USP4
Gene Ontology Biological Process
- negative regulation of protein ubiquitination [IMP]
- proteasome-mediated ubiquitin-dependent protein catabolic process [IBA]
- protein deubiquitination [IDA, IMP]
- protein localization to cell surface [IDA]
- regulation of proteasomal protein catabolic process [IBA]
- regulation of protein stability [IDA]
- spliceosomal tri-snRNP complex assembly [IMP]
Gene Ontology Molecular Function
RB1
Gene Ontology Biological Process
- G1/S transition of mitotic cell cycle [TAS]
- Ras protein signal transduction [IEP]
- androgen receptor signaling pathway [NAS]
- cell cycle arrest [TAS]
- cell cycle checkpoint [TAS]
- chromatin remodeling [TAS]
- maintenance of mitotic sister chromatid cohesion [IMP]
- mitotic cell cycle [TAS]
- mitotic cell cycle checkpoint [TAS]
- myoblast differentiation [IMP]
- negative regulation of G1/S transition of mitotic cell cycle [TAS]
- negative regulation of protein kinase activity [IPI]
- negative regulation of sequence-specific DNA binding transcription factor activity [TAS]
- negative regulation of transcription from RNA polymerase II promoter during mitosis [TAS]
- negative regulation of transcription, DNA-templated [IDA, TAS]
- positive regulation of mitotic metaphase/anaphase transition [IMP]
- positive regulation of transcription, DNA-templated [NAS]
- protein localization to chromosome, centromeric region [IMP]
- regulation of centromere complex assembly [TAS]
- regulation of cohesin localization to chromatin [IMP]
- regulation of lipid kinase activity [IDA]
- regulation of mitotic cell cycle [IMP]
- regulation of transcription involved in G1/S transition of mitotic cell cycle [TAS]
- sister chromatid biorientation [IMP]
Gene Ontology Molecular Function- DNA binding [TAS]
- androgen receptor binding [NAS]
- core promoter binding [IDA]
- identical protein binding [IPI]
- kinase binding [IDA]
- phosphoprotein binding [IPI]
- protein binding [IPI]
- sequence-specific DNA binding transcription factor activity [TAS]
- transcription coactivator activity [NAS]
- transcription factor binding [IPI]
- ubiquitin protein ligase binding [IPI]
- DNA binding [TAS]
- androgen receptor binding [NAS]
- core promoter binding [IDA]
- identical protein binding [IPI]
- kinase binding [IDA]
- phosphoprotein binding [IPI]
- protein binding [IPI]
- sequence-specific DNA binding transcription factor activity [TAS]
- transcription coactivator activity [NAS]
- transcription factor binding [IPI]
- ubiquitin protein ligase binding [IPI]
Gene Ontology Cellular Component
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.
Publication
The de-ubiquitinating enzyme Unp interacts with the retinoblastoma protein.
The ubiquitin pathway is involved in the proteolytic turnover of many short-lived cellular regulatory proteins. Since selective degradation of substrates of this system requires the covalent attachment of a polyubiquitin chain to the substrates, degradation could be counteracted by de-ubiquitinating enzymes (or isopeptidases) which selectively remove the polyubiquitin chain. Unp is a human isopeptidase with still poorly understood biological functions. ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| USP4 RB1 | 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 | - | |
| USP4 RB1 | 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 | - | |
| USP4 RB1 | 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. | Low | - | BioGRID | - | |
| USP4 RB1 | 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 | - |
Curated By
- BioGRID