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P18054 (LOX12_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 158. 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·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Arachidonate 12-lipoxygenase, 12S-type

Short name=12S-LOX
Short name=12S-lipoxygenase
EC=1.13.11.31
Alternative name(s):
Lipoxin synthase 12-LO
EC=3.3.2.-
Platelet-type lipoxygenase 12
Gene names
Name:ALOX12
Synonyms:12LO, LOG12
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length663 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Non-heme iron-containing dioxygenase that catalyzes the stereo-specific peroxidation of free and esterified polyunsaturated fatty acids generating a spectrum of bioactive lipid mediators. Mainly converts arachidonic acid to (12S)-hydroperoxyeicosatetraenoic acid/(12S)-HPETE but can also metabolize linoleic acid. Has a dual activity since it also converts leukotriene A4/LTA4 into both the bioactive lipoxin A4/LXA4 and lipoxin B4/LXB4. Through the production of specific bioactive lipids like (12S)-HPETE it regulates different biological processes including platelet activation. It also probably positively regulates angiogenesis through regulation of the expression of the vascular endothelial growth factor. Plays a role in apoptotic process, promoting the survival of vascular smooth muscle cells for instance. May also play a role in the control of cell migration and proliferation. Ref.12 Ref.16 Ref.17 Ref.19 Ref.20

Catalytic activity

Arachidonate + O2 = (5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyicosa-5,8,10,14-tetraenoate. Ref.11 Ref.12 Ref.13 Ref.14

(7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa-7,9,11,14-tetraenoate + H2O = (5S,6R,15S)-trihydroxy-(7E,9E,11Z,13E)-eicosatetraenoate. Ref.11 Ref.12 Ref.13 Ref.14

(7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa-7,9,11,14-tetraenoate + H2O = (5S,14R,15S)-trihydroxy-(6E,8Z,10E,12E)-eicosatetraenoate.

Cofactor

Binds 1 iron ion per subunit.

Enzyme regulation

Activated by EGF. Ref.15

Pathway

Lipid metabolism; hydroperoxy eicosatetraenoic acid biosynthesis. Ref.11

Subcellular location

Cytoplasmcytosol. Membrane. Note: Membrane association is stimulated by EGF. Ref.13 Ref.15

Tissue specificity

Expressed in vascular smooth muscle cells. Ref.20

Induction

Down-regulated upon starvation, by UV-irradiation and 15-lipoxygenase metabolites. Ref.15 Ref.18

Involvement in disease

Esophageal cancer (ESCR) [MIM:133239]: A malignancy of the esophagus. The most common types are esophageal squamous cell carcinoma and adenocarcinoma. Cancer of the esophagus remains a devastating disease because it is usually not detected until it has progressed to an advanced incurable stage.
Note: Disease susceptibility may be associated with variations affecting the gene represented in this entry. Gln at position 261 may confer interindividual susceptibility to esophageal cancer (Ref.24).

Colorectal cancer (CRC) [MIM:114500]: A complex disease characterized by malignant lesions arising from the inner wall of the large intestine (the colon) and the rectum. Genetic alterations are often associated with progression from premalignant lesion (adenoma) to invasive adenocarcinoma. Risk factors for cancer of the colon and rectum include colon polyps, long-standing ulcerative colitis, and genetic family history.
Note: Disease susceptibility may be associated with variations affecting the gene represented in this entry. Gln at position 261 may confer interindividual susceptibility to colorectal cancer (Ref.24).

Sequence similarities

Belongs to the lipoxygenase family.

Contains 1 lipoxygenase domain.

Contains 1 PLAT domain.

Biophysicochemical properties

Kinetic parameters:

KM=8 µM for arachidonate (Ref.11, at pH 7.0 and 37 degrees Celsius) Ref.11 Ref.12 Ref.13

KM=10 µM for arachidonate (Ref.13, at pH 8.0 and 25 degrees Celsius)

KM=6.2 µM for arachidonate (Ref.12, at pH 7.4)

KM=9 µM for linoleate (Ref.13, at pH 8.0 and 25 degrees Celsius)

KM=7.9 µM for leukotriene A4 (Ref.12, at pH 7.4)

KM=3 µM for eicosa-5,8,11,14,17-pentaenoate (Ref.11, at pH 7.0 and 37 degrees Celsius)

KM=35 µM for eicosa-8,11,14-trienoate (Ref.11, at pH 7.0 and 37 degrees Celsius)

KM=14.3 µM for 5,6-epoxy-8,11,14-eicosatrienoate (Ref.12, at pH 7.4)

