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UniProtKB - P09917 (LOX5_HUMAN)

Entry version 213 (02 Dec 2020)
Sequence version 2 (23 Jan 2007)
Previous versions | rss
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Protein

Polyunsaturated fatty acid 5-lipoxygenase

Gene

ALOX5

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

Catalyzes the oxygenation of arachidonate ((5Z,8Z,11Z,14Z)-eicosatetraenoate) to 5-hydroperoxyeicosatetraenoate (5-HPETE) followed by the dehydration to 5,6- epoxyeicosatetraenoate (Leukotriene A4/LTA4), the first two steps in the biosynthesis of leukotrienes, which are potent mediators of inflammation (PubMed:8631361, PubMed:21233389, PubMed:22516296, PubMed:24282679, PubMed:19022417, PubMed:23246375, PubMed:8615788, PubMed:24893149, PubMed:31664810). Also catalyzes the oxygenation of arachidonate into 8-hydroperoxyicosatetraenoate (8-HPETE) and 12-hydroperoxyicosatetraenoate (12-HPETE) (PubMed:23246375). Displays lipoxin synthase activity being able to convert (15S)-HETE into a conjugate tetraene (PubMed:31664810). Although arachidonate is the preferred substrate, this enzyme can also metabolize oxidized fatty acids derived from arachidonate such as (15S)-HETE, eicosapentaenoate (EPA) such as (18R)- and (18S)-HEPE or docosahexaenoate (DHA) which lead to the formation of specialized pro-resolving mediators (SPM) lipoxin and resolvins E and D respectively, therefore it participates in anti-inflammatory responses (PubMed:21206090, PubMed:31664810, PubMed:8615788, PubMed:17114001, PubMed:32404334). Oxidation of DHA directly inhibits endothelial cell proliferation and sprouting angiogenesis via peroxisome proliferator-activated receptor gamma (PPARgamma) (By similarity). It does not catalyze the oxygenation of linoleic acid and does not convert (5S)-HETE to lipoxin isomers (PubMed:31664810). In addition to inflammatory processes, it participates in dendritic cell migration, wound healing through an antioxidant mechanism based on heme oxygenase-1 (HO-1) regulation expression, monocyte adhesion to the endothelium via ITGAM expression on monocytes (By similarity). Moreover, it helps establish an adaptive humoral immunity by regulating primary resting B cells and follicular helper T cells and participates in the CD40-induced production of reactive oxygen species (ROS) after CD40 ligation in B cells through interaction with PIK3R1 that bridges ALOX5 with CD40 (PubMed:21200133). Also may play a role in glucose homeostasis, regulation of insulin secretion and palmitic acid-induced insulin resistance via AMPK (By similarity). Can regulate bone mineralization and fat cell differentiation increases in induced pluripotent stem cells (By similarity).By similarity13 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

Fe cationPROSITE-ProRule annotation1 PublicationNote: Binds 1 Fe cation per subunit.PROSITE-ProRule annotation1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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

Undergoes a sequential loss of the oxygenase and pseudoperoxidase activities which is dependent on the structural characteristics of the substrate for the reaction, on oxygen concentration and on exposure to phospholipids and calcium (PubMed:8631361). 15-HETE and other 15-mono-hydroxyeicosanoids exhibit the highest inhibitory potencies in their capability of suppressing 5-lipoxygenation of arachidonic acid, whereas the other HETEs, (5S,15S)-dihydroxy-(6E,8Z,11Z,13E)-eicosatetraenoic acid (5,15-diHETE) as well as octadecanoids, are modest or poor inhibitors (PubMed:8615788). The formation of (5S)-hydroperoxy-(15S)-hydroxy-(6E,8Z,11Z,13E)-eicosatetraenoate is strongly stimulated by either hydroperoxypolyenoic fatty acids or arachidonic acid (PubMed:8615788). Arachidonate 5-lipoxygenase and leukotriene A4 synthase activities are allosterically increased by ATP (PubMed:24893149).3 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=13 µM for (5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate1 Publication
  2. KM=11 µM for arachidonic acid1 Publication
  3. KM=1.9 µM for arachidonic acid1 Publication
  4. KM=14 µM for (5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate1 Publication
  5. KM=5.3 µM for arachidonic acid (in the presence of 200 µM ATP)1 Publication
  6. KM=19 µM for (5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate (in the presence of 200 µM ATP)1 Publication
  7. KM=1.6 µM for (5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate (generated in situ from arachidonic acid)1 Publication
  8. KM=4.5 µM for (5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate (generated in situ from arachidonic acid in the presence of 200 µM ATP)1 Publication
  1. Vmax=1 µmol/min/mg enzyme toward arachidonic acid1 Publication
  2. Vmax=0.33 µmol/min/mg enzyme toward (5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate1 Publication
  3. Vmax=4.9 µmol/min/mg enzyme toward arachidonic acid (in the presence of 200 µM ATP)1 Publication
  4. Vmax=1.6 µmol/min/mg enzyme toward (5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate (in the presence of 200 µM ATP)1 Publication
  5. Vmax=0.1 µmol/min/mg enzyme toward (5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate (generated in situ from arachidonic acid)1 Publication
  6. Vmax=2 µmol/min/mg enzyme toward (5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate (generated in situ from arachidonic acid in the presence of 200 µM ATP)1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: leukotriene A4 biosynthesis

