Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - O15296 (LX15B_HUMAN)

Entry version 178 (13 Feb 2019)
Sequence version 3 (11 Jan 2011)
Previous versions | rss
Other tutorials and videosHelp videoFeedback
Protein

Arachidonate 15-lipoxygenase B

Gene

ALOX15B

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. Converts arachidonic acid to 15S-hydroperoxyeicosatetraenoic acid/(15S)-HPETE. Also acts on linoleic acid to produce 13-hydroxyoctadecadienoic acid/13-HPODE. Has no detectable 8S-lipoxygenase activity but reacts with (8S)-HPETE to produce (8S,15S)-diHPETE. May regulate progression through the cell cycle and cell proliferation. May also regulate cytokine secretion by macrophages and therefore play a role in the immune response. May also regulate macrophage differentiation into proatherogenic foam cells.7 Publications

Caution

Despite its homology with mouse Alox8 (AC O35936), it seems not to have any 8S-lipoxygenase activity on arachidonate.Curated

<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 cationPROSITE-ProRule annotation1 PublicationNote: Binds 1 Fe cation per subunit.PROSITE-ProRule annotation1 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=1100 µM for arachidonate (isoform D at pH 7.4 and 20 degrees Celsius)1 Publication
  2. KM=10 µM for linoleate (isoform A at pH 7.4 and 20 degrees Celsius)1 Publication
  3. KM=25 µM for arachidonate (isoform A at pH 7.4 and 20 degrees Celsius)1 Publication
  1. Vmax=4 µmol/min/mg enzyme with arachidonate as substrate (isoform A at pH 7.4 and 20 degrees Celsius)1 Publication
  2. Vmax=2 µmol/min/mg enzyme with arachidonate as substrate (isoform D at pH 7.4 and 20 degrees Celsius)1 Publication
  3. Vmax=4 µmol/min/mg enzyme with linoleate as substrate (isoform A at pH 7.4 and 20 degrees Celsius)1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: 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 bindingi15Calcium 1; via carbonyl oxygen1 Publication1
Metal bindingi17Calcium 1; via carbonyl oxygen1 Publication1
Metal bindingi39Calcium 21 Publication1
Metal bindingi40Calcium 2; via carbonyl oxygen1 Publication1
Metal bindingi42Calcium 2; via carbonyl oxygen1 Publication1
Metal bindingi44Calcium 21 Publication1
Metal bindingi85Calcium 11 Publication1
Metal bindingi86Calcium 1; via carbonyl oxygen1 Publication1
Metal bindingi373Iron; catalyticPROSITE-ProRule annotation1 Publication1
Metal bindingi378Iron; catalyticPROSITE-ProRule annotation1 Publication1
Metal bindingi553Iron; catalyticPROSITE-ProRule annotation1 Publication1
Metal bindingi676Iron; via carboxylate; catalyticPROSITE-ProRule annotation1 Publication1

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

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the 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, Oxidoreductase
Biological processLipid metabolism
LigandCalcium, Iron, Lipid-binding, Metal-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		1.13.11.33 2681

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-2142770 Synthesis of 15-eicosatetraenoic acid derivatives

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

More...UniPathwayi
UPA00881

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...SwissLipidsi		SLP:000000651
SLP:000001469 [O15296-1]
SLP:000001470 [O15296-4]

<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 15-lipoxygenase B (EC:1.13.11.33)
Short name:
15-LOX-B
Alternative name(s):
15-lipoxygenase 2
Short name:
15-LOX-2
Arachidonate 15-lipoxygenase type II
Linoleate 13-lipoxygenase 15-LOb (EC:1.13.11.-)
<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:ALOX15B
<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 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_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

More...EuPathDBi		HostDB:ENSG00000179593.15

Human Gene Nomenclature Database

More...HGNCi		HGNC:434 ALOX15B

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		603697 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_O15296

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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, 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_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>Mutagenesisi39D → A: Abolishes calcium-dependent association with membranes; when associated with A-44 and A-85. 1 Publication1
Mutagenesisi44E → A: Abolishes calcium-dependent association with membranes; when associated with A-39 and A-85. 1 Publication1
Mutagenesisi85D → A: Abolishes calcium-dependent association with membranes; when associated with A-39 and A-44. 1 Publication1
Mutagenesisi602D → Y: No effect on the stereoselectivity of the oxygenation reaction. Completely changes the stereoselectivity of the oxygenation reaction to produce (8S)-HPETE instead of (15S)-HPETE; when associated with H-603. 1 Publication1
Mutagenesisi603V → H: Changes the stereoselectivity of the oxygenation reaction. Completely changes the stereoselectivity of the oxygenation reaction to produce (8S)-HPETE instead of (15S)-HPETE; when associated with Y-602. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		247