Vmax=3 µmol/min/mg enzyme with arachidonate as substrate (Ref.13, at pH 8.0 and 25 degrees Celsius)

Vmax=1.057 µmol/min/mg enzyme with arachidonate as substrate (Ref.12, at pH 7.4)

Vmax=0.0375 µmol/min/mg enzyme with linoleate as substrate (Ref.13, at pH 8.0 and 25 degrees Celsius)

Vmax=0.025 µmol/min/mg enzyme with leukotriene A4 as substrate (Ref.12, at pH 7.4)

Vmax=0.985 µmol/min/mg enzyme with 5,6-epoxy-8,11,14-eicosatrienoate as substrate (Ref.12, at pH 7.4)

pH dependence:

Optimum pH is 7.5-8.0 (for arachidonate 12-lipoxygenase activity).

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentCytoplasm
Membrane
   Coding sequence diversityPolymorphism
   LigandIron
Metal-binding
   Molecular functionDioxygenase
Hydrolase
Oxidoreductase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaging

Inferred from electronic annotation. Source: Ensembl

arachidonic acid metabolic process

Inferred from direct assay Ref.11Ref.13. Source: UniProtKB

cellular component movement

Inferred from mutant phenotype PubMed 14669797. Source: UniProtKB

cellular response to lipid

Inferred from electronic annotation. Source: Ensembl

establishment of skin barrier

Inferred from sequence or structural similarity. Source: UniProtKB

fatty acid oxidation

Inferred from mutant phenotype PubMed 15111312. Source: UniProtKB

hepoxilin biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

hepoxilin metabolic process

Traceable author statement. Source: Reactome

leukotriene A4 metabolic process

Inferred from direct assay Ref.12. Source: UniProtKB

linoleic acid metabolic process

Inferred from direct assay Ref.13. Source: UniProtKB

lipoxin A4 biosynthetic process

Inferred from direct assay Ref.12. Source: UniProtKB

lipoxin B4 biosynthetic process

Inferred from direct assay Ref.12. Source: UniProtKB

lipoxin metabolic process

Traceable author statement. Source: Reactome

lipoxygenase pathway

Inferred from direct assay Ref.13. Source: UniProtKB

negative regulation of apoptotic process

Inferred from mutant phenotype PubMed 15305153. Source: UniProtKB

negative regulation of muscle cell apoptotic process

Inferred from mutant phenotype Ref.20. Source: UniProtKB

negative regulation of platelet aggregation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of angiogenesis

Inferred from mutant phenotype Ref.16. Source: UniProtKB

positive regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell adhesion

Inferred from mutant phenotype PubMed 14669797. Source: UniProtKB

positive regulation of cell growth

Inferred from mutant phenotype PubMed 14767568. Source: UniProtKB

positive regulation of cell migration

Inferred from mutant phenotype Ref.19. Source: UniProtKB

positive regulation of cell proliferation

Inferred from mutant phenotype PubMed 15010818Ref.19Ref.16. Source: UniProtKB

positive regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of endothelial cell differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of endothelial cell migration

Inferred from electronic annotation. Source: Ensembl

positive regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

positive regulation of mitochondrial depolarization

Inferred from electronic annotation. Source: Ensembl

positive regulation of smooth muscle cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of vasodilation

Inferred from electronic annotation. Source: Ensembl

reactive oxygen species metabolic process

Non-traceable author statement PubMed 12858336. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

superoxide anion generation

Non-traceable author statement PubMed 15107407. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay Ref.13. Source: UniProtKB

cytosol

Inferred from direct assay PubMed 15107407Ref.15. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

membrane

Inferred from direct assay Ref.15. Source: UniProtKB

sarcolemma

Inferred from direct assay PubMed 15107407. Source: UniProtKB

   Molecular_functionarachidonate 12-lipoxygenase activity

Inferred from direct assay Ref.11Ref.3Ref.2Ref.13. Source: UniProtKB

hepoxilin A3 synthase activity

Traceable author statement. Source: Reactome

hepoxilin-epoxide hydrolase activity

Inferred from sequence or structural similarity. Source: UniProtKB

iron ion binding

Inferred from electronic annotation. Source: InterPro

linoleate 13S-lipoxygenase activity

Inferred from direct assay Ref.13. Source: UniProtKB

oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen

Traceable author statement. Source: Reactome

protein binding

Inferred from physical interaction PubMed 10727209. Source: IntAct

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 663663Arachidonate 12-lipoxygenase, 12S-type
PRO_0000220682

