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Protein

Arachidonate 12-lipoxygenase, 12R-type

Gene

ALOX12B

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 (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

Fe cationPROSITE-ProRule annotationNote: Binds 1 Fe cation per subunit.PROSITE-ProRule annotation

Pathway: 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.

Pathway: sphingolipid metabolism

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

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

GO - Biological processi

  • arachidonic acid metabolic process Source: UniProtKB
  • ceramide biosynthetic process Source: UniProtKB
  • establishment of skin barrier Source: UniProtKB
  • hepoxilin biosynthetic process Source: UniProtKB
  • linoleic acid metabolic process Source: UniProtKB
  • lipoxygenase pathway Source: UniProtKB
  • oxidation-reduction process Source: UniProtKB
  • positive regulation of gene expression Source: UniProtKB
  • positive regulation of MAPK cascade Source: UniProtKB
  • positive regulation of mucus secretion Source: UniProtKB
  • protein lipidation Source: UniProtKB
  • small molecule metabolic process Source: Reactome
  • sphingolipid metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BRENDAi1.13.11.31. 2681.
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 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:430. ALOX12B.

Subcellular locationi

  • Cytoplasm PROSITE-ProRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Ichthyosis, congenital, autosomal recessive 2 (ARCI2)4 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:242100
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. 2 Publications
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. 2 Publications
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.

Polymorphism and mutation databases

BioMutaiALOX12B.

PTM / Processingi

Molecule processing

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

Proteomic databases

MaxQBiO75342.
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.
GenevisibleiO75342. HS.

Organism-specific databases

HPAiHPA024002.

Interactioni

Binary interactionsi

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

Protein-protein interaction databases

BioGridi106743. 10 interactions.
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.
GeneTreeiENSGT00550000074415.
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

        10         20         30         40         50
MATYKVRVAT GTDLLSGTRD SISLTIVGTQ GESHKQLLNH FGRDFATGAV
60 70 80 90 100
GQYTVQCPQD LGELIIIRLH KERYAFFPKD PWYCNYVQIC APNGRIYHFP
110 120 130 140 150
AYQWMDGYET LALREATGKT TADDSLPVLL EHRKEEIRAK QDFYHWRVFL
160 170 180 190 200
PGLPSYVHIP SYRPPVRRHR NPNRPEWNGY IPGFPILINF KATKFLNLNL
210 220 230 240 250
RYSFLKTASF FVRLGPMALA FKVRGLLDCK HSWKRLKDIR KIFPGKKSVV
260 270 280 290 300
SEYVAEHWAE DTFFGYQYLN GVNPGLIRRC TRIPDKFPVT DDMVAPFLGE
310 320 330 340 350
GTCLQAELEK GNIYLADYRI MEGIPTVELS GRKQHHCAPL CLLHFGPEGK
360 370 380 390 400
MMPIAIQLSQ TPGPDCPIFL PSDSEWDWLL AKTWVRYAEF YSHEAIAHLL
410 420 430 440 450
ETHLIAEAFC LALLRNLPMC HPLYKLLIPH TRYTVQINSI GRAVLLNEGG
460 470 480 490 500
LSAKGMSLGV EGFAGVMVRA LSELTYDSLY LPNDFVERGV QDLPGYYYRD
510 520 530 540 550
DSLAVWNALE KYVTEIITYY YPSDAAVEGD PELQSWVQEI FKECLLGRES
560 570 580 590 600
SGFPRCLRTV PELIRYVTIV IYTCSAKHAA VNTGQMEFTA WMPNFPASMR
610 620 630 640 650
NPPIQTKGLT TLETFMDTLP DVKTTCITLL VLWTLSREPD DRRPLGHFPD
660 670 680 690 700
IHFVEEAPRR SIEAFRQRLN QISHDIRQRN KCLPIPYYYL DPVLIENSIS

I
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. 2 Publications
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. 2 Publications
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi106743. 10 interactions.
IntActiO75342. 2 interactions.
STRINGi9606.ENSP00000315167.

Chemistry

BindingDBiO75342.

PTM databases

PhosphoSiteiO75342.

Polymorphism and mutation databases

BioMutaiALOX12B.

Proteomic databases

MaxQBiO75342.
PaxDbiO75342.
PRIDEiO75342.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi242.
GeneCardsiGC17M007975.
GeneReviewsiALOX12B.
HGNCiHGNC:430. ALOX12B.
HPAiHPA024002.
MIMi242100. phenotype.
603741. gene.
neXtProtiNX_O75342.
Orphaneti79394. Congenital non-bullous ichthyosiform erythroderma.
313. Lamellar ichthyosis.
281122. Self-healing collodion baby.
PharmGKBiPA24722.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG69653.
GeneTreeiENSGT00550000074415.
HOGENOMiHOG000234358.
HOVERGENiHBG005150.
InParanoidiO75342.
KOiK08021.
OMAiYHFPAYQ.
OrthoDBiEOG7V49XR.
PhylomeDBiO75342.
TreeFamiTF105320.

Enzyme and pathway databases

UniPathwayiUPA00222.
UPA00881.
BRENDAi1.13.11.31. 2681.
ReactomeiREACT_150201. Synthesis of 12-eicosatetraenoic acid derivatives.

Miscellaneous databases

GeneWikiiALOX12B.
GenomeRNAii242.
NextBioi966.
PROiO75342.
SOURCEiSearch...

Gene expression databases

BgeeiO75342.
CleanExiHS_ALOX12B.
GenevisibleiO75342. HS.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: June 24, 2015
This is version 140 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

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 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.