Protein detail

DUOX2

Dual oxidase 2 (EC 1.-.-.-) (EC 1.11.1.-) (EC 1.6.3.1) (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)

Protein symbol
DUOX2
UniProt ID
EVMP score
0.38
Frequency
Transmembrane count
7
Protein classification
Basic Information
Protein Names
Dual oxidase 2 (EC 1.-.-.-) (EC 1.11.1.-) (EC 1.6.3.1) (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)
Protein Function
  • ENZYME proteins:Oxidoreductases
  • Human disease related genes:Endocrine and metabolic diseases:Thyroid gland diseases
  • Transporters:Transport Electron Carriers
  • Potential drug targets
  • Enzymes
  • Disease related genes
Transmembrane
602..622; Helical; 1042..1062; Helical; 1077..1097; Helical; 1129..1151; Helical; 1186..1206; Helical; 1224..1244; Helical; 1245..1265; Helical
Transmembrane Count
7
Entrez Gene Symbol
EVMP Score
0.38
Fluorescence & Localization
Function & Pathway
Relations & Evidence

Enzyme-Mediated Modification

0 records.

Ligand-Receptor Signaling

22 records.

CategoryParentDatabaseTransmitterReceiverSecretedPlasma Membrane (Transmembrane)Plasma Membrane (Peripheral)
receptorreceptorGO_IntercellNoYesNoNoNo
receptorreceptorOmniPathNoYesNoNoNo
intracellularintracellularLOCATENoNoNoNoNo
intracellularintracellularGO_IntercellNoNoNoNoNo
intracellularintracellularOmniPathNoNoNoNoNo
cell_surface_enzymecell_surface_enzymeSurfaceomeYesNoNoNoNo
cell_surface_enzymecell_surface_enzymeOmniPathYesNoNoNoNo
transmembranetransmembraneUniProt_locationNoNoNoNoNo
transmembranetransmembraneUniProt_topologyNoNoNoNoNo
transmembranetransmembraneUniProt_keywordNoNoNoNoNo
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Regulatory Interaction Network

0 records.

Protein Complex Composition

1 record.

Component NameComponent Gene SymbolsComponent UniProt IDStoichiometryDatabaseDatabase IDsReferences
DUOX2-DUOXA2 dual oxidase complexDUOX2DUOXA2Q1HG44Q9NRD82:2ComplexPortalintact:EBI-46441596257619041868823514755292

Isolation & Detection Technology

1 record.

EV Isolation MethodDetection MethodNumber of ReferencesReferences
Differential UltracentrifugationSize Exclusion ChromatographyMass spectrometry [LTQ-FT Ultra]Mass spectrometryR Sequencing3351197783138253738716512
Sequence, Structure & Domains

Sequences

Length
1,548
Mass
175,364
Sequence
MLRARPEALMLLGALLTGSLGPSGNQDALSLPWEVQRYDGWFNNLRHHERGAVGCRLQRRVPANYADGVYQALEEPQLPNPRRLSNAATRGIAGLPSLHNRTVLGVFFGYHVLSDVVSVETPGCPAEFLNIRIPPGDPVFDPDQRGDVVLPFQRSRWDPETGRSPSNPRDLANQVTGWLDGSAIYGSSHSWSDALRSFSGGQLASGPDPAFPRDSQNPLLMWAAPDPATGQNGPRGLYAFGAERGNREPFLQALGLLWFRYHNLWAQRLARQHPDWEDEELFQHARKRVIATYQNIAVYEWLPSFLQKTLPEYTGYRPFLDPSISPEFVVASEQFFSTMVPPGVYMRNASCHFRKVLNKGFQSSQALRVCNNYWIRENPNLNSTQEVNELLLGMASQISELEDNIVVEDLRDYWPGPGKFSRTDYVASSIQRGRDMGLPSYSQALLAFGLDIPRNWSDLNPNVDPQVLEATAALYNQDLSQLELLLGGLLESHGDPGPLFSAIVLDQFVRLRDGDRYWFENTRNGLFSKKEIEDIRNTTLRDVLVAVINIDPSALQPNVFVWHKGAPCPQPKQLTTDGLPQCAPLTVLDFFEGSSPGFAITIIALCCLPLVSLLLSGVVAYFRGREHKKLQKKLKESVKKEAAKDGVPAMEWPGPKERSSPIIIQLLSDRCLQVLNRHLTVLRVVQLQPLQQVNLILSNNRGCRTLLLKIPKEYDLVLLFSSEEERGAFVQQLWDFCVRWALGLHVAEMSEKELFRKAVTKQQRERILEIFFRHLFAQVLDINQADAGTLPLDSSQKVREALTCELSRAEFAESLGLKPQDMFVESMFSLADKDGNGYLSFREFLDILVVFMKGSPEDKSRLMFTMYDLDENGFLSKDEFFTMMRSFIEISNNCLSKAQLAEVVESMFRESGFQDKEELTWEDFHFMLRDHDSELRFTQLCVKGGGGGGNGIRDIFKQNISCRVSFITRTPGERSHPQGLGPPAPEAPELGGPGLKKRFGKKAAVPTPRLYTEALQEKMQRGFLAQKLQQYKRFVENYRRHIVCVAIFSAICVGVFADRAYYYGFASPPSDIAQTTLVGIILSRGTAASVSFMFSYILLTMCRNLITFLRETFLNRYVPFDAAVDFHRWIAMAAVVLAILHSAGHAVNVYIFSVSPLSLLACIFPNVFVNDGSKLPQKFYWWFFQTVPGMTGVLLLLVLAIMYVFASHHFRRRSFRGFWLTHHLYILLYALLIIHGSYALIQLPTFHIYFLVPAIIYGGDKLVSLSRKKVEISVVKAELLPSGVTYLQFQRPQGFEYKSGQWVRIACLALGTTEYHPFTLTSAPHEDTLSLHIRAVGPWTTRLREIYSSPKGNGCAGYPKLYLDGPFGEGHQEWHKFEVSVLVGGGIGVTPFASILKDLVFKSSLGSQMLCKKIYFIWVTRTQRQFEWLADIIQEVEENDHQDLVSVHIYVTQLAEKFDLRTTMLYICERHFQKVLNRSLFTGLRSITHFGRPPFEPFFNSLQEVHPQVRKIGVFSCGPPGMTKNVEKACQLVNRQDRAHFMHHYENF

3D Structural Models

Domain & Motif Annotations

Domain (FT)
819..854; EF-hand 1; 855..890; EF-hand 2; 899..934; EF-hand 3; 1084..1266; Ferric oxidoreductase; 1267..1373; FAD-binding FR-type
Region
30..596; Peroxidase-like; mediates peroxidase activity; 960..1245; Interaction with TXNDC11; 971..991; Disordered
Protein Families
Peroxidase family
Sequence Similarities
In the N-terminal section; belongs to the peroxidase family.
Clinical Relevance