Open Targets

More...OpenTargetsi		ENSG00000179593

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA24725

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL2457

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		1389

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		ALOX15B

<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_00002207001 – 676Arachidonate 15-lipoxygenase BAdd BLAST676

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		O15296

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		O15296

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

More...PaxDbi		O15296

PeptideAtlas

More...PeptideAtlasi		O15296

PRoteomics IDEntifications database

More...PRIDEi		O15296

ProteomicsDB human proteome resource

More...ProteomicsDBi		48566
48567 [O15296-2]
48568 [O15296-3]
48569 [O15296-4]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		O15296

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

More...PhosphoSitePlusi		O15296

<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 hair, prostate, lung, ovary, lymph node, spinal cord and cornea.3 Publications

<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

Up-regulated by UV-irradiation.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000179593 Expressed in 107 organ(s), highest expression level in mammalian vulva

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		O15296 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		O15296 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		HPA010562

<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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		106748, 8 interactors

Protein interaction database and analysis system

More...IntActi		O15296, 5 interactors

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000369530

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		O15296

<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

1676
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

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
4NREX-ray2.63A1-676[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		O15296

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

More...SMRi		O15296

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<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 – 124PLATPROSITE-ProRule annotationAdd BLAST123
Domaini125 – 676LipoxygenasePROSITE-ProRule annotationAdd BLAST552

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The PLAT domain can bind calcium ions; this promotes association with membranes.

<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		ENOG410IF0U Eukaryota
ENOG410YN4N LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000161510

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG005150

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		O15296

KEGG Orthology (KO)

More...KOi		K08022

Identification of Orthologs from Complete Genome Data

More...OMAi		EFSIHEA

Database of Orthologous Groups

More...OrthoDBi		385042at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		O15296

TreeFam database of animal gene trees

More...TreeFami		TF105320

Family and domain databases

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

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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (4+)i

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

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

This entry has 4 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform A (identifier: O15296-1) [UniParc]FASTAAdd to basket
Also known as: 15-LOb1

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MAEFRVRVST GEAFGAGTWD KVSVSIVGTR GESPPLPLDN LGKEFTAGAE 
        60         70         80         90        100
EDFQVTLPED VGRVLLLRVH KAPPVLPLLG PLAPDAWFCR WFQLTPPRGG 
       110        120        130        140        150
HLLFPCYQWL EGAGTLVLQE GTAKVSWADH HPVLQQQRQE ELQARQEMYQ 
       160        170        180        190        200
WKAYNPGWPH CLDEKTVEDL ELNIKYSTAK NANFYLQAGS AFAEMKIKGL 
       210        220        230        240        250
LDRKGLWRSL NEMKRIFNFR RTPAAEHAFE HWQEDAFFAS QFLNGLNPVL 
       260        270        280        290        300
IRRCHYLPKN FPVTDAMVAS VLGPGTSLQA ELEKGSLFLV DHGILSGIQT 
       310        320        330        340        350
NVINGKPQFS AAPMTLLYQS PGCGPLLPLA IQLSQTPGPN SPIFLPTDDK 
       360        370        380        390        400
WDWLLAKTWV RNAEFSFHEA LTHLLHSHLL PEVFTLATLR QLPHCHPLFK 
       410        420        430        440        450
LLIPHTRYTL HINTLARELL IVPGQVVDRS TGIGIEGFSE LIQRNMKQLN 
       460        470        480        490        500
YSLLCLPEDI RTRGVEDIPG YYYRDDGMQI WGAVERFVSE IIGIYYPSDE 
       510        520        530        540        550
SVQDDRELQA WVREIFSKGF LNQESSGIPS SLETREALVQ YVTMVIFTCS 
       560        570        580        590        600
AKHAAVSAGQ FDSCAWMPNL PPSMQLPPPT SKGLATCEGF IATLPPVNAT 
       610        620        630        640        650
CDVILALWLL SKEPGDQRPL GTYPDEHFTE EAPRRSIATF QSRLAQISRG 
       660        670 
IQERNQGLVL PYTYLDPPLI ENSVSI
Length:676
Mass (Da):75,857
Last modified:January 11, 2011 - v3
<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:i4F641DF2F9D492C6
GO
Isoform B (identifier: O15296-2) [UniParc]FASTAAdd to basket
Also known as: 15-LOX2sv-b

The sequence of this isoform differs from the canonical sequence as follows:
     401-429: Missing.
     483-527: Missing.

