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Protein

Leukotriene A-4 hydrolase

Gene

LTA4H

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

Enzyme 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; catalytic1
Active sitei297Proton acceptor1 Publication1
Metal bindingi300Zinc; catalytic1
Metal bindingi319Zinc; catalytic1
Sitei376Essential for epoxide hydrolase activity, but not for aminopeptidase activity1
Sitei379Covalently modified during suicide inhibition by leukotrienes1
Active sitei384Proton donor1 Publication1

GO - Molecular functioni

  • aminopeptidase activity Source: UniProtKB
  • epoxide hydrolase activity Source: UniProtKB
  • leukotriene-A4 hydrolase activity Source: UniProtKB
  • metalloaminopeptidase activity Source: GO_Central
  • peptidase activity Source: ProtInc
  • peptide binding Source: GO_Central
  • poly(A) RNA binding Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • leukotriene biosynthetic process Source: UniProtKB
  • leukotriene metabolic process Source: Reactome
  • peptide catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Leukotriene biosynthesis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:HS03372-MONOMER.
ZFISH:HS03372-MONOMER.
BRENDAi3.3.2.6. 2681.
ReactomeiR-HSA-2142691. Synthesis of Leukotrienes (LT) and Eoxins (EX).
R-HSA-6798695. Neutrophil degranulation.
SABIO-RKP09960.
UniPathwayiUPA00878.

Protein family/group databases

MEROPSiM01.004.

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

HGNCiHGNC:6710. LTA4H.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: GO_Central
  • plasma membrane Source: GO_Central
Complete GO annotation...

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.
DrugBankiDB01197. Captopril.
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.

2D gel databases

REPRODUCTION-2DPAGEIPI00219077.

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.
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. 6 interactors.
MINTiMINT-1388946.
STRINGi9606.ENSP00000228740.

Chemistry databases

BindingDBiP09960.

Structurei

Secondary structure

1611
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni14 – 16Combined sources3
Beta strandi17 – 29Combined sources13
Turni30 – 33Combined sources4
Beta strandi34 – 45Combined sources12
Beta strandi50 – 59Combined sources10
Beta strandi61 – 67Combined sources7
Beta strandi74 – 76Combined sources3
Helixi81 – 83Combined sources3
Beta strandi85 – 95Combined sources11
Beta strandi100 – 108Combined sources9
Beta strandi116 – 119Combined sources4
Helixi121 – 123Combined sources3
Beta strandi124 – 129Combined sources6
Beta strandi131 – 134Combined sources4
Turni137 – 140Combined sources4
Helixi141 – 143Combined sources3
Beta strandi155 – 164Combined sources10
Beta strandi167 – 180Combined sources14
Beta strandi182 – 184Combined sources3
Beta strandi187 – 198Combined sources12
Helixi200 – 202Combined sources3
Beta strandi205 – 209Combined sources5
Beta strandi211 – 216Combined sources6
Beta strandi219 – 223Combined sources5
Helixi225 – 227Combined sources3
Helixi228 – 234Combined sources7
Turni235 – 237Combined sources3
Helixi238 – 249Combined sources12
Beta strandi258 – 261Combined sources4
Beta strandi267 – 271Combined sources5
Beta strandi276 – 279Combined sources4
Helixi281 – 283Combined sources3
Beta strandi286 – 288Combined sources3
Turni289 – 291Combined sources3
Helixi292 – 299Combined sources8
Turni300 – 302Combined sources3
Turni304 – 306Combined sources3
Beta strandi307 – 311Combined sources5
Helixi312 – 314Combined sources3
Helixi315 – 334Combined sources20
Helixi336 – 357Combined sources22
Helixi362 – 364Combined sources3
Beta strandi365 – 367Combined sources3
Helixi375 – 378Combined sources4
Helixi382 – 398Combined sources17
Helixi401 – 415Combined sources15
Beta strandi418 – 420Combined sources3
Helixi422 – 432Combined sources11
Helixi434 – 436Combined sources3
Helixi437 – 441Combined sources5
Helixi445 – 450Combined sources6
Turni464 – 466Combined sources3
Helixi467 – 478Combined sources12
Helixi481 – 486Combined sources6
Helixi489 – 492Combined sources4
Helixi497 – 508Combined sources12
Helixi515 – 525Combined sources11
Helixi527 – 529Combined sources3
Helixi533 – 545Combined sources13
Helixi551 – 561Combined sources11
Helixi565 – 577Combined sources13
Helixi579 – 592Combined sources14
Helixi593 – 595Combined sources3
Helixi598 – 608Combined sources11

