BAIT
MATR3
ALS21, MPD2, VCPDM
matrin 3
GO Process (0)
GO Function (3)
GO Component (3)
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
PREY
CAD
carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase
GO Process (11)
GO Function (10)
GO Component (10)
Gene Ontology Biological Process
- 'de novo' pyrimidine nucleobase biosynthetic process [IDA, ISS]
- arginine biosynthetic process [IBA]
- drug metabolic process [ISS]
- glutamine metabolic process [ISS]
- nucleobase-containing small molecule metabolic process [TAS]
- peptidyl-threonine phosphorylation [ISS]
- protein autophosphorylation [ISS]
- pyrimidine nucleobase metabolic process [TAS]
- pyrimidine nucleoside biosynthetic process [TAS]
- small molecule metabolic process [TAS]
- urea cycle [IBA]
Gene Ontology Molecular Function- ATP binding [ISS]
- aspartate binding [ISS]
- aspartate carbamoyltransferase activity [IBA, ISS, TAS]
- carbamoyl-phosphate synthase (ammonia) activity [IBA]
- carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity [IBA, ISS, TAS]
- dihydroorotase activity [IDA, ISS, TAS]
- enzyme binding [IPI]
- identical protein binding [ISS]
- protein kinase activity [ISS]
- zinc ion binding [IDA]
- ATP binding [ISS]
- aspartate binding [ISS]
- aspartate carbamoyltransferase activity [IBA, ISS, TAS]
- carbamoyl-phosphate synthase (ammonia) activity [IBA]
- carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity [IBA, ISS, TAS]
- dihydroorotase activity [IDA, ISS, TAS]
- enzyme binding [IPI]
- identical protein binding [ISS]
- protein kinase activity [ISS]
- zinc ion binding [IDA]
Gene Ontology Cellular Component
Homo sapiens
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.
Publication
Interactome analyses revealed that the U1 snRNP machinery overlaps extensively with the RNAP II machinery and contains multiple ALS/SMA-causative proteins.
Mutations in multiple RNA/DNA binding proteins cause Amyotrophic Lateral Sclerosis (ALS). Included among these are the three members of the FET family (FUS, EWSR1 and TAF15) and the structurally similar MATR3. Here, we characterized the interactomes of these four proteins, revealing that they largely have unique interactors, but share in common an association with U1 snRNP. The latter observation led ... [more]
Sci Rep Dec. 08, 2017; 8(1);8755 [Pubmed: 29884807]
Throughput
- High Throughput
Curated By
- BioGRID