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O15296

- LX15B_HUMAN

UniProt

O15296 - LX15B_HUMAN

Protein

Arachidonate 15-lipoxygenase B

Gene

ALOX15B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 3 (11 Jan 2011)
      Previous versions | rss
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    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

    Catalytic activityi

    Arachidonate + O2 = (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate.
    Linoleate + O2 = (9Z,11E)-13-hydroxyoctadeca-9,11-dienoate.

    Cofactori

    Binds 1 iron ion per subunit.1 PublicationPROSITE-ProRule annotation

    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

    Vmax=4 µmol/min/mg enzyme with arachidonate as substrate (isoform A at pH 7.4 and 20 degrees Celsius)1 Publication

    Vmax=2 µmol/min/mg enzyme with arachidonate as substrate (isoform D at pH 7.4 and 20 degrees Celsius)1 Publication

    Vmax=4 µmol/min/mg enzyme with linoleate as substrate (isoform A at pH 7.4 and 20 degrees Celsius)1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi15 – 151Calcium 1; via carbonyl oxygen1 Publication
    Metal bindingi17 – 171Calcium 1; via carbonyl oxygen1 Publication
    Metal bindingi39 – 391Calcium 21 Publication
    Metal bindingi40 – 401Calcium 2; via carbonyl oxygen1 Publication
    Metal bindingi42 – 421Calcium 2; via carbonyl oxygen1 Publication
    Metal bindingi44 – 441Calcium 21 Publication
    Metal bindingi85 – 851Calcium 11 Publication
    Metal bindingi86 – 861Calcium 1; via carbonyl oxygen1 Publication
    Metal bindingi373 – 3731Iron; catalytic1 PublicationPROSITE-ProRule annotation
    Metal bindingi378 – 3781Iron; catalytic1 PublicationPROSITE-ProRule annotation
    Metal bindingi553 – 5531Iron; catalytic1 PublicationPROSITE-ProRule annotation
    Metal bindingi676 – 6761Iron; via carboxylate; catalytic1 PublicationPROSITE-ProRule annotation

    GO - Molecular functioni

    1. arachidonate 15-lipoxygenase activity Source: UniProtKB
    2. arachidonate 8(S)-lipoxygenase activity Source: Ensembl
    3. calcium ion binding Source: UniProtKB
    4. iron ion binding Source: UniProtKB
    5. linoleate 13S-lipoxygenase activity Source: UniProtKB
    6. lipid binding Source: UniProtKB-KW

    GO - Biological processi

    1. apoptotic process Source: UniProtKB
    2. arachidonic acid metabolic process Source: UniProtKB
    3. hepoxilin biosynthetic process Source: UniProtKB
    4. linoleic acid metabolic process Source: Ensembl
    5. lipid metabolic process Source: UniProtKB
    6. lipoxygenase pathway Source: Reactome
    7. negative regulation of cell cycle Source: UniProtKB
    8. negative regulation of cell migration Source: UniProtKB
    9. negative regulation of cell proliferation Source: UniProtKB
    10. negative regulation of growth Source: UniProtKB
    11. positive regulation of chemokine secretion Source: UniProtKB
    12. positive regulation of keratinocyte differentiation Source: Ensembl
    13. positive regulation of macrophage derived foam cell differentiation Source: UniProtKB
    14. positive regulation of peroxisome proliferator activated receptor signaling pathway Source: Ensembl
    15. prostate gland development Source: UniProtKB
    16. regulation of epithelial cell differentiation Source: UniProtKB
    17. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Dioxygenase, Oxidoreductase

    Keywords - Biological processi

    Lipid metabolism

    Keywords - Ligandi

    Calcium, Iron, Lipid-binding, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_150422. Synthesis of 15-eicosatetraenoic acid derivatives.
    UniPathwayiUPA00881.

    Names & Taxonomyi

    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.-)
    Gene namesi
    Name:ALOX15B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:434. ALOX15B.

