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Protein

Arachidonate 15-lipoxygenase B

Gene

ALOX15B

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. Converts arachidonic acid to 15S-hydroperoxyeicosatetraenoic acid/(15S)-HPETE. Also acts on linoleic acid to produce 13-hydroxyoctadecadienoic acid/13-HPODE. Has no detectable 8S-lipoxygenase activity but reacts with (8S)-HPETE to produce (8S,15S)-diHPETE. May regulate progression through the cell cycle and cell proliferation. May also regulate cytokine secretion by macrophages and therefore play a role in the immune response. May also regulate macrophage differentiation into proatherogenic foam cells.7 Publications

Catalytic activityi

Arachidonate + O2 = (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate.
Linoleate + O2 = (9Z,11E)-13-hydroxyoctadeca-9,11-dienoate.

Cofactori

Fe cationPROSITE-ProRule annotation1 PublicationNote: Binds 1 Fe cation per subunit.PROSITE-ProRule annotation1 Publication

Kineticsi

  1. KM=1100 µM for arachidonate (isoform D at pH 7.4 and 20 degrees Celsius)1 Publication
  2. KM=10 µM for linoleate (isoform A at pH 7.4 and 20 degrees Celsius)1 Publication
  3. KM=25 µM for arachidonate (isoform A at pH 7.4 and 20 degrees Celsius)1 Publication
  1. Vmax=4 µmol/min/mg enzyme with arachidonate as substrate (isoform A at pH 7.4 and 20 degrees Celsius)1 Publication
  2. Vmax=2 µmol/min/mg enzyme with arachidonate as substrate (isoform D at pH 7.4 and 20 degrees Celsius)1 Publication
  3. Vmax=4 µmol/min/mg enzyme with linoleate as substrate (isoform A at pH 7.4 and 20 degrees Celsius)1 Publication

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)DescriptionActionsGraphical viewLength
Metal bindingi15Calcium 1; via carbonyl oxygen1 Publication1
Metal bindingi17Calcium 1; via carbonyl oxygen1 Publication1
Metal bindingi39Calcium 21 Publication1
Metal bindingi40Calcium 2; via carbonyl oxygen1 Publication1
Metal bindingi42Calcium 2; via carbonyl oxygen1 Publication1
Metal bindingi44Calcium 21 Publication1
Metal bindingi85Calcium 11 Publication1
Metal bindingi86Calcium 1; via carbonyl oxygen1 Publication1
Metal bindingi373Iron; catalyticPROSITE-ProRule annotation1 Publication1
Metal bindingi378Iron; catalyticPROSITE-ProRule annotation1 Publication1
Metal bindingi553Iron; catalyticPROSITE-ProRule annotation1 Publication1
Metal bindingi676Iron; via carboxylate; catalyticPROSITE-ProRule annotation1 Publication1

GO - Molecular functioni

  • arachidonate 15-lipoxygenase activity Source: UniProtKB
  • arachidonate 8(S)-lipoxygenase activity Source: Ensembl
  • calcium ion binding Source: UniProtKB
  • iron ion binding Source: UniProtKB
  • linoleate 13S-lipoxygenase activity Source: UniProtKB
  • lipid binding Source: UniProtKB-KW

GO - Biological processi

  • apoptotic process Source: UniProtKB
  • arachidonic acid metabolic process Source: UniProtKB
  • hepoxilin biosynthetic process Source: UniProtKB
  • linoleic acid metabolic process Source: Ensembl
  • lipid metabolic process Source: UniProtKB
  • lipoxygenase pathway Source: Reactome
  • negative regulation of cell cycle Source: UniProtKB
  • negative regulation of cell migration Source: UniProtKB
  • negative regulation of cell proliferation Source: UniProtKB
  • negative regulation of growth Source: UniProtKB
  • positive regulation of chemokine secretion Source: UniProtKB
  • positive regulation of keratinocyte differentiation Source: Ensembl
  • positive regulation of macrophage derived foam cell differentiation Source: UniProtKB
  • positive regulation of peroxisome proliferator activated receptor signaling pathway Source: Ensembl
  • prostate gland development Source: UniProtKB
  • regulation of epithelial cell differentiation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

Lipid metabolism

Keywords - Ligandi

Calcium, Iron, Lipid-binding, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:HS10063-MONOMER.
BRENDAi1.13.11.33. 2681.
ReactomeiR-HSA-2142770. Synthesis of 15-eicosatetraenoic acid derivatives.
UniPathwayiUPA00881.