This protein is involved in the pathway leukotriene A4 biosynthesis, which is part of Lipid metabolism.1 Publication
View all proteins of this organism that are known to be involved in the pathway leukotriene A4 biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 bindingi17Calcium 1; via carbonyl oxygen; structuralBy similarity1
Metal bindingi18Calcium 2; via carbonyl oxygen; structuralBy similarity1
Metal bindingi19Calcium 2; structuralBy similarity1
Metal bindingi44Calcium 2; structuralBy similarity1
Metal bindingi45Calcium 2; via carbonyl oxygen; structuralBy similarity1
Metal bindingi47Calcium 2; structuralBy similarity1
Metal bindingi79Calcium 1; via carbonyl oxygen; structuralBy similarity1
Metal bindingi80Calcium 1; via carbonyl oxygen; structuralBy similarity1
<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>Sitei103Essential for stabilizing binding to COTL11 Publication1
Metal bindingi368Iron; via tele nitrogen; catalyticCombined sources2 Publications1
Metal bindingi373Iron; via tele nitrogen; catalyticCombined sources2 Publications1
Metal bindingi551Iron; via tele nitrogen; catalyticCombined sources2 Publications1
Metal bindingi555Iron; catalyticCombined sources2 Publications1
Metal bindingi674Iron; via carbonyl oxygen; catalyticCombined sources2 Publications1

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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 functionDioxygenase, Hydrolase, Oxidoreductase
Biological processLeukotriene biosynthesis
LigandCalcium, Iron, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		MetaCyc:HS00336-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		1.13.11.34, 2681

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		P09917

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-2142688, Synthesis of 5-eicosatetraenoic acids
R-HSA-2142691, Synthesis of Leukotrienes (LT) and Eoxins (EX)
R-HSA-2142700, Synthesis of Lipoxins (LX)
R-HSA-6785807, Interleukin-4 and Interleukin-13 signaling
R-HSA-6798695, Neutrophil degranulation
R-HSA-9012546, Interleukin-18 signaling
R-HSA-9018676, Biosynthesis of D-series resolvins
R-HSA-9018682, Biosynthesis of maresins
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
R-HSA-9026286, Biosynthesis of DPAn-3-derived protectins and resolvins
R-HSA-9026290, Biosynthesis of DPAn-3-derived maresins
R-HSA-9026403, Biosynthesis of DPAn-3-derived 13-series resolvins
R-HSA-9027604, Biosynthesis of electrophilic Omega-3 PUFA oxo-derivatives

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P09917

SIGNOR Signaling Network Open Resource

More...SIGNORi		P09917

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

More...UniPathwayi		UPA00877

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...SwissLipidsi		SLP:000000669

<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%5Fand%5Ftaxonomy%5Fsection">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:
Polyunsaturated fatty acid 5-lipoxygenaseCurated (EC:1.13.11.-1 Publication)
Alternative name(s):
Arachidonate 5-lipoxygenase (EC:1.13.11.341 Publication)
Short name:
5-LO1 Publication
Short name:
5-lipoxygenase1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:ALOX5Imported
Synonyms:LOG5
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 10

Organism-specific databases

Eukaryotic Pathogen and Host Database Resources

More...EuPathDBi		HostDB:ENSG00000012779.10

Human Gene Nomenclature Database

More...HGNCi		HGNC:435, ALOX5

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		152390, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P09917

<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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Membrane, Nucleus

