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O15296

- LX15B_HUMAN

UniProt

O15296 - LX15B_HUMAN

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Protein

Arachidonate 15-lipoxygenase B

Gene
ALOX15B
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. 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.4 Publications
Linoleate + O2 = (9Z,11E)-13-hydroxyoctadeca-9,11-dienoate.4 Publications

Cofactori

Binds 1 iron ion per subunit.1 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)
  3. KM=25 µM for arachidonate (isoform A at pH 7.4 and 20 degrees Celsius)

Vmax=4 µmol/min/mg enzyme with arachidonate as substrate (isoform A at pH 7.4 and 20 degrees Celsius)

Vmax=2 µmol/min/mg enzyme with arachidonate as substrate (isoform D at pH 7.4 and 20 degrees Celsius)

Vmax=4 µmol/min/mg enzyme with linoleate as substrate (isoform A at pH 7.4 and 20 degrees Celsius)

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi15 – 151Calcium 1; via carbonyl oxygen
Metal bindingi17 – 171Calcium 1; via carbonyl oxygen
Metal bindingi39 – 391Calcium 2
Metal bindingi40 – 401Calcium 2; via carbonyl oxygen
Metal bindingi42 – 421Calcium 2; via carbonyl oxygen
Metal bindingi44 – 441Calcium 2
Metal bindingi85 – 851Calcium 1
Metal bindingi86 – 861Calcium 1; via carbonyl oxygen
Metal bindingi373 – 3731Iron; catalytic
Metal bindingi378 – 3781Iron; catalytic
Metal bindingi553 – 5531Iron; catalytic
Metal bindingi676 – 6761Iron; via carboxylate; catalytic

GO - Molecular functioni

  1. arachidonate 15-lipoxygenase activity Source: UniProtKB
  2. arachidonate 8(S)-lipoxygenase activity Source: Ensembl
  3. calcium ion binding Source: UniProtKB
  4. iron ion binding Source: UniProtKB
  5. linoleate 13S-lipoxygenase activity Source: UniProtKB
  6. lipid binding Source: UniProtKB-KW

GO - Biological processi

  1. apoptotic process Source: UniProtKB
  2. arachidonic acid metabolic process Source: UniProtKB
  3. hepoxilin biosynthetic process Source: UniProtKB
  4. linoleic acid metabolic process Source: Ensembl
  5. lipid metabolic process Source: UniProtKB
  6. lipoxygenase pathway Source: Reactome
  7. negative regulation of cell cycle Source: UniProtKB
  8. negative regulation of cell migration Source: UniProtKB
  9. negative regulation of cell proliferation Source: UniProtKB
  10. negative regulation of growth Source: UniProtKB
  11. positive regulation of chemokine secretion Source: UniProtKB
  12. positive regulation of keratinocyte differentiation Source: Ensembl
  13. positive regulation of macrophage derived foam cell differentiation Source: UniProtKB
  14. positive regulation of peroxisome proliferator activated receptor signaling pathway Source: Ensembl
  15. prostate gland development Source: UniProtKB
  16. regulation of epithelial cell differentiation Source: UniProtKB
  17. small molecule metabolic process Source: Reactome
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

ReactomeiREACT_150422. Synthesis of 15-eicosatetraenoic acid derivatives.
UniPathwayiUPA00881.

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
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:434. ALOX15B.

Subcellular locationi

Isoform A : Nucleus
Note: Other isoforms are excluded from the nucleus.3 Publications
Cytoplasmcytosol. Cell membrane. Cytoplasmcytoskeleton. Membrane; Peripheral membrane protein
Note: Predominantly cytosolic; becomes enriched at membranes upon calcium binding.3 Publications

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytoskeleton Source: UniProtKB
  3. cytosol Source: UniProtKB
  4. extrinsic component of membrane Source: UniProtKB
  5. intracellular Source: UniProtKB
  6. membrane Source: UniProtKB
  7. nucleus Source: UniProtKB
  8. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi39 – 391D → A: Abolishes calcium-dependent association with membranes; when associated with A-44 and A-85. 1 Publication
Mutagenesisi44 – 441E → A: Abolishes calcium-dependent association with membranes; when associated with A-39 and A-85. 1 Publication
Mutagenesisi85 – 851D → A: Abolishes calcium-dependent association with membranes; when associated with A-39 and A-44. 1 Publication
Mutagenesisi602 – 6021D → 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 Publication
Mutagenesisi603 – 6031V → 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 Publication

Organism-specific databases

PharmGKBiPA24725.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 676676Arachidonate 15-lipoxygenase BPRO_0000220700Add
BLAST

Proteomic databases

PaxDbiO15296.
PRIDEiO15296.

