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O75342

- LX12B_HUMAN

UniProt

O75342 - LX12B_HUMAN

Protein

Arachidonate 12-lipoxygenase, 12R-type

Gene

ALOX12B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      Previous versions | rss
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    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 (12R)-hydroperoxyeicosatetraenoic acid/(12R)-HPETE and minor stereoisomers. In the skin, acts upstream of ALOXE3 on the lineolate moiety of esterified omega-hydroxyacyl-sphingosine (EOS) ceramides to produce an epoxy-ketone derivative, a crucial step in the conjugation of omega-hydroxyceramide to membrane proteins. Therefore plays a crucial role in the synthesis of corneocytes lipid envelope and the establishment of the skin barrier to water loss. May also play a role in the regulation of the expression of airway mucins.3 Publications

    Catalytic activityi

    Arachidonate + O2 = (5Z,8Z,10E,14Z)-(12R)-12-hydroperoxyicosa-5,8,10,14-tetraenoate.1 Publication

    Cofactori

    Binds 1 iron ion per subunit.PROSITE-ProRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi398 – 3981Iron; catalyticPROSITE-ProRule annotation
    Metal bindingi403 – 4031Iron; catalyticPROSITE-ProRule annotation
    Metal bindingi578 – 5781Iron; catalyticPROSITE-ProRule annotation
    Metal bindingi582 – 5821Iron; catalyticPROSITE-ProRule annotation
    Metal bindingi701 – 7011Iron; via carboxylate; catalyticPROSITE-ProRule annotation

    GO - Molecular functioni

    1. arachidonate 12-lipoxygenase activity Source: UniProtKB
    2. iron ion binding Source: InterPro
    3. linoleate 9S-lipoxygenase activity Source: UniProtKB
    4. oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Source: UniProtKB
    5. protein binding Source: IntAct

    GO - Biological processi

    1. arachidonic acid metabolic process Source: UniProtKB
    2. ceramide biosynthetic process Source: UniProtKB
    3. establishment of skin barrier Source: UniProtKB
    4. hepoxilin biosynthetic process Source: UniProtKB
    5. linoleic acid metabolic process Source: UniProtKB
    6. lipoxygenase pathway Source: UniProtKB
    7. oxidation-reduction process Source: UniProtKB
    8. positive regulation of gene expression Source: UniProtKB
    9. positive regulation of MAPK cascade Source: UniProtKB
    10. positive regulation of mucus secretion Source: UniProtKB
    11. protein lipidation Source: UniProtKB
    12. small molecule metabolic process Source: Reactome
    13. sphingolipid metabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Dioxygenase, Oxidoreductase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Keywords - Ligandi

    Iron, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_150201. Synthesis of 12-eicosatetraenoic acid derivatives.
    UniPathwayiUPA00222.
    UPA00881.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Arachidonate 12-lipoxygenase, 12R-type (EC:1.13.11.-)
    Short name:
    12R-LOX
    Short name:
    12R-lipoxygenase
    Alternative name(s):
    Epidermis-type lipoxygenase 12
    Gene namesi
    Name:ALOX12B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:430. ALOX12B.

    Subcellular locationi

    Cytoplasm PROSITE-ProRule annotation

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Ichthyosis, congenital, autosomal recessive 2 (ARCI2) [MIM:242100]: A form of autosomal recessive congenital ichthyosis, a disorder of keratinization with abnormal differentiation and desquamation of the epidermis, resulting in abnormal skin scaling over the whole body. The main skin phenotypes are lamellar ichthyosis (LI) and non-bullous congenital ichthyosiform erythroderma (NCIE), although phenotypic overlap within the same patient or among patients from the same family can occur. Lamellar ichthyosis is a condition often associated with an embedment in a collodion-like membrane at birth; skin scales later develop, covering the entire body surface. Non-bullous congenital ichthyosiform erythroderma characterized by fine whitish scaling on an erythrodermal background; larger brownish scales are present on the buttocks, neck and legs.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti24 – 241L → P in ARCI2. 1 Publication
    VAR_069545
    Natural varianti67 – 671I → F in ARCI2. 1 Publication
    VAR_069546
    Natural varianti114 – 1141R → W in ARCI2. 1 Publication
    VAR_069547
    Natural varianti127 – 1271P → S in ARCI2. 1 Publication
    VAR_069548
    Natural varianti195 – 1951F → L in ARCI2; complete loss of the enzyme activity. 1 Publication
    VAR_069549
    Natural varianti318 – 3181Y → C in ARCI2. 1 Publication
    VAR_069550
    Natural varianti382 – 3821K → E in ARCI2; complete loss of the enzyme activity. 1 Publication
    VAR_069551
    Natural varianti383 – 3831T → M in ARCI2. 1 Publication
    VAR_069552
    Natural varianti416 – 4161N → K in ARCI2. 1 Publication
    VAR_069553
    Natural varianti426 – 4261L → P in ARCI2; complete loss of the enzyme activity. 1 Publication
    VAR_015173
    Natural varianti462 – 4621G → D in ARCI2. 1 Publication
    VAR_069554
    Natural varianti488 – 4881R → H in ARCI2; complete loss of the enzyme activity. 1 Publication
    VAR_069555
    Natural varianti521 – 5211Y → C in ARCI2. 2 Publications
    VAR_069556
    Natural varianti527 – 5271V → M in ARCI2. 1 Publication
    VAR_069557
    Natural varianti578 – 5781H → Q in ARCI2; complete loss of the enzyme activity. 1 Publication
    VAR_015174
    Natural varianti597 – 5971A → E in ARCI2. 1 Publication
    VAR_069558
    Natural varianti664 – 6641A → P in ARCI2; complete loss of the enzyme activity. 1 Publication
    VAR_069559
    Natural varianti679 – 6791R → L in ARCI2. 1 Publication
    VAR_069560

