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Protein

Leukotriene A-4 hydrolase

Gene

LTA4H

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

Functioni

Epoxide hydrolase that catalyzes the final step in the biosynthesis of the proinflammatory mediator leukotriene B4. Has also aminopeptidase activity.7 Publications

Catalytic activityi

(7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa-7,9,11,14-tetraenoate + H2O = (6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate.6 Publications

Cofactori

Zn2+3 PublicationsNote: Binds 1 zinc ion per subunit.3 Publications

Activity regulationi

Inhibited by bestatin. Subject to suicide inhibition by leukotriene A4, due to the formation of a covalent adduct at Tyr-379.1 Publication

Pathwayi: leukotriene B4 biosynthesis

This protein is involved in the pathway leukotriene B4 biosynthesis, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway leukotriene B4 biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi296Zinc; catalyticCombined sources7 Publications1
Active sitei297Proton acceptorCombined sources1 Publication1 Publication1
Metal bindingi300Zinc; catalyticCombined sources7 Publications1
Metal bindingi319Zinc; catalyticCombined sources7 Publications1
Sitei376Essential for epoxide hydrolase activity, but not for aminopeptidase activity1
Sitei379Covalently modified during suicide inhibition by leukotrienes1
Active sitei384Proton donorCombined sources1 Publication1 Publication1

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
  • peptide binding Source: GO_Central
  • RNA binding Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Metalloprotease, Protease
Biological processLeukotriene biosynthesis
LigandMetal-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:HS03372-MONOMER
BRENDAi3.3.2.6 2681
ReactomeiR-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-RKiP09960
UniPathwayi
UPA00878

Protein family/group databases

MEROPSiM01.004
MoonProtiP09960

Chemistry databases

SwissLipidsiSLP:000001118

Names & Taxonomyi

Protein namesi
Recommended name:
Leukotriene A-4 hydrolase (EC:3.3.2.6)
Short name:
LTA-4 hydrolase
Alternative name(s):
Leukotriene A(4) hydrolase
Gene namesi
Name:LTA4H
Synonyms:LTA4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

EuPathDBiHostDB:ENSG00000111144.9
HGNCiHGNC:6710 LTA4H
MIMi151570 gene
neXtProtiNX_P09960

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi135Q → A or L: Srongly increased epoxide hydrolase activity. 1 Publication1
Mutagenesisi135Q → A: Strongly reduced aminopeptidase activity. Strongly decreased affinity for leukotriene. Abolishes epoxide hydrolase activity. 1 Publication1
Mutagenesisi137Q → A: No loss of activity. 1 Publication1
Mutagenesisi137Q → L: Aminopeptidase activity strongly impaired, but keeps LTA4 activity. 1 Publication1
Mutagenesisi137Q → N: Aminopeptidase activity almost absent, but keeps LTA4 activity. 1 Publication1
Mutagenesisi140H → Q: Aminopeptidase activity almost absent, but keeps LTA4 activity. 1 Publication1
Mutagenesisi269G → A: No loss of activity. 1 Publication1
Mutagenesisi270G → A: No loss of activity. 1 Publication1
Mutagenesisi271M → L: No loss of activity. 1 Publication1
Mutagenesisi272E → A or D: Complete loss of activity. 1 Publication1
Mutagenesisi272E → Q: Loss of LTA4 activity, and aminopeptidase activity strongly impaired. 1 Publication1
Mutagenesisi273N → A: No loss of activity. 1 Publication1
Mutagenesisi296H → Y: Complete loss of activity. 1 Publication1
Mutagenesisi297E → A: Loss of both activities. 3 Publications1
Mutagenesisi297E → K: Loss of both activities. 3 Publications1
Mutagenesisi297E → Q: Loss of aminopeptidase activity, but keeps LTA4 activity. 3 Publications1
Mutagenesisi300H → L: Complete loss of activity. 1 Publication1
Mutagenesisi319E → A: Complete loss of activity. 1 Publication1
Mutagenesisi372D → N: No loss of activity. 1 Publication1
Mutagenesisi374D → N: No loss of activity. 1 Publication1
Mutagenesisi376D → A: Strongly reduced hydrolysis of peptides starting with Arg. Small effect on hydrolysis of peptides starting with Ala. Strongly reduced epoxide hydrolase activity. 2 Publications1
Mutagenesisi376D → E: Strongly reduced aminopeptidase activity. Abolishes epoxide hydrolase activity. 2 Publications1
Mutagenesisi376D → N: Abolishes aminopeptidase and epoxide hydrolase activity. 2 Publications1
Mutagenesisi385E → Q: Reduced aminopeptidase activity. Minor effect on epoxide hydrolase activity. 1 Publication1
Mutagenesisi564R → A, K or M: Abolishes epoxide hydrolase activity. Reduced aminopeptidase activity. 1 Publication1
Mutagenesisi566K → A or M: Strongly reduced affinity for peptide substrates. Reduced epoxide hydrolase and aminopeptidase activity. 1 Publication1
Mutagenesisi566K → R: No effect on epoxide hydrolase and aminopeptidase activity. 1 Publication1

