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Protein

Arachidonate 12-lipoxygenase, 12S-type

Gene

ALOX12

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

Fe cationNote: Binds 1 Fe cation per subunit.

Enzyme regulationi

Activated by EGF.1 Publication

Kineticsi

  1. KM=8 µM for arachidonate (at pH 7.0 and 37 degrees Celsius)1 Publication
  2. KM=10 µM for arachidonate (at pH 8.0 and 25 degrees Celsius)1 Publication
  3. KM=6.2 µM for arachidonate (at pH 7.4)1 Publication
  4. KM=9 µM for linoleate (at pH 8.0 and 25 degrees Celsius)1 Publication
  5. KM=7.9 µM for leukotriene A4 (at pH 7.4)1 Publication
  6. KM=3 µM for eicosa-5,8,11,14,17-pentaenoate (at pH 7.0 and 37 degrees Celsius)1 Publication
  7. KM=35 µM for eicosa-8,11,14-trienoate (at pH 7.0 and 37 degrees Celsius)1 Publication
  8. KM=14.3 µM for 5,6-epoxy-8,11,14-eicosatrienoate (at pH 7.4)1 Publication
  1. Vmax=3 µmol/min/mg enzyme with arachidonate as substrate (at pH 8.0 and 25 degrees Celsius)1 Publication
  2. Vmax=1.057 µmol/min/mg enzyme with arachidonate as substrate (at pH 7.4)1 Publication
  3. Vmax=0.0375 µmol/min/mg enzyme with linoleate as substrate (at pH 8.0 and 25 degrees Celsius)1 Publication
  4. Vmax=0.025 µmol/min/mg enzyme with leukotriene A4 as substrate (at pH 7.4)1 Publication
  5. Vmax=0.985 µmol/min/mg enzyme with 5,6-epoxy-8,11,14-eicosatrienoate as substrate (at pH 7.4)1 Publication

pH dependencei

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

Pathwayi: hydroperoxy eicosatetraenoic acid biosynthesis

This protein is involved in the pathway hydroperoxy eicosatetraenoic acid biosynthesis, which is part of Lipid metabolism.1 Publication
View all proteins of this organism that are known to be involved in the pathway hydroperoxy eicosatetraenoic acid biosynthesis and in Lipid metabolism.

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

GO - Biological processi

  • aging Source: Ensembl
  • arachidonic acid metabolic process Source: UniProtKB
  • cellular response to lipid Source: Ensembl
  • establishment of skin barrier Source: UniProtKB
  • fatty acid oxidation Source: UniProtKB
  • hepoxilin biosynthetic process Source: UniProtKB
  • hepoxilin metabolic process Source: Reactome
  • leukotriene A4 metabolic process Source: UniProtKB
  • linoleic acid metabolic process Source: UniProtKB
  • lipoxin A4 biosynthetic process Source: UniProtKB
  • lipoxin B4 biosynthetic process Source: UniProtKB
  • lipoxin metabolic process Source: Reactome
  • lipoxygenase pathway Source: UniProtKB
  • movement of cell or subcellular component Source: UniProtKB
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of muscle cell apoptotic process Source: UniProtKB
  • negative regulation of platelet aggregation Source: UniProtKB
  • positive regulation of angiogenesis Source: UniProtKB
  • positive regulation of cell adhesion Source: UniProtKB
  • positive regulation of cell growth Source: UniProtKB
  • positive regulation of cell migration Source: UniProtKB
  • positive regulation of cell proliferation Source: UniProtKB
  • positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
  • positive regulation of endothelial cell differentiation Source: Ensembl
  • positive regulation of endothelial cell migration Source: Ensembl
  • positive regulation of gene expression Source: Ensembl
  • positive regulation of mitochondrial depolarization Source: Ensembl
  • positive regulation of smooth muscle cell proliferation Source: Ensembl
  • positive regulation of vasodilation Source: Ensembl
  • reactive oxygen species metabolic process Source: UniProtKB
  • 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.
BRENDAi1.13.11.31. 2681.
ReactomeiR-HSA-2142696. Synthesis of Hepoxilins (HX) and Trioxilins (TrX).
R-HSA-2142700. Synthesis of Lipoxins (LX).
R-HSA-2142712. Synthesis of 12-eicosatetraenoic acid derivatives.
UniPathwayiUPA00881.

Chemistry

SwissLipidsiSLP:000000670.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:429. ALOX12.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • membrane Source: UniProtKB
  • sarcolemma Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Involvement in diseasei

Esophageal cancer (ESCR)1 Publication
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
Disease descriptionA 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.
See also OMIM:133239
Colorectal cancer (CRC)1 Publication
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
Disease descriptionA 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.
See also OMIM:114500

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.

Chemistry

ChEMBLiCHEMBL3687.
GuidetoPHARMACOLOGYi1387.

Polymorphism and mutation databases

BioMutaiALOX12.
DMDMi125987838.

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei246 – 2461PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP18054.
PeptideAtlasiP18054.
PRIDEiP18054.

