UniProt functional annotation for Q9UBU9



	UniProt functional annotation for Q9UBU9

UniProt code: Q9UBU9.

Organism: Homo sapiens (Human).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

Function: Involved in the nuclear export of mRNA species bearing retroviral constitutive transport elements (CTE) and in the export of mRNA from the nucleus to the cytoplasm (TAP/NFX1 pathway) (PubMed:10924507). The NXF1-NXT1 heterodimer is involved in the export of HSP70 mRNA in conjunction with ALYREF/THOC4 and THOC5 components of the TREX complex (PubMed:18364396, PubMed:19165146, PubMed:9660949). ALYREF/THOC4-bound mRNA is thought to be transferred to the NXF1-NXT1 heterodimer for export (PubMed:18364396, PubMed:19165146, PubMed:9660949). Also involved in nuclear export of m6A-containing mRNAs: interaction between SRSF3 and YTHDC1 facilitates m6A-containing mRNA-binding to both SRSF3 and NXF1, promoting mRNA nuclear export (PubMed:28984244). {ECO:0000269|PubMed:10924507, ECO:0000269|PubMed:18364396, ECO:0000269|PubMed:19165146, ECO:0000269|PubMed:28984244, ECO:0000269|PubMed:9660949}.

Subunit: Heterodimer (via NTF2 domain) with NXT1 (PubMed:11583626). The formation of NXF1-NXT1 heterodimers is required for the NXF1-mediated nuclear mRNA export (PubMed:11583626). Forms a complex with RANBP2/NUP358, NXT1 and RANGAP1 (PubMed:14729961). Associates with the exon junction complex (EJC) and with the transcription/export (TREX) complex (PubMed:11707413, PubMed:22893130). Found in a mRNA complex with UPF3A and UPF3B (PubMed:11546873). Found in a post-splicing complex with RBM8A, UPF1, UPF2, UPF3A, UPF3B and RNPS1 (PubMed:11546874). Interacts (via N-terminus) with DHX9 (via N- terminus); this interaction is direct and negatively regulates NXF1- mediated nuclear export of constitutive transport element (CTE)- containing cellular mRNAs (PubMed:10924507). Interacts with ALYREF/THOC4 (PubMed:11707413, PubMed:14730019, PubMed:19165146, PubMed:23299939). Interacts with FYTTD1/UIF (PubMed:19836239). Interacts with EIF4A3 (PubMed:14730019). Interacts with NUP42 (PubMed:10228171). Interacts with THOC5 (PubMed:19165146, PubMed:23299939). Interacts with CHTOP (PubMed:23299939, PubMed:23826332). Interacts with FRG1 (via N-terminus) (PubMed:21699900). Interacts with LUZP4 (PubMed:25662211). Interacts with FMR1; the interaction occurs in a mRNA-dependent and polyribosomes-independent manner in the nucleus (PubMed:18936162). Interacts with CPSF6 (via N-terminus); this interaction is direct (PubMed:19864460). Interacts with RBM15 (PubMed:17001072). Interacts with RBM15B (PubMed:19586903). Interacts with MCM3AP isoform GANP; this interaction is not mediated by RNA (PubMed:20005110). Interacts with DDX3X (via C-terminus); this interaction may be partly involved in DDX3X nuclear export and in NXF1 localization to stress granules (PubMed:18596238). Interacts with PABPC1/PABP1 (PubMed:18596238). {ECO:0000269|PubMed:10228171, ECO:0000269|PubMed:10924507, ECO:0000269|PubMed:11546873, ECO:0000269|PubMed:11546874, ECO:0000269|PubMed:11583626, ECO:0000269|PubMed:11707413, ECO:0000269|PubMed:12581645, ECO:0000269|PubMed:14729961, ECO:0000269|PubMed:14730019, ECO:0000269|PubMed:17001072, ECO:0000269|PubMed:18596238, ECO:0000269|PubMed:18936162, ECO:0000269|PubMed:19165146, ECO:0000269|PubMed:19369354, ECO:0000269|PubMed:19586903, ECO:0000269|PubMed:19836239, ECO:0000269|PubMed:19864460, ECO:0000269|PubMed:20005110, ECO:0000269|PubMed:21699900, ECO:0000269|PubMed:22893130, ECO:0000269|PubMed:23299939, ECO:0000269|PubMed:23826332, ECO:0000269|PubMed:25662211, ECO:0000269|PubMed:9175835}.

