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O15296 (LX15B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Arachidonate 15-lipoxygenase B

Short name=15-LOX-B
EC=1.13.11.33
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 names
Name:ALOX15B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length676 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Non-heme iron-containing dioxygenase that catalyzes the stereo-specific peroxidation of free and esterified polyunsaturated fatty acids generating a spectrum of bioactive lipid mediators. 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 macrophages differentiation into proatherogenic foam cells. Ref.3 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13

Catalytic activity

Arachidonate + O2 = (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate. Ref.1 Ref.7 Ref.8

Linoleate + O2 = (9Z,11E)-13-hydroxyoctadeca-9,11-dienoate. Ref.1 Ref.7 Ref.8

Cofactor

Binds 1 iron ion per subunit By similarity.

Pathway

Lipid metabolism; hydroperoxy eicosatetraenoic acid biosynthesis. Ref.7

Subcellular location

Isoform A: Nucleus. Note: Other isoforms are excluded from the nucleus. Ref.7 Ref.9

Cytoplasmcytosol. Cell membrane. Cytoplasmcytoskeleton. Note: Predominantly cytosolic but associated with other subcellular location like membranes where it is enriched upon stimulation by calcium. Ref.7 Ref.9

Tissue specificity

Expressed in hair, prostate, lung, ovary, lymph node, spinal cord and cornea. Ref.1 Ref.2 Ref.7

Induction

Up-regulated by UV-irradiation. Ref.12

Sequence similarities

Belongs to the lipoxygenase family.

Contains 1 lipoxygenase domain.

Contains 1 PLAT domain.

Caution

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

Biophysicochemical properties

Kinetic parameters:

KM=1100 µM for arachidonate (isoform D at pH 7.4 and 20 degrees Celsius) Ref.7

KM=10 µM for linoleate (isoform A at pH 7.4 and 20 degrees Celsius)

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)

Sequence caution

The sequence AAD37786.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Cellular componentCell membrane
Cytoplasm
Cytoskeleton
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandIron
Metal-binding
   Molecular functionDioxygenase
Oxidoreductase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Traceable author statement Ref.3. Source: UniProtKB

arachidonic acid metabolic process

Inferred from direct assay Ref.7Ref.8Ref.1. Source: UniProtKB

hepoxilin biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

linoleic acid metabolic process

Inferred from electronic annotation. Source: Ensembl

lipid metabolic process

Traceable author statement Ref.3. Source: UniProtKB

lipoxygenase pathway

Traceable author statement. Source: Reactome

negative regulation of cell cycle

Inferred from direct assay Ref.3. Source: UniProtKB

negative regulation of cell migration

Traceable author statement Ref.3. Source: UniProtKB

negative regulation of cell proliferation

Inferred from direct assay Ref.3. Source: UniProtKB

negative regulation of growth

Inferred from direct assay Ref.3. Source: UniProtKB

positive regulation of chemokine secretion

Inferred from mutant phenotype Ref.11. Source: UniProtKB

positive regulation of keratinocyte differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of macrophage derived foam cell differentiation

Inferred from mutant phenotype Ref.13. Source: UniProtKB

positive regulation of peroxisome proliferator activated receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

prostate gland development

Non-traceable author statement Ref.3. Source: UniProtKB

regulation of epithelial cell differentiation

Non-traceable author statement Ref.3. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytoskeleton

Inferred from direct assay Ref.9. Source: UniProtKB

cytosol

Inferred from direct assay Ref.7Ref.9. Source: UniProtKB

intracellular

Inferred from direct assay Ref.3. Source: UniProtKB

membrane

Inferred from direct assay Ref.7. Source: UniProtKB

nucleus

Inferred from direct assay Ref.9. Source: UniProtKB

plasma membrane

Inferred from direct assay Ref.9. Source: UniProtKB

   Molecular_functionarachidonate 15-lipoxygenase activity

Inferred from direct assay Ref.7Ref.8Ref.1. Source: UniProtKB

arachidonate 8(S)-lipoxygenase activity

Inferred from electronic annotation. Source: Ensembl

iron ion binding

Inferred from electronic annotation. Source: InterPro

linoleate 13S-lipoxygenase activity

Inferred from direct assay Ref.7. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: O15296-1)

