P09917 (LOX5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Arachidonate 5-lipoxygenase
Short name=5-LO
Short name=5-lipoxygenase
EC=1.13.11.34

Gene names

Name:	ALOX5
Synonyms:	LOG5

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	674 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the first step in leukotriene biosynthesis, and thereby plays a role in inflammatory processes. Ref.19
Catalytic activity	Arachidonate + O2 = leukotriene A4 + H2O. Ref.19
Cofactor	Binds 1 iron ion per subunit. Ref.19 Binds 2 calcium ions per subunit By similarity. Ref.19
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.16 Ref.18
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.9 Ref.12 Ref.15 Ref.16 Ref.17
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 process	Leukotriene biosynthesis
Cellular component	Cytoplasm Membrane Nucleus
Coding sequence diversity	Polymorphism
Ligand	Calcium Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	leukotriene biosynthetic process Inferred from direct assay Ref.19. Source: UniProtKB leukotriene production involved in inflammatory response Inferred from electronic annotation. Source: Compara
Cellular_component	cytosol Inferred from direct assay Ref.16. Source: UniProtKB nuclear envelope lumen Inferred from direct assay Ref.12. Source: UniProtKB nuclear matrix Inferred from direct assay Ref.16. Source: UniProtKB nuclear membrane Inferred from direct assay Ref.12. Source: UniProtKB
Molecular_function	arachidonate 5-lipoxygenase activity Inferred from direct assay Ref.19. Source: UniProtKB iron ion binding Inferred from direct assay Ref.19. Source: UniProtKB lipoxygenase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
COTL1	Q14019	4	EBI-79934,EBI-79926

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 674

673

Arachidonate 5-lipoxygenase

PRO_0000220693

Regions

Domain

2 – 118

117

PLAT

Domain

119 – 674

556

Lipoxygenase

Sites

Metal binding

17

1

Calcium 1; via carbonyl oxygen; structural By similarity

Metal binding

18

1

Calcium 2; via carbonyl oxygen; structural By similarity

Metal binding

19

1

Calcium 2; structural By similarity

Metal binding

44

1

Calcium 2; structural By similarity

Metal binding

45

1

Calcium 2; via carbonyl oxygen; structural By similarity

Metal binding

47

1

Calcium 2; structural By similarity

Metal binding

79

1

Calcium 1; via carbonyl oxygen; structural By similarity

Metal binding

80

1

Calcium 1; via carbonyl oxygen; structural By similarity

Metal binding

368

1

Iron; catalytic

Metal binding

373

1

Iron; catalytic

Metal binding

551

1

Iron; catalytic

Metal binding

555

1

Iron; catalytic

Metal binding

674

1

Iron; via carboxylate; catalytic

Site

103

1

Essential for stabilizing binding to COTL1

Amino acid modifications

Modified residue

272

1

Phosphoserine; by MAPKAPK2 Ref.13 Ref.17

Modified residue

524

1

Phosphoserine; by PKA Ref.14

Natural variations

Natural variant

254

1

E → K. Ref.20
Corresponds to variant rs2228065 [ dbSNP | Ensembl ].

VAR_028018

Experimental info

Mutagenesis

103

1

W → A: Abolishes binding to COTL1. Ref.18

Mutagenesis

272

1

S → A: Loss of phosphorylation site. Permits export from the nucleus. Ref.17

Mutagenesis

359

1

D → N: No loss of activity.

Mutagenesis

363

1

H → S or N: Still some substantial activity. Ref.10

Mutagenesis

368

1

H → S, N or A: No activity. Ref.10 Ref.11

Mutagenesis

373

1

H → S or N: No activity. Ref.10 Ref.11

Mutagenesis

377

1

E → Q: No activity. Ref.11

Mutagenesis

391

1

H → A: No activity. Ref.10 Ref.11

Mutagenesis

391

1

H → S or N: Still some substantial activity. Ref.10 Ref.11

Mutagenesis

400

1

H → A: No activity. Ref.10 Ref.11

Mutagenesis

400

1

H → S or N: Still some substantial activity. Ref.10 Ref.11

Mutagenesis

433

1

H → N or A: Almost no loss of activity.

Mutagenesis

524

1

S → A: Prevents phosphorylation by PKA. Ref.14

Mutagenesis

551

1

H → N or A: No activity. Ref.11

Secondary structure

1

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674

Helix Strand Turn

Details...

