Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P18054

- LOX12_HUMAN

UniProt

P18054 - LOX12_HUMAN

Protein

Arachidonate 12-lipoxygenase, 12S-type

Gene

ALOX12

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 160 (01 Oct 2014)
      Sequence version 4 (06 Feb 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    Catalytic activityi

    Arachidonate + O2 = (5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyicosa-5,8,10,14-tetraenoate.
    (7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa-7,9,11,14-tetraenoate + H2O = (5S,6R,15S)-trihydroxy-(7E,9E,11Z,13E)-eicosatetraenoate.
    (7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa-7,9,11,14-tetraenoate + H2O = (5S,14R,15S)-trihydroxy-(6E,8Z,10E,12E)-eicosatetraenoate.

    Cofactori

    Binds 1 iron ion per subunit.

    Enzyme regulationi

    Activated by EGF.1 Publication

    Kineticsi

    1. KM=8 µM for arachidonate (PubMed:1851637, at pH 7.0 and 37 degrees Celsius)3 Publications
    2. KM=10 µM for arachidonate (PubMed:8319693, at pH 8.0 and 25 degrees Celsius)3 Publications
    3. KM=6.2 µM for arachidonate (PubMed:8250832, at pH 7.4)3 Publications
    4. KM=9 µM for linoleate (PubMed:8319693, at pH 8.0 and 25 degrees Celsius)3 Publications
    5. KM=7.9 µM for leukotriene A4 (PubMed:8250832, at pH 7.4)3 Publications
    6. KM=3 µM for eicosa-5,8,11,14,17-pentaenoate (PubMed:1851637, at pH 7.0 and 37 degrees Celsius)3 Publications
    7. KM=35 µM for eicosa-8,11,14-trienoate (PubMed:1851637, at pH 7.0 and 37 degrees Celsius)3 Publications
    8. KM=14.3 µM for 5,6-epoxy-8,11,14-eicosatrienoate (PubMed:8250832, at pH 7.4)3 Publications

    Vmax=3 µmol/min/mg enzyme with arachidonate as substrate (PubMed:8319693, at pH 8.0 and 25 degrees Celsius)3 Publications

    Vmax=1.057 µmol/min/mg enzyme with arachidonate as substrate (PubMed:8250832, at pH 7.4)3 Publications

    Vmax=0.0375 µmol/min/mg enzyme with linoleate as substrate (PubMed:8319693, at pH 8.0 and 25 degrees Celsius)3 Publications

    Vmax=0.025 µmol/min/mg enzyme with leukotriene A4 as substrate (PubMed:8250832, at pH 7.4)3 Publications

    Vmax=0.985 µmol/min/mg enzyme with 5,6-epoxy-8,11,14-eicosatrienoate as substrate (PubMed:8250832, at pH 7.4)3 Publications

    pH dependencei

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi360 – 3601Iron; catalytic
    Metal bindingi365 – 3651Iron; catalytic
    Metal bindingi540 – 5401Iron; catalytic
    Metal bindingi544 – 5441Iron; catalyticPROSITE-ProRule annotation
    Metal bindingi663 – 6631Iron; via carboxylate; catalyticPROSITE-ProRule annotation

    GO - Molecular functioni

    1. arachidonate 12-lipoxygenase activity Source: UniProtKB
    2. hepoxilin A3 synthase activity Source: Reactome
    3. hepoxilin-epoxide hydrolase activity Source: UniProtKB
    4. iron ion binding Source: InterPro
    5. linoleate 13S-lipoxygenase activity Source: UniProtKB
    6. oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Source: Reactome
    7. protein binding Source: IntAct