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.
Isoform B (identifier: O15296-2)

Also known as: 15-LOX2sv-b;

The sequence of this isoform differs from the canonical sequence as follows:
     401-429: Missing.
     483-527: Missing.
Isoform C (identifier: O15296-3)

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.
Isoform D (identifier: O15296-4)

Also known as: 15-LOX2sv-a; 15-LOb2;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 676676Arachidonate 15-lipoxygenase B
PRO_0000220700

Regions

Domain2 – 124123PLAT
Domain125 – 676552Lipoxygenase

Sites

Metal binding3731Iron; catalytic By similarity
Metal binding3781Iron; catalytic By similarity
Metal binding5531Iron; catalytic By similarity
Metal binding6761Iron; via carboxylate; catalytic By similarity

Natural variations

Alternative sequence401 – 42929Missing in isoform B and isoform D.
VSP_003142
Alternative sequence483 – 52745Missing in isoform B.
VSP_003143
Alternative sequence561 – 61757FDSCA…EPGDQ → VRKGQRPRWQAGGDPAPQPH SALSAFSLTPVLGCPTCHPA CSCHHPPPKAWQHARAS in isoform C.
VSP_003144
Alternative sequence618 – 67659Missing in isoform C.
VSP_003145
Natural variant4861R → H. Ref.3
Corresponds to variant rs9895916 [ dbSNP | Ensembl ].
VAR_061334
Natural variant6561Q → R. Ref.1 Ref.2 Ref.3 Ref.6
Corresponds to variant rs4792147 [ dbSNP | Ensembl ].
VAR_024524
Natural variant6761I → V.
Corresponds to variant rs7225107 [ dbSNP | Ensembl ].
VAR_024525

Experimental info

Mutagenesis6021D → 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. Ref.8
Mutagenesis6031V → 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. Ref.8
Sequence conflict2711V → L in AAB61706. Ref.1
Sequence conflict2711V → L in CAC34521. Ref.2
Sequence conflict3381G → C in AAD37786. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Isoform A (15-LOb1) [UniParc].

Last modified January 11, 2011. Version 3.
Checksum: 4F641DF2F9D492C6

FASTA67675,857
        10         20         30         40         50         60 
MAEFRVRVST GEAFGAGTWD KVSVSIVGTR GESPPLPLDN LGKEFTAGAE EDFQVTLPED 

        70         80         90        100        110        120 
VGRVLLLRVH KAPPVLPLLG PLAPDAWFCR WFQLTPPRGG HLLFPCYQWL EGAGTLVLQE 

       130        140        150        160        170        180 
GTAKVSWADH HPVLQQQRQE ELQARQEMYQ WKAYNPGWPH CLDEKTVEDL ELNIKYSTAK 

       190        200        210        220        230        240 
NANFYLQAGS AFAEMKIKGL LDRKGLWRSL NEMKRIFNFR RTPAAEHAFE HWQEDAFFAS 

       250        260        270        280        290        300 
QFLNGLNPVL IRRCHYLPKN FPVTDAMVAS VLGPGTSLQA ELEKGSLFLV DHGILSGIQT 

       310        320        330        340        350        360 
NVINGKPQFS AAPMTLLYQS PGCGPLLPLA IQLSQTPGPN SPIFLPTDDK WDWLLAKTWV 

       370        380        390        400        410        420 
RNAEFSFHEA LTHLLHSHLL PEVFTLATLR QLPHCHPLFK LLIPHTRYTL HINTLARELL 

       430        440        450        460        470        480 
IVPGQVVDRS TGIGIEGFSE LIQRNMKQLN YSLLCLPEDI RTRGVEDIPG YYYRDDGMQI 

       490        500        510        520        530        540 
WGAVERFVSE IIGIYYPSDE SVQDDRELQA WVREIFSKGF LNQESSGIPS SLETREALVQ 

       550        560        570        580        590        600 
YVTMVIFTCS AKHAAVSAGQ FDSCAWMPNL PPSMQLPPPT SKGLATCEGF IATLPPVNAT 

       610        620        630        640        650        660 
CDVILALWLL SKEPGDQRPL GTYPDEHFTE EAPRRSIATF QSRLAQISRG IQERNQGLVL 

       670 
PYTYLDPPLI ENSVSI 

« Hide

Isoform B (15-LOX2sv-b) [UniParc].

