UniProt functional annotation for P49791



	UniProt functional annotation for P49791

UniProt code: P49791.

Organism: Rattus norvegicus (Rat).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus.

Function: Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC essential for normal nucleocytoplasmic transport of proteins and mRNAs. Involved in the quality control and retention of unspliced mRNAs in the nucleus; in association with TPR, regulates the nuclear export of unspliced mRNA species bearing constitutive transport element (CTE) in a NXF1- and KHDRBS1-independent manner. Mediates TPR anchoring to the nuclear membrane at NPC (By similarity). The repeat-containing domain may be involved in anchoring other components of the NPC to the pore membrane. Possible DNA-binding subunit of the nuclear pore complex (NPC) (By similarity). {ECO:0000250}.

Cofactor: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds at least 4 zinc ions per subunit.;

Subunit: Part of the nuclear pore complex (NPC). Interacts with TPR (via coiled coil region); the interaction is direct and provides a link between the core structure and the TPR-containing nuclear basket of the nuclear pore complex (NPC). Interacts with HIKESHI, SENP2 and XPO5 (By similarity). Interacts with RAN; the interaction occurs in a GTP- and GDP-independent manner. Interacts with MCM3AP; this interaction is required for MCM3AP localization at the nuclear pore complex (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P49790, ECO:0000269|PubMed:18611384, ECO:0000269|PubMed:19505478}.

Subcellular location: Nucleus. Nucleus membrane. Nucleus, nuclear pore complex. Note=Dissociates from the NPC structure early during prophase of mitosis. Integrated in the newly assembled nuclear envelope of postmitotic cells early in G1 (By similarity). Localized to the nucleoplasmic side of the nuclear pore complex (NPC) core structure, forming a fibrous structure called the nuclear basket. Tightly associated with the nuclear membrane and lamina. Colocalized with NUP98 and TPR to the nuclear basket at the nucleoplasmic side of the NPC. Detected in diffuse and discrete intranuclear foci. {ECO:0000250}.

Domain: Contains FG repeats. FG repeats are interaction sites for karyopherins (importins, exportins) and form probably an affinity gradient, guiding the transport proteins unidirectionally with their cargo through the NPC. FG repeat regions are highly flexible and lack ordered secondary structure. The overall conservation of FG repeats regarding exact sequence, spacing, and repeat unit length is limited. {ECO:0000305}.

Ptm: Phosphorylated in interphase, hyperphosphorylated during mitosis. May play a role in the reversible disassembly of the nuclear pore complex during mitosis.

Ptm: O-glycosylated during cytokinesis at sites identical or close to phosphorylation sites, this interferes with the phosphorylation status. {ECO:0000250}.

Similarity: Belongs to the NUP153 family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Rattus norvegicus (Rat).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus.



Function:		Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC essential for normal nucleocytoplasmic transport of proteins and mRNAs. Involved in the quality control and retention of unspliced mRNAs in the nucleus; in association with TPR, regulates the nuclear export of unspliced mRNA species bearing constitutive transport element (CTE) in a NXF1- and KHDRBS1-independent manner. Mediates TPR anchoring to the nuclear membrane at NPC (By similarity). The repeat-containing domain may be involved in anchoring other components of the NPC to the pore membrane. Possible DNA-binding subunit of the nuclear pore complex (NPC) (By similarity). {ECO:0000250}.


Cofactor:		Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds at least 4 zinc ions per subunit.;
Subunit:		Part of the nuclear pore complex (NPC). Interacts with TPR (via coiled coil region); the interaction is direct and provides a link between the core structure and the TPR-containing nuclear basket of the nuclear pore complex (NPC). Interacts with HIKESHI, SENP2 and XPO5 (By similarity). Interacts with RAN; the interaction occurs in a GTP- and GDP-independent manner. Interacts with MCM3AP; this interaction is required for MCM3AP localization at the nuclear pore complex (By similarity). {ECO:0000250, ECO:0000250\|UniProtKB:P49790, ECO:0000269\|PubMed:18611384, ECO:0000269\|PubMed:19505478}.
Subcellular location:		Nucleus. Nucleus membrane. Nucleus, nuclear pore complex. Note=Dissociates from the NPC structure early during prophase of mitosis. Integrated in the newly assembled nuclear envelope of postmitotic cells early in G1 (By similarity). Localized to the nucleoplasmic side of the nuclear pore complex (NPC) core structure, forming a fibrous structure called the nuclear basket. Tightly associated with the nuclear membrane and lamina. Colocalized with NUP98 and TPR to the nuclear basket at the nucleoplasmic side of the NPC. Detected in diffuse and discrete intranuclear foci. {ECO:0000250}.
Domain:		Contains FG repeats. FG repeats are interaction sites for karyopherins (importins, exportins) and form probably an affinity gradient, guiding the transport proteins unidirectionally with their cargo through the NPC. FG repeat regions are highly flexible and lack ordered secondary structure. The overall conservation of FG repeats regarding exact sequence, spacing, and repeat unit length is limited. {ECO:0000305}.
Ptm:		Phosphorylated in interphase, hyperphosphorylated during mitosis. May play a role in the reversible disassembly of the nuclear pore complex during mitosis.
Ptm:		O-glycosylated during cytokinesis at sites identical or close to phosphorylation sites, this interferes with the phosphorylation status. {ECO:0000250}.
Similarity:		Belongs to the NUP153 family. {ECO:0000305}.