<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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi14W → A: Impairs interaction with DICER1; when associated with A-76 and A-103. 1 Publication1
Mutagenesisi76W → A: Impairs interaction with DICER1; when associated with A-14 and A-103. 1 Publication1
Mutagenesisi103W → A: Abolishes binding to COTL1. Impairs interaction with DICER; when associated with A-14 and A-76. 2 Publications1
Mutagenesisi272S → A: Loss of phosphorylation site. Permits export from the nucleus. 1 Publication1
Mutagenesisi359D → N: No loss of activity. 1
Mutagenesisi360F → W: Loss of (5S)-lipoxygenase activity; when associated with I-425 and M-426. Loss of (5S)-lipoxygenase activity; when associated with I-425; M-426 and I-604. Exhibits a major (15S)-lipoxygenase activity; when associated with I-425 and M-426. Exhibits a major (15S)-lipoxygenase activity; when associated with I-425; M-426 and I-604. Does not catalyze oxygenation of arachodonic acid to 5-HETE; when associated with I-425: M-426 and I-604. Catalyzes oxygenation of arachodonic acid to form mostly (15S)-HETE and (8S)-HETE but also 12-HETE; when associated with I-425: M-426 and I-604. Abolishes the LTA4-synthase activity; when associated with I-425: M-426 and I-604. Catalyzes oxygenation of linoleic acid to (13S)- and (9S)-HODE; when associated with I-425: M-426 and I-604. Catalyzes oxygenation of (11S)- and (11R)-deutero-linoleic acid to 9-HODE and (13S)-HODE respectively; when associated with I-425: M-426 and I-604. Catalyzes oxygenation of alpha-linolenic acid (ALA) to 13-HOTrE(n-3); when associated with I-425: M-426 and I-604. Catalyzes oxygenation of gamma-linolenic acid (GLA) to 13-HOTrE(n-6) and 10-HOTrE; when associated with I-425: M-426 and I-604. Catalyzes the oxygenation of eicosapentaenoic acid (EPA) to 12- and 15-HEPA; when associated with I-425: M-426 and I-604. Catalyzes the oxygenation of docosahexaenoic acid (DHA) to 10- and 17-HDHA; when associated with I-425: M-426 and I-604. Exhibits a lipoxin synthase activity towards (5S)-HETE as major substrates followed by (5S),(15S)-DiHETE and (15S)-HETE; when associated with I-425: M-426 and I-604. 2 Publications1
Mutagenesisi363H → S or N: Still some substantial activity. 1 Publication1
Mutagenesisi368H → S, N or A: No activity. 2 Publications1
Mutagenesisi373H → S or N: No activity. 2 Publications1
Mutagenesisi377E → Q: No activity. 1 Publication1
Mutagenesisi391H → A: No activity. 2 Publications1
Mutagenesisi391H → S or N: Still some substantial activity. 2 Publications1
Mutagenesisi400H → A: No activity. 2 Publications1
Mutagenesisi400H → S or N: Still some substantial activity. 2 Publications1
Mutagenesisi425A → I: Loss of (5S)-lipoxygenase activity; when associated with W-360 and M-426. Loss of (5S)-lipoxygenase activity; when associated with W-360; M-426 and I-604. Exhibits a major (15S)-lipoxygenase activity; when associated with W-360 and M-426. Exhibits a major (15S)-lipoxygenase activity; when associated with W-360; M-426 and I-604. Does not catalyze oxygenation of arachodonic acid to 5-HETE; when associated with W-360; M-426 and I-604. Catalyzes oxygenation of arachodonic acid to form in majority (15S)-HETE and (8S)-HETE but also 12-HETE; when associated with W-360; M-426 and I-604. Abolishes the LTA4-synthase activity; when associated with W-360; M-426 and I-604. Catalyzes oxygenation of linoleic acid to (13S)- and (9S)-HODE; when associated with W-360; M-426 and I-604. Catalyzes oxygenation of (11S)- and (11R)-deutero-linoleic acid to 9-HODE and (13S)-HODE respectively; when associated with W-360; M-426 and I-604. Catalyzes oxygenation of alpha-linolenic acid (ALA) to 13-HOTrE(n-3); when associated with W-360; M-426 and I-604. Catalyzes oxygenation of gamma-linolenic acid (GLA) to 13-HOTrE(n-6) and 10-HOTrE; when associated with W-360; M-426 and I-604. Catalyzes the oxygenation of eicosapentaenoic acid (EPA) to 12- and 15-HEPA; when associated with W-360; M-426 and I-604. Catalyzes the oxygenation of docosahexaenoic acid (DHA) to 10- and 17-HDHA; when associated with W-360; M-426 and I-604. Exhibits a lipoxin synthase activity towards (5S)-HETE as major substrates followed by (5S),(15S)-DiHETE and (15S)-HETE; when associated with W-360; M-426 and I-604. 2 Publications1