Organism-specific databases

DisGeNETi4048
OpenTargetsiENSG00000111144
PharmGKBiPA24345

Chemistry databases

ChEMBLiCHEMBL4618
DrugBankiDB07102 (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
DB07259 1-(4-thiophen-2-ylphenyl)methanamine
DB02352 3-(Benzyloxy)Pyridin-2-Amine
DB07104 4-amino-N-[4-(benzyloxy)phenyl]butanamide
DB06828 5-[2-(1H-pyrrol-1-yl)ethoxy]-1H-indole
DB01197 Captopril
DB05745 CHR-2797
DB05177 DG051
DB06851 N-(pyridin-3-ylmethyl)aniline
DB08040 N-[(2R)-2-benzyl-4-(hydroxyamino)-4-oxobutanoyl]-L-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
DB03424 Ubenimex
DB07237 {4-[(2R)-pyrrolidin-2-ylmethoxy]phenyl}(4-thiophen-3-ylphenyl)methanone
GuidetoPHARMACOLOGYi1395

Polymorphism and mutation databases

BioMutaiLTA4H
DMDMi126353

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources2 Publications
ChainiPRO_00000951242 – 611Leukotriene A-4 hydrolaseAdd BLAST610

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei73N6-acetyllysineCombined sources1
Modified residuei337N6-acetyllysineCombined sources1
Modified residuei414N6-acetyllysineCombined sources1
Modified residuei416Phosphoserine1 Publication1
Modified residuei573N6-acetyllysineCombined sources1

Post-translational modificationi

Phosphorylation at Ser-416 inhibits enzymatic activity.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP09960
MaxQBiP09960
PaxDbiP09960
PeptideAtlasiP09960
PRIDEiP09960
ProteomicsDBi52284
52285 [P09960-2]
52286 [P09960-3]

2D gel databases

REPRODUCTION-2DPAGEiIPI00219077

PTM databases

iPTMnetiP09960
PhosphoSitePlusiP09960
SwissPalmiP09960

Expressioni

Tissue specificityi

Isoform 1 and isoform 2 are expressed in monocytes, lymphocytes, neutrophils, reticulocytes, platelets and fibroblasts.

Gene expression databases

BgeeiENSG00000111144 Expressed in 233 organ(s), highest expression level in visceral pleura
CleanExiHS_LTA4H
ExpressionAtlasiP09960 baseline and differential
GenevisibleiP09960 HS

Organism-specific databases

HPAiCAB015221
HPA008399
HPA017017

Interactioni

Subunit structurei

Monomer.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
TINF2Q9BSI42EBI-721089,EBI-717399

Protein-protein interaction databases

BioGridi110226, 23 interactors
IntActiP09960, 7 interactors
STRINGi9606.ENSP00000228740

Chemistry databases

BindingDBiP09960

Structurei

Secondary structure

1611
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP09960
SMRiP09960
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09960

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni135 – 137Substrate binding1 Publication3
Regioni267 – 272Substrate binding1 Publication6
Regioni564 – 566Substrate binding1 Publication3

