ARG82
Gene Ontology Biological Process
- inositol phosphate biosynthetic process [IDA]
- negative regulation of transcription from RNA polymerase II promoter [IMP]
- phosphatidylinositol phosphorylation [IDA]
- positive regulation of transcription from RNA polymerase II promoter [IMP]
- protein stabilization [IMP]
- regulation of arginine metabolic process [IMP]
Gene Ontology Molecular Function- inositol tetrakisphosphate 3-kinase activity [IDA]
- inositol tetrakisphosphate 6-kinase activity [IDA]
- inositol-1,3,4,5,6-pentakisphosphate kinase activity [IDA]
- inositol-1,4,5-trisphosphate 3-kinase activity [IMP]
- inositol-1,4,5-trisphosphate 6-kinase activity [IDA]
- phosphatidylinositol 3-kinase activity [IDA]
- protein binding, bridging [IMP, IPI]
- inositol tetrakisphosphate 3-kinase activity [IDA]
- inositol tetrakisphosphate 6-kinase activity [IDA]
- inositol-1,3,4,5,6-pentakisphosphate kinase activity [IDA]
- inositol-1,4,5-trisphosphate 3-kinase activity [IMP]
- inositol-1,4,5-trisphosphate 6-kinase activity [IDA]
- phosphatidylinositol 3-kinase activity [IDA]
- protein binding, bridging [IMP, IPI]
ARG80
Gene Ontology Biological Process
Gene Ontology Molecular Function
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
Recruitment of the yeast MADS-box proteins, ArgRI and Mcm1 by the pleiotropic factor ArgRIII is required for their stability.
Regulation of arginine metabolism requires the integrity of four regulatory proteins, ArgRI, ArgRII, ArgRIII and Mcm1. To characterize further the interactions between the different proteins, we used the two-hybrid system, which showed that ArgRI and Mcm1 interact together, and with ArgRII and ArgRIII, without an arginine requirement. To define the interacting domains of ArgRI and Mcm1 with ArgRIII, we fused ... [more]
Throughput
- Low Throughput
Related interactions
Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
---|---|---|---|---|---|---|
ARG82 ARG80 | Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation. | Low | - | BioGRID | - | |
ARG80 ARG82 | Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation. | Low | - | BioGRID | - | |
ARG82 ARG80 | Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation. | Low | - | BioGRID | - | |
ARG82 ARG80 | Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation. | High | - | BioGRID | - |
Curated By
- BioGRID