    GO - Biological processi

    1. aging Source: Ensembl
    2. arachidonic acid metabolic process Source: UniProtKB
    3. cellular component movement Source: UniProtKB
    4. cellular response to lipid Source: Ensembl
    5. establishment of skin barrier Source: UniProtKB
    6. fatty acid oxidation Source: UniProtKB
    7. hepoxilin biosynthetic process Source: UniProtKB
    8. hepoxilin metabolic process Source: Reactome
    9. leukotriene A4 metabolic process Source: UniProtKB
    10. linoleic acid metabolic process Source: UniProtKB
    11. lipoxin A4 biosynthetic process Source: UniProtKB
    12. lipoxin B4 biosynthetic process Source: UniProtKB
    13. lipoxin metabolic process Source: Reactome
    14. lipoxygenase pathway Source: UniProtKB
    15. negative regulation of apoptotic process Source: UniProtKB
    16. negative regulation of muscle cell apoptotic process Source: UniProtKB
    17. negative regulation of platelet aggregation Source: UniProtKB
    18. positive regulation of angiogenesis Source: UniProtKB
    19. positive regulation of apoptotic process Source: Ensembl
    20. positive regulation of cell adhesion Source: UniProtKB
    21. positive regulation of cell growth Source: UniProtKB
    22. positive regulation of cell migration Source: UniProtKB
    23. positive regulation of cell proliferation Source: UniProtKB
    24. positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
    25. positive regulation of endothelial cell differentiation Source: Ensembl
    26. positive regulation of endothelial cell migration Source: Ensembl
    27. positive regulation of gene expression Source: Ensembl
    28. positive regulation of mitochondrial depolarization Source: Ensembl
    29. positive regulation of smooth muscle cell proliferation Source: Ensembl
    30. positive regulation of vasodilation Source: Ensembl
    31. reactive oxygen species metabolic process Source: UniProtKB
    32. small molecule metabolic process Source: Reactome
    33. superoxide anion generation Source: UniProtKB

    Keywords - Molecular functioni

    Dioxygenase, Hydrolase, Oxidoreductase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Keywords - Ligandi

    Iron, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS03167-MONOMER.
    ReactomeiREACT_150201. Synthesis of 12-eicosatetraenoic acid derivatives.
    REACT_150292. Synthesis of Hepoxilins (HX) and Trioxilins (TrX).
    REACT_150320. Synthesis of Lipoxins (LX).
    UniPathwayiUPA00881.

    Names & Taxonomyi

    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
    Gene namesi
    Name:ALOX12
    Synonyms:12LO, LOG12
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:429. ALOX12.

    Subcellular locationi

    Cytoplasmcytosol. Membrane
    Note: Membrane association is stimulated by EGF.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: UniProtKB
    3. extracellular vesicular exosome Source: UniProt
    4. membrane Source: UniProtKB
    5. sarcolemma Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Esophageal cancer (ESCR) [MIM:133239]: A 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.1 Publication
    Note: 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
    Colorectal cancer (CRC) [MIM:114500]: A 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.1 Publication
    Note: 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

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi355 – 3551H → Q: No effect on catalytic activity. 1 Publication
    Mutagenesisi360 – 3601H → Q or Y: Complete loss of catalytic activity. 1 Publication
    Mutagenesisi365 – 3651H → Q: Complete loss of catalytic activity. 1 Publication
    Mutagenesisi383 – 3831H → Q: Altered catalytic activity and protein expression. 1 Publication
    Mutagenesisi392 – 3921H → Q: No effect on catalytic activity. 1 Publication
    Mutagenesisi416 – 4161K → Q: Reduced catalytic activity. No effect on the stereoselectivity of the oxygenation reaction. 1 Publication
    Mutagenesisi417 – 4171A → I: Reduced catalytic activity. Alters the stereoselectivity of the oxygenation reaction. 1 Publication
    Mutagenesisi418 – 4181V → M: No effect on catalytic activity. No effect on the stereoselectivity of the oxygenation reaction. 1 Publication
    Mutagenesisi540 – 5401H → Q: Complete loss of catalytic activity. 1 Publication

    Organism-specific databases

    MIMi114500. phenotype.
    133239. phenotype.
    PharmGKBiPA45.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 663663Arachidonate 12-lipoxygenase, 12S-typePRO_0000220682Add
    BLAST

    Proteomic databases

    PaxDbiP18054.
    PRIDEiP18054.

    PTM databases

    PhosphoSiteiP18054.

    Expressioni

    Tissue specificityi

    Expressed in vascular smooth muscle cells.1 Publication

    Inductioni

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

    Gene expression databases

    ArrayExpressiP18054.
    BgeeiP18054.
    CleanExiHS_ALOX12.
    GenevestigatoriP18054.

    Organism-specific databases

    HPAiCAB019287.
    HPA010691.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    KRT5P136477EBI-1633210,EBI-702187
    LMNAP025454EBI-1633210,EBI-351935

    Protein-protein interaction databases

    BioGridi106740. 4 interactions.
    IntActiP18054. 4 interactions.
    MINTiMINT-1206406.
    STRINGi9606.ENSP00000251535.

