Formin-binding protein 1 (FNBP1, also known as formin-binding protein 17) contains a N-terminal FER-CIP4 homology (FCH) domain and a C-terminal SH3 domain. It belongs to the CIP4 (Cdc42 interacting protein-4) subfamily of the F-BAR protein family. F-BAR proteins (F for FCH, Fer-CIP4 homology domain) are proteins with an extended CIP4-Fer domain. The F-BAR proteins have been implicated in cell membrane processes such as membrane invagination, tubulation and endocytosis []. FNBP1 was originally isolated as a molecule that binds to the proline-rich region of formin []. It induces tubular membrane invaginations and participates in endocytosis []. It interacts with sorting nexin, SNX2, and is linked to acute myelogeneous leukemia [].
This entry represents the SH3 domain of FNBP1.Formin-binding protein 1 (FNBP1, also known as formin-binding protein 17) contains a N-terminal FER-CIP4 homology (FCH) domain and a C-terminal SH3 domain. It belongs to the CIP4 (Cdc42 interacting protein-4) subfamily of the F-BAR protein family. F-BAR proteins (F for FCH, Fer-CIP4 homology domain) are proteins with an extended CIP4-Fer domain. The F-BAR proteins have been implicated in cell membrane processes such as membrane invagination, tubulation and endocytosis []. FNBP1 was originally isolated as a molecule that binds to the proline-rich region of formin []. It induces tubular membrane invaginations and participates in endocytosis []. It interacts with sorting nexin, SNX2, and is linked to acute myelogeneous leukemia [].
Formin-binding protein 1 (FNBP1, also known as formin-binding protein 17) contains a N-terminal FER-CIP4 homology (FCH) domain and a C-terminal SH3 domain. It belongs to the CIP4 (Cdc42 interacting protein-4) subfamily of the F-BAR protein family. F-BAR proteins (F for FCH, Fer-CIP4 homology domain) are proteins with an extended CIP4-Fer domain. The F-BAR proteins have been implicated in cell membrane processes such as membrane invagination, tubulation and endocytosis []. FNBP1 was originally isolated as a molecule that binds to the proline-rich region of formin []. It induces tubular membrane invaginations and participates in endocytosis []. It interacts with sorting nexin, SNX2, and is linked to acute myelogeneous leukemia [].This entry represents the F-BAR domain of FNBP1. F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization [].