Subunit: (Microbial infection) Interacts with Saimiriine herpesvirus 2 TIP protein. {ECO:0000269|PubMed:9175835}.

Subunit: (Microbial infection) Interacts with human herpes virus 1 (HHV-1) ICP27 protein; this interaction allows efficient export of HHV- 1 early and late transcripts. {ECO:0000269|PubMed:19369354}.

Subunit: (Microbial infection) Interacts (via RNA-binding domain) with Ebolavirus nucleoprotein; this interaction recruits NXF1 to the inclusion bodies were viral replication takes place, probably to export viral mRNA-NXF1 complexes from these sites. {ECO:0000269|PubMed:31940815}.

Subcellular location: Nucleus {ECO:0000269|PubMed:10924507, ECO:0000269|PubMed:18596238, ECO:0000269|PubMed:19864460, ECO:0000269|PubMed:23591820, ECO:0000269|PubMed:25662211}. Nucleus, nucleoplasm {ECO:0000269|PubMed:19324961, ECO:0000269|PubMed:23826332}. Nucleus speckle {ECO:0000269|PubMed:19324961, ECO:0000269|PubMed:23826332}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:23591820}. Nucleus envelope {ECO:0000269|PubMed:18596238, ECO:0000269|PubMed:23591820}. Cytoplasm {ECO:0000269|PubMed:10924507, ECO:0000269|PubMed:18596238, ECO:0000269|PubMed:19324961, ECO:0000269|PubMed:19864460}. Cytoplasm, Stress granule {ECO:0000269|PubMed:18596238}. Note=Localized predominantly in the nucleoplasm and at both the nucleoplasmic and cytoplasmic faces of the nuclear pore complex. Shuttles between the nucleus and the cytoplasm. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. The association with the TREX complex seems to occur in regions surrounding nuclear speckles known as perispeckles (PubMed:23826332). Nucleus; nuclear rim (PubMed:25662211). {ECO:0000269|PubMed:23826332, ECO:0000269|PubMed:25662211}.

Tissue specificity: Expressed ubiquitously.

Domain: The minimal CTE binding domain consists of an RNP-type RNA binding domain (RBD) and leucine-rich repeats. {ECO:0000269|PubMed:11583626}.

Domain: The nucleoporin binding domain consists of a NTF2 domain (also called NTF2-like domain) and a TAP-C domain (also called UBA-like domain). It has 2 nucleoporin-FG-repeats binding sites (one in the NTF2 and the other in the TAP-C domain) which contribute to nucleoporin association and act synergistically to export cellular mRNAs. {ECO:0000269|PubMed:11583626}.

Domain: The NTF2 domain is functional only in the presence of NXT1 and is essential for the export of mRNA from the nucleus. It inhibits RNA binding activity through an intramolecular interaction with the N- terminal RNA binding domain (RBD); the inhibition is removed by an association with the TREX complex, specifically involving ALYREF/THOC4 and THOC5. {ECO:0000269|PubMed:11583626}.

Domain: The TAP-C domain mediates direct interactions with nucleoporin- FG-repeats and is necessary and sufficient for localization of NXF1 to the nuclear rim. The conserved loop 594-NWD-596 of the TAP-C domain has a critical role in the interaction with nucleoporins. {ECO:0000269|PubMed:11583626}.

Domain: The leucine-rich repeats are essential for the export of mRNA from the nucleus. {ECO:0000269|PubMed:11583626}.

Domain: The RNA-binding domain is a non-canonical RNP-type domain. {ECO:0000269|PubMed:11583626}.

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

Annotations taken from UniProtKB at the EBI.


Organism:		Homo sapiens (Human).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.