Beta strand

4 – 10

7

Beta strand

20 – 30

11

Beta strand

36 – 38

3

Beta strand

51 – 56

6

Beta strand

64 – 73

10

Beta strand

75 – 77

3

Beta strand

81 – 89

9

Beta strand

95 – 104

10

Beta strand

106 – 108

3

Beta strand

110 – 113

4

Helix

120 – 122

3

Helix

126 – 142

17

Beta strand

155 – 157

3

Helix

161 – 163

3

Helix

166 – 168

3

Beta strand

171 – 176

6

Helix

178 – 188

11

Helix

192 – 194

3

Helix

205 – 212

8

Turn

213 – 215

3

Helix

218 – 226

9

Helix

230 – 239

10

Helix

260 – 263

4

Turn

264 – 266

3

Helix

273 – 278

6

Beta strand

282 – 286

5

Helix

288 – 290

3

Helix

303 – 306

4

Beta strand

310 – 315

6

Beta strand

321 – 331

11

Beta strand

333 – 336

4

Helix

345 – 365

21

Helix

366 – 372

7

Helix

373 – 386

14

Helix

392 – 397

6

Helix

398 – 400

3

Helix

404 – 414

11

Helix

421 – 423

3

Turn

427 – 431

5

Helix

432 – 441

10

Helix

447 – 449

3

Helix

451 – 457

7

Turn

463 – 465

3

Helix

470 – 493

24

Helix

497 – 501

5

Helix

504 – 515

12

Turn

516 – 520

5

Helix

522 – 524

3

Helix

533 – 547

15

Helix

549 – 555

7

Helix

558 – 562

5

Helix

565 – 567

3

Beta strand

572 – 574

3

Beta strand

579 – 581

3

Helix

585 – 591

7

Helix

595 – 608

14

Helix

629 – 653

25

Helix

665 – 667

3

Beta strand

669 – 671

3

Sequences

	Sequence		Length	Mass (Da)
	P09917 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 36F38C0A9E86BB21	FASTA	674	77,983
	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

References

	« Hide 'large scale' referencesShow '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], 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].
[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], PARTIAL PROTEIN SEQUENCE.
[5]	"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].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"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.
[12]	"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.
[13]	"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.
[14]	"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.
[15]	"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.
[16]	"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.
[17]	"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.
[18]	"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.
[19]	"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.
[20]	"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.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J03600 mRNA. Translation: AAA36183.1.
J03571 mRNA. Translation: AAA65450.1.
J04520 Genomic DNA. Translation: AAA59522.1.
AL731567 Genomic DNA. Translation: CAI41243.1.
BC130332 mRNA. Translation: AAI30333.1.
BC132677 mRNA. Translation: AAI32678.1.
M38191 Genomic DNA. Translation: AAA63212.1.

IPI

IPI00218916.

PIR

DAHUAL. A28117.

RefSeq

NP_000689.1. NM_000698.3.
NP_001243082.1. NM_001256153.1.

UniGene

Hs.89499.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P09917.

ModBase

Search...

Protein-protein interaction databases

IntAct

P09917. 3 interactions.

STRING

9606.ENSP00000363512.

PTM databases

PhosphoSite

P09917.

Polymorphism databases

DMDM

126407.

Proteomic databases

PaxDb

P09917.

PRIDE

P09917.

Protocols and materials databases

DNASU

240.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000374391; ENSP00000363512; ENSG00000012779.
ENST00000574291; ENSP00000459805; ENSG00000262552.

GeneID

240.

KEGG

hsa:240.

UCSC

uc001jce.3. human.

Organism-specific databases

CTD

240.

GeneCards

GC10P045869.

HGNC

HGNC:435. ALOX5.

HPA

CAB005066.

MIM

152390. gene.

neXtProt

NX_P09917.

PharmGKB

PA46.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG69653.

HOGENOM

HOG000234358.

HOVERGEN

HBG005150.

InParanoid

P09917.

KO

K00461.

OMA

PICLLYK.

OrthoDB

EOG46Q6S3.

PhylomeDB

P09917.

Enzyme and pathway databases

BioCyc

MetaCyc:HS00336-MONOMER.

Reactome

REACT_111217. Metabolism.

UniPathway

UPA00877.

Gene expression databases

ArrayExpress

P09917.

Bgee

P09917.

CleanEx

HS_ALOX5.

Genevestigator

P09917.

GermOnline

ENSG00000012779. Homo sapiens.

Family and domain databases

Gene3D

2.60.60.20. 1 hit.

InterPro

IPR008976. Lipase_LipOase.
IPR000907. LipOase.
IPR013819. LipOase_C.
IPR020834. LipOase_CS.
IPR020833. LipOase_Fe_BS.
IPR001024. LipOase_LH2.
IPR001885. LipOase_mml.
[Graphical view]

PANTHER

PTHR11771. PTHR11771. 1 hit.

Pfam

PF00305. Lipoxygenase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]

PRINTS

PR00087. LIPOXYGENASE.
PR00467. MAMLPOXGNASE.

SMART

SM00308. LH2. 1 hit.
[Graphical view]

SUPFAM

SSF49723. Lipase_LipOase. 1 hit.
SSF48484. Lipoxygenase. 1 hit.

PROSITE

PS00711. LIPOXYGENASE_1. 1 hit.
PS00081. LIPOXYGENASE_2. 1 hit.
PS51393. LIPOXYGENASE_3. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P09917.

ChEMBL

CHEMBL215.

ChiTaRS

ALOX5. human.

DrugBank

DB00711. Diethylcarbamazine.
DB00741. Hydrocortisone.
DB01097. Leflunomide.
DB00179. Masoprocol.
DB00939. Meclofenamic acid.
DB01017. Minocycline.
DB00471. Montelukast.
DB01103. Quinacrine.
DB00163. Vitamin E.
DB00744. Zileuton.

EvolutionaryTrace

P09917.

GenomeRNAi

240.

NextBio

956.

PMAP-CutDB

P09917.

SOURCE

Search...

Entry information

Entry name

LOX5_HUMAN

Accession

Primary (citable) accession number: P09917
Secondary accession number(s): Q5JQ14

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 146 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.