Sort   by:  
 Page size 
DNA lesions encountered by replicative polymerases threaten genome stability and cell cycle progression. Here we report the identification of mutations in TRAIP, encoding an E3 RING ubiquitin ligase, in patients with microcephalic primordial dwarfism/Seckel syndrome. We establish that TRAIP relocali...
TRAIP is a functional E3 ubiquitin ligase with a RING finger domain at the N-terminal end. To find TRAIP partners and substrates we used a proximity-dependent biotinylation assay (Bio-ID) which can identify direct protein-protein interaction but also proteins building a complex without requiring di...
ORGANISM(S): Homo sapiens (Human) 
2024-05-07 | PXD006715 | Pride
TRAIP suppresses bladder cancer progression by catalyzing K48-linked polyubiquitination of MYC
BAM files for two WES TRAIP patients
Tumor necrosis factor (TNF) receptor-associated factor (TRAF)-interacting protein (TRAIP), a RING domain-containing E3 ligase, has emerged as a key player in safeguarding genome integrity and is closely linked to cancer. Here, we discovered that TRAIP exhibits low expression in bladder cancer (BLCA)...
ORGANISM(S): Homo sapiens 
2023-12-28 | GSE237002 | GEO
Chemical cross-linking coupled to mass spectrometry was used to study the structure and homodimerization of the E3 ubiquitin ligase TRAIP from Xenopus laevis. The protein was cross-linked with two different concentrations of disuccinimidyl suberate (DSS).
ORGANISM(S): Xenopus laevis (African clawed frog) 
2025-06-27 | PXD058941 | Pride
Cell division is the basis for the propagation of life and requires accurate duplication of all genetic information. DNA damage created during replication (replication stress) is a major cause of cancer, premature aging and a spectrum of other human disorders. TRAIP E3 ubiquitin ligase has been show...
ORGANISM(S): Homo sapiens 
2023-09-01 | GSE201158 | GEO
Sort   by:  
 Page size