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Q9NRD8 (DUOX2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dual oxidase 2

EC=1.11.1.-
EC=1.6.3.1
Alternative name(s):
Large NOX 2
Long NOX 2
NADH/NADPH thyroid oxidase p138-tox
NADPH oxidase/peroxidase DUOX2
NADPH thyroid oxidase 2
Thyroid oxidase 2
p138 thyroid oxidase
Gene names
Name:DUOX2
Synonyms:LNOX2, THOX2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1548 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Generates hydrogen peroxide which is required for the activity of thyroid peroxidase/TPO and lactoperoxidase/LPO. Plays a role in thyroid hormones synthesis and lactoperoxidase-mediated antimicrobial defense at the surface of mucosa. May have its own peroxidase activity through its N-terminal peroxidase-like domain. Ref.8

Catalytic activity

NAD(P)H + O2 = NAD(P)+ + H2O2. Ref.12

Enzyme regulation

Peroxidase activity is inhibited by aminobenzohydrazide By similarity. The NADPH oxidase activity is calcium-dependent. Ref.12

Pathway

Hormone biosynthesis; thyroid hormone biosynthesis.

Subunit structure

Interacts with TXNDC11, TPO and CYBA. Ref.11

Subcellular location

Apical cell membrane; Multi-pass membrane protein. Note: Localizes to the apical membrane of epithelial cells. Ref.10

Tissue specificity

Expressed in colon, small intestine, duodenum and tracheal surface epithelial cells (at protein level). Expressed in thyrocytes. Also detected in kidney, liver, lung, pancreas, prostate, salivary glands, rectum and testis. Ref.1 Ref.2 Ref.8 Ref.9 Ref.10

Developmental stage

Widely expressed in fetal tissues. Ref.2

Induction

By forskolin, thyrotropin and the Th1-specific cytokine IFNG/IFN-gamma. Ref.1 Ref.12

Post-translational modification

N-glycosylated. Ref.6

Involvement in disease

Thyroid dyshormonogenesis 6 (TDH6) [MIM:607200]: A disorder due to a defective conversion of accumulated iodide to organically bound iodine. The iodide organification defect can be partial or complete.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.5 Ref.7 Ref.13 Ref.14

Sequence similarities

In the N-terminal section; belongs to the peroxidase family.

Contains 3 EF-hand domains.

Contains 1 FAD-binding FR-type domain.

Contains 1 ferric oxidoreductase domain.

Ontologies

Keywords
   Biological processHydrogen peroxide
Thyroid hormones biosynthesis
   Cellular componentCell membrane
Membrane
   Coding sequence diversityPolymorphism
   DiseaseCongenital hypothyroidism
Disease mutation
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandCalcium
FAD
Flavoprotein
Metal-binding
NADP
   Molecular functionOxidoreductase
Peroxidase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadenohypophysis morphogenesis

Inferred from electronic annotation. Source: Ensembl

bone mineralization

Inferred from electronic annotation. Source: Ensembl

cuticle development

Inferred from sequence or structural similarity. Source: UniProtKB

cytokine-mediated signaling pathway

Inferred from direct assay PubMed 16111680. Source: UniProtKB

fertilization

Inferred from electronic annotation. Source: Ensembl

hormone biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

hydrogen peroxide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

inner ear development

Inferred from electronic annotation. Source: Ensembl

multicellular organism growth

Inferred from electronic annotation. Source: Ensembl

oxidation-reduction process

Traceable author statement Ref.4. Source: UniProtKB

response to cAMP

Inferred from direct assay PubMed 15062544. Source: UniProtKB

response to virus

Inferred from direct assay PubMed 16111680. Source: UniProtKB

thyroid gland development

Inferred from electronic annotation. Source: Ensembl

thyroid hormone generation

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentapical plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular vesicular exosome

Inferred from direct assay PubMed 19199708. Source: UniProt

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionNAD(P)H oxidase activity

Inferred from direct assay Ref.12. Source: UniProtKB

calcium ion binding

Inferred from direct assay Ref.12. Source: UniProtKB

heme binding

Inferred from electronic annotation. Source: InterPro

peroxidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Chain26 – 15481523Dual oxidase 2
PRO_0000223349

