SH3 Domain GRB2 Like Endophilin B2 (SH3GLB2)

SH3GLB2 could form homodimers and heterodimers with SH3GLB1 in vitro. Mutation analysis indicated that the core coiled-coil region was required for the formation of SH3GLB homodimers and heterodimers, but the SH3 domain was not.The deduced 395-amino acid protein contains an N-terminal domain, a central coiled-coil region, and a C-terminal SH3 domain. SH3GLB2 shares 65% amino acid identity with SH3GLB1, but it has a 23-amino acid extension following the coiled-coil region that is not present in SH3GLB1. RT-PCR and EST database analysis indicated that SH3GLB2 is expressed in many tissues, including skeletal muscle, adipocytes, brain, lung, colon, and mammary gland. SH3GLB2 was expressed in the cytoplasm of transfected HeLa cells and was excluded from nuclei.