ID:SH3G2_HUMAN DESCRIPTION: RecName: Full=Endophilin-A1; AltName: Full=EEN-B1; AltName: Full=Endophilin-1; AltName: Full=SH3 domain protein 2A; AltName: Full=SH3 domain-containing GRB2-like protein 2; FUNCTION: Implicated in synaptic vesicle endocytosis. May recruit other proteins to membranes with high curvature. SUBUNIT: Monomer; in cytoplasm. Homodimer; when associated with membranes (By similarity). Interacts with OPHN1 (By similarity). Interacts with SYNJ1 and DNM1. Interacts with MAP4K3; the interaction appears to regulate MAP4K3-mediated JNK activation. Interacts with PDCD6IP. Interacts with ATX2. INTERACTION: Self; NbExp=2; IntAct=EBI-77938, EBI-77938; Q13444:ADAM15; NbExp=2; IntAct=EBI-77938, EBI-77818; Q13443:ADAM9; NbExp=2; IntAct=EBI-77938, EBI-77903; Q99700:ATXN2; NbExp=4; IntAct=EBI-77938, EBI-697691; P50402:EMD; NbExp=2; IntAct=EBI-77938, EBI-489887; Q99963:SH3GL3; NbExp=4; IntAct=EBI-77938, EBI-473910; SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein. Note=Concentrated in presynaptic nerve terminals in neurons. TISSUE SPECIFICITY: Brain, mostly in frontal cortex. Expressed at high level in fetal cerebellum. DOMAIN: An N-terminal amphipathic helix, the BAR domain and a second amphipathic helix inserted into helix 1 of the BAR domain (N-BAR domain) induce membrane curvature and bind curved membranes. The BAR domain dimer forms a rigid crescent shaped bundle of helices with the pair of second amphipathic helices protruding towards the membrane-binding surface. MISCELLANEOUS: HeLa cells expressing the N-BAR domain of SH3GL2 show tubulation of the plasma membrane. The N-BAR domain binds liposomes and induces formation of tubules from liposomes. The N- terminal amphipathic helix is required for liposome binding. The second amphipathic helix enhances liposome tubulation. SIMILARITY: Belongs to the endophilin family. SIMILARITY: Contains 1 BAR domain. SIMILARITY: Contains 1 SH3 domain.
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on Q99962
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.