Regions

Topological domain26 – 601576Extracellular Potential
Transmembrane602 – 62221Helical; Potential
Topological domain623 – 1041419Cytoplasmic Potential
Transmembrane1042 – 106221Helical; Potential
Topological domain1063 – 107614Extracellular Potential
Transmembrane1077 – 109721Helical; Potential
Topological domain1098 – 114851Cytoplasmic Potential
Transmembrane1149 – 116921Helical; Potential
Topological domain1170 – 118516Extracellular Potential
Transmembrane1186 – 120621Helical; Potential
Topological domain1207 – 122317Cytoplasmic Potential
Transmembrane1224 – 124421Helical; Potential
Transmembrane1245 – 126521Helical; Potential
Topological domain1266 – 1548283Cytoplasmic Potential
Domain819 – 85436EF-hand 1
Domain855 – 89036EF-hand 2
Domain899 – 93436EF-hand 3
Domain1084 – 1266183Ferric oxidoreductase
Domain1267 – 1373107FAD-binding FR-type
Calcium binding832 – 843121 Potential
Calcium binding868 – 879122 Potential
Region30 – 596567Peroxidase-like; mediates peroxidase activity By similarity
Region960 – 1245286Interaction with TXNDC11 By similarity

Amino acid modifications

Glycosylation1001N-linked (GlcNAc...) Potential
Glycosylation3481N-linked (GlcNAc...) Potential
Glycosylation3821N-linked (GlcNAc...) Potential
Glycosylation4551N-linked (GlcNAc...) Potential
Glycosylation5371N-linked (GlcNAc...) Potential

Natural variations

Natural variant361Q → H in TDH6. Ref.14
VAR_025323
Natural variant1381P → L. Ref.2
Corresponds to variant rs2001616 [ dbSNP | Ensembl ].
VAR_025324
Natural variant3761R → W in TDH6. Ref.13
VAR_025325
Natural variant6781H → R.
Corresponds to variant rs57659670 [ dbSNP | Ensembl ].
VAR_061177
Natural variant10671S → L. Ref.1 Ref.2 Ref.4
Corresponds to variant rs269868 [ dbSNP | Ensembl ].
VAR_047075
Natural variant15181G → S in TDH6; the enzyme is non-functional; expressed at the cell surface of cells albeit at low level. Ref.5
VAR_064619

Experimental info

Sequence conflict251N → S in AAF73922. Ref.1
Sequence conflict251N → S in AAF78954. Ref.2
Sequence conflict9841A → V in AAF78954. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9NRD8 [UniParc].

Last modified May 18, 2010. Version 2.
Checksum: 7BAA2350EC0A2A7E

FASTA1,548175,364
        10         20         30         40         50         60 
MLRARPEALM LLGALLTGSL GPSGNQDALS LPWEVQRYDG WFNNLRHHER GAVGCRLQRR 

        70         80         90        100        110        120 
VPANYADGVY QALEEPQLPN PRRLSNAATR GIAGLPSLHN RTVLGVFFGY HVLSDVVSVE 

       130        140        150        160        170        180 
TPGCPAEFLN IRIPPGDPVF DPDQRGDVVL PFQRSRWDPE TGRSPSNPRD LANQVTGWLD 

       190        200        210        220        230        240 
GSAIYGSSHS WSDALRSFSG GQLASGPDPA FPRDSQNPLL MWAAPDPATG QNGPRGLYAF 

       250        260        270        280        290        300 
GAERGNREPF LQALGLLWFR YHNLWAQRLA RQHPDWEDEE LFQHARKRVI ATYQNIAVYE 

       310        320        330        340        350        360 
WLPSFLQKTL PEYTGYRPFL DPSISPEFVV ASEQFFSTMV PPGVYMRNAS CHFRKVLNKG 