Mutagenesisi426N → M: Loss of (5S)-lipoxygenase activity; when associated with W-360 and I-425. Loss of (5S)-lipoxygenase activity; when associated with W-360; I-425 and I-604. Exhibits a major (15S)-lipoxygenase activity; when associated with W-360 and I-425. Exhibits a major (15S)-lipoxygenase activity; when associated with W-360; I-425 and I-604. Does not catalyze oxygenation of arachodonic acid to 5-HETE; when associated with W-360; I-425 and I-604. Catalyzes oxygenation of arachodonic acid to form in majority (15S)-HETE and (8S)-HETE but also 12-HETE; when associated with W-360; I-425 and I-604. Abolishes the LTA4-synthase activity; when associated with W-360; I-425 and I-604. Catalyzes oxygenation of linoleic acid to (13S)- and (9S)-HODE; when associated with W-360; I-425 and I-604. Catalyzes oxygenation of (11S)- and (11R)-deutero-linoleic acid to 9-HODE and (13S)-HODE respectively; when associated with W-360; I-425 and I-604. Catalyzes oxygenation of alpha-linolenic acid (ALA) to 13-HOTrE(n-3); when associated with W-360; I-425 and I-604. Catalyzes oxygenation of gamma-linolenic acid (GLA) to 13-HOTrE(n-6) and 10-HOTrE; when associated with W-360; I-425 and I-604. Catalyzes the oxygenation of eicosapentaenoic acid (EPA) to 12- and 15-HEPA; when associated with W-360; I-425 and I-604. Catalyzes the oxygenation of docosahexaenoic acid (DHA) to 10- and 17-HDHA; when associated with W-360; I-425 and I-604. Exhibits a lipoxin synthase activity towards (5S)-HETE as major substrates followed by (5S),(15S)-DiHETE and (15S)-HETE; when associated with W-360; I-425 and I-604. 2 Publications1
Mutagenesisi433H → N or A: Almost no loss of activity. 1
Mutagenesisi524S → A: Prevents phosphorylation by PKA. 1 Publication1
Mutagenesisi551H → N or A: No activity. 1 Publication1
Mutagenesisi604A → I: Loss of (5S)-lipoxygenase activity. Loss of (5S)-lipoxygenase activity; when associated with W-360; I-425 and M-426. Exhibits a major (15S)-lipoxygenase activity;when associated with W-360; I-425 and M-426. Does not catalyze oxygenation of arachodonic acid to 5-HETE; when associated with W-360; I-425 and M-426. Catalyzes oxygenation of arachodonic acid to form in majority (15S)-HETE and (8S)-HETE but also 12-HETE; when associated with W-360; I-425 and M-426. Abolishes the LTA4-synthase activity; when associated with W-360; I-425 and M-426. Catalyzes oxygenation of linoleic acid to (13S)- and (9 S)-HODE; when associated with W-360; I-425 and M-426. Catalyzes oxygenation of (11S)- and (11R)-deutero-linoleic acid to 9-HODE and (13S)-HODE respectively; when associated with W-360; I-425 and M-426. Catalyzes oxygenation of alpha-linolenic acid (ALA) to 13-HOTrE(n-3); when associated with W-360; I-425 and M-426. Catalyzes oxygenation of gamma-linolenic acid (GLA) to 13-HOTrE(n-6) and 10-HOTrE; when associated with W-360; I-425 and M-426. Catalyzes the oxygenation of eicosapentaenoic acid (EPA) to 12- and 15-HEPA; when associated with W-360; I-425 and M-426. Catalyzes the oxygenation of docosahexaenoic acid (DHA) to 10- and 17-HDHA; when associated with W-360; I-425 and M-426. Exhibits a lipoxin synthase activity towards (5S)-HETE as major substrates followed by (5S),(15S)-DiHETE and (15S)-HETE; when associated with W-360; I-425 and M-426. 2 Publications1
Mutagenesisi664S → A: Does not affect arachidonate 5-lipoxygenase activity. Does not oxygenate arachidonate typical 15-lipoxygenase substrates such as dihomo-gamma-linolenic acid and N-arachidonyl glycine. 1 Publication1
Mutagenesisi664S → D: Enhances affinity for arachidonic acid. Impairs arachidonate 5-lipoxygenase activity. Induces arachidonate 15-lipoxygenase activity. Oxygenates typical arachidonate 15-lipoxygenase substrates such as dihomo-gamma-linolenic acid and N-arachidonyl glycine. Synthesizes lipoxin A4 when incubated with a stable 5-lipoxygenase. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		240