PTM databases

iPTMnetiP18054.
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

BgeeiENSG00000108839.
CleanExiHS_ALOX12.
ExpressionAtlasiP18054. baseline and differential.
GenevisibleiP18054. HS.

Organism-specific databases

HPAiCAB019287.
HPA010691.

Interactioni

Binary interactionsi

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

Protein-protein interaction databases

BioGridi106740. 6 interactions.
IntActiP18054. 4 interactions.
MINTiMINT-1206406.
STRINGi9606.ENSP00000251535.

Chemistry

BindingDBiP18054.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

eggNOGiENOG410IF0U. Eukaryota.
ENOG410YN4N. LUCA.
GeneTreeiENSGT00550000074415.
HOGENOMiHOG000234358.
HOVERGENiHBG005150.
InParanoidiP18054.
KOiK00458.
OMAiMRFHEDK.
OrthoDBiEOG091G04A4.
PhylomeDBiP18054.
TreeFamiTF105320.

Family and domain databases

Gene3Di2.60.60.20. 1 hit.
InterProiIPR000907. LipOase.
IPR013819. LipOase_C.
IPR020834. LipOase_CS.
IPR020833. LipOase_Fe_BS.
IPR001885. LipOase_mml.
IPR001024. PLAT/LH2_dom.
[Graphical view]
PANTHERiPTHR11771. PTHR11771. 1 hit.
PfamiPF00305. Lipoxygenase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]
PRINTSiPR00087. LIPOXYGENASE.
PR00467. MAMLPOXGNASE.
SMARTiSM00308. LH2. 1 hit.
[Graphical view]
SUPFAMiSSF48484. SSF48484. 1 hit.
SSF49723. SSF49723. 1 hit.
PROSITEiPS00711. LIPOXYGENASE_1. 1 hit.
PS00081. LIPOXYGENASE_2. 1 hit.
PS51393. LIPOXYGENASE_3. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P18054-1 [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:
EMBLi
GenBanki
DDBJi
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.

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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi106740. 6 interactions.
IntActiP18054. 4 interactions.
MINTiMINT-1206406.
STRINGi9606.ENSP00000251535.

Chemistry

BindingDBiP18054.
ChEMBLiCHEMBL3687.
GuidetoPHARMACOLOGYi1387.
SwissLipidsiSLP:000000670.

PTM databases

iPTMnetiP18054.
PhosphoSiteiP18054.

Polymorphism and mutation databases

BioMutaiALOX12.
DMDMi125987838.

Proteomic databases

PaxDbiP18054.
PeptideAtlasiP18054.
PRIDEiP18054.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi239.
GeneCardsiALOX12.
H-InvDBHIX0039067.
HGNCiHGNC:429. ALOX12.
HPAiCAB019287.
HPA010691.
MIMi114500. phenotype.
133239. phenotype.
152391. gene.
neXtProtiNX_P18054.
PharmGKBiPA45.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IF0U. Eukaryota.
ENOG410YN4N. LUCA.
GeneTreeiENSGT00550000074415.
HOGENOMiHOG000234358.
HOVERGENiHBG005150.
InParanoidiP18054.
KOiK00458.
OMAiMRFHEDK.
OrthoDBiEOG091G04A4.
PhylomeDBiP18054.
TreeFamiTF105320.

Enzyme and pathway databases

UniPathwayiUPA00881.
BioCyciMetaCyc:HS03167-MONOMER.
BRENDAi1.13.11.31. 2681.
ReactomeiR-HSA-2142696. Synthesis of Hepoxilins (HX) and Trioxilins (TrX).
R-HSA-2142700. Synthesis of Lipoxins (LX).
R-HSA-2142712. Synthesis of 12-eicosatetraenoic acid derivatives.

Miscellaneous databases

EvolutionaryTraceiP18054.
GeneWikiiALOX12.
GenomeRNAii239.
PROiP18054.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000108839.
CleanExiHS_ALOX12.
ExpressionAtlasiP18054. baseline and differential.
GenevisibleiP18054. HS.

Family and domain databases

Gene3Di2.60.60.20. 1 hit.
InterProiIPR000907. LipOase.
IPR013819. LipOase_C.
IPR020834. LipOase_CS.
IPR020833. LipOase_Fe_BS.
IPR001885. LipOase_mml.
IPR001024. PLAT/LH2_dom.
[Graphical view]
PANTHERiPTHR11771. PTHR11771. 1 hit.
PfamiPF00305. Lipoxygenase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]
PRINTSiPR00087. LIPOXYGENASE.
PR00467. MAMLPOXGNASE.
SMARTiSM00308. LH2. 1 hit.
[Graphical view]
SUPFAMiSSF48484. SSF48484. 1 hit.
SSF49723. SSF49723. 1 hit.
PROSITEiPS00711. LIPOXYGENASE_1. 1 hit.
PS00081. LIPOXYGENASE_2. 1 hit.
PS51393. LIPOXYGENASE_3. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: September 7, 2016
This is version 180 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

Similar proteinsi

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