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Literature summary for 2.3.2.26 extracted from

  • Singh, S.; Ng, J.; Nayak, D.; Sivaraman, J.
    Structural insights into a HECT-type E3 ligase AREL1 and its ubiquitination activities in vitro (2019), J. Biol. Chem., 294, 19934-19949 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.3.2.26

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure of the extended HECT domain of AREL1 (amino acids 436-823) at 2.4 A resolution. The extended HECT domain adopts an inverted, T-shaped, bilobed conformation and harbors an additional loop (aa 567-573) absent in other HECT members. The N-terminal extended region (aa 436-482) preceding the HECT domain is indispensable for its stability and activity and without this region, the HECT domain becomes inactive Homo sapiens

Protein Variants

Protein Variants Comment Organism
E701A substitution in the Arel1 HECT domain, substantially increases its autopolyubiquitination and SMAC ubiquitination activity Homo sapiens
additional information deletion of the last three amino acids at the C-terminus of Arel1 completely abrogates Arel1 autoubiquitination and reduces SMAC ubiquitination Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens O15033 isoform Arel1
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Posttranslational Modification

Posttranslational Modification Comment Organism
ubiquitination Arel1 shows autoubiquitination Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
[HECT-E3-ubiquitin-carrier protein Arel1]-S-ubiquitin-L-cysteine + [SMAC]-L-lysine SMAC i.e. proapoptotic protein second mitochondria-derived activator of caspase Homo sapiens [HECT-E3-ubiquitin-carrier protein Arel1]-L-cysteine + [SMAC]-N6-ubiquinyl-L-lysine
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 ?

Synonyms

Synonyms Comment Organism
apoptosis-resistant E3 ligase 1
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 Homo sapiens
AREL1
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 Homo sapiens