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ProteomicsCullin-independent recognition of HHARI substrates by a dynamic RBR catalytic domain
RING-Between-RING (RBR) E3 ligases mediate ubiquitin transfer through an obligate E3- ubiquitin thioester intermediately prior to substrate ubiquitination. While RBRs share a conserved catalytic module, substrate recruitment mechanisms remain enigmatic and the relevant domains have yet to be identi...
ORGANISM(S): Homo sapiens (Human) 
2023-05-24 | PXD030849 | Pride
Kojak Cross-linking mass spectrometry Proxl Skyline Cullin Xl-ms Hhari Ubiquitin Rbr E3 ligase 
ProteomicsQuantitative XL-MS Analysis of HHARI in the presence or absence of 4EHP
RING-Between-RING (RBR) E3 ligases mediate ubiquitin transfer through an obligate E3- ubiquitin thioester intermediately prior to substrate ubiquitination. While RBRs share a conserved catalytic module, substrate recruitment mechanisms remain enigmatic and the relevant domains have yet to be identi...
ORGANISM(S): Homo Sapiens 
2024-07-26 | PXD030871 | panorama
UnknownStructural insights into the mechanism and E2 specificity of the RBR E3 ubiquitin ligase HHARI.
Not available
S-EPMC5548887 | biostudies-literature
UnknownCullin-independent recognition of HHARI substrates by a dynamic RBR catalytic domain.
Not available
S-EPMC9444911 | biostudies-literature
UnknownStructure of the HHARI catalytic domain shows glimpses of a HECT E3 ligase.
Not available
S-EPMC3772753 | biostudies-literature
UnknownStructure of HHARI, a RING-IBR-RING ubiquitin ligase: autoinhibition of an Ariadne-family E3 and insights into ligation mechanism.
Not available
S-EPMC3747818 | biostudies-literature
UnknownStructural Studies of HHARI/UbcH7∼Ub Reveal Unique E2∼Ub Conformational Restriction by RBR RING1.
Not available
S-EPMC5462532 | biostudies-literature
UnknownUBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids.
Not available
S-EPMC3444301 | biostudies-literature
UnknownMolecular insights into RBR E3 ligase ubiquitin transfer mechanisms.
Not available
S-EPMC4967960 | biostudies-literature
UnknownTwo functionally distinct E2/E3 pairs coordinate sequential ubiquitination of a common substrate in Caenorhabditis elegans development.
Not available
S-EPMC5559030 | biostudies-literature
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