    Keywords - Diseasei

    Disease mutation, Ichthyosis

    Organism-specific databases

    MIMi242100. phenotype.
    Orphaneti79394. Congenital non-bullous ichthyosiform erythroderma.
    313. Lamellar ichthyosis.
    281122. Self-healing collodion baby.
    PharmGKBiPA24722.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 701701Arachidonate 12-lipoxygenase, 12R-typePRO_0000220689Add
    BLAST

    Proteomic databases

    PaxDbiO75342.
    PRIDEiO75342.

    PTM databases

    PhosphoSiteiO75342.

    Expressioni

    Tissue specificityi

    Expressed in B-cells, hair follicles, foreskin keratinocytes and adult skin. Also expressed in psoriatic tissue.1 Publication

    Gene expression databases

    BgeeiO75342.
    CleanExiHS_ALOX12B.
    GenevestigatoriO75342.

    Organism-specific databases

    HPAiHPA024002.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ALOXE3Q9BYJ12EBI-6925925,EBI-6925949

    Protein-protein interaction databases

    IntActiO75342. 2 interactions.
    STRINGi9606.ENSP00000315167.

    Structurei

    3D structure databases

    ProteinModelPortaliO75342.
    SMRiO75342. Positions 2-701.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 119118PLATPROSITE-ProRule annotationAdd
    BLAST
    Domaini120 – 701582LipoxygenasePROSITE-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.
    HOGENOMiHOG000234358.
    HOVERGENiHBG005150.
    InParanoidiO75342.
    KOiK08021.
    OMAiYHFPAYQ.
    OrthoDBiEOG7V49XR.
    PhylomeDBiO75342.
    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.

