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P09917

- LOX5_HUMAN

UniProt

P09917 - LOX5_HUMAN

Protein

Arachidonate 5-lipoxygenase

Gene

ALOX5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 162 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalyzes the first step in leukotriene biosynthesis, and thereby plays a role in inflammatory processes.1 Publication

    Catalytic activityi

    Arachidonate + O2 = leukotriene A4 + H2O.1 Publication

    Cofactori

    Binds 1 iron ion per subunit.1 PublicationPROSITE-ProRule annotation
    Binds 2 calcium ions per subunit.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi17 – 171Calcium 1; via carbonyl oxygen; structuralBy similarity
    Metal bindingi18 – 181Calcium 2; via carbonyl oxygen; structuralBy similarity
    Metal bindingi19 – 191Calcium 2; structuralBy similarity
    Metal bindingi44 – 441Calcium 2; structuralBy similarity
    Metal bindingi45 – 451Calcium 2; via carbonyl oxygen; structuralBy similarity
    Metal bindingi47 – 471Calcium 2; structuralBy similarity
    Metal bindingi79 – 791Calcium 1; via carbonyl oxygen; structuralBy similarity
    Metal bindingi80 – 801Calcium 1; via carbonyl oxygen; structuralBy similarity
    Sitei103 – 1031Essential for stabilizing binding to COTL1
    Metal bindingi368 – 3681Iron; catalytic
    Metal bindingi373 – 3731Iron; catalytic
    Metal bindingi551 – 5511Iron; catalytic
    Metal bindingi555 – 5551Iron; catalytic
    Metal bindingi674 – 6741Iron; via carboxylate; catalytic

    GO - Molecular functioni

    1. arachidonate 5-lipoxygenase activity Source: UniProtKB
    2. iron ion binding Source: UniProtKB
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. arachidonic acid metabolic process Source: Reactome
    2. leukotriene biosynthetic process Source: UniProtKB
    3. leukotriene metabolic process Source: Reactome
    4. leukotriene production involved in inflammatory response Source: Ensembl
    5. lipoxin metabolic process Source: Reactome
    6. lipoxygenase pathway Source: Reactome
    7. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Dioxygenase, Oxidoreductase

    Keywords - Biological processi

    Leukotriene biosynthesis

    Keywords - Ligandi

    Calcium, Iron, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS00336-MONOMER.
    ReactomeiREACT_150209. Synthesis of 5-eicosatetraenoic acids.
    REACT_150320. Synthesis of Lipoxins (LX).
    REACT_150420. Synthesis of Leukotrienes (LT) and Eoxins (EX).
    UniPathwayiUPA00877.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Arachidonate 5-lipoxygenase (EC:1.13.11.34)
    Short name:
    5-LO
    Short name:
    5-lipoxygenase
    Gene namesi
    Name:ALOX5
    Synonyms:LOG5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:435. ALOX5.

    Subcellular locationi

    Cytoplasm. Nucleus matrix. Nucleus membrane; Peripheral membrane protein
    Note: Shuttles between cytoplasm and nucleus. Found exclusively in the nucleus, when phosphorylated on Ser-272. Calcium binding promotes translocation from the cytosol and the nuclear matrix to the nuclear envelope and membrane association.