Chemistry databases

SwissLipidsiSLP:000000651.
SLP:000001469. [O15296-1]
SLP:000001470. [O15296-4]

Names & Taxonomyi

Protein namesi
Recommended name:
Arachidonate 15-lipoxygenase B (EC:1.13.11.33)
Short name:
15-LOX-B
Alternative name(s):
15-lipoxygenase 2
Short name:
15-LOX-2
Arachidonate 15-lipoxygenase type II
Linoleate 13-lipoxygenase 15-LOb (EC:1.13.11.-)
Gene namesi
Name:ALOX15B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:434. ALOX15B.

Subcellular locationi

Isoform A :
  • Nucleus

  • Note: Other isoforms are excluded from the nucleus.

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytoskeleton Source: UniProtKB
  • cytosol Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extrinsic component of membrane Source: UniProtKB
  • intracellular Source: UniProtKB
  • membrane Source: UniProtKB
  • nucleus Source: UniProtKB
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi39D → A: Abolishes calcium-dependent association with membranes; when associated with A-44 and A-85. 1 Publication1
Mutagenesisi44E → A: Abolishes calcium-dependent association with membranes; when associated with A-39 and A-85. 1 Publication1
Mutagenesisi85D → A: Abolishes calcium-dependent association with membranes; when associated with A-39 and A-44. 1 Publication1
Mutagenesisi602D → Y: No effect on the stereoselectivity of the oxygenation reaction. Completely changes the stereoselectivity of the oxygenation reaction to produce (8S)-HPETE instead of (15S)-HPETE; when associated with H-603. 1 Publication1
Mutagenesisi603V → H: Changes the stereoselectivity of the oxygenation reaction. Completely changes the stereoselectivity of the oxygenation reaction to produce (8S)-HPETE instead of (15S)-HPETE; when associated with Y-602. 1 Publication1

Organism-specific databases

DisGeNETi247.
OpenTargetsiENSG00000179593.
PharmGKBiPA24725.

Chemistry databases

ChEMBLiCHEMBL2457.
GuidetoPHARMACOLOGYi1389.

Polymorphism and mutation databases

BioMutaiALOX15B.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002207001 – 676Arachidonate 15-lipoxygenase BAdd BLAST676

Proteomic databases

PaxDbiO15296.
PeptideAtlasiO15296.
PRIDEiO15296.

PTM databases

iPTMnetiO15296.
PhosphoSitePlusiO15296.

Expressioni

Tissue specificityi

Expressed in hair, prostate, lung, ovary, lymph node, spinal cord and cornea.3 Publications

Inductioni

Up-regulated by UV-irradiation.1 Publication

Gene expression databases

BgeeiENSG00000179593.
CleanExiHS_ALOX15B.
ExpressionAtlasiO15296. baseline and differential.
GenevisibleiO15296. HS.

Organism-specific databases

HPAiHPA010562.

Interactioni

Protein-protein interaction databases

BioGridi106748. 8 interactors.
IntActiO15296. 2 interactors.
STRINGi9606.ENSP00000369530.

Chemistry databases

BindingDBiO15296.