    Structurei

    Secondary structure

    1
    663
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi182 – 19514
    Beta strandi198 – 2003
    Helixi203 – 2075
    Helixi213 – 2219
    Helixi225 – 23410
    Helixi258 – 26912
    Beta strandi273 – 2775
    Helixi279 – 2813
    Beta strandi300 – 3056
    Beta strandi311 – 3199
    Beta strandi325 – 3273
    Helixi337 – 35721
    Helixi358 – 3647
    Helixi365 – 37814
    Helixi384 – 3896
    Helixi390 – 3923
    Helixi426 – 4349
    Turni438 – 4414
    Helixi443 – 4497
    Helixi459 – 48224
    Helixi486 – 4916
    Helixi493 – 50311
    Turni504 – 5085
    Helixi510 – 5123
    Helixi522 – 53615
    Helixi538 – 5447
    Helixi547 – 5515
    Helixi554 – 5563
    Beta strandi567 – 5715
    Helixi574 – 5807
    Helixi584 – 59714
    Helixi618 – 64326
    Helixi654 – 6563
    Beta strandi657 – 6604

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiP18054.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 114113PLATPROSITE-ProRule annotationAdd
    BLAST
    Domaini115 – 663549LipoxygenasePROSITE-ProRule annotationAdd
    BLAST

    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.
    HOGENOMiHOG000234358.
    HOVERGENiHBG005150.
    InParanoidiP18054.
    KOiK00458.
    OMAiQNQLCHF.
    OrthoDBiEOG7B05CG.
    PhylomeDBiP18054.
    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]

    Sequencei

    Sequence statusi: Complete.

    P18054-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGRYRIRVAT GAWLFSGSYN RVQLWLVGTR GEAELELQLR PARGEEEEFD    50
    HDVAEDLGLL QFVRLRKHHW LVDDAWFCDR ITVQGPGACA EVAFPCYRWV 100
    QGEDILSLPE GTARLPGDNA LDMFQKHREK ELKDRQQIYC WATWKEGLPL 150
    TIAADRKDDL PPNMRFHEEK RLDFEWTLKA GALEMALKRV YTLLSSWNCL 200
    EDFDQIFWGQ KSALAEKVRQ CWQDDELFSY QFLNGANPML LRRSTSLPSR 250
    LVLPSGMEEL QAQLEKELQN GSLFEADFIL LDGIPANVIR GEKQYLAAPL 300
    VMLKMEPNGK LQPMVIQIQP PNPSSPTPTL FLPSDPPLAW LLAKSWVRNS 350
    DFQLHEIQYH LLNTHLVAEV IAVATMRCLP GLHPIFKFLI PHIRYTMEIN 400
    TRARTQLISD GGIFDKAVST GGGGHVQLLR RAAAQLTYCS LCPPDDLADR 450
    GLLGLPGALY AHDALRLWEI IARYVEGIVH LFYQRDDIVK GDPELQAWCR 500
    EITEVGLCQA QDRGFPVSFQ SQSQLCHFLT MCVFTCTAQH AAINQGQLDW 550
    YAWVPNAPCT MRMPPPTTKE DVTMATVMGS LPDVRQACLQ MAISWHLSRR 600
    QPDMVPLGHH KEKYFSGPKP KAVLNQFRTD LEKLEKEITA RNEQLDWPYE 650
    YLKPSCIENS VTI 663
    Length:663
    Mass (Da):75,694
    Last modified:February 6, 2007 - v4
    Checksum:iC4D6D5B320666A77
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti189 – 1924RVYT → PCLH in AAA51533. (PubMed:2244907)Curated
    Sequence conflicti345 – 3451S → C in AAA51533. (PubMed:2244907)Curated
    Sequence conflicti389 – 3891L → P in AAA60056. (PubMed:2377602)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti259 – 2591E → K.
    Corresponds to variant rs4987104 [ dbSNP | Ensembl ].
    VAR_030471
    Natural varianti261 – 2611Q → R.6 Publications
    Corresponds to variant rs1126667 [ dbSNP | Ensembl ].
    VAR_018743
    Natural varianti298 – 2981A → T.
    VAR_004279
    Natural varianti322 – 3221N → S.3 Publications
    Corresponds to variant rs434473 [ dbSNP | Ensembl ].
    VAR_018744
    Natural varianti430 – 4301R → H.1 Publication
    Corresponds to variant rs11571342 [ dbSNP | Ensembl ].
    VAR_018745

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.