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. extracellular space Source: UniProt
    3. nuclear envelope Source: UniProtKB
    4. nuclear envelope lumen Source: UniProtKB
    5. nuclear matrix Source: UniProtKB
    6. nuclear membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi103 – 1031W → A: Abolishes binding to COTL1. 1 Publication
    Mutagenesisi272 – 2721S → A: Loss of phosphorylation site. Permits export from the nucleus. 1 Publication
    Mutagenesisi359 – 3591D → N: No loss of activity.
    Mutagenesisi363 – 3631H → S or N: Still some substantial activity. 1 Publication
    Mutagenesisi368 – 3681H → S, N or A: No activity. 2 Publications
    Mutagenesisi373 – 3731H → S or N: No activity. 2 Publications
    Mutagenesisi377 – 3771E → Q: No activity. 1 Publication
    Mutagenesisi391 – 3911H → A: No activity. 2 Publications
    Mutagenesisi391 – 3911H → S or N: Still some substantial activity. 2 Publications
    Mutagenesisi400 – 4001H → A: No activity. 2 Publications
    Mutagenesisi400 – 4001H → S or N: Still some substantial activity. 2 Publications
    Mutagenesisi433 – 4331H → N or A: Almost no loss of activity.
    Mutagenesisi524 – 5241S → A: Prevents phosphorylation by PKA. 1 Publication
    Mutagenesisi551 – 5511H → N or A: No activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA46.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 674674Arachidonate 5-lipoxygenasePRO_0000220693Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei272 – 2721Phosphoserine; by MAPKAPK22 Publications
    Modified residuei524 – 5241Phosphoserine; by PKA1 Publication

    Post-translational modificationi

    Serine phosphorylation by MAPKAPK2 is stimulated by arachidonic acid. Phosphorylation on Ser-523 by PKA has an inhibitory effect. Phosphorylation on Ser-272 prevents export from the nucleus.3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP09917.
    PaxDbiP09917.
    PRIDEiP09917.

    PTM databases

    PhosphoSiteiP09917.

    Miscellaneous databases

    PMAP-CutDBP09917.

    Expressioni

    Gene expression databases

    ArrayExpressiP09917.
    BgeeiP09917.
    CleanExiHS_ALOX5.
    GenevestigatoriP09917.

    Organism-specific databases

    HPAiCAB005066.

    Interactioni

    Subunit structurei

    Interacts with ALOX5AP and LTC4S. Interacts with COTL1, the interaction is required for stability and efficient catalytic activity.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    COTL1Q140194EBI-79934,EBI-79926
    FGRP097692EBI-79934,EBI-1383732
    HCKP086312EBI-79934,EBI-346340
    PRKACAP176122EBI-79934,EBI-476586
    YES1P079472EBI-79934,EBI-515331

    Protein-protein interaction databases

    BioGridi106741. 10 interactions.
    IntActiP09917. 9 interactions.
    STRINGi9606.ENSP00000363512.

    Structurei

    Secondary structure

    1
    674
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 107
    Beta strandi20 – 3011
    Beta strandi36 – 383
    Beta strandi51 – 566
    Beta strandi64 – 7310
    Beta strandi75 – 773
    Beta strandi81 – 899
    Beta strandi95 – 10410
    Beta strandi106 – 1083
    Beta strandi110 – 1134
    Helixi120 – 1223
    Helixi126 – 14217
    Beta strandi155 – 1573
    Helixi161 – 1633
    Helixi166 – 1683
    Beta strandi171 – 1766
    Helixi178 – 18811
    Helixi192 – 1943
    Helixi205 – 2128
    Turni213 – 2153
    Helixi218 – 2269
    Helixi230 – 23910
    Helixi260 – 2634
    Turni264 – 2663
    Helixi273 – 2786
    Beta strandi282 – 2865
    Helixi288 – 2903
    Helixi303 – 3064
    Beta strandi310 – 3156
    Beta strandi321 – 33111
    Beta strandi333 – 3364
    Helixi345 – 36521
    Helixi366 – 3727
    Helixi373 – 38614
    Helixi392 – 3976
    Helixi398 – 4003
    Helixi404 – 41411
    Helixi421 – 4233
    Turni427 – 4315
    Helixi432 – 44110
    Helixi447 – 4493
    Helixi451 – 4577
    Turni463 – 4653
    Helixi470 – 49324
    Helixi497 – 5015
    Helixi504 – 51512
    Turni516 – 5205
    Helixi522 – 5243
    Helixi533 – 54715
    Helixi549 – 5557
    Helixi558 – 5625
    Helixi565 – 5673
    Beta strandi572 – 5743
    Beta strandi579 – 5813
    Helixi585 – 5917
    Helixi595 – 60814
    Helixi629 – 65325
    Helixi665 – 6673
    Beta strandi669 – 6713

