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P18054

- LOX12_HUMAN

UniProt

P18054 - LOX12_HUMAN

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Protein

Arachidonate 12-lipoxygenase, 12S-type

Gene

ALOX12

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

Functioni

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.5 Publications

Catalytic activityi

Arachidonate + O2 = (5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyicosa-5,8,10,14-tetraenoate.
(7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa-7,9,11,14-tetraenoate + H2O = (5S,6R,15S)-trihydroxy-(7E,9E,11Z,13E)-eicosatetraenoate.
(7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa-7,9,11,14-tetraenoate + H2O = (5S,14R,15S)-trihydroxy-(6E,8Z,10E,12E)-eicosatetraenoate.

Cofactori

Binds 1 iron ion per subunit.

Enzyme regulationi

Activated by EGF.1 Publication

Kineticsi

  1. KM=8 µM for arachidonate (PubMed:1851637, at pH 7.0 and 37 degrees Celsius)3 Publications
  2. KM=10 µM for arachidonate (PubMed:8319693, at pH 8.0 and 25 degrees Celsius)3 Publications
  3. KM=6.2 µM for arachidonate (PubMed:8250832, at pH 7.4)3 Publications
  4. KM=9 µM for linoleate (PubMed:8319693, at pH 8.0 and 25 degrees Celsius)3 Publications
  5. KM=7.9 µM for leukotriene A4 (PubMed:8250832, at pH 7.4)3 Publications
  6. KM=3 µM for eicosa-5,8,11,14,17-pentaenoate (PubMed:1851637, at pH 7.0 and 37 degrees Celsius)3 Publications
  7. KM=35 µM for eicosa-8,11,14-trienoate (PubMed:1851637, at pH 7.0 and 37 degrees Celsius)3 Publications
  8. KM=14.3 µM for 5,6-epoxy-8,11,14-eicosatrienoate (PubMed:8250832, at pH 7.4)3 Publications

Vmax=3 µmol/min/mg enzyme with arachidonate as substrate (PubMed:8319693, at pH 8.0 and 25 degrees Celsius)3 Publications

Vmax=1.057 µmol/min/mg enzyme with arachidonate as substrate (PubMed:8250832, at pH 7.4)3 Publications

Vmax=0.0375 µmol/min/mg enzyme with linoleate as substrate (PubMed:8319693, at pH 8.0 and 25 degrees Celsius)3 Publications

Vmax=0.025 µmol/min/mg enzyme with leukotriene A4 as substrate (PubMed:8250832, at pH 7.4)3 Publications

Vmax=0.985 µmol/min/mg enzyme with 5,6-epoxy-8,11,14-eicosatrienoate as substrate (PubMed:8250832, at pH 7.4)3 Publications

pH dependencei

Optimum pH is 7.5-8.0 (for arachidonate 12-lipoxygenase activity).2 Publications

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi360 – 3601Iron; catalytic
Metal bindingi365 – 3651Iron; catalytic
Metal bindingi540 – 5401Iron; catalytic
Metal bindingi544 – 5441Iron; catalyticPROSITE-ProRule annotation
Metal bindingi663 – 6631Iron; via carboxylate; catalyticPROSITE-ProRule annotation

GO - Molecular functioni

  1. arachidonate 12-lipoxygenase activity Source: UniProtKB
  2. hepoxilin A3 synthase activity Source: Reactome
  3. hepoxilin-epoxide hydrolase activity Source: UniProtKB
  4. iron ion binding Source: InterPro
  5. linoleate 13S-lipoxygenase activity Source: UniProtKB
  6. oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Source: Reactome

