UBE2V1
Gene Ontology Biological Process
- Fc-epsilon receptor signaling pathway [TAS]
- MyD88-dependent toll-like receptor signaling pathway [TAS]
- T cell receptor signaling pathway [TAS]
- cell differentiation [NAS]
- innate immune response [TAS]
- nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway [TAS]
- nucleotide-binding oligomerization domain containing signaling pathway [TAS]
- positive regulation of I-kappaB kinase/NF-kappaB signaling [IMP, TAS]
- positive regulation of NF-kappaB transcription factor activity [IMP]
- positive regulation of transcription, DNA-templated [TAS]
- postreplication repair [IBA]
- protein K63-linked ubiquitination [IDA]
- protein polyubiquitination [TAS]
- regulation of DNA repair [TAS]
- regulation of transcription, DNA-templated [TAS]
- toll-like receptor 10 signaling pathway [TAS]
- toll-like receptor 2 signaling pathway [TAS]
- toll-like receptor 4 signaling pathway [TAS]
- toll-like receptor 5 signaling pathway [TAS]
- toll-like receptor 9 signaling pathway [TAS]
- toll-like receptor TLR1:TLR2 signaling pathway [TAS]
- toll-like receptor TLR6:TLR2 signaling pathway [TAS]
- toll-like receptor signaling pathway [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
STUB1
Gene Ontology Biological Process
- cellular response to misfolded protein [IDA]
- misfolded or incompletely synthesized protein catabolic process [IDA]
- negative regulation of transforming growth factor beta receptor signaling pathway [TAS]
- positive regulation of chaperone-mediated protein complex assembly [IDA]
- positive regulation of proteasomal ubiquitin-dependent protein catabolic process [IDA]
- positive regulation of protein ubiquitination [IDA]
- proteasome-mediated ubiquitin-dependent protein catabolic process [IDA]
- protein K63-linked ubiquitination [IDA]
- protein autoubiquitination [IDA]
- protein maturation [TAS]
- protein polyubiquitination [IDA, IMP]
- regulation of glucocorticoid metabolic process [IDA]
- transforming growth factor beta receptor signaling pathway [TAS]
- ubiquitin-dependent SMAD protein catabolic process [IDA]
- ubiquitin-dependent protein catabolic process [IMP]
Gene Ontology Molecular Function- G-protein coupled receptor binding [IPI]
- Hsp70 protein binding [IDA]
- Hsp90 protein binding [IDA]
- SMAD binding [IDA]
- TPR domain binding [IDA]
- enzyme binding [IPI]
- kinase binding [IPI]
- misfolded protein binding [IDA]
- protein binding [IPI]
- protein binding, bridging [TAS]
- protein homodimerization activity [ISS]
- ubiquitin protein ligase activity [IDA]
- ubiquitin protein ligase binding [IPI]
- ubiquitin-protein transferase activity [IDA, IMP, TAS]
- ubiquitin-ubiquitin ligase activity [ISS]
- G-protein coupled receptor binding [IPI]
- Hsp70 protein binding [IDA]
- Hsp90 protein binding [IDA]
- SMAD binding [IDA]
- TPR domain binding [IDA]
- enzyme binding [IPI]
- kinase binding [IPI]
- misfolded protein binding [IDA]
- protein binding [IPI]
- protein binding, bridging [TAS]
- protein homodimerization activity [ISS]
- ubiquitin protein ligase activity [IDA]
- ubiquitin protein ligase binding [IPI]
- ubiquitin-protein transferase activity [IDA, IMP, TAS]
- ubiquitin-ubiquitin ligase activity [ISS]
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
Chaperoned ubiquitylation--crystal structures of the CHIP U box E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex.
CHIP is a dimeric U box E3 ubiquitin ligase that binds Hsp90 and/or Hsp70 via its TPR-domain, facilitating ubiquitylation of chaperone bound client proteins. We have determined the crystal structure of CHIP bound to an Hsp90 C-terminal decapeptide. The structure explains how CHIP associates with either chaperone type and reveals an unusual asymmetric homodimer in which the protomers adopt radically ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| UBE2V1 STUB1 | 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. | Low | - | BioGRID | - | |
| STUB1 UBE2V1 | 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 | 0.848 | BioGRID | 744383 | |
| STUB1 UBE2V1 | 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 | 2484966 | |
| STUB1 UBE2V1 | 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 | - | |
| STUB1 UBE2V1 | 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 | - | |
| STUB1 UBE2V1 | 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 | 1032731 |
Curated By
- BioGRID