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2ABVmodel-A2-674[»]
    3O8YX-ray2.39A/B1-674[»]
    3V92X-ray2.74A/B1-674[»]
    3V98X-ray2.07A/B1-674[»]
    3V99X-ray2.25A/B1-674[»]
    ProteinModelPortaliP09917.
    SMRiP09917. Positions 2-674.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP09917.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 118117PLATPROSITE-ProRule annotationAdd
    BLAST
    Domaini119 – 674556LipoxygenasePROSITE-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.
    InParanoidiP09917.
    KOiK00461.
    OMAiNYSKAME.
    OrthoDBiEOG7B05CG.
    PhylomeDBiP09917.
    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 (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

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

    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

    MPSYTVTVAT GSQWFAGTDD YIYLSLVGSA GCSEKHLLDK PFYNDFERGA    50
    VDSYDVTVDE ELGEIQLVRI EKRKYWLNDD WYLKYITLKT PHGDYIEFPC 100
    YRWITGDVEV VLRDGRAKLA RDDQIHILKQ HRRKELETRQ KQYRWMEWNP 150
    GFPLSIDAKC HKDLPRDIQF DSEKGVDFVL NYSKAMENLF INRFMHMFQS 200
    SWNDFADFEK IFVKISNTIS ERVMNHWQED LMFGYQFLNG CNPVLIRRCT 250
    ELPEKLPVTT EMVECSLERQ LSLEQEVQQG NIFIVDFELL DGIDANKTDP 300
    CTLQFLAAPI CLLYKNLANK IVPIAIQLNQ IPGDENPIFL PSDAKYDWLL 350
    AKIWVRSSDF HVHQTITHLL RTHLVSEVFG IAMYRQLPAV HPIFKLLVAH 400
    VRFTIAINTK AREQLICECG LFDKANATGG GGHVQMVQRA MKDLTYASLC 450
    FPEAIKARGM ESKEDIPYYF YRDDGLLVWE AIRTFTAEVV DIYYEGDQVV 500
    EEDPELQDFV NDVYVYGMRG RKSSGFPKSV KSREQLSEYL TVVIFTASAQ 550
    HAAVNFGQYD WCSWIPNAPP TMRAPPPTAK GVVTIEQIVD TLPDRGRSCW 600
    HLGAVWALSQ FQENELFLGM YPEEHFIEKP VKEAMARFRK NLEAIVSVIA 650
    ERNKKKQLPY YYLSPDRIPN SVAI 674
    Length:674
    Mass (Da):77,983
    Last modified:January 23, 2007 - v2
    Checksum:i36F38C0A9E86BB21
    GO
    Isoform 2 (identifier: P09917-2) [UniParc]FASTAAdd to Basket

    Also known as: Delta-13

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

    Show »
    Length:617
    Mass (Da):71,564
    Checksum:i3DE1D2FE62471315
    GO
    Isoform 3 (identifier: P09917-3) [UniParc]FASTAAdd to Basket

    Also known as: delta-p10

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

    Show »
    Length:642
    Mass (Da):74,635
    Checksum:iE9A8CCA67CF74DB6
    GO
    Isoform 4 (identifier: P09917-4) [UniParc]FASTAAdd to Basket

    Also known as: delta-10-13

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

    Show »
    Length:533
    Mass (Da):61,244
    Checksum:i6C57FD0816BD2D9E
    GO
    Isoform 5 (identifier: P09917-5) [UniParc]FASTAAdd to Basket

    Also known as: alpha-10

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

    Show »
    Length:484
    Mass (Da):56,291
    Checksum:i4A500F8D7404EC9D
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti254 – 2541E → K.1 Publication
    Corresponds to variant rs2228065 [ dbSNP | Ensembl ].
    VAR_028018