GO - Biological processi

  1. aging Source: Ensembl
  2. arachidonic acid metabolic process Source: UniProtKB
  3. cellular component movement Source: UniProtKB
  4. cellular response to lipid Source: Ensembl
  5. establishment of skin barrier Source: UniProtKB
  6. fatty acid oxidation Source: UniProtKB
  7. hepoxilin biosynthetic process Source: UniProtKB
  8. hepoxilin metabolic process Source: Reactome
  9. leukotriene A4 metabolic process Source: UniProtKB
  10. linoleic acid metabolic process Source: UniProtKB
  11. lipoxin A4 biosynthetic process Source: UniProtKB
  12. lipoxin B4 biosynthetic process Source: UniProtKB
  13. lipoxin metabolic process Source: Reactome
  14. lipoxygenase pathway Source: UniProtKB
  15. negative regulation of apoptotic process Source: UniProtKB
  16. negative regulation of muscle cell apoptotic process Source: UniProtKB
  17. negative regulation of platelet aggregation Source: UniProtKB
  18. positive regulation of angiogenesis Source: UniProtKB
  19. positive regulation of apoptotic process Source: Ensembl
  20. positive regulation of cell adhesion Source: UniProtKB
  21. positive regulation of cell growth Source: UniProtKB
  22. positive regulation of cell migration Source: UniProtKB
  23. positive regulation of cell proliferation Source: UniProtKB
  24. positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
  25. positive regulation of endothelial cell differentiation Source: Ensembl
  26. positive regulation of endothelial cell migration Source: Ensembl
  27. positive regulation of gene expression Source: Ensembl
  28. positive regulation of mitochondrial depolarization Source: Ensembl
  29. positive regulation of smooth muscle cell proliferation Source: Ensembl
  30. positive regulation of vasodilation Source: Ensembl
  31. reactive oxygen species metabolic process Source: UniProtKB
  32. small molecule metabolic process Source: Reactome
  33. superoxide anion generation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Hydrolase, Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS03167-MONOMER.
ReactomeiREACT_150201. Synthesis of 12-eicosatetraenoic acid derivatives.
REACT_150292. Synthesis of Hepoxilins (HX) and Trioxilins (TrX).
REACT_150320. Synthesis of Lipoxins (LX).
UniPathwayiUPA00881.

Names & Taxonomyi

Protein namesi
Recommended name:
Arachidonate 12-lipoxygenase, 12S-type (EC:1.13.11.31)
Short name:
12S-LOX
Short name:
12S-lipoxygenase
Alternative name(s):
Lipoxin synthase 12-LO (EC:3.3.2.-)
Platelet-type lipoxygenase 12
Gene namesi
Name:ALOX12
Synonyms:12LO, LOG12
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:429. ALOX12.

Subcellular locationi

Cytoplasmcytosol. Membrane
Note: Membrane association is stimulated by EGF.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProt
  4. membrane Source: UniProtKB
  5. sarcolemma Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Involvement in diseasei

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.1 Publication
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 (PubMed:17460548).1 Publication
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.1 Publication
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 (PubMed:17460548).1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi355 – 3551H → Q: No effect on catalytic activity. 1 Publication
Mutagenesisi360 – 3601H → Q or Y: Complete loss of catalytic activity. 1 Publication
Mutagenesisi365 – 3651H → Q: Complete loss of catalytic activity. 1 Publication
Mutagenesisi383 – 3831H → Q: Altered catalytic activity and protein expression. 1 Publication
Mutagenesisi392 – 3921H → Q: No effect on catalytic activity. 1 Publication
Mutagenesisi416 – 4161K → Q: Reduced catalytic activity. No effect on the stereoselectivity of the oxygenation reaction. 1 Publication
Mutagenesisi417 – 4171A → I: Reduced catalytic activity. Alters the stereoselectivity of the oxygenation reaction. 1 Publication
Mutagenesisi418 – 4181V → M: No effect on catalytic activity. No effect on the stereoselectivity of the oxygenation reaction. 1 Publication
Mutagenesisi540 – 5401H → Q: Complete loss of catalytic activity. 1 Publication

Organism-specific databases

MIMi114500. phenotype.
133239. phenotype.
PharmGKBiPA45.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 663663Arachidonate 12-lipoxygenase, 12S-typePRO_0000220682Add
BLAST

Proteomic databases

PaxDbiP18054.
PRIDEiP18054.

PTM databases

PhosphoSiteiP18054.