Show »
Length:602
Mass (Da):67,345
Checksum:i8804BB44095695C2
GO
Isoform C (identifier: O15296-3) [UniParc]FASTAAdd to basket
Also known as: 15-LOX2sv-c

The sequence of this isoform differs from the canonical sequence as follows:
     561-617: FDSCAWMPNL...WLLSKEPGDQ → VRKGQRPRWQ...PKAWQHARAS
     618-676: Missing.

Show »
Length:617
Mass (Da):69,136
Checksum:i3F690488B2B766AC
GO
Isoform D (identifier: O15296-4) [UniParc]FASTAAdd to basket
Also known as: 15-LOX2sv-a, 15-LOb2

The sequence of this isoform differs from the canonical sequence as follows:
     401-429: Missing.

Show »
Length:647
Mass (Da):72,523
Checksum:iEE51EEA9221CCC4B
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
I3L1D5I3L1D5_HUMAN
Arachidonate 15-lipoxygenase B
ALOX15B
664Annotation score:

Annotation score:2 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>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAD37786 differs from that shown. Reason: Erroneous gene model prediction.Curated

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 conflicti271V → L in AAB61706 (PubMed:9177185).Curated1
Sequence conflicti271V → L in CAC34521 (PubMed:11350124).Curated1
Sequence conflicti338G → C in AAD37786 (PubMed:15489334).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_061334486R → H1 PublicationCorresponds to variant dbSNP:rs9895916Ensembl.1
Natural variantiVAR_024524656Q → R4 PublicationsCorresponds to variant dbSNP:rs4792147Ensembl.1
Natural variantiVAR_024525676I → V. Corresponds to variant dbSNP:rs7225107Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_003142401 – 429Missing in isoform B and isoform D. 1 PublicationAdd BLAST29
Alternative sequenceiVSP_003143483 – 527Missing in isoform B. 1 PublicationAdd BLAST45
Alternative sequenceiVSP_003144561 – 617FDSCA…EPGDQ → VRKGQRPRWQAGGDPAPQPH SALSAFSLTPVLGCPTCHPA CSCHHPPPKAWQHARAS in isoform C. 1 PublicationAdd BLAST57
Alternative sequenceiVSP_003145618 – 676Missing in isoform C. 1 PublicationAdd BLAST59

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
U78294 mRNA Translation: AAB61706.1
AJ305028
, AJ305029, AJ305030, AJ305031 Genomic DNA Translation: CAC34521.1
AF468051 mRNA Translation: AAL76274.1
AF468052 mRNA Translation: AAL76275.1
AF468053 mRNA Translation: AAL76276.1
AF468054 mRNA Translation: AAL76277.1
AC129492 Genomic DNA No translation available.
CH471108 Genomic DNA Translation: EAW90098.1
CH471108 Genomic DNA Translation: EAW90100.1
BC035217 mRNA Translation: AAH35217.1
BC063647 mRNA Translation: AAH63647.1
AF149095 Genomic DNA Translation: AAD37786.1 Sequence problems.

The Consensus CDS (CCDS) project

More...CCDSi		CCDS11128.1 [O15296-1]
CCDS32558.1 [O15296-4]
CCDS32559.1 [O15296-2]

NCBI Reference Sequences

More...RefSeqi		NP_001034219.1, NM_001039130.1 [O15296-4]
NP_001034220.1, NM_001039131.1 [O15296-2]
NP_001132.2, NM_001141.2 [O15296-1]

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.111256

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000380173; ENSP00000369520; ENSG00000179593 [O15296-4]
ENST00000380183; ENSP00000369530; ENSG00000179593 [O15296-1]
ENST00000573359; ENSP00000460332; ENSG00000179593 [O15296-2]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		247