Sequence similaritiesi

Belongs to the peptidase M1 family.Curated

Phylogenomic databases

eggNOGiKOG1047 Eukaryota
COG0308 LUCA
GeneTreeiENSGT00530000063003
HOGENOMiHOG000293296
HOVERGENiHBG001274
InParanoidiP09960
KOiK01254
OMAiNFEHFWL
OrthoDBiEOG091G02UX
PhylomeDBiP09960
TreeFamiTF300758

Family and domain databases

CDDicd09599 M1_LTA4H, 1 hit
Gene3Di1.10.390.10, 1 hit
1.25.40.320, 1 hit
InterProiView protein in InterPro
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_N
IPR027268 Peptidase_M4/M1_CTD_sf
PANTHERiPTHR11533 PTHR11533, 1 hit
PfamiView protein in Pfam
PF09127 Leuk-A4-hydro_C, 1 hit
PF01433 Peptidase_M1, 1 hit
PRINTSiPR00756 ALADIPTASE
SMARTiView protein in SMART
SM01263 Leuk-A4-hydro_C, 1 hit
SUPFAMiSSF48371 SSF48371, 1 hit
TIGRFAMsiTIGR02411 leuko_A4_hydro, 1 hit
PROSITEiView protein in PROSITE
PS00142 ZINC_PROTEASE, 1 hit

Sequences (4+)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

This 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 '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
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
Length:611
Mass (Da):69,285
Last modified:January 23, 2007 - v2
Checksum:i329BF6D04D4A06E1
GO
Isoform 2 (identifier: P09960-2) [UniParc]FASTAAdd to basket
Also known as: S-LTA4

The sequence of this isoform differs from the canonical sequence as follows:
     511-532: APLPLGHIKRMQEVYNFNAINN → MAAALHSIQVGGRNSFGAKDGN
     533-611: Missing.

Show »
Length:532
Mass (Da):59,733
Checksum:i474891F08B0215A8
GO
Isoform 3 (identifier: P09960-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-53: MPEIVDTCSL...QSQEDNLRSL → MLPQRNLSKRQVPTMHIPVKTRRLLAALK
     511-532: APLPLGHIKRMQEVYNFNAINN → MAAALHSIQVGGRNSFGAKDGN
     533-611: Missing.

Show »
Length:508
Mass (Da):57,300
Checksum:iA1CDA72AF83A875C
GO
Isoform 4 (identifier: P09960-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-53: MPEIVDTCSL...QSQEDNLRSL → MLPQRNLSKRQVPTMHIPVKTRRLLAALK

Note: No experimental confirmation available.
Show »
Length:587
Mass (Da):66,852
Checksum:iA70BF2792A0427C7
GO

Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
B4DEH5B4DEH5_HUMAN
Leukotriene A-4 hydrolase
LTA4H
132Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti115A → T in BX647158 (PubMed:17974005).Curated1
Sequence conflicti123Q → R in BX647158 (PubMed:17974005).Curated1
Sequence conflicti297E → G in BAG60321 (PubMed:14702039).Curated1
Sequence conflicti309N → S in BX647158 (PubMed:17974005).Curated1
Sequence conflicti378A → V in BX647158 (PubMed:17974005).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_051570131Y → H. Corresponds to variant dbSNP:rs45630737Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0411071 – 53MPEIV…NLRSL → MLPQRNLSKRQVPTMHIPVK TRRLLAALK in isoform 3 and isoform 4. 2 PublicationsAdd BLAST53
Alternative sequenceiVSP_041108511 – 532APLPL…NAINN → MAAALHSIQVGGRNSFGAKD GN in isoform 2 and isoform 3. 1 PublicationAdd BLAST22
Alternative sequenceiVSP_041109533 – 611Missing in isoform 2 and isoform 3. 1 PublicationAdd BLAST79

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.
CCDSiCCDS58266.1 [P09960-3]
CCDS58267.1 [P09960-4]
CCDS9059.1 [P09960-1]
PIRiS65947
RefSeqiNP_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]
UniGeneiHs.524648