Expressioni

Tissue specificityi

Expressed in vascular smooth muscle cells.1 Publication

Inductioni

Down-regulated upon starvation, by UV-irradiation and 15-lipoxygenase metabolites.2 Publications

Gene expression databases

BgeeiP18054.
CleanExiHS_ALOX12.
ExpressionAtlasiP18054. baseline and differential.
GenevestigatoriP18054.

Organism-specific databases

HPAiCAB019287.
HPA010691.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
KRT5P136477EBI-1633210,EBI-702187
LMNAP025454EBI-1633210,EBI-351935

Protein-protein interaction databases

BioGridi106740. 4 interactions.
IntActiP18054. 4 interactions.
MINTiMINT-1206406.
STRINGi9606.ENSP00000251535.

Structurei

Secondary structure

1
663
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi182 – 19514
Beta strandi198 – 2003
Helixi203 – 2075
Helixi213 – 2219
Helixi225 – 23410
Helixi258 – 26912
Beta strandi273 – 2775
Helixi279 – 2813
Beta strandi300 – 3056
Beta strandi311 – 3199
Beta strandi325 – 3273
Helixi337 – 35721
Helixi358 – 3647
Helixi365 – 37814
Helixi384 – 3896
Helixi390 – 3923
Helixi426 – 4349
Turni438 – 4414
Helixi443 – 4497
Helixi459 – 48224
Helixi486 – 4916
Helixi493 – 50311
Turni504 – 5085
Helixi510 – 5123
Helixi522 – 53615
Helixi538 – 5447
Helixi547 – 5515
Helixi554 – 5563
Beta strandi567 – 5715
Helixi574 – 5807
Helixi584 – 59714
Helixi618 – 64326
Helixi654 – 6563
Beta strandi657 – 6604

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ABUmodel-A2-663[»]
3D3LX-ray2.60A/B172-663[»]
ProteinModelPortaliP18054.
SMRiP18054. Positions 2-663.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP18054.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 114113PLATPROSITE-ProRule annotationAdd
BLAST
Domaini115 – 663549LipoxygenasePROSITE-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.
InParanoidiP18054.
KOiK00458.
OMAiQNQLCHF.
OrthoDBiEOG7B05CG.
PhylomeDBiP18054.
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]

Sequencei

Sequence statusi: Complete.

P18054 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGRYRIRVAT GAWLFSGSYN RVQLWLVGTR GEAELELQLR PARGEEEEFD
60 70 80 90 100
HDVAEDLGLL QFVRLRKHHW LVDDAWFCDR ITVQGPGACA EVAFPCYRWV
110 120 130 140 150
QGEDILSLPE GTARLPGDNA LDMFQKHREK ELKDRQQIYC WATWKEGLPL
160 170 180 190 200
TIAADRKDDL PPNMRFHEEK RLDFEWTLKA GALEMALKRV YTLLSSWNCL
210 220 230 240 250
EDFDQIFWGQ KSALAEKVRQ CWQDDELFSY QFLNGANPML LRRSTSLPSR
260 270 280 290 300
LVLPSGMEEL QAQLEKELQN GSLFEADFIL LDGIPANVIR GEKQYLAAPL
310 320 330 340 350
VMLKMEPNGK LQPMVIQIQP PNPSSPTPTL FLPSDPPLAW LLAKSWVRNS
360 370 380 390 400
DFQLHEIQYH LLNTHLVAEV IAVATMRCLP GLHPIFKFLI PHIRYTMEIN
410 420 430 440 450
TRARTQLISD GGIFDKAVST GGGGHVQLLR RAAAQLTYCS LCPPDDLADR
460 470 480 490 500
GLLGLPGALY AHDALRLWEI IARYVEGIVH LFYQRDDIVK GDPELQAWCR
510 520 530 540 550
EITEVGLCQA QDRGFPVSFQ SQSQLCHFLT MCVFTCTAQH AAINQGQLDW
560 570 580 590 600
YAWVPNAPCT MRMPPPTTKE DVTMATVMGS LPDVRQACLQ MAISWHLSRR
610 620 630 640 650
QPDMVPLGHH KEKYFSGPKP KAVLNQFRTD LEKLEKEITA RNEQLDWPYE
660
YLKPSCIENS VTI
Length:663
Mass (Da):75,694
Last modified:February 6, 2007 - v4
Checksum:iC4D6D5B320666A77
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti189 – 1924RVYT → PCLH in AAA51533. (PubMed:2244907)Curated
Sequence conflicti345 – 3451S → C in AAA51533. (PubMed:2244907)Curated
Sequence conflicti389 – 3891L → P in AAA60056. (PubMed:2377602)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti259 – 2591E → K.
Corresponds to variant rs4987104 [ dbSNP | Ensembl ].
VAR_030471
Natural varianti261 – 2611Q → R.6 Publications
Corresponds to variant rs1126667 [ dbSNP | Ensembl ].
VAR_018743
Natural varianti298 – 2981A → T.
VAR_004279
Natural varianti322 – 3221N → S.3 Publications
Corresponds to variant rs434473 [ dbSNP | Ensembl ].
VAR_018744
Natural varianti430 – 4301R → H.1 Publication
Corresponds to variant rs11571342 [ dbSNP | Ensembl ].
VAR_018745

