PTBP1
Gene Ontology Biological Process
- RNA splicing [TAS]
- gene expression [TAS]
- mRNA processing [TAS]
- mRNA splicing, via spliceosome [TAS]
- negative regulation of RNA splicing [IDA]
- negative regulation of mRNA splicing, via spliceosome [IDA]
- negative regulation of muscle cell differentiation [IDA]
- regulation of alternative mRNA splicing, via spliceosome [IDA]
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 |
---|---|---|---|---|---|---|
HNRNPK PTBP1 | 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 | 0.843 | BioGRID | 741803 | |
PTBP1 HNRNPK | 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 | 0.2552 | BioGRID | 1263184 | |
PTBP1 HNRNPK | Reconstituted Complex Reconstituted Complex An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator. | Low | - | BioGRID | - | |
HNRNPK PTBP1 | Reconstituted Complex Reconstituted Complex An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator. | Low | - | BioGRID | - | |
PTBP1 HNRNPK | Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation. | Low | - | BioGRID | - | |
HNRNPK PTBP1 | Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation. | Low | - | BioGRID | - |
Curated By
- BioGRID