Function:		Involved in the nuclear export of mRNA species bearing retroviral constitutive transport elements (CTE) and in the export of mRNA from the nucleus to the cytoplasm (TAP/NFX1 pathway) (PubMed:10924507). The NXF1-NXT1 heterodimer is involved in the export of HSP70 mRNA in conjunction with ALYREF/THOC4 and THOC5 components of the TREX complex (PubMed:18364396, PubMed:19165146, PubMed:9660949). ALYREF/THOC4-bound mRNA is thought to be transferred to the NXF1-NXT1 heterodimer for export (PubMed:18364396, PubMed:19165146, PubMed:9660949). Also involved in nuclear export of m6A-containing mRNAs: interaction between SRSF3 and YTHDC1 facilitates m6A-containing mRNA-binding to both SRSF3 and NXF1, promoting mRNA nuclear export (PubMed:28984244). {ECO:0000269\|PubMed:10924507, ECO:0000269\|PubMed:18364396, ECO:0000269\|PubMed:19165146, ECO:0000269\|PubMed:28984244, ECO:0000269\|PubMed:9660949}.


Subunit:		Heterodimer (via NTF2 domain) with NXT1 (PubMed:11583626). The formation of NXF1-NXT1 heterodimers is required for the NXF1-mediated nuclear mRNA export (PubMed:11583626). Forms a complex with RANBP2/NUP358, NXT1 and RANGAP1 (PubMed:14729961). Associates with the exon junction complex (EJC) and with the transcription/export (TREX) complex (PubMed:11707413, PubMed:22893130). Found in a mRNA complex with UPF3A and UPF3B (PubMed:11546873). Found in a post-splicing complex with RBM8A, UPF1, UPF2, UPF3A, UPF3B and RNPS1 (PubMed:11546874). Interacts (via N-terminus) with DHX9 (via N- terminus); this interaction is direct and negatively regulates NXF1- mediated nuclear export of constitutive transport element (CTE)- containing cellular mRNAs (PubMed:10924507). Interacts with ALYREF/THOC4 (PubMed:11707413, PubMed:14730019, PubMed:19165146, PubMed:23299939). Interacts with FYTTD1/UIF (PubMed:19836239). Interacts with EIF4A3 (PubMed:14730019). Interacts with NUP42 (PubMed:10228171). Interacts with THOC5 (PubMed:19165146, PubMed:23299939). Interacts with CHTOP (PubMed:23299939, PubMed:23826332). Interacts with FRG1 (via N-terminus) (PubMed:21699900). Interacts with LUZP4 (PubMed:25662211). Interacts with FMR1; the interaction occurs in a mRNA-dependent and polyribosomes-independent manner in the nucleus (PubMed:18936162). Interacts with CPSF6 (via N-terminus); this interaction is direct (PubMed:19864460). Interacts with RBM15 (PubMed:17001072). Interacts with RBM15B (PubMed:19586903). Interacts with MCM3AP isoform GANP; this interaction is not mediated by RNA (PubMed:20005110). Interacts with DDX3X (via C-terminus); this interaction may be partly involved in DDX3X nuclear export and in NXF1 localization to stress granules (PubMed:18596238). Interacts with PABPC1/PABP1 (PubMed:18596238). {ECO:0000269\|PubMed:10228171, ECO:0000269\|PubMed:10924507, ECO:0000269\|PubMed:11546873, ECO:0000269\|PubMed:11546874, ECO:0000269\|PubMed:11583626, ECO:0000269\|PubMed:11707413, ECO:0000269\|PubMed:12581645, ECO:0000269\|PubMed:14729961, ECO:0000269\|PubMed:14730019, ECO:0000269\|PubMed:17001072, ECO:0000269\|PubMed:18596238, ECO:0000269\|PubMed:18936162, ECO:0000269\|PubMed:19165146, ECO:0000269\|PubMed:19369354, ECO:0000269\|PubMed:19586903, ECO:0000269\|PubMed:19836239, ECO:0000269\|PubMed:19864460, ECO:0000269\|PubMed:20005110, ECO:0000269\|PubMed:21699900, ECO:0000269\|PubMed:22893130, ECO:0000269\|PubMed:23299939, ECO:0000269\|PubMed:23826332, ECO:0000269\|PubMed:25662211, ECO:0000269\|PubMed:9175835}.