Genome annotation databases

EnsembliENST00000228740; ENSP00000228740; ENSG00000111144 [P09960-1]
ENST00000413268; ENSP00000395051; ENSG00000111144 [P09960-3]
ENST00000552789; ENSP00000449958; ENSG00000111144 [P09960-4]
GeneIDi4048
KEGGihsa:4048
UCSCiuc001ten.3 human [P09960-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar 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.
CCDSiCCDS58266.1 [P09960-3]
CCDS58267.1 [P09960-4]
CCDS9059.1 [P09960-1]
PIRiS65947
RefSeqiNP_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]
UniGeneiHs.524648

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GW6X-ray2.20A2-611[»]
1H19X-ray2.10A2-611[»]
1HS6X-ray1.95A1-611[»]
1SQMX-ray2.30A2-611[»]
2R59X-ray1.89A2-611[»]
2VJ8X-ray1.80A1-611[»]
3B7RX-ray1.81L2-611[»]
3B7SX-ray1.47A2-611[»]
3B7TX-ray2.30A2-611[»]
3B7UX-ray1.90X2-611[»]
3CHOX-ray1.80A2-611[»]
3CHPX-ray2.10A2-611[»]
3CHQX-ray2.09A2-611[»]
3CHRX-ray2.20A2-611[»]
3CHSX-ray2.55A2-611[»]
3FH5X-ray1.63A1-611[»]
3FH7X-ray2.05A1-611[»]
3FH8X-ray1.67A1-611[»]
3FHEX-ray2.16A1-611[»]
3FTSX-ray2.33A1-611[»]
3FTUX-ray1.90A1-611[»]
3FTVX-ray1.70A1-611[»]
3FTWX-ray1.85A1-611[»]
3FTXX-ray1.96A1-611[»]
3FTYX-ray2.15A1-611[»]
3FTZX-ray2.00A1-611[»]
3FU0X-ray1.80A1-611[»]
3FU3X-ray2.00A1-611[»]
3FU5X-ray2.30A1-611[»]
3FU6X-ray2.05A1-611[»]
3FUDX-ray2.20A1-611[»]
3FUEX-ray2.38A1-611[»]
3FUFX-ray2.60A1-611[»]
3FUHX-ray1.80A1-611[»]
3FUIX-ray2.20A1-611[»]
3FUJX-ray1.90A1-611[»]
3FUKX-ray1.95A1-611[»]
3FULX-ray2.39A1-611[»]
3FUMX-ray2.15A1-611[»]
3FUNX-ray1.58A1-611[»]
3U9WX-ray1.25A4-611[»]
4DPRX-ray2.02A1-611[»]
4L2LX-ray1.65A1-611[»]
4MKTX-ray1.62A1-611[»]
4MS6X-ray1.72A1-611[»]
4R7LX-ray1.66A1-611[»]
4RSYX-ray1.93A1-611[»]
4RVBX-ray1.93A1-611[»]
5AENX-ray1.86A4-611[»]
5BPPX-ray2.03A1-611[»]
5FWQX-ray2.05A1-611[»]
5N3WX-ray2.30A1-611[»]
5NI2X-ray1.50A2-611[»]
5NI4X-ray1.90A/B/C2-611[»]
5NI6X-ray1.54A2-611[»]
5NIAX-ray1.76A2-611[»]
5NIDX-ray1.57A2-611[»]
5NIEX-ray2.60A/B/C2-611[»]
6ENBX-ray1.84A2-611[»]
6ENCX-ray1.95A2-611[»]
6ENDX-ray2.24A2-611[»]
ProteinModelPortaliP09960
SMRiP09960
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110226, 23 interactors
IntActiP09960, 7 interactors
STRINGi9606.ENSP00000228740