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei424 – 45532Missing in isoform 3. 1 PublicationVSP_053534Add
    BLAST
    Alternative sequencei425 – 533109ANATG…SVKSR → VHGRGGRHLLRGRPGGGGGP GAAGLRERCLRVRHAGPQVL RLPQVGQEPGAAVGVPDRGD LHRLRPARRGQLRPAVPGHV PRRAFYREACEGSHGPIPQE PRGHCQRDC in isoform 4. 1 PublicationVSP_053535Add
    BLAST
    Alternative sequencei485 – 674190Missing in isoform 5. 1 PublicationVSP_053536Add
    BLAST
    Alternative sequencei534 – 674141Missing in isoform 4. 1 PublicationVSP_053537Add
    BLAST
    Alternative sequencei559 – 61557Missing in isoform 2. 2 PublicationsVSP_046998Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03600 mRNA. Translation: AAA36183.1.
    J03571 mRNA. Translation: AAA65450.1.
    HM592258 mRNA. Translation: ADR30798.1.
    HM592259 mRNA. Translation: ADR30799.1.
    HM592260 mRNA. Translation: ADR30800.1.
    HM592261 mRNA. Translation: ADR30801.1.
    J04520 Genomic DNA. Translation: AAA59522.1.
    AL731567 Genomic DNA. Translation: CAI41243.1.
    BC130332 mRNA. Translation: AAI30333.1.
    BC132677 mRNA. Translation: AAI32678.1.
    BC143985 mRNA. Translation: AAI43986.1.
    M38191 Genomic DNA. Translation: AAA63212.1.
    CCDSiCCDS58078.1. [P09917-2]
    CCDS7212.1. [P09917-1]
    PIRiA28117. DAHUAL.
    RefSeqiNP_000689.1. NM_000698.3. [P09917-1]
    NP_001243082.1. NM_001256153.1. [P09917-3]
    NP_001243083.1. NM_001256154.1. [P09917-2]
    UniGeneiHs.89499.

    Genome annotation databases

    EnsembliENST00000374391; ENSP00000363512; ENSG00000012779. [P09917-1]
    ENST00000542434; ENSP00000437634; ENSG00000012779. [P09917-2]
    GeneIDi240.
    KEGGihsa:240.
    UCSCiuc001jce.4. human. [P09917-1]
    uc010qfg.3. human.

    Polymorphism databases

    DMDMi126407.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03600 mRNA. Translation: AAA36183.1 .
    J03571 mRNA. Translation: AAA65450.1 .
    HM592258 mRNA. Translation: ADR30798.1 .
    HM592259 mRNA. Translation: ADR30799.1 .
    HM592260 mRNA. Translation: ADR30800.1 .
    HM592261 mRNA. Translation: ADR30801.1 .
    J04520 Genomic DNA. Translation: AAA59522.1 .
    AL731567 Genomic DNA. Translation: CAI41243.1 .
    BC130332 mRNA. Translation: AAI30333.1 .
    BC132677 mRNA. Translation: AAI32678.1 .
    BC143985 mRNA. Translation: AAI43986.1 .
    M38191 Genomic DNA. Translation: AAA63212.1 .
    CCDSi CCDS58078.1. [P09917-2 ]
    CCDS7212.1. [P09917-1 ]
    PIRi A28117. DAHUAL.
    RefSeqi NP_000689.1. NM_000698.3. [P09917-1 ]
    NP_001243082.1. NM_001256153.1. [P09917-3 ]
    NP_001243083.1. NM_001256154.1. [P09917-2 ]
    UniGenei Hs.89499.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2ABV model - A 2-674 [» ]
    3O8Y X-ray 2.39 A/B 1-674 [» ]
    3V92 X-ray 2.74 A/B 1-674 [» ]
    3V98 X-ray 2.07 A/B 1-674 [» ]
    3V99 X-ray 2.25 A/B 1-674 [» ]
    ProteinModelPortali P09917.
    SMRi P09917. Positions 2-674.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106741. 10 interactions.
    IntActi P09917. 9 interactions.
    STRINGi 9606.ENSP00000363512.