       370        380        390        400        410        420 
FQSSQALRVC NNYWIRENPN LNSTQEVNEL LLGMASQISE LEDNIVVEDL RDYWPGPGKF 

       430        440        450        460        470        480 
SRTDYVASSI QRGRDMGLPS YSQALLAFGL DIPRNWSDLN PNVDPQVLEA TAALYNQDLS 

       490        500        510        520        530        540 
QLELLLGGLL ESHGDPGPLF SAIVLDQFVR LRDGDRYWFE NTRNGLFSKK EIEDIRNTTL 

       550        560        570        580        590        600 
RDVLVAVINI DPSALQPNVF VWHKGAPCPQ PKQLTTDGLP QCAPLTVLDF FEGSSPGFAI 

       610        620        630        640        650        660 
TIIALCCLPL VSLLLSGVVA YFRGREHKKL QKKLKESVKK EAAKDGVPAM EWPGPKERSS 

       670        680        690        700        710        720 
PIIIQLLSDR CLQVLNRHLT VLRVVQLQPL QQVNLILSNN RGCRTLLLKI PKEYDLVLLF 

       730        740        750        760        770        780 
SSEEERGAFV QQLWDFCVRW ALGLHVAEMS EKELFRKAVT KQQRERILEI FFRHLFAQVL 

       790        800        810        820        830        840 
DINQADAGTL PLDSSQKVRE ALTCELSRAE FAESLGLKPQ DMFVESMFSL ADKDGNGYLS 

       850        860        870        880        890        900 
FREFLDILVV FMKGSPEDKS RLMFTMYDLD ENGFLSKDEF FTMMRSFIEI SNNCLSKAQL 

       910        920        930        940        950        960 
AEVVESMFRE SGFQDKEELT WEDFHFMLRD HDSELRFTQL CVKGGGGGGN GIRDIFKQNI 

       970        980        990       1000       1010       1020 
SCRVSFITRT PGERSHPQGL GPPAPEAPEL GGPGLKKRFG KKAAVPTPRL YTEALQEKMQ 

      1030       1040       1050       1060       1070       1080 
RGFLAQKLQQ YKRFVENYRR HIVCVAIFSA ICVGVFADRA YYYGFASPPS DIAQTTLVGI 

      1090       1100       1110       1120       1130       1140 
ILSRGTAASV SFMFSYILLT MCRNLITFLR ETFLNRYVPF DAAVDFHRWI AMAAVVLAIL 

      1150       1160       1170       1180       1190       1200 
HSAGHAVNVY IFSVSPLSLL ACIFPNVFVN DGSKLPQKFY WWFFQTVPGM TGVLLLLVLA 

      1210       1220       1230       1240       1250       1260 
IMYVFASHHF RRRSFRGFWL THHLYILLYA LLIIHGSYAL IQLPTFHIYF LVPAIIYGGD 

      1270       1280       1290       1300       1310       1320 
KLVSLSRKKV EISVVKAELL PSGVTYLQFQ RPQGFEYKSG QWVRIACLAL GTTEYHPFTL 

      1330       1340       1350       1360       1370       1380 
TSAPHEDTLS LHIRAVGPWT TRLREIYSSP KGNGCAGYPK LYLDGPFGEG HQEWHKFEVS 

      1390       1400       1410       1420       1430       1440 
VLVGGGIGVT PFASILKDLV FKSSLGSQML CKKIYFIWVT RTQRQFEWLA DIIQEVEEND 

      1450       1460       1470       1480       1490       1500 
HQDLVSVHIY VTQLAEKFDL RTTMLYICER HFQKVLNRSL FTGLRSITHF GRPPFEPFFN 