Chemistry databases

BindingDBiP09960
ChEMBLiCHEMBL4618
DrugBankiDB07102 (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
DB07259 1-(4-thiophen-2-ylphenyl)methanamine
DB02352 3-(Benzyloxy)Pyridin-2-Amine
DB07104 4-amino-N-[4-(benzyloxy)phenyl]butanamide
DB06828 5-[2-(1H-pyrrol-1-yl)ethoxy]-1H-indole
DB01197 Captopril
DB05745 CHR-2797
DB05177 DG051
DB06851 N-(pyridin-3-ylmethyl)aniline
DB08040 N-[(2R)-2-benzyl-4-(hydroxyamino)-4-oxobutanoyl]-L-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
DB03424 Ubenimex
DB07237 {4-[(2R)-pyrrolidin-2-ylmethoxy]phenyl}(4-thiophen-3-ylphenyl)methanone
GuidetoPHARMACOLOGYi1395
SwissLipidsiSLP:000001118

Protein family/group databases

MEROPSiM01.004
MoonProtiP09960

PTM databases

iPTMnetiP09960
PhosphoSitePlusiP09960
SwissPalmiP09960

Polymorphism and mutation databases

BioMutaiLTA4H
DMDMi126353

2D gel databases

REPRODUCTION-2DPAGEiIPI00219077

Proteomic databases

EPDiP09960
MaxQBiP09960
PaxDbiP09960
PeptideAtlasiP09960
PRIDEiP09960
ProteomicsDBi52284
52285 [P09960-2]
52286 [P09960-3]

Protocols and materials databases

DNASUi4048
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000228740; ENSP00000228740; ENSG00000111144 [P09960-1]
ENST00000413268; ENSP00000395051; ENSG00000111144 [P09960-3]
ENST00000552789; ENSP00000449958; ENSG00000111144 [P09960-4]
GeneIDi4048
KEGGihsa:4048
UCSCiuc001ten.3 human [P09960-1]

Organism-specific databases

CTDi4048
DisGeNETi4048
EuPathDBiHostDB:ENSG00000111144.9
GeneCardsiLTA4H
HGNCiHGNC:6710 LTA4H
HPAiCAB015221
HPA008399
HPA017017
MIMi151570 gene
neXtProtiNX_P09960
OpenTargetsiENSG00000111144
PharmGKBiPA24345
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1047 Eukaryota
COG0308 LUCA
GeneTreeiENSGT00530000063003
HOGENOMiHOG000293296
HOVERGENiHBG001274
InParanoidiP09960
KOiK01254
OMAiNFEHFWL
OrthoDBiEOG091G02UX
PhylomeDBiP09960
TreeFamiTF300758

Enzyme and pathway databases

UniPathwayi
UPA00878

BioCyciMetaCyc:HS03372-MONOMER
BRENDAi3.3.2.6 2681
ReactomeiR-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-RKiP09960

Miscellaneous databases

ChiTaRSiLTA4H human
EvolutionaryTraceiP09960
GenomeRNAii4048
PROiPR:P09960
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000111144 Expressed in 233 organ(s), highest expression level in visceral pleura
CleanExiHS_LTA4H
ExpressionAtlasiP09960 baseline and differential
GenevisibleiP09960 HS

Family and domain databases

CDDicd09599 M1_LTA4H, 1 hit
Gene3Di1.10.390.10, 1 hit
1.25.40.320, 1 hit
InterProiView protein in InterPro
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_N
IPR027268 Peptidase_M4/M1_CTD_sf
PANTHERiPTHR11533 PTHR11533, 1 hit
PfamiView protein in Pfam
PF09127 Leuk-A4-hydro_C, 1 hit
PF01433 Peptidase_M1, 1 hit
PRINTSiPR00756 ALADIPTASE
SMARTiView protein in SMART
SM01263 Leuk-A4-hydro_C, 1 hit
SUPFAMiSSF48371 SSF48371, 1 hit
TIGRFAMsiTIGR02411 leuko_A4_hydro, 1 hit
PROSITEiView protein in PROSITE
PS00142 ZINC_PROTEASE, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiLKHA4_HUMAN
AccessioniPrimary (citable) accession number: P09960
Secondary accession number(s): B4DNQ9
, F8VV40, Q6IAT6, Q9UCT7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: September 12, 2018
This is version 222 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  8. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
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Main funding by: National Institutes of Health

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