Regions

Domain2 – 114113PLAT
Domain115 – 663549Lipoxygenase

Sites

Metal binding3601Iron; catalytic
Metal binding3651Iron; catalytic
Metal binding5401Iron; catalytic
Metal binding5441Iron; catalytic By similarity
Metal binding6631Iron; via carboxylate; catalytic By similarity

Natural variations

Natural variant2591E → K.
Corresponds to variant rs4987104 [ dbSNP | Ensembl ].
VAR_030471
Natural variant2611Q → R. Ref.3 Ref.4 Ref.6 Ref.22 Ref.23 Ref.24
Corresponds to variant rs1126667 [ dbSNP | Ensembl ].
VAR_018743
Natural variant2981A → T.
VAR_004279
Natural variant3221N → S. Ref.1 Ref.2 Ref.4
Corresponds to variant rs434473 [ dbSNP | Ensembl ].
VAR_018744
Natural variant4301R → H. Ref.4
Corresponds to variant rs11571342 [ dbSNP | Ensembl ].
VAR_018745

Experimental info

Mutagenesis3551H → Q: No effect on catalytic activity. Ref.14
Mutagenesis3601H → Q or Y: Complete loss of catalytic activity. Ref.14
Mutagenesis3651H → Q: Complete loss of catalytic activity. Ref.14
Mutagenesis3831H → Q: Altered catalytic activity and protein expression. Ref.14
Mutagenesis3921H → Q: No effect on catalytic activity. Ref.14
Mutagenesis4161K → Q: Reduced catalytic activity. No effect on the stereoselectivity of the oxygenation reaction. Ref.14
Mutagenesis4171A → I: Reduced catalytic activity. Alters the stereoselectivity of the oxygenation reaction. Ref.14
Mutagenesis4181V → M: No effect on catalytic activity. No effect on the stereoselectivity of the oxygenation reaction. Ref.14
Mutagenesis5401H → Q: Complete loss of catalytic activity. Ref.14
Sequence conflict189 – 1924RVYT → PCLH in AAA51533. Ref.1
Sequence conflict3451S → C in AAA51533. Ref.1
Sequence conflict3891L → P in AAA60056. Ref.2

Secondary structure

................................................................ 663
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P18054 [UniParc].

Last modified February 6, 2007. Version 4.
Checksum: C4D6D5B320666A77

FASTA66375,694
        10         20         30         40         50         60 
MGRYRIRVAT GAWLFSGSYN RVQLWLVGTR GEAELELQLR PARGEEEEFD HDVAEDLGLL 

        70         80         90        100        110        120 
QFVRLRKHHW LVDDAWFCDR ITVQGPGACA EVAFPCYRWV QGEDILSLPE GTARLPGDNA 

       130        140        150        160        170        180 
LDMFQKHREK ELKDRQQIYC WATWKEGLPL TIAADRKDDL PPNMRFHEEK RLDFEWTLKA 

       190        200        210        220        230        240 
GALEMALKRV YTLLSSWNCL EDFDQIFWGQ KSALAEKVRQ CWQDDELFSY QFLNGANPML 

       250        260        270        280        290        300 
LRRSTSLPSR LVLPSGMEEL QAQLEKELQN GSLFEADFIL LDGIPANVIR GEKQYLAAPL 

       310        320        330        340        350        360 
VMLKMEPNGK LQPMVIQIQP PNPSSPTPTL FLPSDPPLAW LLAKSWVRNS DFQLHEIQYH 

       370        380        390        400        410        420 
LLNTHLVAEV IAVATMRCLP GLHPIFKFLI PHIRYTMEIN TRARTQLISD GGIFDKAVST 

       430        440        450        460        470        480 
GGGGHVQLLR RAAAQLTYCS LCPPDDLADR GLLGLPGALY AHDALRLWEI IARYVEGIVH 

       490        500        510        520        530        540 
LFYQRDDIVK GDPELQAWCR EITEVGLCQA QDRGFPVSFQ SQSQLCHFLT MCVFTCTAQH 

       550        560        570        580        590        600 
AAINQGQLDW YAWVPNAPCT MRMPPPTTKE DVTMATVMGS LPDVRQACLQ MAISWHLSRR 

       610        620        630        640        650        660 
QPDMVPLGHH KEKYFSGPKP KAVLNQFRTD LEKLEKEITA RNEQLDWPYE YLKPSCIENS 


