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ProteomicsUSP11 deubiquitinates monoubiquitinated SPRTN to repair DNA-protein crosslinks
DNA-protein crosslinks (DPCs) are toxic DNA lesions that interfere with DNA metabolic processes such as replication, transcription, and recombination. SPRTN is a replication-coupled DNA-dependent metalloprotease that degrades proteins crosslinked to DNA to promote DPC repair. SPRTN function is tight...
ORGANISM(S): Homo sapiens (Human) 
2021-04-01 | PXD019923 | Pride
Deubiquitination Dpc Top1-ccs Dpc repair Monoubiquitinated sprtn Sprtn Usp11 
ProteomicsMetalloprotease SPRTN/DVC1 Orchestrates Replication-Coupled DNA-Protein Crosslink Removal
Cytotoxicity of DNA-protein crosslinks (DPCs) is ascribed largely to their ability to block the progression of DNA replication fork. DPCs are frequently occurring in cells, either as a consequence of metabolism or exogenous agents. The mechanism of DPCs removal is not completely understood. Here, we...
ORGANISM(S): Homo sapiens (Human) 
2016-10-06 | PXD004154 | Pride
Dna-protein crosslink 
ProteomicsMetalloprotease SPRTN/DVC1 Orchestrates Replication-Coupled DNA-Protein Crosslink Removal
Cytotoxicity of DNA-protein crosslinks (DPCs) is ascribed largely to their ability to block the progression of DNA replication fork. DPCs are frequently occurring in cells, either as a consequence of metabolism or exogenous agents. The mechanism of DPCs removal is not completely understood. Here, we...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-29 | MSV000080743 | MassIVE
ProteomicsTEX264 coordinates p97- and SPRTN-mediated resolution of topoisomerase 1-DNA adducts
Eukaryotic topoisomerase 1 (TOP1) regulates DNA topology to ensure efficient DNA replication and transcription. TOP1 is also a major driver of endogenous genome instability, particularly when its catalytic intermediate - a covalent TOP1-DNA adduct known as a TOP1 cleavage complex (TOP1cc) - is stabi...
ORGANISM(S): Homo sapiens (Human) 
2020-03-13 | PXD017239 | Pride
Protein-dna adducts Vcp/p97 Top1 Tex264 Dna repair Genome stability Sprtn Dna replication 
GenomicsThe impact of the Sprtn mutation on gene expression in liver tissue
The impact of the Sprtn mutation on gene expression in liver tissue
PRJNA1114029 | ENA
GenomicsEffect of siRNA depletion of SPRTN gene on gene expression in HepG2 cells
Effect of siRNA depletion of SPRTN gene on gene expression in HepG2 cells
PRJNA997332 | ENA
TranscriptomicsThe impact of the Sprtn mutation on gene expression in liver tissue
Biallelic mutations in the SPRTN gene cause an autosomal recessive progeroid disease known as Ruijs–Aalfs syndrome. Patients with Ruijs–Aalfs syndrome display symptoms of premature ageing and typically develop hepatocellular carcinoma during adolescence. To study the functional role of this protein,...
ORGANISM(S): Mus musculus 
2025-09-27 | GSE268005 | GEO
ProteomicsSPARTAN Protease and Checkpoint Kinase 1 Cross-Activation Loop Safeguards Genome Stability
DNA-protein crosslinks (DPCs) are abundant DNA lesions, which constantly challenge genome stability by interfering with DNA replication. SPARTAN (SPRTN) protease plays a central role in DPCs repair in proliferative vertebrate cells. SPRTN is a constitutive part of the DNA replication machinery and i...
ORGANISM(S): Homo sapiens (Human) 
2019-11-08 | PXD006741 | Pride
Cancer Spartan protease Dna-protein crosslinks Ageing Genome stability Chk1 kinase Dna replication 
ProteomicsDNA replication regulates SPRTN- and Proteasome-dependent DPC proteolysis
DNA-protein crosslinks (DPCs) are bulky DNA lesions that interfere with DNA metabolism and therefore threaten genomic integrity. Recent studies implicate the metalloprotease SPRTN in S-phase removal of DPCs, but how SPRTN activity is coupled to DNA replication is unknown. Using Xenopus egg e...
ORGANISM(S): Xenopus laevis (African clawed frog) 
2019-02-13 | PXD008831 | Pride
Plasmid pull-down Pp-ms Dpc repair Dna repair Xenopus egg extract Dna replication 
UnknownUSP11 mediates repair of DNA-protein cross-links by deubiquitinating SPRTN metalloprotease.
Not available
S-EPMC7960550 | biostudies-literature
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