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Entry version 200 (13 Feb 2019)
Sequence version 4 (06 Feb 2007)
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Protein

Arachidonate 12-lipoxygenase, 12S-type

Gene

ALOX12

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

Non-heme iron-containing dioxygenase that catalyzes the stereo-specific peroxidation of free and esterified polyunsaturated fatty acids generating a spectrum of bioactive lipid mediators. Mainly converts arachidonic acid to (12S)-hydroperoxyeicosatetraenoic acid/(12S)-HPETE but can also metabolize linoleic acid. Has a dual activity since it also converts leukotriene A4/LTA4 into both the bioactive lipoxin A4/LXA4 and lipoxin B4/LXB4. Through the production of specific bioactive lipids like (12S)-HPETE it regulates different biological processes including platelet activation. It also probably positively regulates angiogenesis through regulation of the expression of the vascular endothelial growth factor. Plays a role in apoptotic process, promoting the survival of vascular smooth muscle cells for instance. May also play a role in the control of cell migration and proliferation.5 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

Fe cationNote: Binds 1 Fe cation per subunit.

<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

Activated by EGF.1 Publication

<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=8 µM for arachidonate (at pH 7.0 and 37 degrees Celsius)1 Publication
  2. KM=10 µM for arachidonate (at pH 8.0 and 25 degrees Celsius)1 Publication
  3. KM=6.2 µM for arachidonate (at pH 7.4)1 Publication
  4. KM=9 µM for linoleate (at pH 8.0 and 25 degrees Celsius)1 Publication
  5. KM=7.9 µM for leukotriene A4 (at pH 7.4)1 Publication
  6. KM=3 µM for eicosa-5,8,11,14,17-pentaenoate (at pH 7.0 and 37 degrees Celsius)1 Publication
  7. KM=35 µM for eicosa-8,11,14-trienoate (at pH 7.0 and 37 degrees Celsius)1 Publication
  8. KM=14.3 µM for 5,6-epoxy-8,11,14-eicosatrienoate (at pH 7.4)1 Publication
  1. Vmax=3 µmol/min/mg enzyme with arachidonate as substrate (at pH 8.0 and 25 degrees Celsius)1 Publication
  2. Vmax=1.057 µmol/min/mg enzyme with arachidonate as substrate (at pH 7.4)1 Publication
  3. Vmax=0.0375 µmol/min/mg enzyme with linoleate as substrate (at pH 8.0 and 25 degrees Celsius)1 Publication
  4. Vmax=0.025 µmol/min/mg enzyme with leukotriene A4 as substrate (at pH 7.4)1 Publication
  5. Vmax=0.985 µmol/min/mg enzyme with 5,6-epoxy-8,11,14-eicosatrienoate as substrate (at pH 7.4)1 Publication

pH dependencei

Optimum pH is 7.5-8.0 (for arachidonate 12-lipoxygenase activity).2 Publications

<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: hydroperoxy eicosatetraenoic acid biosynthesis

This protein is involved in the pathway hydroperoxy eicosatetraenoic acid biosynthesis, which is part of Lipid metabolism.1 Publication
View all proteins of this organism that are known to be involved in the pathway hydroperoxy eicosatetraenoic acid 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 bindingi360Iron; catalytic1
Metal bindingi365Iron; catalytic1
Metal bindingi540Iron; catalytic1
Metal bindingi544Iron; catalyticPROSITE-ProRule annotation1
Metal bindingi663Iron; via carboxylate; catalyticPROSITE-ProRule annotation1

<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

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 functionDioxygenase, Hydrolase, Oxidoreductase
Biological processFatty acid metabolism, Lipid metabolism
LigandIron, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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BioCyci
MetaCyc:HS03167-MONOMER

BRENDA Comprehensive Enzyme Information System

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BRENDAi
1.13.11.31 2681

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-2142696 Synthesis of Hepoxilins (HX) and Trioxilins (TrX)
R-HSA-2142700 Synthesis of Lipoxins (LX)
R-HSA-2142712 Synthesis of 12-eicosatetraenoic acid derivatives
R-HSA-9018677 Biosynthesis of DHA-derived SPMs
R-HSA-9025106 Biosynthesis of DPAn-6 SPMs
R-HSA-9026290 Biosynthesis of DPAn-3-derived maresins