PTM databases

PhosphoSiteiO15296.

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

ArrayExpressiO15296.
BgeeiO15296.
CleanExiHS_ALOX15B.
GenevestigatoriO15296.

Organism-specific databases

HPAiHPA010562.

Interactioni

Protein-protein interaction databases

BioGridi106748. 3 interactions.
STRINGi9606.ENSP00000369530.

Structurei

Secondary structure

1
676
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 108
Beta strandi20 – 3011
Beta strandi50 – 567
Beta strandi63 – 7210
Turni77 – 793
Beta strandi87 – 959
Beta strandi102 – 1109
Beta strandi115 – 1195
Turni126 – 1283
Helixi132 – 14817
Beta strandi161 – 1633
Helixi167 – 1693
Helixi172 – 1743
Helixi178 – 19720
Helixi212 – 2154
Helixi216 – 2194
Helixi223 – 2319
Helixi235 – 24410
Helixi265 – 2728
Helixi278 – 2847
Beta strandi287 – 2915
Helixi293 – 2953
Beta strandi314 – 3196
Turni321 – 3233
Beta strandi326 – 33611
Helixi350 – 37021
Turni371 – 3733
Helixi374 – 3774
Helixi379 – 39113
Helixi397 – 4026
Helixi403 – 4064
Helixi409 – 41911
Helixi426 – 4305
Helixi434 – 44613
Helixi451 – 4544
Helixi456 – 4627
Helixi472 – 49524
Helixi499 – 5035
Helixi506 – 51813
Turni519 – 5224
Helixi524 – 5263
Helixi535 – 54915
Helixi551 – 5577
Helixi560 – 5645
Helixi567 – 5693
Beta strandi574 – 5763
Beta strandi580 – 5834
Helixi587 – 5937
Helixi597 – 61115
Helixi631 – 65626
Helixi667 – 6693
Beta strandi670 – 6734

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4NREX-ray2.63A1-676[»]
ProteinModelPortaliO15296.
SMRiO15296. Positions 2-676.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 124123PLATAdd
BLAST
Domaini125 – 676552LipoxygenaseAdd
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the lipoxygenase family.
Contains 1 PLAT domain.

Phylogenomic databases

eggNOGiNOG69653.
HOVERGENiHBG005150.
InParanoidiO15296.
KOiK08022.
OMAiIQTNVIN.
OrthoDBiEOG7B05CG.
PhylomeDBiO15296.
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]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

