HIST1H1C
Gene Ontology Molecular Function
Gene Ontology Cellular Component
RPS3
Gene Ontology Biological Process
- DNA catabolic process, endonucleolytic [IBA, IDA]
- RNA metabolic process [TAS]
- SRP-dependent cotranslational protein targeting to membrane [TAS]
- cellular protein metabolic process [TAS]
- cellular response to DNA damage stimulus [IEP]
- cytoplasmic translation [IBA]
- gene expression [TAS]
- mRNA metabolic process [TAS]
- negative regulation of DNA repair [IMP]
- nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [TAS]
- positive regulation of DNA N-glycosylase activity [IDA]
- positive regulation of NF-kappaB transcription factor activity [IMP]
- positive regulation of apoptotic signaling pathway [IDA]
- translation [IC, NAS, TAS]
- translational elongation [TAS]
- translational initiation [NAS, TAS]
- translational termination [TAS]
- viral life cycle [TAS]
- viral process [TAS]
- viral transcription [TAS]
Gene Ontology Molecular Function- DNA-(apurinic or apyrimidinic site) lyase activity [IDA]
- NF-kappaB binding [IPI]
- damaged DNA binding [IDA]
- enzyme binding [IPI]
- iron-sulfur cluster binding [NAS]
- mRNA binding [IDA]
- oxidized purine nucleobase lesion DNA N-glycosylase activity [IBA]
- poly(A) RNA binding [IDA]
- protein binding [IPI]
- protein kinase A binding [IPI]
- protein kinase binding [IPI]
- structural constituent of ribosome [IDA, NAS]
- DNA-(apurinic or apyrimidinic site) lyase activity [IDA]
- NF-kappaB binding [IPI]
- damaged DNA binding [IDA]
- enzyme binding [IPI]
- iron-sulfur cluster binding [NAS]
- mRNA binding [IDA]
- oxidized purine nucleobase lesion DNA N-glycosylase activity [IBA]
- poly(A) RNA binding [IDA]
- protein binding [IPI]
- protein kinase A binding [IPI]
- protein kinase binding [IPI]
- structural constituent of ribosome [IDA, NAS]
Gene Ontology Cellular Component
Cross-Linking-MS (XL-MS)
An interaction is detected between two proteins using chemically reactive or photo-activatable cross-linking reagents that covalently link amino acids in close proximity, followed by mass spectrometry analysis to identify the linked peptides (reviewed in PMID 37406423, 37104977). Experiments may be carried with live cells or cell lysates in which all proteins are expressed at endogenous levels (e.g. PMID 34349018, 35235311) or with recombinant proteins (e.g., PMID 28537071).
Publication
Cysteine-enabled cleavability to advance cross-linking mass spectrometry for global analysis of endogenous protein-protein interactions.
Cross-linking mass spectrometry (XL-MS) is a powerful technology for probing protein-protein interactions (PPIs) and elucidating architectures of protein complexes at the systems level. While successful, the proteome coverage remains limited. To expand the scope of global PPI profiling, we introduce an innovative cysteine-based cleavable XL-MS platform using non-cleavable heterobifunctional lysine-cysteine (K-C) cross-linkers. The oxidation-induced transformation of cysteine cleavability enables unambiguous ... [more]
Throughput
- High Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| RPS3 HIST1H1C | Affinity Capture-MS Affinity Capture-MS An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods. | High | 1 | BioGRID | 3234103 | |
| RPS3 HIST1H1C | Affinity Capture-MS Affinity Capture-MS An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods. | High | 1 | BioGRID | 3113633 |
Curated By
- BioGRID