Subunit:		(Microbial infection) Interacts with Saimiriine herpesvirus 2 TIP protein. {ECO:0000269\|PubMed:9175835}.
Subunit:		(Microbial infection) Interacts with human herpes virus 1 (HHV-1) ICP27 protein; this interaction allows efficient export of HHV- 1 early and late transcripts. {ECO:0000269\|PubMed:19369354}.
Subunit:		(Microbial infection) Interacts (via RNA-binding domain) with Ebolavirus nucleoprotein; this interaction recruits NXF1 to the inclusion bodies were viral replication takes place, probably to export viral mRNA-NXF1 complexes from these sites. {ECO:0000269\|PubMed:31940815}.
Subcellular location:		Nucleus {ECO:0000269\|PubMed:10924507, ECO:0000269\|PubMed:18596238, ECO:0000269\|PubMed:19864460, ECO:0000269\|PubMed:23591820, ECO:0000269\|PubMed:25662211}. Nucleus, nucleoplasm {ECO:0000269\|PubMed:19324961, ECO:0000269\|PubMed:23826332}. Nucleus speckle {ECO:0000269\|PubMed:19324961, ECO:0000269\|PubMed:23826332}. Nucleus, nuclear pore complex {ECO:0000269\|PubMed:23591820}. Nucleus envelope {ECO:0000269\|PubMed:18596238, ECO:0000269\|PubMed:23591820}. Cytoplasm {ECO:0000269\|PubMed:10924507, ECO:0000269\|PubMed:18596238, ECO:0000269\|PubMed:19324961, ECO:0000269\|PubMed:19864460}. Cytoplasm, Stress granule {ECO:0000269\|PubMed:18596238}. Note=Localized predominantly in the nucleoplasm and at both the nucleoplasmic and cytoplasmic faces of the nuclear pore complex. Shuttles between the nucleus and the cytoplasm. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. The association with the TREX complex seems to occur in regions surrounding nuclear speckles known as perispeckles (PubMed:23826332). Nucleus; nuclear rim (PubMed:25662211). {ECO:0000269\|PubMed:23826332, ECO:0000269\|PubMed:25662211}.
Tissue specificity:		Expressed ubiquitously.
Domain:		The minimal CTE binding domain consists of an RNP-type RNA binding domain (RBD) and leucine-rich repeats. {ECO:0000269\|PubMed:11583626}.
Domain:		The nucleoporin binding domain consists of a NTF2 domain (also called NTF2-like domain) and a TAP-C domain (also called UBA-like domain). It has 2 nucleoporin-FG-repeats binding sites (one in the NTF2 and the other in the TAP-C domain) which contribute to nucleoporin association and act synergistically to export cellular mRNAs. {ECO:0000269\|PubMed:11583626}.
Domain:		The NTF2 domain is functional only in the presence of NXT1 and is essential for the export of mRNA from the nucleus. It inhibits RNA binding activity through an intramolecular interaction with the N- terminal RNA binding domain (RBD); the inhibition is removed by an association with the TREX complex, specifically involving ALYREF/THOC4 and THOC5. {ECO:0000269\|PubMed:11583626}.
Domain:		The TAP-C domain mediates direct interactions with nucleoporin- FG-repeats and is necessary and sufficient for localization of NXF1 to the nuclear rim. The conserved loop 594-NWD-596 of the TAP-C domain has a critical role in the interaction with nucleoporins. {ECO:0000269\|PubMed:11583626}.
Domain:		The leucine-rich repeats are essential for the export of mRNA from the nucleus. {ECO:0000269\|PubMed:11583626}.
Domain:		The RNA-binding domain is a non-canonical RNP-type domain. {ECO:0000269\|PubMed:11583626}.
Similarity:		Belongs to the NXF family. {ECO:0000305}.