MalaCards human disease database

More...MalaCardsi		ALOX5

Open Targets

More...OpenTargetsi		ENSG00000012779

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA46

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		P09917, Tclin

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL215

Drug and drug target database

More...DrugBanki		DB14001, alpha-Tocopherol succinate
DB00233, Aminosalicylic acid
DB01014, Balsalazide
DB09061, Cannabidiol
DB14002, D-alpha-Tocopherol acetate
DB11994, Diacerein
DB00586, Diclofenac
DB00711, Diethylcarbamazine
DB12010, Fostamatinib
DB01892, Hyperforin
DB04725, Licofelone
DB00179, Masoprocol
DB00939, Meclofenamic acid
DB14009, Medical Cannabis
DB00244, Mesalazine
DB01017, Minocycline
DB05431, MLN-977
DB00471, Montelukast
DB09285, Morniflumate
DB14011, Nabiximols
DB11133, Omega-3 fatty acids
DB13168, Omega-6 fatty acids
DB02709, Resveratrol
DB13174, Rhein
DB00795, Sulfasalazine
DB00163, Vitamin E
DB00744, Zileuton

DrugCentral

More...DrugCentrali		P09917

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		1385

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		ALOX5

Domain mapping of disease mutations (DMDM)

More...DMDMi		126407

<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 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002206931 – 674Polyunsaturated fatty acid 5-lipoxygenaseAdd BLAST674

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 residuei272Phosphoserine; by MAPKAPK22 Publications1
Modified residuei524Phosphoserine; by PKA2 Publications1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

Serine phosphorylation by MAPKAPK2 is stimulated by arachidonic acid (PubMed:11844797, PubMed:18978352). Phosphorylation on Ser-524 by PKA has an inhibitory effect (PubMed:15280375). Phosphorylation on Ser-272 prevents export from the nucleus (PubMed:11844797, PubMed:18978352). Phosphorylation at Ser-524 is stimulated by 8-bromo-3',5'-cyclic AMP or prostaglandin E2 (PubMed:26210919).4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P09917

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		P09917

MaxQB - The MaxQuant DataBase

More...MaxQBi		P09917

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

More...PaxDbi		P09917

PeptideAtlas

More...PeptideAtlasi		P09917

PRoteomics IDEntifications database

More...PRIDEi		P09917

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		52278 [P09917-1]
7233

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P09917

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

More...PhosphoSitePlusi		P09917

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000012779, Expressed in blood and 222 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P09917, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P09917, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000012779, Tissue enhanced (blood, bone marrow, lymphoid tissue)

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer (PubMed:22516296, PubMed:21233389).

Interacts with ALOX5AP and LTC4S (PubMed:19233132).

Interacts with COTL1, the interaction is required for stability and efficient catalytic activity (PubMed:19807693).

Interacts with PIK3R1; this interaction bridges ALOX5 with CD40 after CD40 ligation in B cells and leads to the production of reactive oxygen species (ROS) (PubMed:21200133).

Interacts (via PLAT domain) with DICER1 (via Dicer dsRNA-binding fold domain); this interaction enhances arachidonate 5-lipoxygenase activity and modifies the miRNA precursor processing activity of DICER1 (PubMed:19022417).

6 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		106741, 71 interactors

Database of interacting proteins

More...DIPi		DIP-30950N

Protein interaction database and analysis system

More...IntActi		P09917, 64 interactors

Molecular INTeraction database

More...MINTi		P09917

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000363512

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P09917

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P09917, protein

<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

1674
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...SMRi		P09917

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P09917

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini2 – 118PLATPROSITE-ProRule annotationAdd BLAST117
Domaini119 – 674LipoxygenasePROSITE-ProRule annotationAdd BLAST556

<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 lipoxygenase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG502QQSP, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000156111

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_004282_3_3_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P09917

Identification of Orthologs from Complete Genome Data

More...OMAi		FPDMIKS

Database of Orthologous Groups

More...OrthoDBi		385042at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P09917

TreeFam database of animal gene trees

More...TreeFami		TF105320

Family and domain databases

Conserved Domains Database

More...CDDi		cd01753, PLAT_LOX, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR000907, LipOase
IPR013819, LipOase_C
IPR036226, LipOase_C_sf
IPR020834, LipOase_CS
IPR020833, LipOase_Fe_BS
IPR001885, LipOase_mml
IPR001024, PLAT/LH2_dom
IPR036392, PLAT/LH2_dom_sf
IPR042062, PLAT_LOX_verte

The PANTHER Classification System

More...PANTHERi		PTHR11771, PTHR11771, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00305, Lipoxygenase, 1 hit
PF01477, PLAT, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00087, LIPOXYGENASE
PR00467, MAMLPOXGNASE

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00308, LH2, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF48484, SSF48484, 1 hit
SSF49723, SSF49723, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00711, LIPOXYGENASE_1, 1 hit
PS00081, LIPOXYGENASE_2, 1 hit
PS51393, LIPOXYGENASE_3, 1 hit
PS50095, PLAT, 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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (5+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

This entry describes 5 <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. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Note: Additional isoforms seem to exist.