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS11084.1.
PIRiA38283.
RefSeqiNP_000688.2. NM_000697.2.
UniGeneiHs.654431.

Genome annotation databases

EnsembliENST00000251535; ENSP00000251535; ENSG00000108839.
GeneIDi239.
KEGGihsa:239.
UCSCiuc002gdx.4. human.

Polymorphism databases

DMDMi125987838.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

SeattleSNPs
Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS11084.1.
PIRi A38283.
RefSeqi NP_000688.2. NM_000697.2.
UniGenei Hs.654431.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2ABU model - A 2-663 [» ]
3D3L X-ray 2.60 A/B 172-663 [» ]
ProteinModelPortali P18054.
SMRi P18054. Positions 2-663.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106740. 4 interactions.
IntActi P18054. 4 interactions.
MINTi MINT-1206406.
STRINGi 9606.ENSP00000251535.

Chemistry

BindingDBi P18054.
ChEMBLi CHEMBL3687.

PTM databases

PhosphoSitei P18054.

Polymorphism databases

DMDMi 125987838.

Proteomic databases

PaxDbi P18054.
PRIDEi P18054.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000251535 ; ENSP00000251535 ; ENSG00000108839 .
GeneIDi 239.
KEGGi hsa:239.
UCSCi uc002gdx.4. human.

Organism-specific databases

CTDi 239.
GeneCardsi GC17P006899.
H-InvDB HIX0039067.
HGNCi HGNC:429. ALOX12.
HPAi CAB019287.
HPA010691.
MIMi 114500. phenotype.
133239. phenotype.
152391. gene.
neXtProti NX_P18054.
PharmGKBi PA45.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG69653.
GeneTreei ENSGT00550000074415.
HOGENOMi HOG000234358.
HOVERGENi HBG005150.
InParanoidi P18054.
KOi K00458.
OMAi QNQLCHF.
OrthoDBi EOG7B05CG.
PhylomeDBi P18054.
TreeFami TF105320.

Enzyme and pathway databases

UniPathwayi UPA00881 .
BioCyci MetaCyc:HS03167-MONOMER.
Reactomei REACT_150201. Synthesis of 12-eicosatetraenoic acid derivatives.
REACT_150292. Synthesis of Hepoxilins (HX) and Trioxilins (TrX).
REACT_150320. Synthesis of Lipoxins (LX).

Miscellaneous databases

EvolutionaryTracei P18054.
GeneWikii ALOX12.
GenomeRNAii 239.
NextBioi 952.
PROi P18054.
SOURCEi Search...

Gene expression databases

Bgeei P18054.
CleanExi HS_ALOX12.
ExpressionAtlasi P18054. baseline and differential.
Genevestigatori P18054.

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], 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. 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.
    , 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. 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. 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.

Entry informationi

Entry nameiLOX12_HUMAN
AccessioniPrimary (citable) accession number: P18054
Secondary accession number(s): O95569, Q6ISF8, Q9UQM4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: February 6, 2007
Last modified: October 29, 2014
This is version 161 of the entry and version 4 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, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: 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