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ProteomicsThe length of a ubiquitin chain is a general determinant for selective recognition by ubiquitin-binding proteins.
The attachment of differently linked ubiquitin (Ub) chains of varying length to proteins is a prevalent posttranslational modification in eukaryotic cells. The fate of a modified protein is determined by Ub-binding proteins (UBPs) that interact with Ub chains in a linkage-selective manner. Therefore...
ORGANISM(S): Homo sapiens (Human) 
2020-04-20 | PXD015877 | Pride
Chain-length Ubiquitin Ub-binding proteins Posttranslational modification 
ProteomicsK48- and K63-linked ubiquitin chain interactome reveals branch- and length-specific ubiquitin interactors
Ubiquitin-interactor co-pulldown coupled with mass spectrometry used to elucidate K48- and K63-linked interactomes including those of Ub chains of varying length (Ub-Ub3) and heterotypic branched Ub chains. Ubiquitin-interactors were enriched from human HeLa and yeast s. cerevisiae cell lysate with ...
ORGANISM(S): Candida albicans 
2024-05-15 | PXD051890 | Pride
Branched ubiquitin chains / interactor / protein-protein interaction / proteomics / proteostasis / ubiquitin 
ModelsProctor2007 - Age related decline of proteolysis, ubiquitin-proteome system
Proctor2007 - Age related decline of proteolysis, ubiquitin-proteome system This is a stochastic model of the ubiquitin-proteasome system for a generic pool of native proteins (NatP), which have a half-life of about 10 hours under normal conditions. It is assumed that these ...
2024-09-02 | BIOMD0000000105 | BioModels
TranscriptomicsThe tumor antigen PRAME is a substrate recognition subunit of a Cul2-based ubiquitin ligase and is associated with active NFY promoters
The human tumor antigen PRAME (Preferentially expressed antigen of melanoma) is frequently overexpressed in tumors. High PRAME levels correlate with poor clinical outcome of several cancers, but the mechanisms by which PRAME could be involved in tumorigenesis remain largely elusive. We applied prote...
ORGANISM(S): Homo sapiens 
2011-07-29 | E-GEOD-26439 | biostudies-arrayexpress
ProteomicsStructural ubiquitin contributes to K48 linkage-specificity of the HECT ligase Tom1
Homologous to E6AP C-Terminus (HECT) ubiquitin ligases play key roles in essential pathways such as DNA repair, cell cycle control or protein quality control. Tom1 is one of five HECT ubiquitin E3 ligases in budding yeast S. cerevisiae and prototypical for a ligase with pleiotropic functions such as...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2025-08-07 | PXD062321 | Pride
Hect  ubiquitin  orphan quality control  huwe1  tom1  protein ubiquitylation  cryo-em 
UnknownThe Length of a Ubiquitin Chain: A General Factor for Selective Recognition by Ubiquitin-Binding Proteins.
Not available
S-EPMC7384046 | biostudies-literature
ProteomicsMARCH1 ubiquitination of MHC II generates a branched K63/K11 ubiquitin chain.
Major histocompatibility class II (MHC II) is critical for adaptive immunity. MHC II intracellular trafficking and degradation is regulated by ubiquitination, with poly-ubiquitination (Ub) of MHC II directing it away from the plasma membrane. The MHC II poly-Ub chain that dictates the fate and funct...
ORGANISM(S): Mus musculus (Mouse) 
2025-12-01 | PXD063057 | Pride
Ubiquitin Mhcii Ub-code Aqua peptides 
UnknownK48- and K63-linked ubiquitin chain interactome reveals branch- and length-specific ubiquitin interactors.
Not available
S-EPMC11109483 | biostudies-literature
ProteomicsUbiquitin chain types on ubiquitinated VPS34 in the presence or absence of UBE3C in vitro LC-MSMS
We identified VPS34 as the direct substrate of UBE3C E3 ligase in vivo and in vitro. Next, to analyze the ubiquitin chain on VPS34 that was assembled by UBE3C in vitro.
ORGANISM(S): Homo sapiens (Human) 
2021-02-17 | PXD023986 | Pride
Ubiquitin chain types Vps34 Ube3c 
ProteomicsUbiquitin chain editing promotes p97/VCP-dependent removal of RPA from DNA
DNA repair requires dynamic control of proteins on single-stranded DNA (ssDNA), yet how ubiquitin signaling regulates ssDNA-bound factors remains poorly understood. Here we identify in human cells a ubiquitin chain editing mechanism that promotes extraction of replication protein A (RPA) from ssDNA....
ORGANISM(S): Homo sapiens (Human) 
2026-09-16 | PXD061008 | Pride
Ubiquitin Zup1 P97/vcp Deubiquitinase 
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