ING1
Gene Ontology Biological Process
Gene Ontology Molecular Function
PCNA
Gene Ontology Biological Process
- DNA repair [TAS]
- DNA strand elongation involved in DNA replication [TAS]
- G1/S transition of mitotic cell cycle [TAS]
- base-excision repair [TAS]
- cell proliferation [TAS]
- epithelial cell differentiation [IEP]
- leading strand elongation [IBA]
- mismatch repair [IDA]
- mitotic cell cycle [TAS]
- nucleotide-excision repair [TAS]
- nucleotide-excision repair, DNA gap filling [TAS]
- positive regulation of deoxyribonuclease activity [IDA]
- regulation of transcription involved in G1/S transition of mitotic cell cycle [TAS]
- telomere maintenance [TAS]
- telomere maintenance via recombination [TAS]
- telomere maintenance via semi-conservative replication [TAS]
- transcription-coupled nucleotide-excision repair [TAS]
- translesion synthesis [IDA]
Gene Ontology Molecular Function- DNA polymerase binding [IPI]
- DNA polymerase processivity factor activity [IBA]
- MutLalpha complex binding [IDA]
- dinucleotide insertion or deletion binding [IDA]
- identical protein binding [IPI]
- protein binding [IPI]
- purine-specific mismatch base pair DNA N-glycosylase activity [IDA]
- receptor tyrosine kinase binding [IPI]
- DNA polymerase binding [IPI]
- DNA polymerase processivity factor activity [IBA]
- MutLalpha complex binding [IDA]
- dinucleotide insertion or deletion binding [IDA]
- identical protein binding [IPI]
- protein binding [IPI]
- purine-specific mismatch base pair DNA N-glycosylase activity [IDA]
- receptor tyrosine kinase binding [IPI]
Gene Ontology Cellular Component
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.
Publication
UV-induced binding of ING1 to PCNA regulates the induction of apoptosis.
Previous studies have shown that UV-induced binding of p21(WAF1) to PCNA through the PCNA-interacting protein (PIP) domain in p21(WAF1) promotes a switch from DNA replication to DNA repair by altering the PCNA protein complex. Here we show that the p33(ING1b) isoform of the ING1 candidate tumour suppressor contains a PIP domain. UV rapidly induces p33(ING1b) to bind PCNA competitively through ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| ING1 PCNA | Affinity Capture-Western Affinity Capture-Western 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 identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins. | Low | - | BioGRID | - | |
| ING1 PCNA | Affinity Capture-Western Affinity Capture-Western 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 identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins. | Low | - | BioGRID | - | |
| PCNA ING1 | 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 | 3437608 |
Curated By
- BioGRID