    Chemistry

    BindingDBi P09917.
    ChEMBLi CHEMBL215.
    DrugBanki DB00711. Diethylcarbamazine.
    DB00741. Hydrocortisone.
    DB01097. Leflunomide.
    DB00179. Masoprocol.
    DB00939. Meclofenamic acid.
    DB01017. Minocycline.
    DB00471. Montelukast.
    DB01103. Quinacrine.
    DB00163. Vitamin E.
    DB00744. Zileuton.
    GuidetoPHARMACOLOGYi 1385.

    PTM databases

    PhosphoSitei P09917.

    Polymorphism databases

    DMDMi 126407.

    Proteomic databases

    MaxQBi P09917.
    PaxDbi P09917.
    PRIDEi P09917.

    Protocols and materials databases

    DNASUi 240.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000374391 ; ENSP00000363512 ; ENSG00000012779 . [P09917-1 ]
    ENST00000542434 ; ENSP00000437634 ; ENSG00000012779 . [P09917-2 ]
    GeneIDi 240.
    KEGGi hsa:240.
    UCSCi uc001jce.4. human. [P09917-1 ]
    uc010qfg.3. human.

    Organism-specific databases

    CTDi 240.
    GeneCardsi GC10P045869.
    HGNCi HGNC:435. ALOX5.
    HPAi CAB005066.
    MIMi 152390. gene.
    neXtProti NX_P09917.
    PharmGKBi PA46.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG69653.
    HOGENOMi HOG000234358.
    HOVERGENi HBG005150.
    InParanoidi P09917.
    KOi K00461.
    OMAi NYSKAME.
    OrthoDBi EOG7B05CG.
    PhylomeDBi P09917.
    TreeFami TF105320.

    Enzyme and pathway databases

    UniPathwayi UPA00877 .
    BioCyci MetaCyc:HS00336-MONOMER.
    Reactomei REACT_150209. Synthesis of 5-eicosatetraenoic acids.
    REACT_150320. Synthesis of Lipoxins (LX).
    REACT_150420. Synthesis of Leukotrienes (LT) and Eoxins (EX).

    Miscellaneous databases

    ChiTaRSi ALOX5. human.
    EvolutionaryTracei P09917.
    GeneWikii Arachidonate_5-lipoxygenase.
    GenomeRNAii 240.
    NextBioi 35497584.
    PMAP-CutDB P09917.
    PROi P09917.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P09917.
    Bgeei P09917.
    CleanExi HS_ALOX5.
    Genevestigatori P09917.

