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P09917 (LOX5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 160. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Arachidonate 5-lipoxygenase

Short name=5-LO
Short name=5-lipoxygenase
EC=1.13.11.34
Gene names
Name:ALOX5
Synonyms:LOG5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length674 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the first step in leukotriene biosynthesis, and thereby plays a role in inflammatory processes. Ref.20

Catalytic activity

Arachidonate + O2 = leukotriene A4 + H2O. Ref.20

Cofactor

Binds 1 iron ion per subunit. Ref.20

Binds 2 calcium ions per subunit By similarity. Ref.20

Pathway

Lipid metabolism; leukotriene A4 biosynthesis.

Subunit structure

Interacts with ALOX5AP and LTC4S. Interacts with COTL1, the interaction is required for stability and efficient catalytic activity. Ref.17 Ref.19

Subcellular location

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. Ref.10 Ref.13 Ref.16 Ref.17 Ref.18

Post-translational modification

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.

Sequence similarities

Belongs to the lipoxygenase family.

Contains 1 lipoxygenase domain.

Contains 1 PLAT domain.

Ontologies

Keywords
   Biological processLeukotriene biosynthesis
   Cellular componentCytoplasm
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandCalcium
Iron
Metal-binding
   Molecular functionDioxygenase
Oxidoreductase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processarachidonic acid metabolic process

Traceable author statement. Source: Reactome

leukotriene biosynthetic process

Inferred from direct assay Ref.20. Source: UniProtKB

leukotriene metabolic process

Traceable author statement. Source: Reactome

leukotriene production involved in inflammatory response

Inferred from electronic annotation. Source: Ensembl

lipoxin metabolic process

Traceable author statement. Source: Reactome

lipoxygenase pathway

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Inferred from direct assay Ref.17. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 22664934. Source: UniProt

nuclear envelope

Inferred from direct assay Ref.17. Source: UniProtKB

nuclear envelope lumen

Inferred from direct assay Ref.13. Source: UniProtKB

nuclear matrix

Inferred from direct assay Ref.17. Source: UniProtKB

nuclear membrane

Inferred from direct assay Ref.13. Source: UniProtKB

   Molecular_functionarachidonate 5-lipoxygenase activity

Inferred from direct assay Ref.20. Source: UniProtKB

iron ion binding

Inferred from direct assay Ref.20. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 11297527PubMed 11785969Ref.17. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

COTL1Q140194EBI-79934,EBI-79926

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: P09917-1)

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.
Isoform 2 (identifier: P09917-2)

Also known as: Delta-13;

The sequence of this isoform differs from the canonical sequence as follows:
     559-615: Missing.
Isoform 3 (identifier: P09917-3)

Also known as: delta-p10;

The sequence of this isoform differs from the canonical sequence as follows:
     424-455: Missing.
Isoform 4 (identifier: P09917-4)

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.
Isoform 5 (identifier: P09917-5)

Also known as: alpha-10;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 674674Arachidonate 5-lipoxygenase
PRO_0000220693

Regions

Domain2 – 118117PLAT
Domain119 – 674556Lipoxygenase

Sites

Metal binding171Calcium 1; via carbonyl oxygen; structural By similarity
Metal binding181Calcium 2; via carbonyl oxygen; structural By similarity
Metal binding191Calcium 2; structural By similarity
Metal binding441Calcium 2; structural By similarity
Metal binding451Calcium 2; via carbonyl oxygen; structural By similarity
Metal binding471Calcium 2; structural By similarity
Metal binding791Calcium 1; via carbonyl oxygen; structural By similarity
Metal binding801Calcium 1; via carbonyl oxygen; structural By similarity
Metal binding3681Iron; catalytic
Metal binding3731Iron; catalytic
Metal binding5511Iron; catalytic
Metal binding5551Iron; catalytic
Metal binding6741Iron; via carboxylate; catalytic
Site1031Essential for stabilizing binding to COTL1

Amino acid modifications

Modified residue2721Phosphoserine; by MAPKAPK2 Ref.14 Ref.18
Modified residue5241Phosphoserine; by PKA Ref.15

Natural variations

Alternative sequence424 – 45532Missing in isoform 3.
VSP_053534
Alternative sequence425 – 533109ANATG…SVKSR → VHGRGGRHLLRGRPGGGGGP GAAGLRERCLRVRHAGPQVL RLPQVGQEPGAAVGVPDRGD LHRLRPARRGQLRPAVPGHV PRRAFYREACEGSHGPIPQE PRGHCQRDC in isoform 4.
VSP_053535
Alternative sequence485 – 674190Missing in isoform 5.
VSP_053536
Alternative sequence534 – 674141Missing in isoform 4.
VSP_053537
Alternative sequence559 – 61557Missing in isoform 2.
VSP_046998
Natural variant2541E → K. Ref.21
Corresponds to variant rs2228065 [ dbSNP | Ensembl ].
VAR_028018