Structurei

Secondary structure

1676
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 10Combined sources8
Beta strandi20 – 30Combined sources11
Beta strandi50 – 56Combined sources7
Beta strandi63 – 72Combined sources10
Turni77 – 79Combined sources3
Beta strandi87 – 95Combined sources9
Beta strandi102 – 110Combined sources9
Beta strandi115 – 119Combined sources5
Turni126 – 128Combined sources3
Helixi132 – 148Combined sources17
Beta strandi161 – 163Combined sources3
Helixi167 – 169Combined sources3
Helixi172 – 174Combined sources3
Helixi178 – 197Combined sources20
Helixi212 – 215Combined sources4
Helixi216 – 219Combined sources4
Helixi223 – 231Combined sources9
Helixi235 – 244Combined sources10
Helixi265 – 272Combined sources8
Helixi278 – 284Combined sources7
Beta strandi287 – 291Combined sources5
Helixi293 – 295Combined sources3
Beta strandi314 – 319Combined sources6
Turni321 – 323Combined sources3
Beta strandi326 – 336Combined sources11
Helixi350 – 370Combined sources21
Turni371 – 373Combined sources3
Helixi374 – 377Combined sources4
Helixi379 – 391Combined sources13
Helixi397 – 402Combined sources6
Helixi403 – 406Combined sources4
Helixi409 – 419Combined sources11
Helixi426 – 430Combined sources5
Helixi434 – 446Combined sources13
Helixi451 – 454Combined sources4
Helixi456 – 462Combined sources7
Helixi472 – 495Combined sources24
Helixi499 – 503Combined sources5
Helixi506 – 518Combined sources13
Turni519 – 522Combined sources4
Helixi524 – 526Combined sources3
Helixi535 – 549Combined sources15
Helixi551 – 557Combined sources7
Helixi560 – 564Combined sources5
Helixi567 – 569Combined sources3
Beta strandi574 – 576Combined sources3
Beta strandi580 – 583Combined sources4
Helixi587 – 593Combined sources7
Helixi597 – 611Combined sources15
Helixi631 – 656Combined sources26
Helixi667 – 669Combined sources3
Beta strandi670 – 673Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4NREX-ray2.63A1-676[»]
ProteinModelPortaliO15296.
SMRiO15296.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 124PLATPROSITE-ProRule annotationAdd BLAST123
Domaini125 – 676LipoxygenasePROSITE-ProRule annotationAdd BLAST552

Domaini

The PLAT domain can bind calcium ions; this promotes association with membranes.

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.
HOVERGENiHBG005150.
InParanoidiO15296.
KOiK08022.
OMAiLVLPYTY.
OrthoDBiEOG091G04A4.
PhylomeDBiO15296.
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]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform A (identifier: O15296-1) [UniParc]FASTAAdd to basket
Also known as: 15-LOb1

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAEFRVRVST GEAFGAGTWD KVSVSIVGTR GESPPLPLDN LGKEFTAGAE
60 70 80 90 100
EDFQVTLPED VGRVLLLRVH KAPPVLPLLG PLAPDAWFCR WFQLTPPRGG
110 120 130 140 150
HLLFPCYQWL EGAGTLVLQE GTAKVSWADH HPVLQQQRQE ELQARQEMYQ
160 170 180 190 200
WKAYNPGWPH CLDEKTVEDL ELNIKYSTAK NANFYLQAGS AFAEMKIKGL
210 220 230 240 250
LDRKGLWRSL NEMKRIFNFR RTPAAEHAFE HWQEDAFFAS QFLNGLNPVL
260 270 280 290 300
IRRCHYLPKN FPVTDAMVAS VLGPGTSLQA ELEKGSLFLV DHGILSGIQT
310 320 330 340 350
NVINGKPQFS AAPMTLLYQS PGCGPLLPLA IQLSQTPGPN SPIFLPTDDK
360 370 380 390 400
WDWLLAKTWV RNAEFSFHEA LTHLLHSHLL PEVFTLATLR QLPHCHPLFK
410 420 430 440 450
LLIPHTRYTL HINTLARELL IVPGQVVDRS TGIGIEGFSE LIQRNMKQLN
460 470 480 490 500
YSLLCLPEDI RTRGVEDIPG YYYRDDGMQI WGAVERFVSE IIGIYYPSDE
510 520 530 540 550
SVQDDRELQA WVREIFSKGF LNQESSGIPS SLETREALVQ YVTMVIFTCS
560 570 580 590 600
AKHAAVSAGQ FDSCAWMPNL PPSMQLPPPT SKGLATCEGF IATLPPVNAT
610 620 630 640 650
CDVILALWLL SKEPGDQRPL GTYPDEHFTE EAPRRSIATF QSRLAQISRG
660 670
IQERNQGLVL PYTYLDPPLI ENSVSI
Length:676
Mass (Da):75,857
Last modified:January 11, 2011 - v3
Checksum:i4F641DF2F9D492C6
GO
Isoform B (identifier: O15296-2) [UniParc]FASTAAdd to basket
Also known as: 15-LOX2sv-b

The sequence of this isoform differs from the canonical sequence as follows:
     401-429: Missing.
     483-527: Missing.