VTI 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and expression of human arachidonate 12-lipoxygenase."
Yoshimoto T., Yamamoto Y., Arakawa T., Suzuki H., Yamamoto S., Yokoyama C., Tanabe T., Toh H.
Biochem. Biophys. Res. Commun. 172:1230-1235(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-322.
[2]"Molecular cloning, primary structure, and expression of the human platelet/erythroleukemia cell 12-lipoxygenase."
Funk C.D., Furci L., Fitzgerald G.A.
Proc. Natl. Acad. Sci. U.S.A. 87:5638-5642(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-322.
[3]"Cloning of the cDNA for human 12-lipoxygenase."
Izumi T., Hoshiko S., Raadmark O., Samuelsson B.
Proc. Natl. Acad. Sci. U.S.A. 87:7477-7481(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-261.
[4]SeattleSNPs variation discovery resource
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-261; SER-322 AND HIS-430.
[5]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [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], VARIANT ARG-261.
[7]"Structure and chromosomal localization of human arachidonate 12-lipoxygenase gene."
Yoshimoto T., Arakawa T., Hada T., Yamamoto S., Takahashi E.
J. Biol. Chem. 267:24805-24809(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-112.
[8]"Characterization of human 12-lipoxygenase genes."
Funk C.D., Funk L.B., Fitzgerald G.A., Samuelsson B.
Proc. Natl. Acad. Sci. U.S.A. 89:3962-3966(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-45.
[9]"Epidermis contains platelet-type 12-lipoxygenase that is overexpressed in germinal layer keratinocytes in psoriasis."
Hussain H., Shornick L.P., Shannon V.R., Wilson J.D., Funk C.D., Pentland A.P., Holtzman M.J.
Am. J. Physiol. 266:C243-C253(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 340-427.
Tissue: Skin.
[10]"EU-IMAGE: full-insert length sequencing of human cDNA clones."
Persson A.E., Lundeberg J., Uhlen M.
Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 531-663.
[11]"Catalytic properties of human platelet 12-lipoxygenase as compared with the enzymes of other origins."
Hada T., Ueda N., Takahashi Y., Yamamoto S.
Biochim. Biophys. Acta 1083:89-93(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, KINETIC PARAMETERS, PATHWAY, SUBSTRATE SPECIFICITY.
[12]"Lipoxin synthase activity of human platelet 12-lipoxygenase."
Romano M., Chen X.S., Takahashi Y., Yamamoto S., Funk C.D., Serhan C.N.
Biochem. J. 296:127-133(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN LIPOXIN SYNTHESIS, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, REACTION MECHANISM.
[13]"Purification and characterization of recombinant histidine-tagged human platelet 12-lipoxygenase expressed in a baculovirus/insect cell system."
Chen X.S., Brash A.R., Funk C.D.
Eur. J. Biochem. 214:845-852(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, KINETIC PARAMETERS, PH DEPENDENCE, SUBCELLULAR LOCATION.
[14]"Structure-function properties of human platelet 12-lipoxygenase: chimeric enzyme and in vitro mutagenesis studies."
Chen X.S., Funk C.D.
FASEB J. 7:694-701(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-355; HIS-360; HIS-365; HIS-383; HIS-392; LYS-416; ALA-417; VAL-418 AND HIS-540.
[15]"12-Lipoxygenase in A431 cells: genetic identity, modulation of expression, and intracellular localization."
Hagmann W., Gao X., Timar J., Chen Y.Q., Strohmaier A.R., Fahrenkopf C., Kagawa D., Lee M., Zacharek A., Honn K.V.
Exp. Cell Res. 228:197-205(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, ENZYME REGULATION, INDUCTION.
[16]"Platelet-type 12-lipoxygenase in a human prostate carcinoma stimulates angiogenesis and tumor growth."
Nie D., Hillman G.G., Geddes T., Tang K., Pierson C., Grignon D.J., Honn K.V.
Cancer Res. 58:4047-4051(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ANGIOGENESIS.
[17]"Mechanisms regulating tumor angiogenesis by 12-lipoxygenase in prostate cancer cells."
Nie D., Krishnamoorthy S., Jin R., Tang K., Chen Y., Qiao Y., Zacharek A., Guo Y., Milanini J., Pages G., Honn K.V.
J. Biol. Chem. 281:18601-18609(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ANGIOGENESIS.
[18]"Reciprocal regulation of 12- and 15-lipoxygenases by UV-irradiation in human keratinocytes."
Yoo H., Jeon B., Jeon M.S., Lee H., Kim T.Y.
FEBS Lett. 582:3249-3253(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY UV.
[19]"Up-regulation of 12(S)-lipoxygenase induces a migratory phenotype in colorectal cancer cells."
Klampfl T., Bogner E., Bednar W., Mager L., Massudom D., Kalny I., Heinzle C., Berger W., Staettner S., Karner J., Klimpfinger M., Fuerstenberger G., Krieg P., Marian B.
Exp. Cell Res. 318:768-778(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL MIGRATION.
[20]"12S-Lipoxygenase is necessary for human vascular smooth muscle cell survival."
Weisinger G., Grafi-Cohen M., Hirsh M., Knoll E., Sharon O., Many A., Limor R., Stern N.
Exp. Cell Res. 319:1586-1593(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN APOPTOTIC PROCESS, TISSUE SPECIFICITY.
[21]"Crystal structure of the lipoxygenase domain of human arachidonate 12-lipoxygenase, 12s-type."
Structural genomics consortium (SGC)
Submitted (FEB-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 172-662 IN COMPLEX WITH IRON IONS.
[22]"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 ARG-261.
[23]"Associations of functional polymorphisms in cyclooxygenase-2 and platelet 12-lipoxygenase with risk of occurrence and advanced disease status of colorectal cancer."
Tan W., Wu J., Zhang X., Guo Y., Liu J., Sun T., Zhang B., Zhao D., Yang M., Yu D., Lin D.
Carcinogenesis 28:1197-1201(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ARG-261, INVOLVEMENT IN COLORECTAL CANCER.
[24]"Platelet 12-lipoxygenase Arg261Gln polymorphism: functional characterization and association with risk of esophageal squamous cell carcinoma in combination with COX-2 polymorphisms."
Guo Y., Zhang X., Tan W., Miao X., Sun T., Zhao D., Lin D.
Pharmacogenet. Genomics 17:197-205(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ARG-261, INVOLVEMENT IN ESOPHAGEAL CANCER.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M62982 mRNA. Translation: AAA51533.1.
M35418 mRNA. Translation: AAA60056.1.
M58704 mRNA. Translation: AAA59523.1.
AY527817 Genomic DNA. Translation: AAS00094.1.
AC040977 Genomic DNA. No translation available.
BC069557 mRNA. Translation: AAH69557.1.
D12638 Genomic DNA. Translation: BAA02162.1.
M87004 Genomic DNA. Translation: AAA51587.1.
S68587 mRNA. Translation: AAD14020.1.
AF143883 mRNA. Translation: AAD32700.1.
CCDSCCDS11084.1.
PIRA38283.
RefSeqNP_000688.2. NM_000697.2.
UniGeneHs.654431.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2ABUmodel-A2-663[»]
3D3LX-ray2.60A/B172-663[»]
ProteinModelPortalP18054.
SMRP18054. Positions 2-663.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106740. 4 interactions.
IntActP18054. 4 interactions.
MINTMINT-1206406.
STRING9606.ENSP00000251535.