    O75342-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATYKVRVAT GTDLLSGTRD SISLTIVGTQ GESHKQLLNH FGRDFATGAV    50
    GQYTVQCPQD LGELIIIRLH KERYAFFPKD PWYCNYVQIC APNGRIYHFP 100
    AYQWMDGYET LALREATGKT TADDSLPVLL EHRKEEIRAK QDFYHWRVFL 150
    PGLPSYVHIP SYRPPVRRHR NPNRPEWNGY IPGFPILINF KATKFLNLNL 200
    RYSFLKTASF FVRLGPMALA FKVRGLLDCK HSWKRLKDIR KIFPGKKSVV 250
    SEYVAEHWAE DTFFGYQYLN GVNPGLIRRC TRIPDKFPVT DDMVAPFLGE 300
    GTCLQAELEK GNIYLADYRI MEGIPTVELS GRKQHHCAPL CLLHFGPEGK 350
    MMPIAIQLSQ TPGPDCPIFL PSDSEWDWLL AKTWVRYAEF YSHEAIAHLL 400
    ETHLIAEAFC LALLRNLPMC HPLYKLLIPH TRYTVQINSI GRAVLLNEGG 450
    LSAKGMSLGV EGFAGVMVRA LSELTYDSLY LPNDFVERGV QDLPGYYYRD 500
    DSLAVWNALE KYVTEIITYY YPSDAAVEGD PELQSWVQEI FKECLLGRES 550
    SGFPRCLRTV PELIRYVTIV IYTCSAKHAA VNTGQMEFTA WMPNFPASMR 600
    NPPIQTKGLT TLETFMDTLP DVKTTCITLL VLWTLSREPD DRRPLGHFPD 650
    IHFVEEAPRR SIEAFRQRLN QISHDIRQRN KCLPIPYYYL DPVLIENSIS 700
    I 701
    Length:701
    Mass (Da):80,356
    Last modified:November 1, 1998 - v1
    Checksum:iC334075759F8B077
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti24 – 241L → P in ARCI2. 1 Publication
    VAR_069545
    Natural varianti67 – 671I → F in ARCI2. 1 Publication
    VAR_069546
    Natural varianti94 – 941G → S.
    Corresponds to variant rs8077661 [ dbSNP | Ensembl ].
    VAR_050000
    Natural varianti114 – 1141R → W in ARCI2. 1 Publication
    VAR_069547
    Natural varianti127 – 1271P → S in ARCI2. 1 Publication
    VAR_069548
    Natural varianti195 – 1951F → L in ARCI2; complete loss of the enzyme activity. 1 Publication
    VAR_069549
    Natural varianti318 – 3181Y → C in ARCI2. 1 Publication
    VAR_069550
    Natural varianti382 – 3821K → E in ARCI2; complete loss of the enzyme activity. 1 Publication
    VAR_069551
    Natural varianti383 – 3831T → M in ARCI2. 1 Publication
    VAR_069552
    Natural varianti416 – 4161N → K in ARCI2. 1 Publication
    VAR_069553
    Natural varianti426 – 4261L → P in ARCI2; complete loss of the enzyme activity. 1 Publication
    VAR_015173
    Natural varianti462 – 4621G → D in ARCI2. 1 Publication
    VAR_069554
    Natural varianti488 – 4881R → H in ARCI2; complete loss of the enzyme activity. 1 Publication
    VAR_069555
    Natural varianti521 – 5211Y → C in ARCI2. 2 Publications
    VAR_069556
    Natural varianti527 – 5271V → M in ARCI2. 1 Publication
    VAR_069557
    Natural varianti578 – 5781H → Q in ARCI2; complete loss of the enzyme activity. 1 Publication
    VAR_015174
    Natural varianti597 – 5971A → E in ARCI2. 1 Publication
    VAR_069558
    Natural varianti664 – 6641A → P in ARCI2; complete loss of the enzyme activity. 1 Publication
    VAR_069559
    Natural varianti679 – 6791R → L in ARCI2. 1 Publication
    VAR_069560

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF038461 mRNA. Translation: AAC39770.1.
    AF059250 mRNA. Translation: AAC79680.1.
    AJ305026, AJ305027 Genomic DNA. Translation: CAC34520.1.
    BC041058 mRNA. Translation: AAH41058.1.
    CCDSiCCDS11129.1.
    RefSeqiNP_001130.1. NM_001139.2.
    UniGeneiHs.136574.

    Genome annotation databases

    EnsembliENST00000319144; ENSP00000315167; ENSG00000179477.
    GeneIDi242.
    KEGGihsa:242.
    UCSCiuc002gjy.1. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Protein Spotlight

    about water - Issue 153 of September 2013

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF038461 mRNA. Translation: AAC39770.1 .
    AF059250 mRNA. Translation: AAC79680.1 .
    AJ305026 , AJ305027 Genomic DNA. Translation: CAC34520.1 .
    BC041058 mRNA. Translation: AAH41058.1 .
    CCDSi CCDS11129.1.
    RefSeqi NP_001130.1. NM_001139.2.
    UniGenei Hs.136574.

    3D structure databases

    ProteinModelPortali O75342.
    SMRi O75342. Positions 2-701.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi O75342. 2 interactions.
    STRINGi 9606.ENSP00000315167.

    Chemistry

    BindingDBi O75342.

    PTM databases

    PhosphoSitei O75342.

    Proteomic databases

    PaxDbi O75342.
    PRIDEi O75342.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000319144 ; ENSP00000315167 ; ENSG00000179477 .
    GeneIDi 242.
    KEGGi hsa:242.
    UCSCi uc002gjy.1. human.

    Organism-specific databases

    CTDi 242.
    GeneCardsi GC17M007975.
    GeneReviewsi ALOX12B.
    HGNCi HGNC:430. ALOX12B.
    HPAi HPA024002.
    MIMi 242100. phenotype.
    603741. gene.
    neXtProti NX_O75342.
    Orphaneti 79394. Congenital non-bullous ichthyosiform erythroderma.
    313. Lamellar ichthyosis.
    281122. Self-healing collodion baby.
    PharmGKBi PA24722.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG69653.
    HOGENOMi HOG000234358.
    HOVERGENi HBG005150.
    InParanoidi O75342.
    KOi K08021.
    OMAi YHFPAYQ.
    OrthoDBi EOG7V49XR.
    PhylomeDBi O75342.
    TreeFami TF105320.

    Enzyme and pathway databases

    UniPathwayi UPA00222 .
    UPA00881 .
    Reactomei REACT_150201. Synthesis of 12-eicosatetraenoic acid derivatives.

