09960 |
Genetic variation databases
BioMutai | LTA4H |
DMDMi | 126353 |
2D gel databases
REPRODUCTION-2DPAGEi | IPI00219077 |
Proteomic databases
CPTACi | CPTAC-92 CPTAC-93 |
EPDi | P09960 |
jPOSTi | P09960 |
MassIVEi | P09960 |
MaxQBi | P09960 |
PaxDbi | P09960 |
PeptideAtlasi | P09960 |
PRIDEi | P09960 |
ProteomicsDBi | 28779 52284 [P09960-1] 52285 [P09960-2] 52286 [P09960-3] |
Protocols and materials databases
Antibodypediai | 4453, 490 antibodies |
DNASUi | 4048 |
Genome annotation databases
Ensembli | ENST00000228740; ENSP00000228740; ENSG00000111144 [P09960-1] ENST00000413268; ENSP00000395051; ENSG00000111144 [P09960-3] ENST00000552789; ENSP00000449958; ENSG00000111144 [P09960-4] |
GeneIDi | 4048 |
KEGGi | hsa:4048 |
UCSCi | uc001ten.3, human [P09960-1] |
Organism-specific databases
CTDi | 4048 |
DisGeNETi | 4048 |
GeneCardsi | LTA4H |
HGNCi | HGNC:6710, LTA4H |
HPAi | ENSG00000111144, Low tissue specificity |
MIMi | 151570, gene |
neXtProti | NX_P09960 |
OpenTargetsi | ENSG00000111144 |
PharmGKBi | PA24345 |
VEuPathDBi | HostDB:ENSG00000111144.9 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG1047, Eukaryota |
GeneTreei | ENSGT00940000156375 |
HOGENOMi | CLU_014505_0_0_1 |
InParanoidi | P09960 |
OMAi | NSNFRMK |
PhylomeDBi | P09960 |
TreeFami | TF300758 |
Enzyme and pathway databases
UniPathwayi | UPA00878 |
BioCyci | MetaCyc:HS03372-MONOMER |
BRENDAi | 3.3.2.6, 2681 |
PathwayCommonsi | P09960 |
Reactomei | R-HSA-2142691, Synthesis of Leukotrienes (LT) and Eoxins (EX) R-HSA-6798695, Neutrophil degranulation R-HSA-9018676, Biosynthesis of D-series resolvins R-HSA-9018681, Biosynthesis of protectins R-HSA-9018896, Biosynthesis of E-series 18(S)-resolvins R-HSA-9020265, Biosynthesis of aspirin-triggered D-series resolvins R-HSA-9023661, Biosynthesis of E-series 18(R)-resolvins |
SABIO-RKi | P09960 |
Miscellaneous databases
BioGRID-ORCSi | 4048, 4 hits in 877 CRISPR screens |
ChiTaRSi | LTA4H, human |
EvolutionaryTracei | P09960 |
GenomeRNAii | 4048 |
Pharosi | P09960, Tchem |
PROi | PR:P09960 |
RNActi | P09960, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000111144, Expressed in visceral pleura and 246 other tissues |
ExpressionAtlasi | P09960, baseline and differential |
Genevisiblei | P09960, HS |
Family and domain databases
CDDi | cd09599, M1_LTA4H, 1 hit |
Gene3Di | 1.10.390.10, 1 hit 1.25.40.320, 1 hit 2.60.40.1730, 1 hit |
InterProi | View protein in InterPro IPR042097, Aminopeptidase_N-like_N IPR016024, ARM-type_fold IPR012777, LTA4H IPR038502, M1_LTA-4_hydro/amino_C_sf IPR034015, M1_LTA4H IPR001930, Peptidase_M1 IPR015211, Peptidase_M1_C IPR014782, Peptidase_M1_dom IPR027268, Peptidase_M4/M1_CTD_sf |
PANTHERi | PTHR45726, PTHR45726, 1 hit |
Pfami | View protein in Pfam PF09127, Leuk-A4-hydro_C, 1 hit PF01433, Peptidase_M1, 1 hit |
PRINTSi | PR00756, ALADIPTASE |
SMARTi | View protein in SMART SM01263, Leuk-A4-hydro_C, 1 hit |
SUPFAMi | SSF48371, SSF48371, 1 hit SSF63737, SSF63737, 1 hit |
TIGRFAMsi | TIGR02411, leuko_A4_hydro, 1 hit |
PROSITEi | View protein in PROSITE PS00142, ZINC_PROTEASE, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | LKHA4_HUMAN | |
Accessioni | P09960Primary (citable) accession number: P09960 Secondary accession number(s): B4DNQ9 Q9UCT7 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 1, 1989 |
Last sequence update: | January 23, 2007 | |
Last modified: | February 10, 2021 | |
This is version 237 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, Direct protein sequencing, Reference proteomeDocuments
- Peptidase families
Classification of peptidase families and list of entries - Human chromosome 12
Human chromosome 12: entries, gene names and cross-references to MIM - Human entries with genetic variants
List of human entries with genetic variants - Human variants curated from literature reports
Index of human variants curated from literature reports - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families