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P18054

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

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UniPathwayi
UPA00881

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...
SwissLipidsi
SLP:000000670

<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:
Arachidonate 12-lipoxygenase, 12S-type (EC:1.13.11.31)
Short name:
12S-LOX
Short name:
12S-lipoxygenase
Alternative name(s):
Lipoxin synthase 12-LO (EC:3.3.2.-)
Platelet-type lipoxygenase 12
<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:ALOX12
Synonyms:12LO, LOG12
<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 17

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000108839.11

Human Gene Nomenclature Database

More...
HGNCi
HGNC:429 ALOX12

Online Mendelian Inheritance in Man (OMIM)

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MIMi
152391 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P18054

<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

<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

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Esophageal cancer (ESCR)1 Publication
Disease susceptibility may be associated with variations affecting the gene represented in this entry. Gln at position 261 may confer interindividual susceptibility to esophageal cancer (PubMed:17460548).1 Publication
Disease descriptionA malignancy of the esophagus. The most common types are esophageal squamous cell carcinoma and adenocarcinoma. Cancer of the esophagus remains a devastating disease because it is usually not detected until it has progressed to an advanced incurable stage.
See also OMIM:133239
Colorectal cancer (CRC)1 Publication
Disease susceptibility may be associated with variations affecting the gene represented in this entry. Gln at position 261 may confer interindividual susceptibility to colorectal cancer (PubMed:17460548).1 Publication
Disease descriptionA complex disease characterized by malignant lesions arising from the inner wall of the large intestine (the colon) and the rectum. Genetic alterations are often associated with progression from premalignant lesion (adenoma) to invasive adenocarcinoma. Risk factors for cancer of the colon and rectum include colon polyps, long-standing ulcerative colitis, and genetic family history.
See also OMIM:114500

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>Mutagenesisi355H → Q: No effect on catalytic activity. 1 Publication1
Mutagenesisi360H → Q or Y: Complete loss of catalytic activity. 1 Publication1
Mutagenesisi365H → Q: Complete loss of catalytic activity. 1 Publication1
Mutagenesisi383H → Q: Altered catalytic activity and protein expression. 1 Publication1
Mutagenesisi392H → Q: No effect on catalytic activity. 1 Publication1
Mutagenesisi416K → Q: Reduced catalytic activity. No effect on the stereoselectivity of the oxygenation reaction. 1 Publication1
Mutagenesisi417A → I: Reduced catalytic activity. Alters the stereoselectivity of the oxygenation reaction. 1 Publication1
Mutagenesisi418V → M: No effect on catalytic activity. No effect on the stereoselectivity of the oxygenation reaction. 1 Publication1
Mutagenesisi540H → Q: Complete loss of catalytic activity. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
239
MIMi114500 phenotype
133239 phenotype

Open Targets

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OpenTargetsi
ENSG00000108839

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA45

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL3687

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
1387

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
ALOX12

Domain mapping of disease mutations (DMDM)

More...
DMDMi
125987838

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002206821 – 663Arachidonate 12-lipoxygenase, 12S-typeAdd BLAST663

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 residuei246PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P18054

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

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PaxDbi
P18054

PeptideAtlas

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PeptideAtlasi
P18054

PRoteomics IDEntifications database

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PRIDEi
P18054

ProteomicsDB human proteome resource

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ProteomicsDBi
53540

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P18054

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

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PhosphoSitePlusi
P18054

<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

Expressed in vascular smooth muscle cells.1 Publication

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Down-regulated upon starvation, by UV-irradiation and 15-lipoxygenase metabolites.2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000108839 Expressed in 122 organ(s), highest expression level in ectocervix

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P18054 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P18054 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB019287
HPA010691

<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%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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
106740, 8 interactors

Protein interaction database and analysis system

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IntActi
P18054, 4 interactors

Molecular INTeraction database

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MINTi
P18054

STRING: functional protein association networks

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STRINGi
9606.ENSP00000251535

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P18054

<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

1663
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2ABUmodel-A2-663[»]
3D3LX-ray2.60A/B172-663[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P18054

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

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SMRi
P18054

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
P18054

<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_and_domains_section">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 – 114PLATPROSITE-ProRule annotationAdd BLAST113
Domaini115 – 663LipoxygenasePROSITE-ProRule annotationAdd BLAST549