      1510       1520       1530       1540 
SLQEVHPQVR KIGVFSCGPP GMTKNVEKAC QLVNRQDRAH FMHHYENF 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of two human thyroid cDNAs encoding new members of the NADPH oxidase family."
De Deken X., Wang D., Many M.-C., Costagliola S., Libert F., Vassart G., Dumont J.E., Miot F.
J. Biol. Chem. 275:23227-23233(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, TISSUE SPECIFICITY, VARIANT LEU-1067.
Tissue: Thyroid.
[2]"Tyrosine cross-linking of extracellular matrix is catalyzed by Duox, a multidomain oxidase/peroxidase with homology to the phagocyte oxidase subunit gp91phox."
Edens W.A., Sharling L., Cheng G., Shapira R., Kinkade J.M., Lee T., Edens H.A., Tang X., Sullards C., Flaherty D.B., Benian G.M., Lambeth J.D.
J. Cell Biol. 154:879-891(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS LEU-138 AND LEU-1067, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
Tissue: Pancreas and Thyroid.
[3]"Analysis of the DNA sequence and duplication history of human chromosome 15."
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A. expand/collapse author list , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Purification of a novel flavoprotein involved in the thyroid NADPH oxidase. Cloning of the porcine and human cDNAs."
Dupuy C., Ohayon R., Valent A., Noel-Hudson M.-S., Deme D., Virion A.
J. Biol. Chem. 274:37265-37269(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 339-1548, VARIANT LEU-1067.
Tissue: Thyroid.
[5]"Compound heterozygosity for a novel hemizygous missense mutation and a partial deletion affecting the catalytic core of the H2O2-generating enzyme DUOX2 associated with transient congenital hypothyroidism."
Hoste C., Rigutto S., Van Vliet G., Miot F., De Deken X.
Hum. Mutat. 31:E1304-E1319(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1509-1548, VARIANT TDH6 SER-1518, CHARACTERIZATION OF VARIANT TDH6 SER-1518.
[6]"Characterization of ThOX proteins as components of the thyroid H(2)O(2)-generating system."
De Deken X., Wang D., Dumont J.E., Miot F.
Exp. Cell Res. 273:187-196(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION.
[7]"Inactivating mutations in the gene for thyroid oxidase 2 (THOX2) and congenital hypothyroidism."
Moreno J.C., Bikker H., Kempers M.J.E., van Trotsenburg A.S., Baas F., de Vijlder J.J.M., Vulsma T., Ris-Stalpers C.
N. Engl. J. Med. 347:95-102(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN TDH6.
[8]"Dual oxidases represent novel hydrogen peroxide sources supporting mucosal surface host defense."
Geiszt M., Witta J., Baffi J., Lekstrom K., Leto T.L.
FASEB J. 17:1502-1504(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[9]"NADPH oxidase-dependent acid production in airway epithelial cells."
Schwarzer C., Machen T.E., Illek B., Fischer H.
J. Biol. Chem. 279:36454-36461(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[10]"Dual oxidase2 is expressed all along the digestive tract."
Ameziane-El-Hassani R., Benfares N., Caillou B., Talbot M., Sabourin J.-C., Belotte V., Morand S., Gnidehou S., Agnandji D., Ohayon R., Kaniewski J., Noel-Hudson M.-S., Bidart J.-M., Schlumberger M., Virion A., Dupuy C.
Am. J. Physiol. 288:G933-G942(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[11]"Identification of a novel partner of duox: EFP1, a thioredoxin-related protein."
Wang D., De Deken X., Milenkovic M., Song Y., Pirson I., Dumont J.E., Miot F.
J. Biol. Chem. 280:3096-3103(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TXNDC11; TPO AND CYBA.
[12]"Dual oxidase-2 has an intrinsic Ca2+-dependent H2O2-generating activity."
Ameziane-El-Hassani R., Morand S., Boucher J.L., Frapart Y.-M., Apostolou D., Agnandji D., Gnidehou S., Ohayon R., Noel-Hudson M.-S., Francon J., Lalaoui K., Virion A., Dupuy C.
J. Biol. Chem. 280:30046-30054(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION.
[13]"Persistent mild hypothyroidism associated with novel sequence variants of the DUOX2 gene in two siblings."
Vigone M.C., Fugazzola L., Zamproni I., Passoni A., Di Candia S., Chiumello G., Persani L., Weber G.
Hum. Mutat. 26:395-395(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT TDH6 TRP-376.
[14]"Three mutations (p.Q36H, p.G418fsX482, and g.IVS19-2A-->C) in the dual oxidase 2 gene responsible for congenital goiter and iodide organification defect."
Varela V., Rivolta C.M., Esperante S.A., Gruneiro-Papendieck L., Chiesa A., Targovnik H.M.
Clin. Chem. 52:182-191(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT TDH6 HIS-36.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF230496 mRNA. Translation: AAF73922.1.
AF267981 mRNA. Translation: AAF78954.1.
AC091117 Genomic DNA. No translation available.
AF181972 mRNA. Translation: AAF20055.1.
GU174495 Genomic DNA. Translation: ADB22378.1.
CCDSCCDS10117.1.
RefSeqNP_054799.4. NM_014080.4.
UniGeneHs.71377.