    Subcellular locationi

    Isoform A : Nucleus
    Note: Other isoforms are excluded from the nucleus.
    Cytoplasmcytosol. Cell membrane. Cytoplasmcytoskeleton. Membrane; Peripheral membrane protein
    Note: Predominantly cytosolic; becomes enriched at membranes upon calcium binding.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytoskeleton Source: UniProtKB
    3. cytosol Source: UniProtKB
    4. extrinsic component of membrane Source: UniProtKB
    5. intracellular Source: UniProtKB
    6. membrane Source: UniProtKB
    7. nucleus Source: UniProtKB
    8. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi39 – 391D → A: Abolishes calcium-dependent association with membranes; when associated with A-44 and A-85. 1 Publication
    Mutagenesisi44 – 441E → A: Abolishes calcium-dependent association with membranes; when associated with A-39 and A-85. 1 Publication
    Mutagenesisi85 – 851D → A: Abolishes calcium-dependent association with membranes; when associated with A-39 and A-44. 1 Publication
    Mutagenesisi602 – 6021D → 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 Publication
    Mutagenesisi603 – 6031V → 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 Publication

    Organism-specific databases

    PharmGKBiPA24725.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 676676Arachidonate 15-lipoxygenase BPRO_0000220700Add
    BLAST

    Proteomic databases

    PaxDbiO15296.
    PRIDEiO15296.

    PTM databases

    PhosphoSiteiO15296.

    Expressioni

    Tissue specificityi

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

    Inductioni

    Up-regulated by UV-irradiation.1 Publication

    Gene expression databases

    ArrayExpressiO15296.
    BgeeiO15296.
    CleanExiHS_ALOX15B.
    GenevestigatoriO15296.

    Organism-specific databases

    HPAiHPA010562.

    Interactioni

    Protein-protein interaction databases

    BioGridi106748. 3 interactions.
    STRINGi9606.ENSP00000369530.

    Structurei

    Secondary structure

    1
    676
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 108
    Beta strandi20 – 3011
    Beta strandi50 – 567
    Beta strandi63 – 7210
    Turni77 – 793
    Beta strandi87 – 959
    Beta strandi102 – 1109
    Beta strandi115 – 1195
    Turni126 – 1283
    Helixi132 – 14817
    Beta strandi161 – 1633
    Helixi167 – 1693
    Helixi172 – 1743
    Helixi178 – 19720
    Helixi212 – 2154
    Helixi216 – 2194
    Helixi223 – 2319
    Helixi235 – 24410
    Helixi265 – 2728
    Helixi278 – 2847
    Beta strandi287 – 2915
    Helixi293 – 2953
    Beta strandi314 – 3196
    Turni321 – 3233
    Beta strandi326 – 33611
    Helixi350 – 37021
    Turni371 – 3733
    Helixi374 – 3774
    Helixi379 – 39113
    Helixi397 – 4026
    Helixi403 – 4064
    Helixi409 – 41911
    Helixi426 – 4305
    Helixi434 – 44613
    Helixi451 – 4544
    Helixi456 – 4627
    Helixi472 – 49524
    Helixi499 – 5035
    Helixi506 – 51813
    Turni519 – 5224
    Helixi524 – 5263
    Helixi535 – 54915
    Helixi551 – 5577
    Helixi560 – 5645
    Helixi567 – 5693
    Beta strandi574 – 5763
    Beta strandi580 – 5834
    Helixi587 – 5937
    Helixi597 – 61115
    Helixi631 – 65626
    Helixi667 – 6693
    Beta strandi670 – 6734

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4NREX-ray2.63A1-676[»]
    ProteinModelPortaliO15296.
    SMRiO15296. Positions 2-676.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 124123PLATPROSITE-ProRule annotationAdd
    BLAST
    Domaini125 – 676552LipoxygenasePROSITE-ProRule annotationAdd
    BLAST

    Domaini

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

    Sequence similaritiesi

    Belongs to the lipoxygenase family.Curated
    Contains 1 lipoxygenase domain.PROSITE-ProRule annotation
    Contains 1 PLAT domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG69653.
    HOVERGENiHBG005150.
    InParanoidiO15296.
    KOiK08022.
    OMAiIQTNVIN.
    OrthoDBiEOG7B05CG.
    PhylomeDBiO15296.
    TreeFamiTF105320.

