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ProteomicsBRCA1/BARD1 intrinsically disordered regions facilitate chromatin recruitment and ubiquitylation
BRCA1/BARD1 is a tumor suppressor E3 ubiquitin (Ub) ligase with roles in DNA damage repair and in transcriptional regulation. BRCA1/BARD1 RING domains interact with nucleosomes to facilitate mono-ubiquitylation of distinct residues on the C-terminal tail of histone H2A. These enzymatic domains const...
ORGANISM(S): Homo sapiens (Human) 
2023-06-21 | PXD035345 | Pride
Kojak Brca1 Cancer Nucleosome Cross-linking mass spectrometry Proxl H2a Xl-ms Bard1 Tumor Ubiquitin ligase 
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 
ProteomicsHDX-MS of HSPB5 and HSPB1 and chimeras
HDX-MS data of HSPB1, HSPB5, and B1/B5 chimeras collected at 4 sec exchange, with fully deuterated, and undeuterated controls.
ORGANISM(S): Homo sapiens (Human) 
2026-09-21 | PXD076277 | Pride
Hspb5 Hspb1 Hdx-ms 
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 
PXD030871 | panorama
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