Show »
Length:602
Mass (Da):67,345
Checksum:i8804BB44095695C2
GO
Isoform C (identifier: O15296-3) [UniParc]FASTAAdd to basket
Also known as: 15-LOX2sv-c

The sequence of this isoform differs from the canonical sequence as follows:
     561-617: FDSCAWMPNL...WLLSKEPGDQ → VRKGQRPRWQ...PKAWQHARAS
     618-676: Missing.

Show »
Length:617
Mass (Da):69,136
Checksum:i3F690488B2B766AC
GO
Isoform D (identifier: O15296-4) [UniParc]FASTAAdd to basket
Also known as: 15-LOX2sv-a, 15-LOb2

The sequence of this isoform differs from the canonical sequence as follows:
     401-429: Missing.

Show »
Length:647
Mass (Da):72,523
Checksum:iEE51EEA9221CCC4B
GO

Sequence cautioni

The sequence AAD37786 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti271V → L in AAB61706 (PubMed:9177185).Curated1
Sequence conflicti271V → L in CAC34521 (PubMed:11350124).Curated1
Sequence conflicti338G → C in AAD37786 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_061334486R → H.1 PublicationCorresponds to variant rs9895916dbSNPEnsembl.1
Natural variantiVAR_024524656Q → R.4 PublicationsCorresponds to variant rs4792147dbSNPEnsembl.1
Natural variantiVAR_024525676I → V.Corresponds to variant rs7225107dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_003142401 – 429Missing in isoform B and isoform D. 1 PublicationAdd BLAST29
Alternative sequenceiVSP_003143483 – 527Missing in isoform B. 1 PublicationAdd BLAST45
Alternative sequenceiVSP_003144561 – 617FDSCA…EPGDQ → VRKGQRPRWQAGGDPAPQPH SALSAFSLTPVLGCPTCHPA CSCHHPPPKAWQHARAS in isoform C. 1 PublicationAdd BLAST57
Alternative sequenceiVSP_003145618 – 676Missing in isoform C. 1 PublicationAdd BLAST59

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U78294 mRNA. Translation: AAB61706.1.
AJ305028
, AJ305029, AJ305030, AJ305031 Genomic DNA. Translation: CAC34521.1.
AF468051 mRNA. Translation: AAL76274.1.
AF468052 mRNA. Translation: AAL76275.1.
AF468053 mRNA. Translation: AAL76276.1.
AF468054 mRNA. Translation: AAL76277.1.
AC129492 Genomic DNA. No translation available.
CH471108 Genomic DNA. Translation: EAW90098.1.
CH471108 Genomic DNA. Translation: EAW90100.1.
BC035217 mRNA. Translation: AAH35217.1.
BC063647 mRNA. Translation: AAH63647.1.
AF149095 Genomic DNA. Translation: AAD37786.1. Sequence problems.
CCDSiCCDS11128.1. [O15296-1]
CCDS32558.1. [O15296-4]
CCDS32559.1. [O15296-2]
RefSeqiNP_001034219.1. NM_001039130.1. [O15296-4]
NP_001034220.1. NM_001039131.1. [O15296-2]
NP_001132.2. NM_001141.2. [O15296-1]
UniGeneiHs.111256.

