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Protein

Arachidonate 5-lipoxygenase

Gene

ALOX5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

Protein has several cofactor binding sites:
  • Fe cationPROSITE-ProRule annotation1 PublicationNote: Binds 1 Fe cation per subunit.PROSITE-ProRule annotation1 Publication
  • Ca2+By similarityNote: Binds 2 calcium ions per subunit.By similarity

Pathwayi: leukotriene A4 biosynthesis

This protein is involved in the pathway leukotriene A4 biosynthesis, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway leukotriene A4 biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi17Calcium 1; via carbonyl oxygen; structuralBy similarity1
Metal bindingi18Calcium 2; via carbonyl oxygen; structuralBy similarity1
Metal bindingi19Calcium 2; structuralBy similarity1
Metal bindingi44Calcium 2; structuralBy similarity1
Metal bindingi45Calcium 2; via carbonyl oxygen; structuralBy similarity1
Metal bindingi47Calcium 2; structuralBy similarity1
Metal bindingi79Calcium 1; via carbonyl oxygen; structuralBy similarity1
Metal bindingi80Calcium 1; via carbonyl oxygen; structuralBy similarity1
Sitei103Essential for stabilizing binding to COTL11
Metal bindingi368Iron; catalytic1
Metal bindingi373Iron; catalytic1
Metal bindingi551Iron; catalytic1
Metal bindingi555Iron; catalytic1
Metal bindingi674Iron; via carboxylate; catalytic1

GO - Molecular functioni

  • arachidonate 5-lipoxygenase activity Source: UniProtKB
  • iron ion binding Source: UniProtKB

GO - Biological processi

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.
ZFISH:HS00336-MONOMER.
BRENDAi1.13.11.34. 2681.
ReactomeiR-HSA-2142688. Synthesis of 5-eicosatetraenoic acids.
R-HSA-2142691. Synthesis of Leukotrienes (LT) and Eoxins (EX).
R-HSA-2142700. Synthesis of Lipoxins (LX).
R-HSA-6798695. Neutrophil degranulation.
SABIO-RKP09917.
SIGNORiP09917.
UniPathwayiUPA00877.

Chemistry databases

SwissLipidsiSLP:000000669.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:435. ALOX5.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • extracellular space Source: UniProtKB
  • nuclear envelope Source: UniProtKB
  • nuclear envelope lumen Source: UniProtKB
  • nuclear matrix Source: UniProtKB
  • nuclear membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi103W → A: Abolishes binding to COTL1. 1 Publication1
Mutagenesisi272S → A: Loss of phosphorylation site. Permits export from the nucleus. 1 Publication1
Mutagenesisi359D → N: No loss of activity. 1
Mutagenesisi363H → S or N: Still some substantial activity. 1 Publication1
Mutagenesisi368H → S, N or A: No activity. 2 Publications1
Mutagenesisi373H → S or N: No activity. 2 Publications1
Mutagenesisi377E → Q: No activity. 1 Publication1
Mutagenesisi391H → A: No activity. 2 Publications1
Mutagenesisi391H → S or N: Still some substantial activity. 2 Publications1
Mutagenesisi400H → A: No activity. 2 Publications1
Mutagenesisi400H → S or N: Still some substantial activity. 2 Publications1
Mutagenesisi433H → N or A: Almost no loss of activity. 1
Mutagenesisi524S → A: Prevents phosphorylation by PKA. 1 Publication1
Mutagenesisi551H → N or A: No activity. 1 Publication1

Organism-specific databases

DisGeNETi240.
MalaCardsiALOX5.
OpenTargetsiENSG00000012779.
ENSG00000275565.
PharmGKBiPA46.

Chemistry databases

ChEMBLiCHEMBL215.
DrugBankiDB00233. 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.
GuidetoPHARMACOLOGYi1385.

Polymorphism and mutation databases

BioMutaiALOX5.
DMDMi126407.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002206931 – 674Arachidonate 5-lipoxygenaseAdd BLAST674

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei272Phosphoserine; by MAPKAPK22 Publications1
Modified residuei524Phosphoserine; by PKA1 Publication1

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

EPDiP09917.
MaxQBiP09917.
PaxDbiP09917.
PeptideAtlasiP09917.
PRIDEiP09917.

PTM databases

iPTMnetiP09917.
PhosphoSitePlusiP09917.

Miscellaneous databases

PMAP-CutDBP09917.

