ERCC3
Gene Ontology Biological Process
- 7-methylguanosine mRNA capping [TAS]
- DNA repair [IMP, TAS]
- DNA topological change [IMP]
- apoptotic process [IMP]
- gene expression [TAS]
- hair cell differentiation [IMP]
- nucleotide-excision repair [IMP, TAS]
- nucleotide-excision repair, DNA damage removal [TAS]
- nucleotide-excision repair, DNA duplex unwinding [IMP]
- nucleotide-excision repair, DNA incision [IMP]
- positive regulation of apoptotic process [IDA]
- positive regulation of transcription from RNA polymerase II promoter [IDA]
- positive regulation of viral transcription [TAS]
- protein localization [IMP]
- regulation of mitotic cell cycle phase transition [IMP]
- response to UV [IMP]
- response to oxidative stress [IMP]
- termination of RNA polymerase I transcription [TAS]
- transcription elongation from RNA polymerase I promoter [TAS]
- transcription elongation from RNA polymerase II promoter [TAS]
- transcription from RNA polymerase I promoter [TAS]
- transcription from RNA polymerase II promoter [IDA, IMP, TAS]
- transcription initiation from RNA polymerase I promoter [TAS]
- transcription initiation from RNA polymerase II promoter [TAS]
- transcription-coupled nucleotide-excision repair [IDA, TAS]
- viral process [TAS]
Gene Ontology Molecular Function- 3'-5' DNA helicase activity [IDA, IMP]
- ATPase activity [IDA]
- DNA binding [TAS]
- DNA-dependent ATPase activity [IDA, IMP]
- RNA polymerase II carboxy-terminal domain kinase activity [IDA]
- damaged DNA binding [NAS]
- protein C-terminus binding [IPI]
- protein N-terminus binding [IPI]
- protein binding [IPI]
- protein kinase activity [IDA]
- transcription factor binding [IDA]
- 3'-5' DNA helicase activity [IDA, IMP]
- ATPase activity [IDA]
- DNA binding [TAS]
- DNA-dependent ATPase activity [IDA, IMP]
- RNA polymerase II carboxy-terminal domain kinase activity [IDA]
- damaged DNA binding [NAS]
- protein C-terminus binding [IPI]
- protein N-terminus binding [IPI]
- protein binding [IPI]
- protein kinase activity [IDA]
- transcription factor binding [IDA]
Gene Ontology Cellular Component
- holo TFIIH complex [IDA, TAS]
- nucleoplasm [IDA, TAS]
- nucleus [TAS]
TUBG1
Gene Ontology Biological Process
Gene Ontology Molecular Function
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 TFIIH subunit p89 (XPB) localizes to the centrosome during mitosis.
The general transcription factor II H (TFIIH), comprised of a core complex and an associated CAK-complex, functions in transcription, DNA repair and cell cycle control. Mutations of the two largest subunits, p89 (XPB) and p80 (XPD), cause the hereditary cancer-prone syndrome xeroderma pigmentosum.The TFIIH subunit p89 was monitored during interphase and cell division by immunofluorescence staining, GFP-fusion constructs including deletions, ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| TUBG1 ERCC3 | 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