Genome annotation databases

EnsembliENST00000380173; ENSP00000369520; ENSG00000179593. [O15296-4]
ENST00000380183; ENSP00000369530; ENSG00000179593. [O15296-1]
ENST00000573359; ENSP00000460332; ENSG00000179593. [O15296-2]
GeneIDi247.
KEGGihsa:247.
UCSCiuc002gju.4. human. [O15296-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U78294 mRNA. Translation: AAB61706.1.
AJ305028
, AJ305029, AJ305030, AJ305031 Genomic DNA. Translation: CAC34521.1.
AF468051 mRNA. Translation: AAL76274.1.
AF468052 mRNA. Translation: AAL76275.1.
AF468053 mRNA. Translation: AAL76276.1.
AF468054 mRNA. Translation: AAL76277.1.
AC129492 Genomic DNA. No translation available.
CH471108 Genomic DNA. Translation: EAW90098.1.
CH471108 Genomic DNA. Translation: EAW90100.1.
BC035217 mRNA. Translation: AAH35217.1.
BC063647 mRNA. Translation: AAH63647.1.
AF149095 Genomic DNA. Translation: AAD37786.1. Sequence problems.
CCDSiCCDS11128.1. [O15296-1]
CCDS32558.1. [O15296-4]
CCDS32559.1. [O15296-2]
RefSeqiNP_001034219.1. NM_001039130.1. [O15296-4]
NP_001034220.1. NM_001039131.1. [O15296-2]
NP_001132.2. NM_001141.2. [O15296-1]
UniGeneiHs.111256.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4NREX-ray2.63A1-676[»]
ProteinModelPortaliO15296.
SMRiO15296.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106748. 8 interactors.
IntActiO15296. 2 interactors.
STRINGi9606.ENSP00000369530.

Chemistry databases

BindingDBiO15296.
ChEMBLiCHEMBL2457.
GuidetoPHARMACOLOGYi1389.
SwissLipidsiSLP:000000651.
SLP:000001469. [O15296-1]
SLP:000001470. [O15296-4]

PTM databases

iPTMnetiO15296.
PhosphoSitePlusiO15296.

Polymorphism and mutation databases

BioMutaiALOX15B.

Proteomic databases

PaxDbiO15296.
PeptideAtlasiO15296.
PRIDEiO15296.

Protocols and materials databases

DNASUi247.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000380173; ENSP00000369520; ENSG00000179593. [O15296-4]
ENST00000380183; ENSP00000369530; ENSG00000179593. [O15296-1]
ENST00000573359; ENSP00000460332; ENSG00000179593. [O15296-2]
GeneIDi247.
KEGGihsa:247.
UCSCiuc002gju.4. human. [O15296-1]

Organism-specific databases

CTDi247.
DisGeNETi247.
GeneCardsiALOX15B.
H-InvDBHIX0027139.
HGNCiHGNC:434. ALOX15B.
HPAiHPA010562.
MIMi603697. gene.
neXtProtiNX_O15296.
OpenTargetsiENSG00000179593.
PharmGKBiPA24725.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IF0U. Eukaryota.
ENOG410YN4N. LUCA.
GeneTreeiENSGT00550000074415.
HOVERGENiHBG005150.
InParanoidiO15296.
KOiK08022.
OMAiLVLPYTY.
OrthoDBiEOG091G04A4.
PhylomeDBiO15296.
TreeFamiTF105320.

Enzyme and pathway databases

UniPathwayiUPA00881.
BioCyciZFISH:HS10063-MONOMER.
BRENDAi1.13.11.33. 2681.
ReactomeiR-HSA-2142770. Synthesis of 15-eicosatetraenoic acid derivatives.

Miscellaneous databases

ChiTaRSiALOX15B. human.
GeneWikiiALOX15B.
GenomeRNAii247.
PROiO15296.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000179593.
CleanExiHS_ALOX15B.
ExpressionAtlasiO15296. baseline and differential.
GenevisibleiO15296. 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 nameiLX15B_HUMAN
AccessioniPrimary (citable) accession number: O15296
Secondary accession number(s): D3DTR2
, Q8IYQ2, Q8TEV3, Q8TEV4, Q8TEV5, Q8TEV6, Q9UKM4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: January 11, 2011
Last modified: November 30, 2016
This is version 163 of the entry and version 3 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

Caution

Despite its homology with mouse Alox8 (AC O35936), it seems not to have any 8S-lipoxygenase activity on arachidonate.Curated

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.