Expressioni

Gene expression databases

BgeeiENSG00000012779.
CleanExiHS_ALOX5.
ExpressionAtlasiP09917. baseline and differential.
GenevisibleiP09917. HS.

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
CEP57L1Q8IYX8-23EBI-79934,EBI-10181988
CEP63Q96MT83EBI-79934,EBI-741977
COTL1Q140194EBI-79934,EBI-79926
FGRP097692EBI-79934,EBI-1383732
HCKP086312EBI-79934,EBI-346340
HHIPL2Q6UWX43EBI-79934,EBI-10196655
MAD1L1Q9Y6D95EBI-79934,EBI-742610
MEOX1P502213EBI-79934,EBI-2864512
NUTM1Q86Y263EBI-79934,EBI-10178410
PRKACAP176122EBI-79934,EBI-476586
RELQ048643EBI-79934,EBI-307352
SYCE1Q8N0S23EBI-79934,EBI-6872807
YES1P079472EBI-79934,EBI-515331

Protein-protein interaction databases

BioGridi106741. 56 interactors.
DIPiDIP-30950N.
IntActiP09917. 20 interactors.
STRINGi9606.ENSP00000363512.

Chemistry databases

BindingDBiP09917.

Structurei

Secondary structure

1674
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 10Combined sources7
Beta strandi20 – 30Combined sources11
Beta strandi36 – 38Combined sources3
Beta strandi51 – 56Combined sources6
Beta strandi64 – 73Combined sources10
Beta strandi75 – 77Combined sources3
Beta strandi81 – 89Combined sources9
Beta strandi95 – 104Combined sources10
Beta strandi106 – 108Combined sources3
Beta strandi110 – 113Combined sources4
Helixi120 – 122Combined sources3
Helixi126 – 142Combined sources17
Beta strandi155 – 157Combined sources3
Helixi161 – 163Combined sources3
Helixi166 – 168Combined sources3
Beta strandi171 – 176Combined sources6
Helixi178 – 188Combined sources11
Helixi192 – 194Combined sources3
Helixi205 – 212Combined sources8
Turni213 – 215Combined sources3
Helixi218 – 226Combined sources9
Helixi230 – 239Combined sources10
Helixi260 – 263Combined sources4
Turni264 – 266Combined sources3
Helixi273 – 278Combined sources6
Beta strandi282 – 286Combined sources5
Helixi288 – 290Combined sources3
Beta strandi297 – 300Combined sources4
Helixi303 – 306Combined sources4
Beta strandi310 – 315Combined sources6
Beta strandi321 – 331Combined sources11
Beta strandi333 – 336Combined sources4
Helixi345 – 365Combined sources21
Helixi366 – 372Combined sources7
Helixi373 – 386Combined sources14
Helixi392 – 397Combined sources6
Helixi398 – 400Combined sources3
Helixi404 – 414Combined sources11
Helixi421 – 423Combined sources3
Turni427 – 431Combined sources5
Helixi432 – 441Combined sources10
Helixi447 – 449Combined sources3
Helixi451 – 457Combined sources7
Turni463 – 465Combined sources3
Helixi470 – 493Combined sources24
Helixi497 – 501Combined sources5
Helixi504 – 515Combined sources12
Turni516 – 520Combined sources5
Helixi522 – 524Combined sources3
Helixi533 – 547Combined sources15
Helixi549 – 555Combined sources7
Helixi558 – 562Combined sources5
Helixi565 – 567Combined sources3
Beta strandi572 – 574Combined sources3
Beta strandi579 – 581Combined sources3
Helixi585 – 591Combined sources7
Helixi595 – 608Combined sources14
Helixi629 – 653Combined sources25
Helixi665 – 667Combined sources3
Beta strandi669 – 671Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09917.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 118PLATPROSITE-ProRule annotationAdd BLAST117
Domaini119 – 674LipoxygenasePROSITE-ProRule annotationAdd BLAST556

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG410IF0U. Eukaryota.
ENOG410YN4N. LUCA.
GeneTreeiENSGT00550000074415.
HOGENOMiHOG000234358.
HOVERGENiHBG005150.
InParanoidiP09917.
KOiK00461.
OMAiMQHWKED.
OrthoDBiEOG091G04A4.
PhylomeDBiP09917.
TreeFamiTF105320.