    Family and domain databases

    Gene3Di2.60.60.20. 1 hit.
    InterProiIPR008976. Lipase_LipOase.
    IPR000907. LipOase.
    IPR013819. LipOase_C.
    IPR020834. LipOase_CS.
    IPR020833. LipOase_Fe_BS.
    IPR001885. LipOase_mml.
    IPR001024. PLAT/LH2_dom.
    [Graphical view]
    PANTHERiPTHR11771. PTHR11771. 1 hit.
    PfamiPF00305. Lipoxygenase. 1 hit.
    PF01477. PLAT. 1 hit.
    [Graphical view]
    PRINTSiPR00087. LIPOXYGENASE.
    PR00467. MAMLPOXGNASE.
    SMARTiSM00308. LH2. 1 hit.
    [Graphical view]
    SUPFAMiSSF48484. SSF48484. 1 hit.
    SSF49723. SSF49723. 1 hit.
    PROSITEiPS00711. LIPOXYGENASE_1. 1 hit.
    PS00081. LIPOXYGENASE_2. 1 hit.
    PS51393. LIPOXYGENASE_3. 1 hit.
    PS50095. PLAT. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    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

    MAEFRVRVST GEAFGAGTWD KVSVSIVGTR GESPPLPLDN LGKEFTAGAE    50
    EDFQVTLPED VGRVLLLRVH KAPPVLPLLG PLAPDAWFCR WFQLTPPRGG 100
    HLLFPCYQWL EGAGTLVLQE GTAKVSWADH HPVLQQQRQE ELQARQEMYQ 150
    WKAYNPGWPH CLDEKTVEDL ELNIKYSTAK NANFYLQAGS AFAEMKIKGL 200
    LDRKGLWRSL NEMKRIFNFR RTPAAEHAFE HWQEDAFFAS QFLNGLNPVL 250
    IRRCHYLPKN FPVTDAMVAS VLGPGTSLQA ELEKGSLFLV DHGILSGIQT 300
    NVINGKPQFS AAPMTLLYQS PGCGPLLPLA IQLSQTPGPN SPIFLPTDDK 350
    WDWLLAKTWV RNAEFSFHEA LTHLLHSHLL PEVFTLATLR QLPHCHPLFK 400
    LLIPHTRYTL HINTLARELL IVPGQVVDRS TGIGIEGFSE LIQRNMKQLN 450
    YSLLCLPEDI RTRGVEDIPG YYYRDDGMQI WGAVERFVSE IIGIYYPSDE 500
    SVQDDRELQA WVREIFSKGF LNQESSGIPS SLETREALVQ YVTMVIFTCS 550
    AKHAAVSAGQ FDSCAWMPNL PPSMQLPPPT SKGLATCEGF IATLPPVNAT 600
    CDVILALWLL SKEPGDQRPL GTYPDEHFTE EAPRRSIATF QSRLAQISRG 650
    IQERNQGLVL PYTYLDPPLI ENSVSI 676
    Length:676
    Mass (Da):75,857
    Last modified:January 11, 2011 - v3
    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

    Sequence cautioni

    The sequence AAD37786.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti271 – 2711V → L in AAB61706. (PubMed:9177185)Curated
    Sequence conflicti271 – 2711V → L in CAC34521. (PubMed:11350124)Curated
    Sequence conflicti338 – 3381G → C in AAD37786. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti486 – 4861R → H.1 Publication
    Corresponds to variant rs9895916 [ dbSNP | Ensembl ].
    VAR_061334
    Natural varianti656 – 6561Q → R.4 Publications
    Corresponds to variant rs4792147 [ dbSNP | Ensembl ].
    VAR_024524
    Natural varianti676 – 6761I → V.
    Corresponds to variant rs7225107 [ dbSNP | Ensembl ].
    VAR_024525

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei401 – 42929Missing in isoform B and isoform D. 1 PublicationVSP_003142Add
    BLAST
    Alternative sequencei483 – 52745Missing in isoform B. 1 PublicationVSP_003143Add
    BLAST
    Alternative sequencei561 – 61757FDSCA…EPGDQ → VRKGQRPRWQAGGDPAPQPH SALSAFSLTPVLGCPTCHPA CSCHHPPPKAWQHARAS in isoform C. 1 PublicationVSP_003144Add
    BLAST
    Alternative sequencei618 – 67659Missing in isoform C. 1 PublicationVSP_003145Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.