<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

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eggNOGi
ENOG410IF0U Eukaryota
ENOG410YN4N LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000155191

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000234358

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG005150

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P18054

KEGG Orthology (KO)

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KOi
K00458

Identification of Orthologs from Complete Genome Data

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OMAi
MTITWHL

Database of Orthologous Groups

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OrthoDBi
385042at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P18054

TreeFam database of animal gene trees

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TreeFami
TF105320

Family and domain databases

Integrated resource of protein families, domains and functional sites

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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

The PANTHER Classification System

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PANTHERi
PTHR11771 PTHR11771, 1 hit

Pfam protein domain database

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

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00087 LIPOXYGENASE
PR00467 MAMLPOXGNASE

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00308 LH2, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF48484 SSF48484, 1 hit
SSF49723 SSF49723, 1 hit

PROSITE; a protein domain and family database

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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_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>Sequence (1+)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.

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

P18054-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGRYRIRVAT GAWLFSGSYN RVQLWLVGTR GEAELELQLR PARGEEEEFD
60 70 80 90 100
HDVAEDLGLL QFVRLRKHHW LVDDAWFCDR ITVQGPGACA EVAFPCYRWV
110 120 130 140 150
QGEDILSLPE GTARLPGDNA LDMFQKHREK ELKDRQQIYC WATWKEGLPL
160 170 180 190 200
TIAADRKDDL PPNMRFHEEK RLDFEWTLKA GALEMALKRV YTLLSSWNCL
210 220 230 240 250
EDFDQIFWGQ KSALAEKVRQ CWQDDELFSY QFLNGANPML LRRSTSLPSR
260 270 280 290 300
LVLPSGMEEL QAQLEKELQN GSLFEADFIL LDGIPANVIR GEKQYLAAPL
310 320 330 340 350
VMLKMEPNGK LQPMVIQIQP PNPSSPTPTL FLPSDPPLAW LLAKSWVRNS
360 370 380 390 400
DFQLHEIQYH LLNTHLVAEV IAVATMRCLP GLHPIFKFLI PHIRYTMEIN
410 420 430 440 450
TRARTQLISD GGIFDKAVST GGGGHVQLLR RAAAQLTYCS LCPPDDLADR
460 470 480 490 500
GLLGLPGALY AHDALRLWEI IARYVEGIVH LFYQRDDIVK GDPELQAWCR
510 520 530 540 550
EITEVGLCQA QDRGFPVSFQ SQSQLCHFLT MCVFTCTAQH AAINQGQLDW
560 570 580 590 600
YAWVPNAPCT MRMPPPTTKE DVTMATVMGS LPDVRQACLQ MAISWHLSRR
610 620 630 640 650
QPDMVPLGHH KEKYFSGPKP KAVLNQFRTD LEKLEKEITA RNEQLDWPYE
660
YLKPSCIENS VTI
Length:663
Mass (Da):75,694
Last modified:February 6, 2007 - v4
<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:iC4D6D5B320666A77
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
K7ENN9K7ENN9_HUMAN
Arachidonate 12-lipoxygenase, 12S-t...
ALOX12
147Annotation 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 conflicti189 – 192RVYT → PCLH in AAA51533 (PubMed:2244907).Curated4
Sequence conflicti345S → C in AAA51533 (PubMed:2244907).Curated1
Sequence conflicti389L → P in AAA60056 (PubMed:2377602).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_030471259E → K. Corresponds to variant dbSNP:rs4987104Ensembl.1
Natural variantiVAR_018743261Q → R6 PublicationsCorresponds to variant dbSNP:rs1126667Ensembl.1
Natural variantiVAR_004279298A → T. 1
Natural variantiVAR_018744322N → S3 PublicationsCorresponds to variant dbSNP:rs434473Ensembl.1
Natural variantiVAR_018745430R → H1 PublicationCorresponds to variant dbSNP:rs11571342Ensembl.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
M62982 mRNA Translation: AAA51533.1
M35418 mRNA Translation: AAA60056.1
M58704 mRNA Translation: AAA59523.1
AY527817 Genomic DNA Translation: AAS00094.1
AC040977 Genomic DNA No translation available.
BC069557 mRNA Translation: AAH69557.1
D12638 Genomic DNA Translation: BAA02162.1
M87004 Genomic DNA Translation: AAA51587.1
S68587 mRNA Translation: AAD14020.1
AF143883 mRNA Translation: AAD32700.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS11084.1