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

MAEFRVRVST GEAFGAGTWD KVSVSIVGTR GESPPLPLDN LGKEFTAGAE    50
EDFQVTLPED VGRVLLLRVH KAPPVLPLLG PLAPDAWFCR WFQLTPPRGG 100
HLLFPCYQWL EGAGTLVLQE GTAKVSWADH HPVLQQQRQE ELQARQEMYQ 150
WKAYNPGWPH CLDEKTVEDL ELNIKYSTAK NANFYLQAGS AFAEMKIKGL 200
LDRKGLWRSL NEMKRIFNFR RTPAAEHAFE HWQEDAFFAS QFLNGLNPVL 250
IRRCHYLPKN FPVTDAMVAS VLGPGTSLQA ELEKGSLFLV DHGILSGIQT 300
NVINGKPQFS AAPMTLLYQS PGCGPLLPLA IQLSQTPGPN SPIFLPTDDK 350
WDWLLAKTWV RNAEFSFHEA LTHLLHSHLL PEVFTLATLR QLPHCHPLFK 400
LLIPHTRYTL HINTLARELL IVPGQVVDRS TGIGIEGFSE LIQRNMKQLN 450
YSLLCLPEDI RTRGVEDIPG YYYRDDGMQI WGAVERFVSE IIGIYYPSDE 500
SVQDDRELQA WVREIFSKGF LNQESSGIPS SLETREALVQ YVTMVIFTCS 550
AKHAAVSAGQ FDSCAWMPNL PPSMQLPPPT SKGLATCEGF IATLPPVNAT 600
CDVILALWLL SKEPGDQRPL GTYPDEHFTE EAPRRSIATF QSRLAQISRG 650
IQERNQGLVL PYTYLDPPLI ENSVSI 676
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 AAD37786.1 differs from that shown. Reason: Erroneous gene model prediction.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti486 – 4861R → H.1 Publication
Corresponds to variant rs9895916 [ dbSNP | Ensembl ].
VAR_061334
Natural varianti656 – 6561Q → R.4 Publications
Corresponds to variant rs4792147 [ dbSNP | Ensembl ].
VAR_024524
Natural varianti676 – 6761I → V.
Corresponds to variant rs7225107 [ dbSNP | Ensembl ].
VAR_024525

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei401 – 42929Missing in isoform B and isoform D. VSP_003142Add
BLAST
Alternative sequencei483 – 52745Missing in isoform B. VSP_003143Add
BLAST
Alternative sequencei561 – 61757FDSCA…EPGDQ → VRKGQRPRWQAGGDPAPQPH SALSAFSLTPVLGCPTCHPA CSCHHPPPKAWQHARAS in isoform C. VSP_003144Add
BLAST
Alternative sequencei618 – 67659Missing in isoform C. VSP_003145Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti271 – 2711V → L in AAB61706. 1 Publication
Sequence conflicti271 – 2711V → L in CAC34521. 1 Publication
Sequence conflicti338 – 3381G → C in AAD37786. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.3. human. [O15296-1]
uc002gjv.3. human. [O15296-4]
uc002gjw.3. human. [O15296-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
CCDSi CCDS11128.1. [O15296-1 ]
CCDS32558.1. [O15296-4 ]
CCDS32559.1. [O15296-2 ]
RefSeqi NP_001034219.1. NM_001039130.1. [O15296-4 ]
NP_001034220.1. NM_001039131.1. [O15296-2 ]
NP_001132.2. NM_001141.2. [O15296-1 ]
UniGenei Hs.111256.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4NRE X-ray 2.63 A 1-676 [» ]
ProteinModelPortali O15296.
SMRi O15296. Positions 2-676.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106748. 3 interactions.
STRINGi 9606.ENSP00000369530.

Chemistry

BindingDBi O15296.
ChEMBLi CHEMBL2457.

PTM databases

PhosphoSitei O15296.

Proteomic databases

PaxDbi O15296.
PRIDEi O15296.

Protocols and materials databases

DNASUi 247.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000380173 ; ENSP00000369520 ; ENSG00000179593 . [O15296-4 ]
ENST00000380183 ; ENSP00000369530 ; ENSG00000179593 . [O15296-1 ]
ENST00000573359 ; ENSP00000460332 ; ENSG00000179593 . [O15296-2 ]
GeneIDi 247.
KEGGi hsa:247.
UCSCi uc002gju.3. human. [O15296-1 ]
uc002gjv.3. human. [O15296-4 ]
uc002gjw.3. human. [O15296-2 ]

Organism-specific databases

CTDi 247.
GeneCardsi GC17P007942.
H-InvDB HIX0027139.
HGNCi HGNC:434. ALOX15B.
HPAi HPA010562.
MIMi 603697. gene.
neXtProti NX_O15296.
PharmGKBi PA24725.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG69653.
HOVERGENi HBG005150.
InParanoidi O15296.
KOi K08022.
OMAi IQTNVIN.
OrthoDBi EOG7B05CG.
PhylomeDBi O15296.
TreeFami TF105320.

Enzyme and pathway databases

UniPathwayi UPA00881 .
Reactomei REACT_150422. Synthesis of 15-eicosatetraenoic acid derivatives.

