RAD23A
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
UBC
Gene Ontology Biological Process
- DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [TAS]
- DNA repair [TAS]
- Fc-epsilon receptor signaling pathway [TAS]
- G1/S transition of mitotic cell cycle [TAS]
- G2/M transition of mitotic cell cycle [TAS]
- I-kappaB kinase/NF-kappaB signaling [TAS]
- JNK cascade [TAS]
- MyD88-dependent toll-like receptor signaling pathway [TAS]
- MyD88-independent toll-like receptor signaling pathway [TAS]
- Notch receptor processing [TAS]
- Notch signaling pathway [TAS]
- RNA metabolic process [TAS]
- T cell receptor signaling pathway [TAS]
- TRIF-dependent toll-like receptor signaling pathway [TAS]
- activation of MAPK activity [TAS]
- anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process [TAS]
- antigen processing and presentation of exogenous peptide antigen via MHC class I [TAS]
- antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent [TAS]
- antigen processing and presentation of peptide antigen via MHC class I [TAS]
- apoptotic process [TAS]
- apoptotic signaling pathway [TAS]
- carbohydrate metabolic process [TAS]
- cellular response to hypoxia [TAS]
- cytokine-mediated signaling pathway [TAS]
- endosomal transport [TAS]
- epidermal growth factor receptor signaling pathway [TAS]
- fibroblast growth factor receptor signaling pathway [TAS]
- gene expression [TAS]
- glucose metabolic process [TAS]
- glycogen biosynthetic process [TAS]
- innate immune response [TAS]
- intracellular transport of virus [TAS]
- ion transmembrane transport [TAS]
- mRNA metabolic process [TAS]
- membrane organization [TAS]
- mitotic cell cycle [TAS]
- negative regulation of apoptotic process [TAS]
- negative regulation of epidermal growth factor receptor signaling pathway [TAS]
- negative regulation of transcription from RNA polymerase II promoter [TAS]
- negative regulation of transforming growth factor beta receptor signaling pathway [TAS]
- negative regulation of type I interferon production [TAS]
- negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [TAS]
- neurotrophin TRK receptor signaling pathway [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 [TAS]
- positive regulation of NF-kappaB transcription factor activity [TAS]
- positive regulation of apoptotic process [TAS]
- positive regulation of transcription from RNA polymerase II promoter [TAS]
- positive regulation of type I interferon production [TAS]
- positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [TAS]
- protein polyubiquitination [TAS]
- regulation of apoptotic process [TAS]
- regulation of transcription from RNA polymerase II promoter in response to hypoxia [TAS]
- regulation of type I interferon production [TAS]
- regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [TAS]
- small molecule metabolic process [TAS]
- stress-activated MAPK cascade [TAS]
- toll-like receptor 10 signaling pathway [TAS]
- toll-like receptor 2 signaling pathway [TAS]
- toll-like receptor 3 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]
- transcription initiation from RNA polymerase II promoter [TAS]
- transcription, DNA-templated [TAS]
- transforming growth factor beta receptor signaling pathway [TAS]
- transmembrane transport [TAS]
- viral life cycle [TAS]
- viral process [TAS]
- viral protein processing [TAS]
- virion assembly [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Co-crystal Structure
Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.
Publication
Binding of HIV-1 Vpr protein to the human homolog of the yeast DNA repair protein RAD23 (hHR23A) requires its xeroderma pigmentosum complementation group C binding (XPCB) domain as well as the ubiquitin-associated 2 (UBA2) domain.
The human homolog of the yeast DNA repair protein RAD23, hHR23A, has been found previously to interact with the human immunodeficiency virus, type 1 accessory protein Vpr. hHR23A is a modular protein containing an N-terminal ubiquitin-like (UBL) domain and two ubiquitin-associated domains (UBA1 and UBA2) separated by a xeroderma pigmentosum complementation group C binding (XPCB) domain. All domains are connected ... [more]
Throughput
- Low Throughput
Additional Notes
- #LPPI
- Likely protein-protein interaction
- NMR
- Rad23 binds di-UbK48 in vitro
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| RAD23A UBC | 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 | 666104 | |
| RAD23A UBC | 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 | 733640 | |
| RAD23A UBC | Co-crystal Structure Co-crystal Structure Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex. | Low | - | BioGRID | 665429 | |
| RAD23A UBC | Co-crystal Structure Co-crystal Structure Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex. | Low | - | BioGRID | 1101384 | |
| RAD23A UBC | Co-crystal Structure Co-crystal Structure Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex. | Low | - | BioGRID | 665464 | |
| UBC RAD23A | Protein-peptide Protein-peptide An interaction is detected between a protein and a peptide derived from an interaction partner. This includes phage display experiments. | High | - | BioGRID | 2621819 | |
| UBC RAD23A | Protein-peptide Protein-peptide An interaction is detected between a protein and a peptide derived from an interaction partner. This includes phage display experiments. | Low | - | BioGRID | 682085 | |
| UBC RAD23A | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | - | |
| UBC RAD23A | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | 2621838 | |
| RAD23A UBC | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | 2621856 | |
| RAD23A UBC | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | 1100992 | |
| UBC RAD23A | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | 684418 | |
| RAD23A UBC | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | 1100710 | |
| RAD23A UBC | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | 445688 | |
| RAD23A UBC | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | 665431 | |
| UBC RAD23A | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low/High | - | BioGRID | 3515613 | |
| UBC RAD23A | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | 1257416 | |
| RAD23A UBC | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | 732998 | |
| RAD23A UBC | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | 1101084 | |
| RAD23A UBC | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | 814657 | |
| UBC RAD23A | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low/High | - | BioGRID | 814424 | |
| UBC RAD23A | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | 3322661 | |
| RAD23A UBC | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | 679430 | |
| RAD23A UBC | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | 727424 | |
| RAD23A UBC | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | 560210 | |
| UBC RAD23A | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | 680114 | |
| UBC RAD23A | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | High | - | BioGRID | 2881107 | |
| RAD23A UBC | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | 3325334 | |
| UBC RAD23A | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | High | - | BioGRID | 2296881 |
Curated By
- BioGRID