BAIT
HSD17B10
17b-HSD10, ABAD, CAMR, DUPXp11.22, ERAB, HADH2, HCD2, MHBD, MRPP2, MRX17, MRX31, MRXS10, SCHAD, SDR5C1, RP3-339A18.2
hydroxysteroid (17-beta) dehydrogenase 10
GO Process (4)
GO Function (4)
GO Component (4)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
PREY
ASS1
AA408052, ASS, Ass-1, fold, RP23-442G9.2
argininosuccinate synthetase 1
GO Process (11)
GO Function (4)
GO Component (12)
Gene Ontology Biological Process
- arginine biosynthetic process [IBA, ISO]
- argininosuccinate metabolic process [IBA, ISO]
- aspartate metabolic process [ISO]
- cellular response to laminar fluid shear stress [ISO]
- citrulline metabolic process [ISO]
- negative regulation of leukocyte cell-cell adhesion [ISO]
- positive regulation of nitric oxide biosynthetic process [ISO]
- response to glucocorticoid [ISO]
- response to mycotoxin [ISO]
- response to zinc ion [ISO]
- urea cycle [IBA, ISO]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Mus musculus
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
Short-chain 3-hydroxyacyl-coenzyme A dehydrogenase associates with a protein super-complex integrating multiple metabolic pathways.
Proteins involved in mitochondrial metabolic pathways engage in functionally relevant multi-enzyme complexes. We previously described an interaction between short-chain 3-hydroxyacyl-coenzyme A dehydrogenase (SCHAD) and glutamate dehydrogenase (GDH) explaining the clinical phenotype of hyperinsulinism in SCHAD-deficient patients and adding SCHAD to the list of mitochondrial proteins capable of forming functional, multi-pathway complexes. In this work, we provide evidence of SCHAD's involvement ... [more]
PLoS ONE Apr. 13, 2012; 7(4);e35048 [Pubmed: 22496890]
Throughput
- Low Throughput
Curated By
- BioGRID