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[»]
ProteinModelPortaliP09960.
SMRiP09960.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09960.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni135 – 137Substrate binding3
Regioni267 – 272Substrate binding6
Regioni564 – 566Substrate binding3

Sequence similaritiesi

Belongs to the peptidase M1 family.Curated

Phylogenomic databases

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

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR012777. Leukotriene_A4_hydrolase.
IPR001930. Peptidase_M1.
IPR015211. Peptidase_M1_C.
IPR014782. Peptidase_M1_N.
[Graphical view]
PANTHERiPTHR11533. PTHR11533. 1 hit.
PfamiPF09127. Leuk-A4-hydro_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSiPR00756. ALADIPTASE.
SMARTiSM01263. Leuk-A4-hydro_C. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
TIGRFAMsiTIGR02411. leuko_A4_hydro. 1 hit.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

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

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

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 rs45630737dbSNPEnsembl.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

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[»]
ProteinModelPortaliP09960.
SMRiP09960.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110226. 23 interactors.
IntActiP09960. 6 interactors.
MINTiMINT-1388946.
STRINGi9606.ENSP00000228740.

Chemistry databases

BindingDBiP09960.
ChEMBLiCHEMBL4618.
DrugBankiDB01197. Captopril.
GuidetoPHARMACOLOGYi1395.
SwissLipidsiSLP:000001118.

Protein family/group databases

MEROPSiM01.004.

PTM databases

iPTMnetiP09960.
PhosphoSitePlusiP09960.
SwissPalmiP09960.

Polymorphism and mutation databases

BioMutaiLTA4H.
DMDMi126353.

2D gel databases

REPRODUCTION-2DPAGEIPI00219077.

Proteomic databases

EPDiP09960.
MaxQBiP09960.
PaxDbiP09960.
PeptideAtlasiP09960.
PRIDEiP09960.

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.
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.
OMAiEFANSNF.
OrthoDBiEOG091G02UX.
PhylomeDBiP09960.
TreeFamiTF300758.

Enzyme and pathway databases

UniPathwayiUPA00878.
BioCyciMetaCyc:HS03372-MONOMER.
ZFISH:HS03372-MONOMER.
BRENDAi3.3.2.6. 2681.
ReactomeiR-HSA-2142691. Synthesis of Leukotrienes (LT) and Eoxins (EX).
R-HSA-6798695. Neutrophil degranulation.
SABIO-RKP09960.

Miscellaneous databases

ChiTaRSiLTA4H. human.
EvolutionaryTraceiP09960.
GenomeRNAii4048.
PROiP09960.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000111144.
CleanExiHS_LTA4H.
ExpressionAtlasiP09960. baseline and differential.
GenevisibleiP09960. HS.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR012777. Leukotriene_A4_hydrolase.
IPR001930. Peptidase_M1.
IPR015211. Peptidase_M1_C.
IPR014782. Peptidase_M1_N.
[Graphical view]
PANTHERiPTHR11533. PTHR11533. 1 hit.
PfamiPF09127. Leuk-A4-hydro_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSiPR00756. ALADIPTASE.
SMARTiSM01263. Leuk-A4-hydro_C. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
TIGRFAMsiTIGR02411. leuko_A4_hydro. 1 hit.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLKHA4_HUMAN
AccessioniPrimary (citable) accession number: P09960
Secondary accession number(s): B4DNQ9
, F8VV40, Q6IAT6, Q9UCT7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 205 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. Peptidase families
    Classification of peptidase families and list of entries
  8. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.