HNRNPC
Gene Ontology Biological Process
Gene Ontology Molecular Function- RNA binding [NAS]
- RNA polymerase II core promoter proximal region sequence-specific DNA binding [IDA]
- RNA polymerase II distal enhancer sequence-specific DNA binding [IDA]
- identical protein binding [IPI]
- mRNA 3'-UTR binding [IDA]
- nucleosomal DNA binding [IDA]
- poly(A) RNA binding [IDA]
- poly(U) RNA binding [IDA]
- protein binding [IPI]
- RNA binding [NAS]
- RNA polymerase II core promoter proximal region sequence-specific DNA binding [IDA]
- RNA polymerase II distal enhancer sequence-specific DNA binding [IDA]
- identical protein binding [IPI]
- mRNA 3'-UTR binding [IDA]
- nucleosomal DNA binding [IDA]
- poly(A) RNA binding [IDA]
- poly(U) RNA binding [IDA]
- protein binding [IPI]
Gene Ontology Cellular Component
AKAP9
Gene Ontology Biological Process
- G2/M transition of mitotic cell cycle [TAS]
- cellular response to cAMP [IMP]
- mitotic cell cycle [TAS]
- positive regulation of peptidyl-serine phosphorylation [IMP]
- positive regulation of potassium ion transmembrane transporter activity [IMP]
- regulation of heart rate by cardiac conduction [IMP]
- regulation of membrane repolarization [IMP]
- regulation of ventricular cardiac muscle cell membrane repolarization [IMP]
- synaptic transmission [TAS]
- transport [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
PhoXplex: Combining Phospho-enrichable Cross-Linking with Isobaric Labeling for Quantitative Proteome-Wide Mapping of Protein Interfaces.
Integrating cross-linking mass spectrometry (XL-MS) into structural biology workflows provides valuable information about the spatial arrangement of amino acid stretches, which can guide elucidation of protein assembly architecture. Additionally, the combination of XL-MS with peptide quantitation techniques is a powerful approach to delineate protein interface dynamics across diverse conditions. While XL-MS is increasingly effective with isolated proteins or small complexes, ... [more]
Throughput
- High Throughput
Additional Notes
- High confidence XL-MS protein interactions have an FDR < 10%.
- TBDSPP (tBu-PhoX) Cross-Linking
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| HNRNPC AKAP9 | 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 | - | |
| HNRNPC AKAP9 | Proximity Label-MS Proximity Label-MS An interaction is inferred when a bait-enzyme fusion protein selectively modifies a vicinal protein with a diffusible reactive product, followed by affinity capture of the modified protein and identification by mass spectrometric methods. | High | - | BioGRID | 2783657 |
Curated By
- BioGRID