Family and domain databases

Gene3Di2.60.60.20. 1 hit.
InterProiIPR000907. 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. AlignAdd to basket

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)DescriptionActionsGraphical viewLength
Natural variantiVAR_028018254E → K.1 PublicationCorresponds to variant rs2228065dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_053534424 – 455Missing in isoform 3. 1 PublicationAdd BLAST32
Alternative sequenceiVSP_053535425 – 533ANATG…SVKSR → VHGRGGRHLLRGRPGGGGGP GAAGLRERCLRVRHAGPQVL RLPQVGQEPGAAVGVPDRGD LHRLRPARRGQLRPAVPGHV PRRAFYREACEGSHGPIPQE PRGHCQRDC in isoform 4. 1 PublicationAdd BLAST109
Alternative sequenceiVSP_053536485 – 674Missing in isoform 5. 1 PublicationAdd BLAST190
Alternative sequenceiVSP_053537534 – 674Missing in isoform 4. 1 PublicationAdd BLAST141
Alternative sequenceiVSP_046998559 – 615Missing in isoform 2. 2 PublicationsAdd BLAST57

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_000698.4. [P09917-1]
NP_001243082.1. NM_001256153.2. [P09917-3]
NP_001243083.1. NM_001256154.2. [P09917-2]
NP_001307790.1. NM_001320861.1.
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.5. human. [P09917-1]

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:
EMBLi
GenBanki
DDBJi
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_000698.4. [P09917-1]
NP_001243082.1. NM_001256153.2. [P09917-3]
NP_001243083.1. NM_001256154.2. [P09917-2]
NP_001307790.1. NM_001320861.1.
UniGeneiHs.89499.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106741. 56 interactors.
DIPiDIP-30950N.
IntActiP09917. 20 interactors.
STRINGi9606.ENSP00000363512.

Chemistry databases

BindingDBiP09917.
ChEMBLiCHEMBL215.
DrugBankiDB00233. 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.
GuidetoPHARMACOLOGYi1385.
SwissLipidsiSLP:000000669.

PTM databases

iPTMnetiP09917.
PhosphoSitePlusiP09917.

Polymorphism and mutation databases

BioMutaiALOX5.
DMDMi126407.

Proteomic databases

EPDiP09917.
MaxQBiP09917.
PaxDbiP09917.
PeptideAtlasiP09917.
PRIDEiP09917.

Protocols and materials databases

DNASUi240.
Structural Biology KnowledgebaseSearch...

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.5. human. [P09917-1]

Organism-specific databases

CTDi240.
DisGeNETi240.
GeneCardsiALOX5.
HGNCiHGNC:435. ALOX5.
HPAiCAB005066.
MalaCardsiALOX5.
MIMi152390. gene.
neXtProtiNX_P09917.
OpenTargetsiENSG00000012779.
ENSG00000275565.
PharmGKBiPA46.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IF0U. Eukaryota.
ENOG410YN4N. LUCA.
GeneTreeiENSGT00550000074415.
HOGENOMiHOG000234358.
HOVERGENiHBG005150.
InParanoidiP09917.
KOiK00461.
OMAiMQHWKED.
OrthoDBiEOG091G04A4.
PhylomeDBiP09917.
TreeFamiTF105320.

Enzyme and pathway databases

UniPathwayiUPA00877.
BioCyciMetaCyc:HS00336-MONOMER.
ZFISH:HS00336-MONOMER.
BRENDAi1.13.11.34. 2681.
ReactomeiR-HSA-2142688. Synthesis of 5-eicosatetraenoic acids.
R-HSA-2142691. Synthesis of Leukotrienes (LT) and Eoxins (EX).
R-HSA-2142700. Synthesis of Lipoxins (LX).
R-HSA-6798695. Neutrophil degranulation.
SABIO-RKP09917.
SIGNORiP09917.

Miscellaneous databases

ChiTaRSiALOX5. human.
EvolutionaryTraceiP09917.
GeneWikiiArachidonate_5-lipoxygenase.
GenomeRNAii240.
PMAP-CutDBP09917.
PROiP09917.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000012779.
CleanExiHS_ALOX5.
ExpressionAtlasiP09917. baseline and differential.
GenevisibleiP09917. HS.

Family and domain databases

Gene3Di2.60.60.20. 1 hit.
InterProiIPR000907. 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.
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ProtoNetiSearch...

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: November 30, 2016
This is version 184 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.