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TranscriptomicsThe conserved ubiquitin-like protein Hub1 plays a critical role in splicing in human cells
Different from canonical ubiquitin-like proteins, Hub1 does not form covalent conjugates with substrates but binds proteins non-covalently. In Saccharomyces cerevisiae, Hub1 associates with spliceosomes and mediates alternative splicing of SRC1, without affecting pre-mRNA splicing generally. Human H...
ORGANISM(S): Homo sapiens 
2014-05-30 | E-GEOD-56878 | biostudies-arrayexpress
ProteomicsE2/E3-independent ubiquitin-like protein conjugation by Urm1 is directly coupled to cysteine persulfidation
Posttranslational modifications by ubiquitin-like proteins (UBL) are essential for nearly all cellular processes. Ubiquitin related modifier 1 (Urm1) is a non-canonical UBL which plays a key role in tRNA anticodon thiolation as a sulfur carrier protein (SCP). While Urm1 has also been observed to con...
ORGANISM(S): Chaetomium Thermophilum (ncbitaxon:209285) Saccharomyces Cerevisiae (ncbitaxon:4932) Homo Sapiens (ncbitaxon:9606) 
2021-11-16 | MSV000088390 | MassIVE
TranscriptomicsThe histone H2B ubiquitin ligase RNF20 is required for MLL-rearranged leukemia
MLL-fusions are potent oncogenes that initiate aggressive forms of acute leukemia. As aberrant transcriptional regulators, MLL-fusion proteins alter gene expression in hematopoietic cells through interactions with the histone H3 lysine 79 (H3K79) methyltransferase DOT1L. Notably, interference with M...
ORGANISM(S): Mus musculus 
2013-02-19 | E-GEOD-43725 | biostudies-arrayexpress
TranscriptomicsE2-RING expansion of the NEDD8 cascade confers specificity to cullin modification
Ubiquitin and ubiquitin-like proteins (UBLs) are directed to targets by cascades of E1, E2, and E3 enzymes. The largest ubiquitin E3 subclass consists of cullin-RING ligases (CRLs), which contain one each of several cullins (CUL1, -2, -3, -4, or -5) and RING proteins (RBX1 or -2). CRLs are activated...
ORGANISM(S): Mus musculus 
2009-03-23 | E-GEOD-14088 | biostudies-arrayexpress
TranscriptomicsPupylated proteins in Corynebacterium glutamicum revealed by MudPIT analysis
In a manner similar to ubiquitin, the prokaryotic ubiquitin-like protein (Pup) has been shown to target proteins for degradation via the proteasome in mycobacteria. However, not all actinobacteria possessing the Pup protein also harbor a proteasome, suggesting fates for pupylated proteins other than...
ORGANISM(S): Corynebacterium glutamicum ATCC 13032 
2014-06-24 | E-GEOD-48038 | biostudies-arrayexpress
UnknownUbiquitin-like prokaryotic MoaD as a fusion tag for expression of heterologous proteins in Escherichia coli.
Not available
S-EPMC3906898 | biostudies-literature
TranscriptomicsUBL5 is essential for pre-mRNA splicing and sister chromatid cohesion in human cells
UBL5 is an atypical ubiquitin-like protein, whose function in metazoans remains largely unexplored. We show that UBL5 is required for sister chromatid cohesion maintenance in human cells. UBL5 primarily associates with spliceosomal proteins, and UBL5 depletion decreases pre-mRNA splicing efficiency,...
ORGANISM(S): Homo sapiens 
2014-08-05 | E-GEOD-59376 | biostudies-arrayexpress
ProteomicsUbiquitination at the Parkin ubiquitin-like domain suggests a new mechanism for Parkin activation
The mitochondrial kinase PINK1 and the cytosolic ubiquitin ligase (E3) Parkin is involved in mitochondrial quality control. PINK1, which phosphorylates ubiquitin at serine 65 residue and the ubiquitin-like (Ubl) domain of Parkin at serine 65 residue, promotes the Parkin activation and translocation ...
ORGANISM(S): Homo Sapiens (human) 
2022-08-24 | PXD026554 | JPOST Repository
ProteomicsSystem-wide analysis of SUMOylation dynamics in response to replication stress reveals novel SUMO target proteins and acceptor lysines relevant for genome stability
Genotoxic agents can cause replication fork stalling in dividing cells due to DNA lesions, eventually leading to replication fork collapse when the damage is not repaired. Small Ubiquitin-like Modifiers (SUMOs) are known to counteract replication stress, nevertheless, only a small number of relevant...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-31 | MSV000080851 | MassIVE
ProteomicsProteome-wide identification of SUMO2 modification sites
Posttranslational modification with small ubiquitin-like modifiers (SUMOs) alters the function of proteins involved in diverse cellular processes. SUMOs are conjugated to lysine residues in target proteins by SUMO-specific enzymes. Although proteomic studies have identified hundreds of sumoylated su...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-29 | MSV000080741 | MassIVE
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