    Miscellaneous databases

    GeneWikii ALOX12B.
    GenomeRNAii 242.
    NextBioi 966.
    PROi O75342.
    SOURCEi Search...

    Gene expression databases

    Bgeei O75342.
    CleanExi HS_ALOX12B.
    Genevestigatori O75342.

    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

    1. "A 12R-lipoxygenase in human skin: mechanistic evidence, molecular cloning, and expression."
      Boeglin W.E., Kim R.B., Brash A.R.
      Proc. Natl. Acad. Sci. U.S.A. 95:6744-6749(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
      Tissue: Hair follicle.
    2. "Human 12(R)-lipoxygenase and the mouse ortholog. Molecular cloning, expression, and gene chromosomal assignment."
      Sun D., McDonnell M., Chen X.-S., Lakkis M.M., Li H., Isaacs S.N., Elsea S.H., Patel P.I., Funk C.D.
      J. Biol. Chem. 273:33540-33547(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
      Tissue: B-cell.
    3. "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].
    4. "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].
      Tissue: Brain.
    5. "Lipoxygenases mediate the effect of essential fatty acid in skin barrier formation: a proposed role in releasing omega-hydroxyceramide for construction of the corneocyte lipid envelope."
      Zheng Y., Yin H., Boeglin W.E., Elias P.M., Crumrine D., Beier D.R., Brash A.R.
      J. Biol. Chem. 286:24046-24056(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY.
    6. "A role for 12R-lipoxygenase in MUC5AC expression by respiratory epithelial cells."
      Garcia-Verdugo I., BenMohamed F., Tattermusch S., Leduc D., Charpigny G., Chignard M., Ollero M., Touqui L.
      Eur. Respir. J. 40:714-723(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MUCUS PRODUCTION.
    7. "Lipoxygenase-3 (ALOXE3) and 12(R)-lipoxygenase (ALOX12B) are mutated in non-bullous congenital ichthyosiform erythroderma (NCIE) linked to chromosome 17p13.1."
      Jobard F., Lefevre C., Karaduman A., Blanchet-Bardon C., Emre S., Weissenbach J., Ozguc M., Lathrop M., Prud'homme J.-F., Fischer J.
      Hum. Mol. Genet. 11:107-113(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ARCI2 PRO-426 AND GLN-578.
    8. "Mutations associated with a congenital form of ichthyosis (NCIE) inactivate the epidermal lipoxygenases 12R-LOX and eLOX3."
      Yu Z., Schneider C., Boeglin W.E., Brash A.R.
      Biochim. Biophys. Acta 1686:238-247(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANTS ARCI2 PRO-426 AND GLN-578.
    9. "Mutation spectrum and functional analysis of epidermis-type lipoxygenases in patients with autosomal recessive congenital ichthyosis."
      Eckl K.M., Krieg P., Kuester W., Traupe H., Andre F., Wittstruck N., Fuerstenberger G., Hennies H.C.
      Hum. Mutat. 26:351-361(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ARCI2 PRO-24; TRP-114; SER-127; CYS-318; MET-383; LYS-416; HIS-488; CYS-521; PRO-664 AND LEU-679, CHARACTERIZATION OF VARIANTS ARCI2 HIS-488 AND PRO-664.
    10. "Molecular analysis of 250 patients with autosomal recessive congenital ichthyosis: evidence for mutation hotspots in ALOXE3 and allelic heterogeneity in ALOX12B."
      Eckl K.M., de Juanes S., Kurtenbach J., Naetebus M., Lugassy J., Oji V., Traupe H., Preil M.L., Martinez F., Smolle J., Harel A., Krieg P., Sprecher E., Hennies H.C.
      J. Invest. Dermatol. 129:1421-1428(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ARCI2 LEU-195 AND GLU-382, CHARACTERIZATION OF VARIANTS ARCI2 LEU-195 AND GLU-382.
    11. "Genotypic and clinical spectrum of self-improving collodion ichthyosis: ALOX12B, ALOXE3, and TGM1 mutations in Scandinavian patients."
      Vahlquist A., Bygum A., Gaanemo A., Virtanen M., Hellstroem-Pigg M., Strauss G., Brandrup F., Fischer J.
      J. Invest. Dermatol. 130:438-443(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ARCI2 PHE-67; ASP-462; CYS-521; MET-527 AND GLU-597.

    Entry informationi

    Entry nameiLX12B_HUMAN
    AccessioniPrimary (citable) accession number: O75342
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 11, 2001
    Last sequence update: November 1, 1998
    Last modified: October 1, 2014
    This is version 133 of the entry and version 1 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

    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. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3