Miscellaneous databases

ChiTaRSi ALOX15B. human.
GeneWikii ALOX15B.
GenomeRNAii 247.
NextBioi 985.
PROi O15296.
SOURCEi Search...

Gene expression databases

ArrayExpressi O15296.
Bgeei O15296.
CleanExi HS_ALOX15B.
Genevestigatori O15296.

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] (ISOFORM A), VARIANT ARG-656, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
    Tissue: Skin.
  2. "A gene cluster encoding human epidermis-type lipoxygenases at chromosome 17p13.1: cloning, physical mapping, and expression."
    Krieg P., Marks F., Fuerstenberger G.
    Genomics 73:323-330(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ARG-656, TISSUE SPECIFICITY.
  3. "Evidence that arachidonate 15-lipoxygenase 2 is a negative cell cycle regulator in normal prostate epithelial cells."
    Tang S., Bhatia B., Maldonado C.J., Yang P., Newman R.A., Liu J., Chandra D., Traag J., Klein R.D., Fischer S.M., Chopra D., Shen J., Zhau H.E., Chung L.W.K., Tang D.G.
    J. Biol. Chem. 277:16189-16201(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B; C AND D), VARIANTS HIS-486 AND ARG-656, FUNCTION IN CELL CYCLE PROGRESSION.
  4. "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].
  5. 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] (ISOFORM A), VARIANT ARG-656.
    Tissue: Skin.
  7. "Differential characteristics of human 15-lipoxygenase isozymes and a novel splice variant of 15S-lipoxygenase."
    Kilty I., Logan A., Vickers P.J.
    Eur. J. Biochem. 266:83-93(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 337-484, ALTERNATIVE SPLICING (ISOFORMS A AND D), CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, KINETIC PARAMETERS, PATHWAY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  8. "Identification of amino acid determinants of the positional specificity of mouse 8S-lipoxygenase and human 15S-lipoxygenase-2."
    Jisaka M., Kim R.B., Boeglin W.E., Brash A.R.
    J. Biol. Chem. 275:1287-1293(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A 15S-LIPOXYGENASE, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-602 AND VAL-603.
  9. "Subcellular localization and tumor-suppressive functions of 15-lipoxygenase 2 (15-LOX2) and its splice variants."
    Bhatia B., Maldonado C.J., Tang S., Chandra D., Klein R.D., Chopra D., Shappell S.B., Yang P., Newman R.A., Tang D.G.
    J. Biol. Chem. 278:25091-25100(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELL PROLIFERATION, SUBCELLULAR LOCATION.
  10. "Double dioxygenation by mouse 8S-lipoxygenase: specific formation of a potent peroxisome proliferator-activated receptor alpha agonist."
    Jisaka M., Iwanaga C., Takahashi N., Goto T., Kawada T., Yamamoto T., Ikeda I., Nishimura K., Nagaya T., Fushiki T., Yokota K.
    Biochem. Biophys. Res. Commun. 338:136-143(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "15-Lipoxygenase-2 expression in human macrophages induces chemokine secretion and T cell migration."
    Danielsson K.N., Rydberg E.K., Ingelsten M., Akyuerek L.M., Jirholt P., Ullstroem C., Forsberg G.B., Boren J., Wiklund O., Hulten L.M.
    Atherosclerosis 199:34-40(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CYTOKINE SECRETION.
  12. "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.
  13. "Arachidonate 15-lipoxygenase type B knockdown leads to reduced lipid accumulation and inflammation in atherosclerosis."
    Magnusson L.U., Lundqvist A., Karlsson M.N., Skalen K., Levin M., Wiklund O., Boren J., Hulten L.M.
    PLoS ONE 7:E43142-E43142(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "The structure of human 15-lipoxygenase-2 with a substrate mimic."
    Kobe M.J., Neau D.B., Mitchell C.E., Bartlett S.G., Newcomer M.E.
    J. Biol. Chem. 289:8562-8569(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.63 ANGSTROMS) IN COMPLEX WITH CALCIUM AND IRON, CATALYTIC ACTIVITY, COFACTOR, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-39; GLU-44 AND ASP-85.

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: September 3, 2014
This is version 142 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.

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

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