HLCS
Gene Ontology Biological Process
Gene Ontology Molecular Function
ACACB
Gene Ontology Biological Process
- acetyl-CoA metabolic process [IDA]
- biotin metabolic process [TAS]
- carnitine shuttle [TAS]
- cellular lipid metabolic process [TAS]
- energy reserve metabolic process [TAS]
- positive regulation of cellular metabolic process [TAS]
- protein homotetramerization [IDA]
- small molecule metabolic process [TAS]
- vitamin metabolic process [TAS]
- water-soluble vitamin metabolic process [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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.
Publication
The N-terminal domain of human holocarboxylase synthetase facilitates biotinylation via direct interaction with the substrate protein.
Human holocarboxylase synthetase shows a high degree of sequence homology in the catalytic domain with bacterial biotin ligases such as Escherichia coli BirA, but differs in the length and sequence of the N-terminus. Despite several studies having been undertaken on the N-terminal region of hHCS, the role of this region remains unclear. We determined the structure of the N-terminal domain ... [more]
Throughput
- Low Throughput
Additional Notes
- Biotinylation
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| HLCS ACACB | 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 | - |
Curated By
- BioGRID