HNRNPA2B1
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
HNRNPK
Gene Ontology Biological Process
- RNA processing [TAS]
- RNA splicing [TAS]
- gene expression [TAS]
- mRNA splicing, via spliceosome [IC, TAS]
- positive regulation of low-density lipoprotein particle receptor biosynthetic process [IMP]
- positive regulation of receptor-mediated endocytosis [IMP]
- positive regulation of transcription from RNA polymerase II promoter [IMP]
- regulation of lipid transport by positive regulation of transcription from RNA polymerase II promoter [IMP]
- regulation of low-density lipoprotein particle clearance [IMP]
- signal transduction [TAS]
Gene Ontology Molecular Function- RNA binding [TAS]
- RNA polymerase II core promoter proximal region sequence-specific DNA binding [IMP]
- RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [IMP]
- poly(A) RNA binding [IDA]
- protein binding [IPI]
- single-stranded DNA binding [TAS]
- RNA binding [TAS]
- RNA polymerase II core promoter proximal region sequence-specific DNA binding [IMP]
- RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [IMP]
- poly(A) RNA binding [IDA]
- protein binding [IPI]
- single-stranded DNA binding [TAS]
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
Cross-linking mass spectrometry discovers, evaluates, and corroborates structures and protein-protein interactions in the human cell.
Significant recent advances in structural biology, particularly in the field of cryoelectron microscopy, have dramatically expanded our ability to create structural models of proteins and protein complexes. However, many proteins remain refractory to these approaches because of their low abundance, low stability, or-in the case of complexes-simply not having yet been analyzed. Here, we demonstrate the power of using cross-linking ... [more]
Throughput
- High Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| HNRNPA2B1 HNRNPK | 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 | 3358234 | |
| HNRNPA2B1 HNRNPK | 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 | 2786356 |
Curated By
- BioGRID