Chemistry

BindingDBP18054.
ChEMBLCHEMBL3687.

PTM databases

PhosphoSiteP18054.

Polymorphism databases

DMDM125987838.

Proteomic databases

PaxDbP18054.
PRIDEP18054.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000251535; ENSP00000251535; ENSG00000108839.
GeneID239.
KEGGhsa:239.
UCSCuc002gdx.4. human.

Organism-specific databases

CTD239.
GeneCardsGC17P006899.
H-InvDBHIX0039067.
HGNCHGNC:429. ALOX12.
HPACAB019287.
HPA010691.
MIM114500. phenotype.
133239. phenotype.
152391. gene.
neXtProtNX_P18054.
PharmGKBPA45.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG69653.
HOGENOMHOG000234358.
HOVERGENHBG005150.
InParanoidP18054.
KOK00458.
OMAQNQLCHF.
OrthoDBEOG7B05CG.
PhylomeDBP18054.
TreeFamTF105320.

Enzyme and pathway databases

BioCycMetaCyc:HS03167-MONOMER.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00881.

Gene expression databases

ArrayExpressP18054.
BgeeP18054.
CleanExHS_ALOX12.
GenevestigatorP18054.

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

EvolutionaryTraceP18054.
GeneWikiALOX12.
GenomeRNAi239.
NextBio952.
PROP18054.
SOURCESearch...

Entry information

Entry nameLOX12_HUMAN
AccessionPrimary (citable) accession number: P18054
Secondary accession number(s): O95569, Q6ISF8, Q9UQM4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: February 6, 2007
Last modified: July 9, 2014
This is version 158 of the entry and version 4 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 17

Human chromosome 17: entries, gene names and cross-references to MIM