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:247

UCSC genome browser

More...UCSCi		uc002gju.4 human [O15296-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

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

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U78294 mRNA Translation: AAB61706.1
AJ305028
, AJ305029, AJ305030, AJ305031 Genomic DNA Translation: CAC34521.1
AF468051 mRNA Translation: AAL76274.1
AF468052 mRNA Translation: AAL76275.1
AF468053 mRNA Translation: AAL76276.1
AF468054 mRNA Translation: AAL76277.1
AC129492 Genomic DNA No translation available.
CH471108 Genomic DNA Translation: EAW90098.1
CH471108 Genomic DNA Translation: EAW90100.1
BC035217 mRNA Translation: AAH35217.1
BC063647 mRNA Translation: AAH63647.1
AF149095 Genomic DNA Translation: AAD37786.1 Sequence problems.
CCDSiCCDS11128.1 [O15296-1]
CCDS32558.1 [O15296-4]
CCDS32559.1 [O15296-2]
RefSeqiNP_001034219.1, NM_001039130.1 [O15296-4]
NP_001034220.1, NM_001039131.1 [O15296-2]
NP_001132.2, NM_001141.2 [O15296-1]
UniGeneiHs.111256

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4NREX-ray2.63A1-676[»]
ProteinModelPortaliO15296
SMRiO15296
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106748, 8 interactors
IntActiO15296, 5 interactors
STRINGi9606.ENSP00000369530

Chemistry databases

BindingDBiO15296
ChEMBLiCHEMBL2457
GuidetoPHARMACOLOGYi1389
SwissLipidsiSLP:000000651
SLP:000001469 [O15296-1]
SLP:000001470 [O15296-4]

PTM databases

iPTMnetiO15296
PhosphoSitePlusiO15296

Polymorphism and mutation databases

BioMutaiALOX15B

Proteomic databases

EPDiO15296
jPOSTiO15296
PaxDbiO15296
PeptideAtlasiO15296
PRIDEiO15296
ProteomicsDBi48566
48567 [O15296-2]
48568 [O15296-3]
48569 [O15296-4]

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		247
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000380173; ENSP00000369520; ENSG00000179593 [O15296-4]
ENST00000380183; ENSP00000369530; ENSG00000179593 [O15296-1]
ENST00000573359; ENSP00000460332; ENSG00000179593 [O15296-2]
GeneIDi247
KEGGihsa:247
UCSCiuc002gju.4 human [O15296-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		247
DisGeNETi247
EuPathDBiHostDB:ENSG00000179593.15

GeneCards: human genes, protein and diseases

More...GeneCardsi		ALOX15B

H-Invitational Database, human transcriptome db

More...H-InvDBi		HIX0027139
HGNCiHGNC:434 ALOX15B
HPAiHPA010562
MIMi603697 gene
neXtProtiNX_O15296
OpenTargetsiENSG00000179593
PharmGKBiPA24725

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiENOG410IF0U Eukaryota
ENOG410YN4N LUCA
GeneTreeiENSGT00940000161510
HOVERGENiHBG005150
InParanoidiO15296
KOiK08022
OMAiEFSIHEA
OrthoDBi385042at2759
PhylomeDBiO15296
TreeFamiTF105320

Enzyme and pathway databases

UniPathwayi
UPA00881

BRENDAi1.13.11.33 2681
ReactomeiR-HSA-2142770 Synthesis of 15-eicosatetraenoic acid derivatives

Miscellaneous databases

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

More...ChiTaRSi		ALOX15B human

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		ALOX15B

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

More...GenomeRNAii		247

Protein Ontology

More...PROi		PR:O15296

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000179593 Expressed in 107 organ(s), highest expression level in mammalian vulva
ExpressionAtlasiO15296 baseline and differential
GenevisibleiO15296 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

More...ProtoNeti		Search...

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

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiLX15B_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: O15296
Secondary accession number(s): D3DTR2
, Q8IYQ2, Q8TEV3, Q8TEV4, Q8TEV5, Q8TEV6, Q9UKM4
<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: January 11, 2001
Last sequence update: January 11, 2011
Last modified: February 13, 2019
This is version 178 of the entry and version 3 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. SIMILARITY comments
    Index of protein domains and families
  2. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  6. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  7. PATHWAY comments
    Index of metabolic and biosynthesis pathways
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again