This entry has 5 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 1 (identifier: P09917-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
MPSYTVTVAT GSQWFAGTDD YIYLSLVGSA GCSEKHLLDK PFYNDFERGA 
        60         70         80         90        100
VDSYDVTVDE ELGEIQLVRI EKRKYWLNDD WYLKYITLKT PHGDYIEFPC 
       110        120        130        140        150
YRWITGDVEV VLRDGRAKLA RDDQIHILKQ HRRKELETRQ KQYRWMEWNP 
       160        170        180        190        200
GFPLSIDAKC HKDLPRDIQF DSEKGVDFVL NYSKAMENLF INRFMHMFQS 
       210        220        230        240        250
SWNDFADFEK IFVKISNTIS ERVMNHWQED LMFGYQFLNG CNPVLIRRCT 
       260        270        280        290        300
ELPEKLPVTT EMVECSLERQ LSLEQEVQQG NIFIVDFELL DGIDANKTDP 
       310        320        330        340        350
CTLQFLAAPI CLLYKNLANK IVPIAIQLNQ IPGDENPIFL PSDAKYDWLL 
       360        370        380        390        400
AKIWVRSSDF HVHQTITHLL RTHLVSEVFG IAMYRQLPAV HPIFKLLVAH 
       410        420        430        440        450
VRFTIAINTK AREQLICECG LFDKANATGG GGHVQMVQRA MKDLTYASLC 
       460        470        480        490        500
FPEAIKARGM ESKEDIPYYF YRDDGLLVWE AIRTFTAEVV DIYYEGDQVV 
       510        520        530        540        550
EEDPELQDFV NDVYVYGMRG RKSSGFPKSV KSREQLSEYL TVVIFTASAQ 
       560        570        580        590        600
HAAVNFGQYD WCSWIPNAPP TMRAPPPTAK GVVTIEQIVD TLPDRGRSCW 
       610        620        630        640        650
HLGAVWALSQ FQENELFLGM YPEEHFIEKP VKEAMARFRK NLEAIVSVIA 
       660        670 
ERNKKKQLPY YYLSPDRIPN SVAI
Length:674
Mass (Da):77,983
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:i36F38C0A9E86BB21
GO
Isoform 2 (identifier: P09917-2) [UniParc]FASTAAdd to basket
Also known as: Delta-13

The sequence of this isoform differs from the canonical sequence as follows:
     559-615: Missing.

Show »
Length:617
Mass (Da):71,564
Checksum:i3DE1D2FE62471315
GO
Isoform 3 (identifier: P09917-3) [UniParc]FASTAAdd to basket
Also known as: delta-p10

The sequence of this isoform differs from the canonical sequence as follows:
     424-455: Missing.

Show »
Length:642
Mass (Da):74,635
Checksum:iE9A8CCA67CF74DB6
GO
Isoform 4 (identifier: P09917-4) [UniParc]FASTAAdd to basket
Also known as: delta-10-13

The sequence of this isoform differs from the canonical sequence as follows:
     425-533: ANATGGGGHV...SGFPKSVKSR → VHGRGGRHLL...EPRGHCQRDC
     534-674: Missing.

Show »
Length:533
Mass (Da):61,244
Checksum:i6C57FD0816BD2D9E
GO
Isoform 5 (identifier: P09917-5) [UniParc]FASTAAdd to basket
Also known as: alpha-10

The sequence of this isoform differs from the canonical sequence as follows:
     485-674: Missing.

Show »
Length:484
Mass (Da):56,291
Checksum:i4A500F8D7404EC9D
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
A0A087X109A0A087X109_HUMAN
Polyunsaturated fatty acid 5-lipoxy...
ALOX5
139Annotation 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>

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_028018254E → K Decreases arachidonate 5-lipoxygenase activity. Increases leukotriene A4 synthase activity. 2 PublicationsCorresponds to variant dbSNP:rs2228065Ensembl.1
Natural variantiVAR_083301337P → S Decreases arachidonate 5-lipoxygenase activity. 1 Publication1
Natural variantiVAR_083302447A → S Increases arachidonate 5-lipoxygenase activity. 1 Publication1
Natural variantiVAR_083303549A → V Decreases arachidonate 5-lipoxygenase activity. 1 Publication1
Natural variantiVAR_083304577P → L Does not affect arachidonate 5-lipoxygenase activity. 1 Publication1
Natural variantiVAR_083305591T → M Increases arachidonate 5-lipoxygenase activity. Does not affect leukotriene A4 synthase activity. 1 Publication1
Natural variantiVAR_083306656K → Q Increases arachidonate 5-lipoxygenase activity. 1 Publication1

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.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_053534424 – 455Missing in isoform 3. 1 PublicationAdd BLAST32
Alternative sequenceiVSP_053535425 – 533ANATG…SVKSR → VHGRGGRHLLRGRPGGGGGP GAAGLRERCLRVRHAGPQVL RLPQVGQEPGAAVGVPDRGD LHRLRPARRGQLRPAVPGHV PRRAFYREACEGSHGPIPQE PRGHCQRDC in isoform 4. 1 PublicationAdd BLAST109
Alternative sequenceiVSP_053536485 – 674Missing in isoform 5. 1 PublicationAdd BLAST190
Alternative sequenceiVSP_053537534 – 674Missing in isoform 4. 1 PublicationAdd BLAST141
Alternative sequenceiVSP_046998559 – 615Missing in isoform 2. 2 PublicationsAdd BLAST57