    Genome annotation databases

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

    Polymorphism databases

    DMDMi125987838.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    SeattleSNPs
    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS11084.1.
    PIRi A38283.
    RefSeqi NP_000688.2. NM_000697.2.
    UniGenei Hs.654431.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2ABU model - A 2-663 [» ]
    3D3L X-ray 2.60 A/B 172-663 [» ]
    ProteinModelPortali P18054.
    SMRi P18054. Positions 2-663.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106740. 4 interactions.
    IntActi P18054. 4 interactions.
    MINTi MINT-1206406.
    STRINGi 9606.ENSP00000251535.

    Chemistry

    BindingDBi P18054.
    ChEMBLi CHEMBL3687.

    PTM databases

    PhosphoSitei P18054.

    Polymorphism databases

    DMDMi 125987838.

    Proteomic databases

    PaxDbi P18054.
    PRIDEi P18054.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000251535 ; ENSP00000251535 ; ENSG00000108839 .
    GeneIDi 239.
    KEGGi hsa:239.
    UCSCi uc002gdx.4. human.

    Organism-specific databases

    CTDi 239.
    GeneCardsi GC17P006899.
    H-InvDB HIX0039067.
    HGNCi HGNC:429. ALOX12.
    HPAi CAB019287.
    HPA010691.
    MIMi 114500. phenotype.
    133239. phenotype.
    152391. gene.
    neXtProti NX_P18054.
    PharmGKBi PA45.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG69653.
    HOGENOMi HOG000234358.
    HOVERGENi HBG005150.
    InParanoidi P18054.
    KOi K00458.
    OMAi QNQLCHF.
    OrthoDBi EOG7B05CG.
    PhylomeDBi P18054.
    TreeFami TF105320.

    Enzyme and pathway databases

    UniPathwayi UPA00881 .
    BioCyci MetaCyc:HS03167-MONOMER.
    Reactomei REACT_150201. Synthesis of 12-eicosatetraenoic acid derivatives.
    REACT_150292. Synthesis of Hepoxilins (HX) and Trioxilins (TrX).
    REACT_150320. Synthesis of Lipoxins (LX).

    Miscellaneous databases

    EvolutionaryTracei P18054.
    GeneWikii ALOX12.
    GenomeRNAii 239.
    NextBioi 952.
    PROi P18054.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P18054.
    Bgeei P18054.
    CleanExi HS_ALOX12.
    Genevestigatori P18054.

