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Literature summary for 1.21.99.4 extracted from

  • Zavacki, A.M.; Arrojo E Drigo, R.; Freitas, B.C.; Chung, M.; Harney, J.W.; Egri, P.; Wittmann, G.; Fekete, C.; Gereben, B.; Bianco, A.C.
    The E3 ubiquitin ligase TEB4 mediates degradation of type 2 iodothyronine deiodinase (2009), Mol. Cell. Biol., 29, 5339-5347.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.21.99.4

Cloned(Commentary)

Cloned (Comment) Organism
into a D10 vector Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum
-
 Homo sapiens 5783
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-thyroxine + AH2 Homo sapiens
-
 3,5,3'-triiodo-L-thyronine + iodide + A + H+
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-thyroxine + AH2
-
 Homo sapiens 3,5,3'-triiodo-L-thyronine + iodide + A + H+
-
 ?

Subunits

Subunits Comment Organism
dimer
-
 Homo sapiens

Synonyms

Synonyms Comment Organism
type 2 iodothyronine deiodinase
-
 Homo sapiens

Expression

Organism Comment Expression
Homo sapiens substrate-dependent down-regulation, WSB-1-mediated ubiquitination inactivates the enzyme and targets it for proteasomal degradation, TEB4 interacts with the enzyme and mediates loss of activity and protein down
Homo sapiens ubiquitinated enzyme can be reactivated and rescued from proteosomal degradation by the von Hippel-Lindau protein-interacting deubiquitinating enzyme-1, TEB4 knockdown increases activity and protein level of iodothyronine deiodinase 2 up