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
J03600 mRNA Translation: AAA36183.1
J03571 mRNA Translation: AAA65450.1
HM592258 mRNA Translation: ADR30798.1
HM592259 mRNA Translation: ADR30799.1
HM592260 mRNA Translation: ADR30800.1
HM592261 mRNA Translation: ADR30801.1
J04520 Genomic DNA Translation: AAA59522.1
AL731567 Genomic DNA No translation available.
BC130332 mRNA Translation: AAI30333.1
BC132677 mRNA Translation: AAI32678.1
BC143985 mRNA Translation: AAI43986.1
M38191 Genomic DNA Translation: AAA63212.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS58078.1 [P09917-2]
CCDS7212.1 [P09917-1]

Protein sequence database of the Protein Information Resource

More...PIRi		A28117, DAHUAL

NCBI Reference Sequences

More...RefSeqi		NP_000689.1, NM_000698.4 [P09917-1]
NP_001243082.1, NM_001256153.2 [P09917-3]
NP_001243083.1, NM_001256154.2 [P09917-2]
NP_001307790.1, NM_001320861.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000374391; ENSP00000363512; ENSG00000012779 [P09917-1]
ENST00000542434; ENSP00000437634; ENSG00000012779 [P09917-2]
ENST00000610656; ENSP00000484468; ENSG00000275565 [P09917-1]
ENST00000622021; ENSP00000479958; ENSG00000275565 [P09917-2]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		240

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:240

UCSC genome browser

More...UCSCi		uc001jce.5, human [P09917-1]

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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03600 mRNA Translation: AAA36183.1
J03571 mRNA Translation: AAA65450.1
HM592258 mRNA Translation: ADR30798.1
HM592259 mRNA Translation: ADR30799.1
HM592260 mRNA Translation: ADR30800.1
HM592261 mRNA Translation: ADR30801.1
J04520 Genomic DNA Translation: AAA59522.1
AL731567 Genomic DNA No translation available.
BC130332 mRNA Translation: AAI30333.1
BC132677 mRNA Translation: AAI32678.1
BC143985 mRNA Translation: AAI43986.1
M38191 Genomic DNA Translation: AAA63212.1
CCDSiCCDS58078.1 [P09917-2]
CCDS7212.1 [P09917-1]
PIRiA28117, DAHUAL
RefSeqiNP_000689.1, NM_000698.4 [P09917-1]
NP_001243082.1, NM_001256153.2 [P09917-3]
NP_001243083.1, NM_001256154.2 [P09917-2]
NP_001307790.1, NM_001320861.1

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
2ABVmodel-A2-674[»]
3O8YX-ray2.39A/B1-674[»]
3V92X-ray2.74A/B1-674[»]
3V98X-ray2.07A/B1-674[»]
3V99X-ray2.25A/B1-674[»]
6N2WX-ray2.71A/B1-674[»]
6NCFX-ray2.87A/B/C/D1-674[»]
SMRiP09917
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi106741, 71 interactors
DIPiDIP-30950N
IntActiP09917, 64 interactors
MINTiP09917
STRINGi9606.ENSP00000363512

Chemistry databases

BindingDBiP09917
ChEMBLiCHEMBL215
DrugBankiDB14001, alpha-Tocopherol succinate
DB00233, Aminosalicylic acid
DB01014, Balsalazide
DB09061, Cannabidiol
DB14002, D-alpha-Tocopherol acetate
DB11994, Diacerein
DB00586, Diclofenac
DB00711, Diethylcarbamazine
DB12010, Fostamatinib
DB01892, Hyperforin
DB04725, Licofelone
DB00179, Masoprocol
DB00939, Meclofenamic acid
DB14009, Medical Cannabis
DB00244, Mesalazine
DB01017, Minocycline
DB05431, MLN-977
DB00471, Montelukast
DB09285, Morniflumate
DB14011, Nabiximols
DB11133, Omega-3 fatty acids
DB13168, Omega-6 fatty acids
DB02709, Resveratrol
DB13174, Rhein
DB00795, Sulfasalazine
DB00163, Vitamin E
DB00744, Zileuton
DrugCentraliP09917
GuidetoPHARMACOLOGYi1385
SwissLipidsiSLP:000000669

