Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.3.2.26 extracted from

  • Jaeckl, M.; Stollmaier, C.; Strohaeker, T.; Hyz, K.; Maspero, E.; Polo, S.; Wiesner, S.
    beta-Sheet augmentation is a conserved mechanism of priming HECT E3 ligases for ubiquitiniquitin ligation (2018), J. Mol. Biol., 430, 3218-3233 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
Huwe1 C-lobe-ubiquitin crystal structure at 2.8 A resolution, by molecular replacement and solution NMR spectroscopy Homo sapiens
Smurf2 C-lobe-ubiquitin crystal structure at 2.8 A resolution, by molecular replacement and solution NMR spectroscopy Homo sapiens

Protein Variants

Protein Variants Comment Organism
A349P mutant is defective in thioester formation Homo sapiens
A713P mutant is defective in thioester formation Homo sapiens
DELTA382-385 HECT domain mutant, capable of forming DTT-sensitive HECT-ubiquitin thioesters, defective in polyubiquitination Homo sapiens
DELTA383-385 HECT domain mutant, capable of forming DTT-sensitive HECT-ubiquitin thioesters, defective in polyubiquitination Homo sapiens
DELTA384-385 HECT domain mutant, capable of forming DTT-sensitive HECT-ubiquitin thioesters, defective in polyubiquitination Homo sapiens
E748A mutant produces thioester levels comparable to the wild-type and shows enhanced polyubiquitination activity Homo sapiens
G383A/L384A mutant produces thioester levels comparable to the wild-type Homo sapiens
L346P mutation abolishes E2-E3 transthiolation and consequently polyubiquitination activity Homo sapiens
L384A mutant produces thioester levels comparable to the wild-type Homo sapiens
V747A/E748A mutant produces thioester levels comparable to the wild-type Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q7Z6Z7 isoform Huwe1
-
Homo sapiens Q9HAU4 isoform Smurf2
-

Synonyms

Synonyms Comment Organism
Huwe1
-
Homo sapiens
Smurf2
-
Homo sapiens

General Information

General Information Comment Organism
physiological function the Huwe1 HECT domain prioritizes K6- and K48-polyubiquitin chains and does not interact with ubiquitin in a non-covalent manner. The architecture of the C-lobe-ubiquitin intermediate is conserved between Huwe1 and Smurf2 and involves a reorientation of the very C-terminal residues. The individual sequence composition of the Huwe1 C-terminal tail modulates ubiquitination activity, without affecting thioester formation Homo sapiens