Literature summary for 2.3.2.26 extracted from

Singh, S.; Sivaraman, J.
Crystal structure of HECT domain of UBE3C E3 ligase and its ubiquitination activity (2020), Biochem. J., 477, 905-923 .

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structure of the HECT domain of UBE3C (amino acids 744-1083) with an additional fifty N-terminal amino acids (aa 693-743) at 2.7 A. The UBE3C HECT domain forms an open, L-shaped, bilobed conformation, having a large N-lobe and a small C-lobe. The N-terminal region (aa 693-743) preceding the UBE3C HECT domain as well as a loop region (aa 758-762) in the N-lobe of the HECT domain affect the stability and activity of UBE3C HECT domain	Homo sapiens

Crystallization (Comment)

Organism

crystal structure of the HECT domain of UBE3C (amino acids 744-1083) with an additional fifty N-terminal amino acids (aa 693-743) at 2.7 A. The UBE3C HECT domain forms an open, L-shaped, bilobed conformation, having a large N-lobe and a small C-lobe. The N-terminal region (aa 693-743) preceding the UBE3C HECT domain as well as a loop region (aa 758-762) in the N-lobe of the HECT domain affect the stability and activity of UBE3C HECT domain

Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
K1013Q	mutation increases the formation of E3-Ub thioester intermediate and shows 2fold enhanced ubiquitination activity	Homo sapiens
additional information	the deletion of the last three amino acids at the C-terminal completely abrogates UBE3C activity. Deletion of a loop of amino acids 758-762 decreases temperature stability and leads to lack of autoubiquitination but does not affect E2-E3 transthiolation process	Homo sapiens
Q961A	mutation of residues in the HECT domain, substantial decrease in autoubiquitination activity and in the formation of E3-Ub thioester intermediate	Homo sapiens
Q961E	mutation substantially reduces the formation of E3-Ub thioester intermediate	Homo sapiens
Q961E/K1013Q	mutant shows a reduced level of autoubiquitination activity	Homo sapiens
Ser1049	mutation of residues in the HECT domain, substantial decrease in autoubiquitination activity	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q15386	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
ubiquitination	residue Lys903 in the UBE3C HECT domain is a major site of autoubiquitination	Homo sapiens

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	UBE3C HECT domain assembles K48-linked polyubiquitin chains	Homo sapiens	?	-	-

Synonyms

Synonyms	Comment	Organism
Ube3C	-	Homo sapiens
ubiquitin-protein ligase E3C	-	Homo sapiens

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
34.5	-	melting temperature, HECT domain lacking loop residues 758-762	Homo sapiens
41	-	melting temperature, HECT domain	Homo sapiens