PTM databases

iPTMnetiP09917
PhosphoSitePlusiP09917

Polymorphism and mutation databases

BioMutaiALOX5
DMDMi126407

Proteomic databases

jPOSTiP09917
MassIVEiP09917
MaxQBiP09917
PaxDbiP09917
PeptideAtlasiP09917
PRIDEiP09917
ProteomicsDBi52278 [P09917-1]
7233

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		3906, 749 antibodies

The DNASU plasmid repository

More...DNASUi		240

Genome annotation databases

EnsembliENST00000374391; ENSP00000363512; ENSG00000012779 [P09917-1]
ENST00000542434; ENSP00000437634; ENSG00000012779 [P09917-2]
ENST00000610656; ENSP00000484468; ENSG00000275565 [P09917-1]
ENST00000622021; ENSP00000479958; ENSG00000275565 [P09917-2]
GeneIDi240
KEGGihsa:240
UCSCiuc001jce.5, human [P09917-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		240
DisGeNETi240
EuPathDBiHostDB:ENSG00000012779.10

GeneCards: human genes, protein and diseases

More...GeneCardsi		ALOX5
HGNCiHGNC:435, ALOX5
HPAiENSG00000012779, Tissue enhanced (blood, bone marrow, lymphoid tissue)
MalaCardsiALOX5
MIMi152390, gene
neXtProtiNX_P09917
OpenTargetsiENSG00000012779
PharmGKBiPA46

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiENOG502QQSP, Eukaryota
GeneTreeiENSGT00940000156111
HOGENOMiCLU_004282_3_3_1
InParanoidiP09917
OMAiFPDMIKS
OrthoDBi385042at2759
PhylomeDBiP09917
TreeFamiTF105320

Enzyme and pathway databases

UniPathwayiUPA00877
BioCyciMetaCyc:HS00336-MONOMER
BRENDAi1.13.11.34, 2681
PathwayCommonsiP09917
ReactomeiR-HSA-2142688, Synthesis of 5-eicosatetraenoic acids
R-HSA-2142691, Synthesis of Leukotrienes (LT) and Eoxins (EX)
R-HSA-2142700, Synthesis of Lipoxins (LX)
R-HSA-6785807, Interleukin-4 and Interleukin-13 signaling
R-HSA-6798695, Neutrophil degranulation
R-HSA-9012546, Interleukin-18 signaling
R-HSA-9018676, Biosynthesis of D-series resolvins
R-HSA-9018682, Biosynthesis of maresins
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
R-HSA-9026286, Biosynthesis of DPAn-3-derived protectins and resolvins
R-HSA-9026290, Biosynthesis of DPAn-3-derived maresins
R-HSA-9026403, Biosynthesis of DPAn-3-derived 13-series resolvins
R-HSA-9027604, Biosynthesis of electrophilic Omega-3 PUFA oxo-derivatives
SABIO-RKiP09917
SIGNORiP09917

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		240, 19 hits in 848 CRISPR screens

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

More...ChiTaRSi		ALOX5, human
EvolutionaryTraceiP09917

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		Arachidonate_5-lipoxygenase

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

More...GenomeRNAii		240
PharosiP09917, Tclin

Protein Ontology

More...PROi		PR:P09917
RNActiP09917, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000012779, Expressed in blood and 222 other tissues
ExpressionAtlasiP09917, baseline and differential
GenevisibleiP09917, HS

Family and domain databases

CDDicd01753, PLAT_LOX, 1 hit
InterProiView protein in InterPro
IPR000907, LipOase
IPR013819, LipOase_C
IPR036226, LipOase_C_sf
IPR020834, LipOase_CS
IPR020833, LipOase_Fe_BS
IPR001885, LipOase_mml
IPR001024, PLAT/LH2_dom
IPR036392, PLAT/LH2_dom_sf
IPR042062, PLAT_LOX_verte
PANTHERiPTHR11771, PTHR11771, 1 hit
PfamiView protein in Pfam
PF00305, Lipoxygenase, 1 hit
PF01477, PLAT, 1 hit
PRINTSiPR00087, LIPOXYGENASE
PR00467, MAMLPOXGNASE
SMARTiView protein in SMART
SM00308, LH2, 1 hit
SUPFAMiSSF48484, SSF48484, 1 hit
SSF49723, SSF49723, 1 hit
PROSITEiView protein in PROSITE
PS00711, LIPOXYGENASE_1, 1 hit
PS00081, LIPOXYGENASE_2, 1 hit
PS51393, LIPOXYGENASE_3, 1 hit
PS50095, PLAT, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		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 nameiLOX5_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: P09917
Secondary accession number(s): B7ZLS0
, E5FPY5, E5FPY7, E5FPY8, Q5JQ14
<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%5Fand%5Fisoforms">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 2, 2020
This is version 213 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, Direct protein sequencing, Reference proteome

Documents

  1. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families
  6. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  7. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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