BAIT
SH3GL2
9530001L19Rik, AI120490, AW555077, B930049H17Rik, EEN-B1, SH3PA, Sh3d2a, RP23-158E10.3
SH3-domain GRB2-like 2
GO Process (2)
GO Function (2)
GO Component (2)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Mus musculus
PREY
AMPH
amphiphysin
GO Process (2)
GO Function (5)
GO Component (5)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Mus musculus
Reconstituted Complex
An interaction is detected between purified proteins in vitro.
Publication
Characterization of Endophilin B1b, a brain-specific membrane-associated lysophosphatidic acid acyl transferase with properties distinct from endophilin A1.
We have characterized mammalian endophilin B1, a novel member of the endophilins and a representative of their B subgroup. The endophilins B show the same domain organization as the endophilins A, which contain an N-terminal domain responsible for lipid binding and lysophosphatidic acid acyl transferase activity, a central coiled-coil domain for oligomerization, a less conserved linker region, and a C-terminal ... [more]
J. Biol. Chem. Feb. 07, 2003; 278(6);4160-7 [Pubmed: 12456676]
Throughput
- Low Throughput
Additional Notes
- Figure 2
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| SH3GL2 AMPH | Co-fractionation Co-fractionation Interaction inferred from the presence of two or more protein subunits in a partially purified protein preparation. If co-fractionation is demonstrated between 3 or more proteins, then add them as a complex. | High | 0.8075 | BioGRID | 2666731 |
Curated By
- BioGRID