GNB2L1
Gene Ontology Biological Process
- activation of cysteine-type endopeptidase activity involved in apoptotic process [IMP]
- negative regulation of Wnt signaling pathway [ISS]
- negative regulation of cell growth [IDA]
- negative regulation of gene expression [IMP]
- negative regulation of hydrogen peroxide-induced neuron death [IGI]
- negative regulation of phagocytosis [IMP]
- negative regulation of protein kinase B signaling [IMP]
- negative regulation of protein tyrosine kinase activity [IDA]
- negative regulation of translation [ISS]
- positive regulation of GTPase activity [IDA]
- positive regulation of apoptotic process [IDA, IMP]
- positive regulation of cAMP catabolic process [IMP]
- positive regulation of cell migration [IDA]
- positive regulation of cyclic-nucleotide phosphodiesterase activity [IMP]
- positive regulation of gastrulation [ISS]
- positive regulation of intrinsic apoptotic signaling pathway [IMP]
- positive regulation of mitochondrial depolarization [IMP]
- positive regulation of proteasomal ubiquitin-dependent protein catabolic process [IDA]
- positive regulation of protein homooligomerization [IDA, IMP]
- positive regulation of protein phosphorylation [IDA]
- regulation of cell cycle [IDA]
- regulation of cell division [ISS]
- regulation of establishment of cell polarity [ISS]
- regulation of protein localization [ISS]
Gene Ontology Molecular Function- SH2 domain binding [IDA]
- cysteine-type endopeptidase activator activity involved in apoptotic process [IMP]
- enzyme binding [IPI]
- ion channel inhibitor activity [ISS]
- poly(A) RNA binding [IDA]
- protein binding [IPI]
- protein complex scaffold [TAS]
- protein homodimerization activity [IDA]
- protein kinase C binding [IDA]
- protein phosphatase binding [IPI]
- protein tyrosine kinase inhibitor activity [IDA]
- receptor binding [NAS]
- receptor tyrosine kinase binding [IDA]
- SH2 domain binding [IDA]
- cysteine-type endopeptidase activator activity involved in apoptotic process [IMP]
- enzyme binding [IPI]
- ion channel inhibitor activity [ISS]
- poly(A) RNA binding [IDA]
- protein binding [IPI]
- protein complex scaffold [TAS]
- protein homodimerization activity [IDA]
- protein kinase C binding [IDA]
- protein phosphatase binding [IPI]
- protein tyrosine kinase inhibitor activity [IDA]
- receptor binding [NAS]
- receptor tyrosine kinase binding [IDA]
Gene Ontology Cellular Component
RPS16
Gene Ontology Biological Process
- RNA metabolic process [TAS]
- SRP-dependent cotranslational protein targeting to membrane [TAS]
- cellular protein metabolic process [TAS]
- gene expression [TAS]
- mRNA metabolic process [TAS]
- nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [TAS]
- rRNA processing [IMP]
- ribosomal small subunit biogenesis [IMP]
- translation [IC, NAS, TAS]
- translational elongation [TAS]
- translational initiation [TAS]
- translational termination [TAS]
- viral life cycle [TAS]
- viral process [TAS]
- viral transcription [TAS]
Gene Ontology Molecular Function
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
Two-Dimensional Fractionation Method for Proteome-Wide Cross-Linking Mass Spectrometry Analysis.
Cross-linking mass spectrometry (XL-MS) is an emergent technology for studying protein-protein interactions (PPIs) and elucidating architectures of protein complexes. The development of various MS-cleavable cross-linkers has facilitated the identification of cross-linked peptides, enabling XL-MS studies at the systems level. However, the scope and depth of cellular networks revealed by current XL-MS technologies remain limited. Due to the inherently broad dynamic ... [more]
Throughput
- High Throughput
Additional Notes
- In vitro cross-linking-mass spectrometry (XL-MS) was carried out using HEK-293 cell lysates and the cross-linking reagent DSSO (disuccinimidyl sulfoxide). High confidence protein interactions were identified based on cross-linked peptides having an FDR =< 0.3%.
- In vitro cross-linking-mass spectrometry (XL-MS) was carried out using HEK-293 cell lysates and the cross-linking reagent DSSO (disuccinimidyl sulfoxide). High confidence protein interactions were identified based on cross-linked peptides having an FDR =< 0.3%.
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| RPS16 GNB2L1 | 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 | - | BioGRID | 3368476 | |
| GNB2L1 RPS16 | 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 | - | BioGRID | 3365986 | |
| GNB2L1 RPS16 | Co-fractionation Co-fractionation Interaction inferred from the presence of two or more protein subunits in a partially purified protein preparation. If co-fractionation is demonstrated between 3 or more proteins, then add them as a complex. | High | - | BioGRID | 924980 | |
| RPS16 GNB2L1 | Cross-Linking-MS (XL-MS) 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). | High | - | BioGRID | - | |
| GNB2L1 RPS16 | Cross-Linking-MS (XL-MS) 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). | High | - | BioGRID | - |
Curated By
- BioGRID