Checksum: 8804BB44095695C2
Show »

FASTA60267,345
Isoform C (15-LOX2sv-c) [UniParc].

Checksum: 3F690488B2B766AC
Show »

FASTA61769,136
Isoform D (15-LOX2sv-a) (15-LOb2) [UniParc].

Checksum: EE51EEA9221CCC4B
Show »

FASTA64772,523

References

« Hide 'large scale' references
[1]"Discovery of a second 15S-lipoxygenase in humans."
Brash A.R., Boeglin W.E., Chang M.S.
Proc. Natl. Acad. Sci. U.S.A. 94:6148-6152(1997) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U78294 mRNA. Translation: AAB61706.1.
AJ305028 expand/collapse EMBL AC list , 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.
RefSeqNP_001034219.1. NM_001039130.1.
NP_001034220.1. NM_001039131.1.
NP_001132.2. NM_001141.2.
UniGeneHs.111256.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4NREX-ray2.63A1-676[»]
ProteinModelPortalO15296.
SMRO15296. Positions 2-676.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106748. 3 interactions.
STRING9606.ENSP00000369530.

Chemistry

BindingDBO15296.
ChEMBLCHEMBL2457.

PTM databases

PhosphoSiteO15296.

Proteomic databases

PaxDbO15296.
PRIDEO15296.

Protocols and materials databases

DNASU247.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000380173; ENSP00000369520; ENSG00000179593. [O15296-4]
ENST00000380183; ENSP00000369530; ENSG00000179593. [O15296-1]
ENST00000573359; ENSP00000460332; ENSG00000179593. [O15296-2]
GeneID247.
KEGGhsa:247.
UCSCuc002gju.3. human. [O15296-1]
uc002gjv.3. human. [O15296-4]
uc002gjw.3. human. [O15296-2]

Organism-specific databases

CTD247.
GeneCardsGC17P007942.
H-InvDBHIX0027139.
HGNCHGNC:434. ALOX15B.
HPAHPA010562.
MIM603697. gene.
neXtProtNX_O15296.
PharmGKBPA24725.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG69653.
HOVERGENHBG005150.
InParanoidO15296.
KOK08022.
OMAIQTNVIN.
OrthoDBEOG7B05CG.
PhylomeDBO15296.
TreeFamTF105320.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
UniPathwayUPA00881.

Gene expression databases

ArrayExpressO15296.
BgeeO15296.
CleanExHS_ALOX15B.
GenevestigatorO15296.

Family and domain databases

Gene3D2.60.60.20. 1 hit.
InterProIPR008976. Lipase_LipOase.
IPR000907. LipOase.
IPR013819. LipOase_C.
IPR020834. LipOase_CS.
IPR020833. LipOase_Fe_BS.
IPR001885. LipOase_mml.
IPR001024. PLAT/LH2_dom.
[Graphical view]
PANTHERPTHR11771. PTHR11771. 1 hit.
PfamPF00305. Lipoxygenase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]
PRINTSPR00087. LIPOXYGENASE.
PR00467. MAMLPOXGNASE.
SMARTSM00308. LH2. 1 hit.
[Graphical view]
SUPFAMSSF48484. SSF48484. 1 hit.
SSF49723. SSF49723. 1 hit.
PROSITEPS00711. LIPOXYGENASE_1. 1 hit.
PS00081. LIPOXYGENASE_2. 1 hit.
PS51393. LIPOXYGENASE_3. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSALOX15B. human.
GeneWikiALOX15B.
GenomeRNAi247.
NextBio985.
PROO15296.
SOURCESearch...

Entry information

Entry nameLX15B_HUMAN
AccessionPrimary (citable) accession number: O15296
Secondary accession number(s): D3DTR2 expand/collapse secondary AC list , Q8IYQ2, Q8TEV3, Q8TEV4, Q8TEV5, Q8TEV6, Q9UKM4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: January 11, 2011
Last modified: April 16, 2014
This is version 138 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

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