Protein sequence database of the Protein Information Resource

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PIRi
A38283

NCBI Reference Sequences

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RefSeqi
NP_000688.2, NM_000697.2

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.654431

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000251535; ENSP00000251535; ENSG00000108839

Database of genes from NCBI RefSeq genomes

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GeneIDi
239

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:239

UCSC genome browser

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UCSCi
uc002gdx.4 human

Keywords - Coding sequence diversityi

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_references_section">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

SeattleSNPs
Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M62982 mRNA Translation: AAA51533.1
M35418 mRNA Translation: AAA60056.1
M58704 mRNA Translation: AAA59523.1
AY527817 Genomic DNA Translation: AAS00094.1
AC040977 Genomic DNA No translation available.
BC069557 mRNA Translation: AAH69557.1
D12638 Genomic DNA Translation: BAA02162.1
M87004 Genomic DNA Translation: AAA51587.1
S68587 mRNA Translation: AAD14020.1
AF143883 mRNA Translation: AAD32700.1
CCDSiCCDS11084.1
PIRiA38283
RefSeqiNP_000688.2, NM_000697.2
UniGeneiHs.654431

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2ABUmodel-A2-663[»]
3D3LX-ray2.60A/B172-663[»]
ProteinModelPortaliP18054
SMRiP18054
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106740, 8 interactors
IntActiP18054, 4 interactors
MINTiP18054
STRINGi9606.ENSP00000251535

Chemistry databases

BindingDBiP18054
ChEMBLiCHEMBL3687
GuidetoPHARMACOLOGYi1387
SwissLipidsiSLP:000000670

PTM databases

iPTMnetiP18054
PhosphoSitePlusiP18054

Polymorphism and mutation databases

BioMutaiALOX12
DMDMi125987838

Proteomic databases

jPOSTiP18054
PaxDbiP18054
PeptideAtlasiP18054
PRIDEiP18054
ProteomicsDBi53540

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000251535; ENSP00000251535; ENSG00000108839
GeneIDi239
KEGGihsa:239
UCSCiuc002gdx.4 human

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
239
DisGeNETi239
EuPathDBiHostDB:ENSG00000108839.11

GeneCards: human genes, protein and diseases

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GeneCardsi
ALOX12

H-Invitational Database, human transcriptome db

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H-InvDBi
HIX0039067
HGNCiHGNC:429 ALOX12
HPAiCAB019287
HPA010691
MIMi114500 phenotype
133239 phenotype
152391 gene
neXtProtiNX_P18054
OpenTargetsiENSG00000108839
PharmGKBiPA45

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiENOG410IF0U Eukaryota
ENOG410YN4N LUCA
GeneTreeiENSGT00940000155191
HOGENOMiHOG000234358
HOVERGENiHBG005150
InParanoidiP18054
KOiK00458
OMAiMTITWHL
OrthoDBi385042at2759
PhylomeDBiP18054
TreeFamiTF105320

Enzyme and pathway databases

UniPathwayi
UPA00881

BioCyciMetaCyc:HS03167-MONOMER
BRENDAi1.13.11.31 2681
ReactomeiR-HSA-2142696 Synthesis of Hepoxilins (HX) and Trioxilins (TrX)
R-HSA-2142700 Synthesis of Lipoxins (LX)
R-HSA-2142712 Synthesis of 12-eicosatetraenoic acid derivatives
R-HSA-9018677 Biosynthesis of DHA-derived SPMs
R-HSA-9025106 Biosynthesis of DPAn-6 SPMs
R-HSA-9026290 Biosynthesis of DPAn-3-derived maresins
SABIO-RKiP18054

Miscellaneous databases

EvolutionaryTraceiP18054

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
ALOX12

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

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GenomeRNAii
239

Protein Ontology

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PROi
PR:P18054

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000108839 Expressed in 122 organ(s), highest expression level in ectocervix
ExpressionAtlasiP18054 baseline and differential
GenevisibleiP18054 HS

Family and domain databases

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
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

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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 nameiLOX12_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: P18054
Secondary accession number(s): O95569, Q6ISF8, Q9UQM4
<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: November 1, 1990
Last sequence update: February 6, 2007
Last modified: February 13, 2019
This is version 200 of the entry and version 4 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, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  7. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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