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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

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

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>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
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi296Zinc; catalyticCombined sources7 Publications1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei297Proton acceptorCombined sources1 Publication1 Publication1
Metal bindingi300Zinc; catalyticCombined sources7 Publications1
Metal bindingi319Zinc; catalyticCombined sources7 Publications1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei376Essential for epoxide hydrolase activity, but not for aminopeptidase activity1
Sitei379Covalently modified during suicide inhibition by leukotrienes1
Active sitei384Proton donorCombined sources1 Publication1 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • 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
  • zinc ion binding Source: UniProtKB

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

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

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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BioCyci
MetaCyc:HS03372-MONOMER

BRENDA Comprehensive Enzyme Information System

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BRENDAi
3.3.2.6 2681

Reactome - a knowledgebase of biological pathways and processes

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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-RK: Biochemical Reaction Kinetics Database

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SABIO-RKi
P09960

UniPathway: a resource for the exploration and annotation of metabolic pathways

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UniPathwayi
UPA00878

Protein family/group databases

MEROPS protease database

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MEROPSi
M01.004

MoonProt database of moonlighting proteins

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MoonProti
P09960

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...
SwissLipidsi
SLP:000001118

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:LTA4H
Synonyms:LTA4
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 12

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000111144.9

Human Gene Nomenclature Database

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HGNCi
HGNC:6710 LTA4H

Online Mendelian Inheritance in Man (OMIM)

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MIMi
151570 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P09960

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

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

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

DisGeNET

More...
DisGeNETi
4048

Open Targets

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OpenTargetsi
ENSG00000111144

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA24345

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL4618

Drug and drug target database

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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
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

IUPHAR/BPS Guide to PHARMACOLOGY

More...
GuidetoPHARMACOLOGYi
1395

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
LTA4H

Domain mapping of disease mutations (DMDM)

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DMDMi
126353

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources2 Publications
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000951242 – 611Leukotriene A-4 hydrolaseAdd BLAST610

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei73N6-acetyllysineCombined sources1
Modified residuei337N6-acetyllysineCombined sources1
Modified residuei414N6-acetyllysineCombined sources1
Modified residuei416Phosphoserine1 Publication1
Modified residuei573N6-acetyllysineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylation at Ser-416 inhibits enzymatic activity.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P09960

MaxQB - The MaxQuant DataBase

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MaxQBi
P09960

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P09960

PeptideAtlas

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PeptideAtlasi
P09960

PRoteomics IDEntifications database

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PRIDEi
P09960

ProteomicsDB human proteome resource

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ProteomicsDBi
52284
52285 [P09960-2]
52286 [P09960-3]

2D gel databases

REPRODUCTION-2DPAGE

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REPRODUCTION-2DPAGEi
IPI00219077

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P09960

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P09960

SwissPalm database of S-palmitoylation events

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SwissPalmi
P09960

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000111144 Expressed in 233 organ(s), highest expression level in visceral pleura

CleanEx database of gene expression profiles

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CleanExi
HS_LTA4H

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P09960 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P09960 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB015221
HPA008399
HPA017017

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer.3 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
110226, 23 interactors

Protein interaction database and analysis system

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IntActi
P09960, 7 interactors

STRING: functional protein association networks

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STRINGi
9606.ENSP00000228740

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P09960

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

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

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P09960

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P09960

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P09960

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni135 – 137Substrate binding1 Publication3
Regioni267 – 272Substrate binding1 Publication6
Regioni564 – 566Substrate binding1 Publication3

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the peptidase M1 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG1047 Eukaryota
COG0308 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000156375

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000293296

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG001274

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P09960

KEGG Orthology (KO)

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KOi
K01254

Identification of Orthologs from Complete Genome Data

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OMAi
NSNFRMK

Database of Orthologous Groups

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OrthoDBi
EOG091G02UX

Database for complete collections of gene phylogenies

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PhylomeDBi
P09960

TreeFam database of animal gene trees

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TreeFami
TF300758

Family and domain databases

Conserved Domains Database

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CDDi
cd09599 M1_LTA4H, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.390.10, 1 hit
1.25.40.320, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View 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

The PANTHER Classification System

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PANTHERi
PTHR11533 PTHR11533, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF09127 Leuk-A4-hydro_C, 1 hit
PF01433 Peptidase_M1, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00756 ALADIPTASE

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM01263 Leuk-A4-hydro_C, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF48371 SSF48371, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR02411 leuko_A4_hydro, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00142 ZINC_PROTEASE, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (4+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> 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.

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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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>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:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>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
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_051570131Y → H. Corresponds to variant dbSNP:rs45630737Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>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:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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.

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS58266.1 [P09960-3]
CCDS58267.1 [P09960-4]
CCDS9059.1 [P09960-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
S65947

NCBI Reference Sequences

More...
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]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.524648

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000228740; ENSP00000228740; ENSG00000111144 [P09960-1]
ENST00000413268; ENSP00000395051; ENSG00000111144 [P09960-3]
ENST00000552789; ENSP00000449958; ENSG00000111144 [P09960-4]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
4048

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:4048

UCSC genome browser

More...
UCSCi
uc001ten.3 human [P09960-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

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:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
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

The DNASU plasmid repository

More...
DNASUi
4048
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

Comparative Toxicogenomics Database

More...
CTDi
4048
DisGeNETi4048
EuPathDBiHostDB:ENSG00000111144.9

GeneCards: human genes, protein and diseases

More...
GeneCardsi
LTA4H
HGNCiHGNC:6710 LTA4H
HPAiCAB015221
HPA008399
HPA017017
MIMi151570 gene
neXtProtiNX_P09960
OpenTargetsiENSG00000111144
PharmGKBiPA24345

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1047 Eukaryota
COG0308 LUCA
GeneTreeiENSGT00940000156375
HOGENOMiHOG000293296
HOVERGENiHBG001274
InParanoidiP09960
KOiK01254
OMAiNSNFRMK
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

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
LTA4H human
EvolutionaryTraceiP09960

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
4048

Protein Ontology

More...
PROi
PR:P09960

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiLKHA4_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P09960
Secondary accession number(s): B4DNQ9
, F8VV40, Q6IAT6, Q9UCT7
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: December 5, 2018
This is version 224 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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

Documents

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