Nuclear pore complex protein Nup98-Nup96 (NUP98)
The protein contains 1817 amino acids for an estimated molecular weight of 197579 Da.
Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. NUP98 and NUP96 are involved in the bidirectional transport across the NPC. May anchor NUP153 and TPR to the NPC. In cooperation with DHX9, plays a role in transcription and alternative splicing activation of a subset of genes (PubMed:28221134). Involved in the localization of DHX9 in discrete intranuclear foci (GLFG-body) (PubMed:28221134).', '(Microbial infection) Binds HIV-1 capsid-nucleocapsid (HIV-1 CA-NC) complexes and may thereby promote the integration of the virus in the host nucleus (in vitro) (PubMed:23523133). Binding affinity to HIV-1 CA-NC complexes bearing the capsid change ASN-74-ASP is reduced (in vitro) (PubMed:23523133). (updated: June 17, 2020)
Protein identification was indicated in the following studies:
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
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| Variant | Description |
|---|---|
| a breast cancer sample; somatic mutation |
Biological Process
Intracellular transport of virus
Mitotic nuclear membrane reassembly
Mitotic spindle organization
MRNA export from nucleus
Nuclear pore complex assembly
Nuclear pore organization
Nucleocytoplasmic transport
Positive regulation of mRNA splicing, via spliceosome
Posttranscriptional tethering of RNA polymerase II gene DNA at nuclear periphery
Protein import into nucleus
Protein sumoylation
Regulation of cellular response to heat
Regulation of gene silencing by miRNA
Regulation of glycolytic process
RNA export from nucleus
Telomere tethering at nuclear periphery
TRNA export from nucleus
Viral life cycle
Viral process
Viral transcription
Cellular Component
Cytosol
Host cell
Intracellular membrane-bounded organelle
Nuclear body
Nuclear envelope
Nuclear inclusion body
Nuclear membrane
Nuclear periphery
Nuclear pore
Nuclear pore cytoplasmic filaments
Nuclear pore nuclear basket
Nuclear pore outer ring
Nucleoplasm
Ribonucleoprotein complex
The reference OMIM entry for this protein is 601021
Nucleoporin, 98-kd; nup98 nup98-nup96 precursor protein, included
Nucleoporin, 96-kd, included; nup96, included
Nup98/nsd1 fusion gene, included
Nup98/nsd3 fusion gene, included
Nup98/pmx1 fusion gene, included
Nup98/hoxa9 fusion gene, incl
DESCRIPTION
In eukaryotic cells, the nucleus is spatially and functionally separated from the cytoplasm by the nuclear envelope. All molecular transport across the nuclear envelope takes place exclusively through the nuclear pore. Small molecules, such as ions and polypeptides smaller than approximately 40 kD, pass freely through the nuclear pore, but larger molecules require a carrier protein. The nuclear pore is formed by the nuclear pore complex (NPC), an 8-fold symmetrical structure composed of multiple copies of about 30 different proteins called nucleoporins. The NUP98 gene encodes a NUP98-NUP96 precursor protein that is cleaved by its own peptidase activity to produce 2 distinct nucleoporins, NUP98 and NUP96. Alternative splicing also generates NUP98 transcripts that encode NUP98, but not NUP96. NUP98 is a peripheral nucleoporin located at both the cytoplasmic and nuclear sides of the central channel of the NPC. It contains a characteristic gly-leu-phe-gly (GFLG) repeat region that contributes to nuclear-cytoplasmic trafficking, including mRNA export. NUP98 also plays roles in gene expression, mitotic checkpoint, and pathogenesis. NUP96 is a scaffold component of the NPC (review by Iwamoto et al., 2010).CLONING
Fontoura et al. (1999) identified NUP96 as a nucleoporin with a predicted molecular mass of 96 kD. NUP96 is generated through an unusual biogenesis pathway that involves synthesis of a 186-kD precursor protein. Proteolytic cleavage of the precursor yields 2 nucleoporins: NUP98 and NUP96. NUP96 is proteolytically cleaved in vivo. NUP96 is localized to the nucleoplasmic side of the NPC at or near the nucleoplasmic basket. The correct targeting of both NUP96 and NUP98 to the nucleoplasmic side of the NPC was found to be dependent on proteolytic cleavage, suggesting that the cleavage process may regulate NPC assembly. In their review, Iwamoto et al. (2010) noted that alternative splicing produces 4 human NUP98 variants. Variants 1 and 4 are generated by alternative splicing in exon 20 and are translated into the NUP98-NUP96 precursor protein. Variants 2 and 3 are generated without splicing in exon 20 and are translated into NUP98 connected to a 57-amino acid polypeptide tail that is removed from NUP98 by autocleavage. Variants 1 and 4 differ from one another due to alternative splicing in exon 29, and variants 2 and 3 differ from one another due to alternative splicing in exon 10.MAPPING
Nakamura et al. (1996) mapped the NUP98 gene to 11p15 by analysis of a panel of somatic cell hybrids and by pulsed field gel electrophoresis.GENE FUNCTION
By immunogold electron microscopy, Radu et al. (1995) localized the NUP98 protein to the nucleoplasmic side of the nuclear pore. Nakamura et al. (1996) stated that ligand blot analysis suggested that NUP98 functions as a docking protein for cytosol-mediated docking of import substrates. The docking function has been localized to the N-terminal half of NUP98, the part of NUP98 that is retained in the NUP98/HOXA9 fusion (Radu et al., 1995). Rosenblum and Blobel (1999) determined that no protease is involved in the processing of the NUP98-NUP96 precursor, but the molecule specifically cleaves itself between phe863 and ser864. The 2 fragments then form a low-affinity complex. Von Kobbe et al. (2000) demonstrated that NUP98 is a target of the vesicular stomatitis virus M protein-mediated inhibition of mRNA nuclear export. Enninga et al. (2002) demons ... More on the omim web site
June 30, 2020: Protein entry updated
Automatic update: OMIM entry 601021 was added.
June 29, 2020: Protein entry updated
Automatic update: Entry updated from uniprot information.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).