    Genome annotation databases

    EnsembliENST00000380173; ENSP00000369520; ENSG00000179593. [O15296-4]
    ENST00000380183; ENSP00000369530; ENSG00000179593. [O15296-1]
    ENST00000573359; ENSP00000460332; ENSG00000179593. [O15296-2]
    GeneIDi247.
    KEGGihsa:247.
    UCSCiuc002gju.3. human. [O15296-1]
    uc002gjv.3. human. [O15296-4]
    uc002gjw.3. human. [O15296-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    CCDSi CCDS11128.1. [O15296-1 ]
    CCDS32558.1. [O15296-4 ]
    CCDS32559.1. [O15296-2 ]
    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 ]
    UniGenei Hs.111256.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4NRE X-ray 2.63 A 1-676 [» ]
    ProteinModelPortali O15296.
    SMRi O15296. Positions 2-676.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106748. 3 interactions.
    STRINGi 9606.ENSP00000369530.

    Chemistry

    BindingDBi O15296.
    ChEMBLi CHEMBL2457.

    PTM databases

    PhosphoSitei O15296.

    Proteomic databases

    PaxDbi O15296.
    PRIDEi O15296.

    Protocols and materials databases

    DNASUi 247.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000380173 ; ENSP00000369520 ; ENSG00000179593 . [O15296-4 ]
    ENST00000380183 ; ENSP00000369530 ; ENSG00000179593 . [O15296-1 ]
    ENST00000573359 ; ENSP00000460332 ; ENSG00000179593 . [O15296-2 ]
    GeneIDi 247.
    KEGGi hsa:247.
    UCSCi uc002gju.3. human. [O15296-1 ]
    uc002gjv.3. human. [O15296-4 ]
    uc002gjw.3. human. [O15296-2 ]

    Organism-specific databases

    CTDi 247.
    GeneCardsi GC17P007942.
    H-InvDB HIX0027139.
    HGNCi HGNC:434. ALOX15B.
    HPAi HPA010562.
    MIMi 603697. gene.
    neXtProti NX_O15296.
    PharmGKBi PA24725.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG69653.
    HOVERGENi HBG005150.
    InParanoidi O15296.
    KOi K08022.
    OMAi IQTNVIN.
    OrthoDBi EOG7B05CG.
    PhylomeDBi O15296.
    TreeFami TF105320.

    Enzyme and pathway databases

    UniPathwayi UPA00881 .
    Reactomei REACT_150422. Synthesis of 15-eicosatetraenoic acid derivatives.

    Miscellaneous databases

    ChiTaRSi ALOX15B. human.
    GeneWikii ALOX15B.
    GenomeRNAii 247.
    NextBioi 985.
    PROi O15296.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O15296.
    Bgeei O15296.
    CleanExi HS_ALOX15B.
    Genevestigatori O15296.

