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Literature summary for 2.3.2.26 extracted from

  • Lu, K.; Li, P.; Zhang, M.; Xing, G.; Li, X.; Zhou, W.; Bartlam, M.; Zhang, L.; Rao, Z.; He, F.
    Pivotal role of the C2 domain of the Smurf1 ubiquitin ligase in substrate selection (2011), J. Biol. Chem., 286, 16861-16870.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherihia coli Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
C2 domain, to 1.96 A resolution. The Smurf1 C2 domain possesses a typical anti-parallel beta-sandwich fold. The Smurf1 C2 domain exerts a key role in localization to the plasma membrane. Lysine residues, Lys-28 and Lys-85, within the C2 domain are important for Smurf1 localization at the plasma membrane, regulation on cell migration, and robust ligase activity toward RhoA, which further supports a Ca2+-independent localization mechanism for Smurf1 Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
additional information autoinhibition mechanism of domains C2-HECT is not observed in isoform Smurf1 Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane the isoform Smurf1 C2 domain exerts a key role in localization to the plasma membrane. Lysine residues, Lys-28 and Lys-85, within the C2 domain are important for Smurf1 localization at the plasma membrane Homo sapiens 16020
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Organism

Organism UniProt Comment Textmining
Homo sapiens Q9HCE7 isoform Smurf1
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information C2 domain of isoform Smurf1 functions in substrate selection Homo sapiens ?
-
?

Synonyms

Synonyms Comment Organism
Smurf1
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Homo sapiens