Experimental info

Mutagenesis1031W → A: Abolishes binding to COTL1. Ref.19
Mutagenesis2721S → A: Loss of phosphorylation site. Permits export from the nucleus. Ref.18
Mutagenesis3591D → N: No loss of activity.
Mutagenesis3631H → S or N: Still some substantial activity. Ref.11
Mutagenesis3681H → S, N or A: No activity. Ref.11 Ref.12
Mutagenesis3731H → S or N: No activity. Ref.11 Ref.12
Mutagenesis3771E → Q: No activity. Ref.12
Mutagenesis3911H → A: No activity. Ref.11 Ref.12
Mutagenesis3911H → S or N: Still some substantial activity. Ref.11 Ref.12
Mutagenesis4001H → A: No activity. Ref.11 Ref.12
Mutagenesis4001H → S or N: Still some substantial activity. Ref.11 Ref.12
Mutagenesis4331H → N or A: Almost no loss of activity.
Mutagenesis5241S → A: Prevents phosphorylation by PKA. Ref.15
Mutagenesis5511H → N or A: No activity. Ref.12

Secondary structure

................................................................................................................ 674
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 36F38C0A9E86BB21

FASTA67477,983
        10         20         30         40         50         60 
MPSYTVTVAT GSQWFAGTDD YIYLSLVGSA GCSEKHLLDK PFYNDFERGA VDSYDVTVDE 

        70         80         90        100        110        120 
ELGEIQLVRI EKRKYWLNDD WYLKYITLKT PHGDYIEFPC YRWITGDVEV VLRDGRAKLA 

       130        140        150        160        170        180 
RDDQIHILKQ HRRKELETRQ KQYRWMEWNP GFPLSIDAKC HKDLPRDIQF DSEKGVDFVL 

       190        200        210        220        230        240 
NYSKAMENLF INRFMHMFQS SWNDFADFEK IFVKISNTIS ERVMNHWQED LMFGYQFLNG 

       250        260        270        280        290        300 
CNPVLIRRCT ELPEKLPVTT EMVECSLERQ LSLEQEVQQG NIFIVDFELL DGIDANKTDP 

       310        320        330        340        350        360 
CTLQFLAAPI CLLYKNLANK IVPIAIQLNQ IPGDENPIFL PSDAKYDWLL AKIWVRSSDF 

       370        380        390        400        410        420 
HVHQTITHLL RTHLVSEVFG IAMYRQLPAV HPIFKLLVAH VRFTIAINTK AREQLICECG 

       430        440        450        460        470        480 
LFDKANATGG GGHVQMVQRA MKDLTYASLC FPEAIKARGM ESKEDIPYYF YRDDGLLVWE 

       490        500        510        520        530        540 
AIRTFTAEVV DIYYEGDQVV EEDPELQDFV NDVYVYGMRG RKSSGFPKSV KSREQLSEYL 

       550        560        570        580        590        600 
TVVIFTASAQ HAAVNFGQYD WCSWIPNAPP TMRAPPPTAK GVVTIEQIVD TLPDRGRSCW 

       610        620        630        640        650        660 
HLGAVWALSQ FQENELFLGM YPEEHFIEKP VKEAMARFRK NLEAIVSVIA ERNKKKQLPY 

       670 
YYLSPDRIPN SVAI 

« Hide

Isoform 2 (Delta-13) [UniParc].

Checksum: 3DE1D2FE62471315
Show »

FASTA61771,564
Isoform 3 (delta-p10) [UniParc].

Checksum: E9A8CCA67CF74DB6
Show »

FASTA64274,635
Isoform 4 (delta-10-13) [UniParc].

Checksum: 6C57FD0816BD2D9E
Show »

FASTA53361,244
Isoform 5 (alpha-10) [UniParc].

