2.3.2.31: RBR-type E3 ubiquitin transferase
This is an abbreviated version!
For detailed information about RBR-type E3 ubiquitin transferase, go to the full flat file.
Word Map on EC 2.3.2.31
Reaction
Synonyms
ARIH1, ARIH2, HHARI, HOIP, Parkin, parkin RBR E3 ubiquitin ligase, PRKN, RBR E3, RBR-type E3, RBR-type E3 ligase, RBX1, RFA1, RFA4, RING Finger ABA-Related, RNF144, RNF144A, RNF144AA, RNF144AB, RNF144B, RNF19A, RNF19B, RNF217, RNF31, Triad1
ECTree
2.3.2.31 RBR-type E3 ubiquitin transferaseAdvanced search results
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results (Engineering
Engineering on EC 2.3.2.31 - RBR-type E3 ubiquitin transferase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C361A
-
mutation in isoform RFA4, affects its own ubiquitination and capability to ubiquitinate PYL4
C431S/H433A
RING2 mutant, able to trap the catalytic parkin-ubiquitin intermediate
E321A/C431S/H433A
UBR2 patch mutant of parkin. In contrast to C431S/H433A, this mutant is defective in ubiquitin charging even in the presence of phosphoubiquitin
H302A/E321A/C431S/H433A
60fold reduced in ubiquitin charging of the RING2
T341N
mimic of mutant T415N in parkin, decreases HHARI's ligase activity substantially
additional information
additional information
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mutants in ARIH1's UBA-to-RING1 helix, RING1, RING1-to-IBR helix, and RING2 domains display activity profile signatures corresponding to intrinsic RBR E3 activities of ubiquitin transfer from UBCH7 to ARIH1, alignment of the RING2 active site, and intrinsic ability of RING2 to mediate ligation
additional information
mutants in ARIH1's UBA-to-RING1 helix, RING1, RING1-to-IBR helix, and RING2 domains display activity profile signatures corresponding to intrinsic RBR E3 activities of ubiquitin transfer from UBCH7 to ARIH1, alignment of the RING2 active site, and intrinsic ability of RING2 to mediate ligation
