Skip Header

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

P09917

- LOX5_HUMAN

UniProt

P09917 - LOX5_HUMAN

(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)

Protein

Arachidonate 5-lipoxygenase

Gene

ALOX5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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

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
Complete GO annotation...

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
Complete GO annotation...

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

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.
GeneTreeiENSGT00550000074415.
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

        10         20         30         40         50
MPSYTVTVAT GSQWFAGTDD YIYLSLVGSA GCSEKHLLDK PFYNDFERGA
60 70 80 90 100
VDSYDVTVDE ELGEIQLVRI EKRKYWLNDD WYLKYITLKT PHGDYIEFPC
110 120 130 140 150
YRWITGDVEV VLRDGRAKLA RDDQIHILKQ HRRKELETRQ KQYRWMEWNP
160 170 180 190 200
GFPLSIDAKC HKDLPRDIQF DSEKGVDFVL NYSKAMENLF INRFMHMFQS
210 220 230 240 250
SWNDFADFEK IFVKISNTIS ERVMNHWQED LMFGYQFLNG CNPVLIRRCT
260 270 280 290 300
ELPEKLPVTT EMVECSLERQ LSLEQEVQQG NIFIVDFELL DGIDANKTDP
310 320 330 340 350
CTLQFLAAPI CLLYKNLANK IVPIAIQLNQ IPGDENPIFL PSDAKYDWLL
360 370 380 390 400
AKIWVRSSDF HVHQTITHLL RTHLVSEVFG IAMYRQLPAV HPIFKLLVAH
410 420 430 440 450
VRFTIAINTK AREQLICECG LFDKANATGG GGHVQMVQRA MKDLTYASLC
460 470 480 490 500
FPEAIKARGM ESKEDIPYYF YRDDGLLVWE AIRTFTAEVV DIYYEGDQVV
510 520 530 540 550
EEDPELQDFV NDVYVYGMRG RKSSGFPKSV KSREQLSEYL TVVIFTASAQ
560 570 580 590 600
HAAVNFGQYD WCSWIPNAPP TMRAPPPTAK GVVTIEQIVD TLPDRGRSCW
610 620 630 640 650
HLGAVWALSQ FQENELFLGM YPEEHFIEKP VKEAMARFRK NLEAIVSVIA
660 670
ERNKKKQLPY YYLSPDRIPN SVAI
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]
ENST00000610656; ENSP00000484468; ENSG00000275565. [P09917-1]
ENST00000622021; ENSP00000479958; ENSG00000275565. [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 DB00233. Aminosalicylic Acid.
DB01014. Balsalazide.
DB00586. Diclofenac.
DB00711. Diethylcarbamazine.
DB00179. Masoprocol.
DB00939. Meclofenamic acid.
DB00244. Mesalazine.
DB01017. Minocycline.
DB00471. Montelukast.
DB00795. Sulfasalazine.
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 ]
ENST00000610656 ; ENSP00000484468 ; ENSG00000275565 . [P09917-1 ]
ENST00000622021 ; ENSP00000479958 ; ENSG00000275565 . [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.
GeneTreei ENSGT00550000074415.
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

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

« Hide 'large scale' publications
  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 29, 2014
This is version 163 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