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

BRENDA support

Literature summary for 2.3.2.31 extracted from

  • Dove, K.K.; Stieglitz, B.; Duncan, E.D.; Rittinger, K.; Klevit, R.E.
    Molecular insights into RBR E3 ligase ubiquitin transfer mechanisms (2016), EMBO Rep., 17, 1221-1235 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.3.2.31

Protein Variants

Protein Variants Comment Organism
E352A moderate reduction of ubiquitination activity Homo sapiens
R363A no observable effect Homo sapiens
T341N mimic of mutant T415N in parkin, decreases HHARI's ligase activity substantially Homo sapiens
W336A moderate reduction of ubiquitination activity Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
Homo sapiens Q9Y4X5 isoform ARIH1
-

Synonyms

Synonyms Comment Organism
ARIH1
-
 Homo sapiens
HHARI
-
 Homo sapiens
RNF144
-
 Homo sapiens

General Information

General Information Comment Organism
physiological function RING1 domains of HHARI promote open sate E2-ubiquitin conjugates. RING1 opening of E2-ubiquitin enforces ubiquitin transfer via the RING2 active site Cys. The hydrophobic surface of ubiquitin is required for transfer of ubiquitin to the RBR active site. Mutations that ablate ubiquitin binding to HHARI RING2 also decrease RBR ligase activity Homo sapiens
physiological function RING1 domains of RNF144 promote open sate E2-ubiquitin conjugates. RING1 opening of E2-ubiquitin enforces ubiquitin transfer via the RING2 active site Cys Homo sapiens