Checksum: 4A500F8D7404EC9D
Show »

FASTA48456,291

References

« Hide 'large scale' references
[1]"Cloning of the cDNA for human 5-lipoxygenase."
Dixon R.A.F., Jones R.E., Diehl R.E., Bennett C.D., Kargman S., Rouzer C.A.
Proc. Natl. Acad. Sci. U.S.A. 85:416-420(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
[2]"Molecular cloning and amino acid sequence of human 5-lipoxygenase."
Matsumoto T., Funk C.D., Raadmark O., Hoeoeg J.-O., Joernvall H., Samuelsson B.
Proc. Natl. Acad. Sci. U.S.A. 85:26-30(1988) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"Characterization of the human 5-lipoxygenase gene."
Funk C.D., Hoshiko S., Matsumoto T., Raadmark O., Samuelsson B.
Proc. Natl. Acad. Sci. U.S.A. 86:2587-2591(1989) [PubMed] [Europe PMC] [Abstract]
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]"The structure of human 5-lipoxygenase."
Gilbert N.C., Bartlett S.G., Waight M.T., Neau D.B., Boeglin W.E., Brash A.R., Newcomer M.E.
Science 331:217-219(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS58078.1. [P09917-2]
CCDS7212.1. [P09917-1]
PIRDAHUAL. A28117.
RefSeqNP_000689.1. NM_000698.3. [P09917-1]
NP_001243082.1. NM_001256153.1. [P09917-3]
NP_001243083.1. NM_001256154.1. [P09917-2]
UniGeneHs.89499.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP09917.
SMRP09917. Positions 2-674.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106741. 10 interactions.
IntActP09917. 3 interactions.
STRING9606.ENSP00000363512.

Chemistry

BindingDBP09917.
ChEMBLCHEMBL215.
DrugBankDB00711. Diethylcarbamazine.
DB00741. Hydrocortisone.
DB01097. Leflunomide.
DB00179. Masoprocol.
DB00939. Meclofenamic acid.
DB01017. Minocycline.
DB00471. Montelukast.
DB01103. Quinacrine.
DB00163. Vitamin E.
DB00744. Zileuton.
GuidetoPHARMACOLOGY1385.

PTM databases

PhosphoSiteP09917.

Polymorphism databases

DMDM126407.

Proteomic databases

MaxQBP09917.
PaxDbP09917.
PRIDEP09917.

Protocols and materials databases

DNASU240.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000374391; ENSP00000363512; ENSG00000012779. [P09917-1]
ENST00000542434; ENSP00000437634; ENSG00000012779. [P09917-2]
ENST00000574291; ENSP00000459805; ENSG00000262552. [P09917-1]
GeneID240.
KEGGhsa:240.
UCSCuc001jce.4. human. [P09917-1]
uc010qfg.3. human.

Organism-specific databases

CTD240.
GeneCardsGC10P045869.
HGNCHGNC:435. ALOX5.
HPACAB005066.
MIM152390. gene.
neXtProtNX_P09917.
PharmGKBPA46.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG69653.
HOGENOMHOG000234358.
HOVERGENHBG005150.
InParanoidP09917.
KOK00461.
OMANYSKAME.
OrthoDBEOG7B05CG.
PhylomeDBP09917.
TreeFamTF105320.

Enzyme and pathway databases

BioCycMetaCyc:HS00336-MONOMER.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00877.

Gene expression databases

ArrayExpressP09917.
BgeeP09917.
CleanExHS_ALOX5.
GenevestigatorP09917.

Family and domain databases

Gene3D2.60.60.20. 1 hit.
InterProIPR008976. Lipase_LipOase.
IPR000907. LipOase.
IPR013819. LipOase_C.
IPR020834. LipOase_CS.
IPR020833. LipOase_Fe_BS.
IPR001885. LipOase_mml.
IPR001024. PLAT/LH2_dom.
[Graphical view]
PANTHERPTHR11771. PTHR11771. 1 hit.
PfamPF00305. Lipoxygenase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]
PRINTSPR00087. LIPOXYGENASE.
PR00467. MAMLPOXGNASE.
SMARTSM00308. LH2. 1 hit.
[Graphical view]
SUPFAMSSF48484. SSF48484. 1 hit.
SSF49723. SSF49723. 1 hit.
PROSITEPS00711. LIPOXYGENASE_1. 1 hit.
PS00081. LIPOXYGENASE_2. 1 hit.
PS51393. LIPOXYGENASE_3. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSALOX5. human.
EvolutionaryTraceP09917.
GeneWikiArachidonate_5-lipoxygenase.
GenomeRNAi240.
NextBio35497584.
PMAP-CutDBP09917.
PROP09917.
SOURCESearch...

Entry information

Entry nameLOX5_HUMAN
AccessionPrimary (citable) accession number: P09917
Secondary accession number(s): B7ZLS0 expand/collapse secondary AC list , E5FPY5, E5FPY7, E5FPY8, Q5JQ14
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 160 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM