TNKS
Gene Ontology Biological Process
- mitotic spindle organization [TAS]
- negative regulation of DNA binding [IDA]
- peptidyl-serine phosphorylation [IDA]
- peptidyl-threonine phosphorylation [IDA]
- positive regulation of canonical Wnt signaling pathway [IMP]
- positive regulation of telomere maintenance via telomerase [IDA, IMP]
- positive regulation of transcription from RNA polymerase II promoter [IDA]
- protein ADP-ribosylation [IDA]
- protein auto-ADP-ribosylation [IDA]
- protein localization to chromosome, telomeric region [IMP]
- protein poly-ADP-ribosylation [IDA]
- protein polyubiquitination [IDA]
- regulation of telomere maintenance via telomerase [IC]
- spindle assembly [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
TNKS
Gene Ontology Biological Process
- mitotic spindle organization [TAS]
- negative regulation of DNA binding [IDA]
- peptidyl-serine phosphorylation [IDA]
- peptidyl-threonine phosphorylation [IDA]
- positive regulation of canonical Wnt signaling pathway [IMP]
- positive regulation of telomere maintenance via telomerase [IDA, IMP]
- positive regulation of transcription from RNA polymerase II promoter [IDA]
- protein ADP-ribosylation [IDA]
- protein auto-ADP-ribosylation [IDA]
- protein localization to chromosome, telomeric region [IMP]
- protein poly-ADP-ribosylation [IDA]
- protein polyubiquitination [IDA]
- regulation of telomere maintenance via telomerase [IC]
- spindle assembly [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Biochemical Activity (Ribosylation)
An interaction is inferred from the biochemical effect of one protein upon another, for example, GTP-GDP exchange activity or phosphorylation of a substrate by a kinase. The bait protein executes the activity on the substrate hit protein. A Modification value is recorded for interactions of this type with the possible values Phosphorylation, Ubiquitination, Sumoylation, Dephosphorylation, Methylation, Prenylation, Acetylation, Deubiquitination, Proteolytic Processing, Glucosylation, Nedd(Rub1)ylation, Deacetylation, No Modification, Demethylation.
Publication
Poly-ADP ribosylation of PTEN by tankyrases promotes PTEN degradation and tumor growth.
PTEN [phosphatidylinositol (3,4,5)-trisphosphate phosphatase and tensin homolog deleted from chromosome 10], a phosphatase and critical tumor suppressor, is regulated by numerous post-translational modifications, including phosphorylation, ubiquitination, acetylation, and SUMOylation, which affect PTEN localization and protein stability. Here we report ADP-ribosylation as a new post-translational modification of PTEN. We identified PTEN as a novel substrate of tankyrases, which are members of ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| TNKS TNKS | Biochemical Activity Biochemical Activity An interaction is inferred from the biochemical effect of one protein upon another, for example, GTP-GDP exchange activity or phosphorylation of a substrate by a kinase. The bait protein executes the activity on the substrate hit protein. A Modification value is recorded for interactions of this type with the possible values Phosphorylation, Ubiquitination, Sumoylation, Dephosphorylation, Methylation, Prenylation, Acetylation, Deubiquitination, Proteolytic Processing, Glucosylation, Nedd(Rub1)ylation, Deacetylation, No Modification, Demethylation. | Low | - | BioGRID | 3556111 | |
| TNKS TNKS | Biochemical Activity Biochemical Activity An interaction is inferred from the biochemical effect of one protein upon another, for example, GTP-GDP exchange activity or phosphorylation of a substrate by a kinase. The bait protein executes the activity on the substrate hit protein. A Modification value is recorded for interactions of this type with the possible values Phosphorylation, Ubiquitination, Sumoylation, Dephosphorylation, Methylation, Prenylation, Acetylation, Deubiquitination, Proteolytic Processing, Glucosylation, Nedd(Rub1)ylation, Deacetylation, No Modification, Demethylation. | Low | - | BioGRID | 303925 | |
| TNKS TNKS | Biochemical Activity Biochemical Activity An interaction is inferred from the biochemical effect of one protein upon another, for example, GTP-GDP exchange activity or phosphorylation of a substrate by a kinase. The bait protein executes the activity on the substrate hit protein. A Modification value is recorded for interactions of this type with the possible values Phosphorylation, Ubiquitination, Sumoylation, Dephosphorylation, Methylation, Prenylation, Acetylation, Deubiquitination, Proteolytic Processing, Glucosylation, Nedd(Rub1)ylation, Deacetylation, No Modification, Demethylation. | Low | - | BioGRID | 859844 |
Curated By
- BioGRID