    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 1), PARTIAL PROTEIN SEQUENCE.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. Erratum
      Matsumoto T., Funk C.D., Raadmark O., Hoeoeg J.-O., Joernvall H., Samuelsson B.
      Proc. Natl. Acad. Sci. U.S.A. 85:3406-3406(1988)
    4. "Molecular cloning and amino acid sequence of human 5-lipoxygenase."
      Matsumoto T., Funk C.D., Raadmark O., Hoeoeg J.-O., Joernvall H., Samuelsson B.
      Adv. Prostaglandin Thromboxane Leukotriene Res. 19:466-469(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
    5. "Novel 5-lipoxygenase isoforms affect the biosynthesis of 5-lipoxygenase products."
      Boudreau L.H., Bertin J., Robichaud P.P., Laflamme M., Ouellette R.J., Flamand N., Surette M.E.
      FASEB J. 25:1097-1105(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4 AND 5).
    6. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORMS 1 AND 2).
      Tissue: Brain.
    8. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-50.
    9. "Characterization of the human 5-lipoxygenase gene promoter."
      Hoshiko S., Raadmark O., Samuelsson B.
      Proc. Natl. Acad. Sci. U.S.A. 87:9073-9077(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
    10. "Reversible, calcium-dependent membrane association of human leukocyte 5-lipoxygenase."
      Rouzer C.A., Samuelsson B.
      Proc. Natl. Acad. Sci. U.S.A. 84:7393-7397(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    11. "Evaluation of the role of conserved His and Met residues among lipoxygenases by site-directed mutagenesis of recombinant human 5-lipoxygenase."
      Nguyen T., Falgueyret J.-P., Abramowitz M., Riendeau D.
      J. Biol. Chem. 266:22057-22062(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF HIS-363; HIS-368; HIS-373; HIS-391 AND HIS-400.
    12. "Mutagenesis studies on the amino acid residues involved in the iron-binding and the activity of human 5-lipoxygenase."
      Ishii S., Noguchi M., Miyano M., Matsumoto T., Noma M.
      Biochem. Biophys. Res. Commun. 182:1482-1490(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF HIS-368; HIS-373; GLU-377; HIS-391; HIS-400 AND HIS-551.
    13. "5-lipoxygenase and 5-lipoxygenase-activating protein are localized in the nuclear envelope of activated human leukocytes."
      Woods J.W., Evans J.F., Ethier D., Scott S., Vickers P.J., Hearn L., Heibein J.A., Charleson S., Singer I.I.
      J. Exp. Med. 178:1935-1946(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    14. "Arachidonic acid promotes phosphorylation of 5-lipoxygenase at Ser-271 by MAPK-activated protein kinase 2 (MK2)."
      Werz O., Szellas D., Steinhilber D., Radmark O.
      J. Biol. Chem. 277:14793-14800(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-272.
    15. "Protein kinase A inhibits leukotriene synthesis by phosphorylation of 5-lipoxygenase on serine 523."
      Luo M., Jones S.M., Phare S.M., Coffey M.J., Peters-Golden M., Brock T.G.
      J. Biol. Chem. 279:41512-41520(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-524, MUTAGENESIS OF SER-524.
    16. "Arachidonic acid regulates the translocation of 5-lipoxygenase to the nuclear membranes in human neutrophils."
      Flamand N., Lefebvre J., Surette M.E., Picard S., Borgeat P.
      J. Biol. Chem. 281:129-136(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    17. "Distinct parts of leukotriene C(4) synthase interact with 5-lipoxygenase and 5-lipoxygenase activating protein."
      Strid T., Svartz J., Franck N., Hallin E., Ingelsson B., Soederstroem M., Hammarstroem S.
      Biochem. Biophys. Res. Commun. 381:518-522(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ALOX5AP AND LTC4S, SUBCELLULAR LOCATION.
    18. "Phosphorylation of serine 271 on 5-lipoxygenase and its role in nuclear export."
      Flamand N., Luo M., Peters-Golden M., Brock T.G.
      J. Biol. Chem. 284:306-313(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-272, MUTAGENESIS OF SER-272.
    19. "Coactosin-like protein functions as a stabilizing chaperone for 5-lipoxygenase: role of tryptophan 102."
      Esser J., Rakonjac M., Hofmann B., Fischer L., Provost P., Schneider G., Steinhilber D., Samuelsson B., Radmark O.
      Biochem. J. 425:265-274(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH COTL1, MUTAGENESIS OF TRP-103.
    20. Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH IRON ION, COFACTOR, CATALYTIC ACTIVITY, FUNCTION.
    21. "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 LYS-254.

    Entry informationi

    Entry nameiLOX5_HUMAN
    AccessioniPrimary (citable) accession number: P09917
    Secondary accession number(s): B7ZLS0
    , E5FPY5, E5FPY7, E5FPY8, Q5JQ14
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 162 of the entry and version 2 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: 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