3D structure databases

ProteinModelPortalQ9NRD8.
SMRQ9NRD8. Positions 43-540, 772-928.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000267837.

Protein family/group databases

PeroxiBase3338. HsDuOx02.
TCDB5.B.1.2.2. the phagocyte (gp91(phox)) nadph oxidase family.

PTM databases

PhosphoSiteQ9NRD8.

Polymorphism databases

DMDM296434485.

Proteomic databases

PaxDbQ9NRD8.
PRIDEQ9NRD8.

Protocols and materials databases

DNASU50506.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000603300; ENSP00000475084; ENSG00000140279.
GeneID50506.
KEGGhsa:50506.
UCSCuc001zun.3. human.

Organism-specific databases

CTD50506.
GeneCardsGC15M045384.
H-InvDBHIX0038086.
HGNCHGNC:13273. DUOX2.
MIM606759. gene.
607200. phenotype.
neXtProtNX_Q9NRD8.
Orphanet95716. Familial thyroid dyshormonogenesis.
226316. Genetic transient congenital hypothyroidism.
PharmGKBPA27517.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG287712.
HOGENOMHOG000231774.
HOVERGENHBG080428.
KOK13411.
OrthoDBEOG7GN2KV.
PhylomeDBQ9NRD8.
TreeFamTF105424.

Enzyme and pathway databases

BRENDA1.6.3.1. 2681.
SABIO-RKQ9NRD8.
UniPathwayUPA00194.

Gene expression databases

BgeeQ9NRD8.
CleanExHS_DUOX2.
GenevestigatorQ9NRD8.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
1.10.640.10. 1 hit.
InterProIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR013112. FAD-bd_8.
IPR017927. Fd_Rdtase_FAD-bd.
IPR013130. Fe3_Rdtase_TM_dom.
IPR013121. Fe_red_NAD-bd_6.
IPR010255. Haem_peroxidase.
IPR002007. Haem_peroxidase_animal.
IPR019791. Haem_peroxidase_animal_subgr.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamPF03098. An_peroxidase. 1 hit.
PF13499. EF-hand_7. 1 hit.
PF08022. FAD_binding_8. 1 hit.
PF01794. Ferric_reduct. 1 hit.
PF08030. NAD_binding_6. 1 hit.
[Graphical view]
PRINTSPR00457. ANPEROXIDASE.
SMARTSM00054. EFh. 2 hits.
[Graphical view]
SUPFAMSSF48113. SSF48113. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 3 hits.
PS51384. FAD_FR. 1 hit.
PS50292. PEROXIDASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDUOX2. human.
GeneWikiDual_oxidase_2.
GenomeRNAi50506.
NextBio53066.
PROQ9NRD8.
SOURCESearch...

Entry information

Entry nameDUOX2_HUMAN
AccessionPrimary (citable) accession number: Q9NRD8
Secondary accession number(s): A8MQ13 expand/collapse secondary AC list , D2XI64, Q9NR02, Q9UHF9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2006
Last sequence update: May 18, 2010
Last modified: July 9, 2014
This is version 116 of the entry and version 2 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

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 15

Human chromosome 15: entries, gene names and cross-references to MIM