| Ensembl ID | Symbol | Entrez ID | RBD | RBPome | PRI | Expresion | Pathway | Phenotype | Paralog | Ortholog | GO |
|---|---|---|---|---|---|---|---|---|---|---|---|
The vertebrate Tap protein is a member of the NXF family of shuttling transport receptors for nuclear export of mRNA. Tap has a modular structure, and its most C-terminal domain is important for binding to FG repeat-containing nuclear pore proteins (FG-nucleoporins) and is sufficient to mediate nuclear shuttling [1]. The structure of the C-terminal domain is composed of four helices [1]. The structure is related to the UBA domain.
The vertebrate Tap protein is a member of the NXF family of shuttling transport receptors for nuclear export of mRNA. Tap has a modular structure, and its most C-terminal domain is important for binding to FG repeat-containing nuclear pore proteins (FG-nucleoporins) and is sufficient to mediate nuclear shuttling [PUBMED:11875519]. The structure of the C-terminal domain is composed of four helices [PUBMED:11875519]. The structure is related to the UBA domain.
Grant RP, Hurt E, Neuhaus D, Stewart M; , Nat Struct Biol 2002;9:247-251.: Structure of the C-terminal FG-nucleoporin binding domain of Tap/NXF1. PUBMED:11875519 EPMC:11875519.