    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], VARIANT SER-322.
    2. "Molecular cloning, primary structure, and expression of the human platelet/erythroleukemia cell 12-lipoxygenase."
      Funk C.D., Furci L., Fitzgerald G.A.
      Proc. Natl. Acad. Sci. U.S.A. 87:5638-5642(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-322.
    3. Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-261.
    4. SeattleSNPs variation discovery resource
      Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-261; SER-322 AND HIS-430.
    5. "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].
    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], VARIANT ARG-261.
    7. "Structure and chromosomal localization of human arachidonate 12-lipoxygenase gene."
      Yoshimoto T., Arakawa T., Hada T., Yamamoto S., Takahashi E.
      J. Biol. Chem. 267:24805-24809(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-112.
    8. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-45.
    9. "Epidermis contains platelet-type 12-lipoxygenase that is overexpressed in germinal layer keratinocytes in psoriasis."
      Hussain H., Shornick L.P., Shannon V.R., Wilson J.D., Funk C.D., Pentland A.P., Holtzman M.J.
      Am. J. Physiol. 266:C243-C253(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 340-427.
      Tissue: Skin.
    10. "EU-IMAGE: full-insert length sequencing of human cDNA clones."
      Persson A.E., Lundeberg J., Uhlen M.
      Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 531-663.
    11. "Catalytic properties of human platelet 12-lipoxygenase as compared with the enzymes of other origins."
      Hada T., Ueda N., Takahashi Y., Yamamoto S.
      Biochim. Biophys. Acta 1083:89-93(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, KINETIC PARAMETERS, PATHWAY, SUBSTRATE SPECIFICITY.
    12. "Lipoxin synthase activity of human platelet 12-lipoxygenase."
      Romano M., Chen X.S., Takahashi Y., Yamamoto S., Funk C.D., Serhan C.N.
      Biochem. J. 296:127-133(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN LIPOXIN SYNTHESIS, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, REACTION MECHANISM.
    13. "Purification and characterization of recombinant histidine-tagged human platelet 12-lipoxygenase expressed in a baculovirus/insect cell system."
      Chen X.S., Brash A.R., Funk C.D.
      Eur. J. Biochem. 214:845-852(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, KINETIC PARAMETERS, PH DEPENDENCE, SUBCELLULAR LOCATION.
    14. "Structure-function properties of human platelet 12-lipoxygenase: chimeric enzyme and in vitro mutagenesis studies."
      Chen X.S., Funk C.D.
      FASEB J. 7:694-701(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-355; HIS-360; HIS-365; HIS-383; HIS-392; LYS-416; ALA-417; VAL-418 AND HIS-540.
    15. "12-Lipoxygenase in A431 cells: genetic identity, modulation of expression, and intracellular localization."
      Hagmann W., Gao X., Timar J., Chen Y.Q., Strohmaier A.R., Fahrenkopf C., Kagawa D., Lee M., Zacharek A., Honn K.V.
      Exp. Cell Res. 228:197-205(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, ENZYME REGULATION, INDUCTION.
    16. "Platelet-type 12-lipoxygenase in a human prostate carcinoma stimulates angiogenesis and tumor growth."
      Nie D., Hillman G.G., Geddes T., Tang K., Pierson C., Grignon D.J., Honn K.V.
      Cancer Res. 58:4047-4051(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ANGIOGENESIS.
    17. "Mechanisms regulating tumor angiogenesis by 12-lipoxygenase in prostate cancer cells."
      Nie D., Krishnamoorthy S., Jin R., Tang K., Chen Y., Qiao Y., Zacharek A., Guo Y., Milanini J., Pages G., Honn K.V.
      J. Biol. Chem. 281:18601-18609(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ANGIOGENESIS.
    18. "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.
    19. Cited for: FUNCTION IN CELL MIGRATION.
    20. "12S-Lipoxygenase is necessary for human vascular smooth muscle cell survival."
      Weisinger G., Grafi-Cohen M., Hirsh M., Knoll E., Sharon O., Many A., Limor R., Stern N.
      Exp. Cell Res. 319:1586-1593(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN APOPTOTIC PROCESS, TISSUE SPECIFICITY.
    21. "Crystal structure of the lipoxygenase domain of human arachidonate 12-lipoxygenase, 12s-type."
      Structural genomics consortium (SGC)
      Submitted (FEB-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 172-662 IN COMPLEX WITH IRON IONS.
    22. "Arachidonate lipoxygenase (ALOX) and cyclooxygenase (COX) polymorphisms and colon cancer risk."
      Goodman J.E., Bowman E.D., Chanock S.J., Alberg A.J., Harris C.C.
      Carcinogenesis 25:2467-2472(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ARG-261.
    23. "Associations of functional polymorphisms in cyclooxygenase-2 and platelet 12-lipoxygenase with risk of occurrence and advanced disease status of colorectal cancer."
      Tan W., Wu J., Zhang X., Guo Y., Liu J., Sun T., Zhang B., Zhao D., Yang M., Yu D., Lin D.
      Carcinogenesis 28:1197-1201(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ARG-261, INVOLVEMENT IN COLORECTAL CANCER.
    24. "Platelet 12-lipoxygenase Arg261Gln polymorphism: functional characterization and association with risk of esophageal squamous cell carcinoma in combination with COX-2 polymorphisms."
      Guo Y., Zhang X., Tan W., Miao X., Sun T., Zhao D., Lin D.
      Pharmacogenet. Genomics 17:197-205(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ARG-261, INVOLVEMENT IN ESOPHAGEAL CANCER.

    Entry informationi

    Entry nameiLOX12_HUMAN
    AccessioniPrimary (citable) accession number: P18054
    Secondary accession number(s): O95569, Q6ISF8, Q9UQM4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: February 6, 2007
    Last modified: October 1, 2014
    This is version 160 of the entry and version 4 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

    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