    Family and domain databases

    Gene3Di 2.60.60.20. 1 hit.
    InterProi IPR008976. Lipase_LipOase.
    IPR000907. LipOase.
    IPR013819. LipOase_C.
    IPR020834. LipOase_CS.
    IPR020833. LipOase_Fe_BS.
    IPR001885. LipOase_mml.
    IPR001024. PLAT/LH2_dom.
    [Graphical view ]
    PANTHERi PTHR11771. PTHR11771. 1 hit.
    Pfami PF00305. Lipoxygenase. 1 hit.
    PF01477. PLAT. 1 hit.
    [Graphical view ]
    PRINTSi PR00087. LIPOXYGENASE.
    PR00467. MAMLPOXGNASE.
    SMARTi SM00308. LH2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48484. SSF48484. 1 hit.
    SSF49723. SSF49723. 1 hit.
    PROSITEi PS00711. LIPOXYGENASE_1. 1 hit.
    PS00081. LIPOXYGENASE_2. 1 hit.
    PS51393. LIPOXYGENASE_3. 1 hit.
    PS50095. PLAT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), VARIANT ARG-656, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
      Tissue: Skin.
    2. "A gene cluster encoding human epidermis-type lipoxygenases at chromosome 17p13.1: cloning, physical mapping, and expression."
      Krieg P., Marks F., Fuerstenberger G.
      Genomics 73:323-330(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ARG-656, TISSUE SPECIFICITY.
    3. "Evidence that arachidonate 15-lipoxygenase 2 is a negative cell cycle regulator in normal prostate epithelial cells."
      Tang S., Bhatia B., Maldonado C.J., Yang P., Newman R.A., Liu J., Chandra D., Traag J., Klein R.D., Fischer S.M., Chopra D., Shen J., Zhau H.E., Chung L.W.K., Tang D.G.
      J. Biol. Chem. 277:16189-16201(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B; C AND D), VARIANTS HIS-486 AND ARG-656, FUNCTION IN CELL CYCLE PROGRESSION.
    4. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A), VARIANT ARG-656.
      Tissue: Skin.
    7. "Differential characteristics of human 15-lipoxygenase isozymes and a novel splice variant of 15S-lipoxygenase."
      Kilty I., Logan A., Vickers P.J.
      Eur. J. Biochem. 266:83-93(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 337-484, ALTERNATIVE SPLICING (ISOFORMS A AND D), CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, KINETIC PARAMETERS, PATHWAY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    8. "Identification of amino acid determinants of the positional specificity of mouse 8S-lipoxygenase and human 15S-lipoxygenase-2."
      Jisaka M., Kim R.B., Boeglin W.E., Brash A.R.
      J. Biol. Chem. 275:1287-1293(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A 15S-LIPOXYGENASE, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-602 AND VAL-603.
    9. "Subcellular localization and tumor-suppressive functions of 15-lipoxygenase 2 (15-LOX2) and its splice variants."
      Bhatia B., Maldonado C.J., Tang S., Chandra D., Klein R.D., Chopra D., Shappell S.B., Yang P., Newman R.A., Tang D.G.
      J. Biol. Chem. 278:25091-25100(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CELL PROLIFERATION, SUBCELLULAR LOCATION.
    10. "Double dioxygenation by mouse 8S-lipoxygenase: specific formation of a potent peroxisome proliferator-activated receptor alpha agonist."
      Jisaka M., Iwanaga C., Takahashi N., Goto T., Kawada T., Yamamoto T., Ikeda I., Nishimura K., Nagaya T., Fushiki T., Yokota K.
      Biochem. Biophys. Res. Commun. 338:136-143(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "15-Lipoxygenase-2 expression in human macrophages induces chemokine secretion and T cell migration."
      Danielsson K.N., Rydberg E.K., Ingelsten M., Akyuerek L.M., Jirholt P., Ullstroem C., Forsberg G.B., Boren J., Wiklund O., Hulten L.M.
      Atherosclerosis 199:34-40(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CYTOKINE SECRETION.
    12. "Reciprocal regulation of 12- and 15-lipoxygenases by UV-irradiation in human keratinocytes."
      Yoo H., Jeon B., Jeon M.S., Lee H., Kim T.Y.
      FEBS Lett. 582:3249-3253(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY UV.
    13. "Arachidonate 15-lipoxygenase type B knockdown leads to reduced lipid accumulation and inflammation in atherosclerosis."
      Magnusson L.U., Lundqvist A., Karlsson M.N., Skalen K., Levin M., Wiklund O., Boren J., Hulten L.M.
      PLoS ONE 7:E43142-E43142(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. "The structure of human 15-lipoxygenase-2 with a substrate mimic."
      Kobe M.J., Neau D.B., Mitchell C.E., Bartlett S.G., Newcomer M.E.
      J. Biol. Chem. 289:8562-8569(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.63 ANGSTROMS) IN COMPLEX WITH CALCIUM AND IRON, CATALYTIC ACTIVITY, COFACTOR, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-39; GLU-44 AND ASP-85.

    Entry informationi

    Entry nameiLX15B_HUMAN
    AccessioniPrimary (citable) accession number: O15296
    Secondary accession number(s): D3DTR2
    , Q8IYQ2, Q8TEV3, Q8TEV4, Q8TEV5, Q8TEV6, Q9UKM4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 11, 2001
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 143 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Caution

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

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

    External Data

    Dasty 3