Nuclear transport factor 2 (NUTF2)
The protein contains 127 amino acids for an estimated molecular weight of 14478 Da.
Mediates the import of GDP-bound RAN from the cytoplasm into the nucleus which is essential for the function of RAN in cargo receptor-mediated nucleocytoplasmic transport. Thereby, plays indirectly a more general role in cargo receptor-mediated nucleocytoplasmic transport. Interacts with GDP-bound RAN in the cytosol, recruits it to the nuclear pore complex via its interaction with nucleoporins and promotes its nuclear import. (updated: Jan. 31, 2018)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
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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Biological Process
MRNA transport
Negative regulation of vascular endothelial growth factor production
Nucleocytoplasmic transport
Obsolete protein import into nucleus, translocation
Positive regulation of protein import into nucleus
Protein export from nucleus
Protein import into nucleus
Protein localization to nuclear pore
The reference OMIM entry for this protein is 605813
Nuclear transport factor 2
Ntf2
Placental protein 15; pp15
DESCRIPTION
Molecular trafficking between the cytoplasm and nucleus occurs through proteinaceous structures called nuclear pore complexes, which span the double membrane of the nuclear envelope and permit both passive diffusion and active transport. Proteins destined for import typically contain a nuclear localization signal (NLS), which is rich in basic residues, and interact with an NLS receptor (e.g., KPNA2; 600685) before docking to the nuclear envelope and interacting with a nucleoporin (e.g., NUP62; 605815).CLONING
By screening a placenta cDNA library for placental protein-15 (PP15), an inhibitory molecule in the lymphocyte transformation test, Grundmann et al. (1988) isolated a cDNA encoding PP15. The deduced 127-amino acid protein contains a putative ribosome-binding site. Using biochemical purification methods and micropeptide sequencing, followed by PCR, Paschal and Gerace (1995) determined that NTF2 is encoded by the PP15 cDNA.GENE FUNCTION
By functional analysis in NUP62-depleted cells, Paschal and Gerace (1995) showed that NTF2 is required for nuclear protein import after the association of the NLS ligand with the nuclear envelope. Reconstituting permeabilized cells with NTF2 and RANBP1 (601180), as well as with a 'docking fraction' that probably contained an NLS receptor, showed that these elements all perform distinct and necessary functions for nuclear protein import. Paschal and Gerace (1995) concluded that NTF2 interacts with NUP62 and acts after the docking step in the nuclear protein import pathway. Using an in vitro nuclear import system, Ribbeck et al. (1998) found evidence that NTF2 is required for the nuclear import and reaccumulation of RAN (601179), a molecule that is depleted from the nucleus as RAN-GTP complexed with exported cargo. By mutation analysis and biochemical studies, they determined that nuclear reaccumulation of RAN is mediated by direct interaction between the 2 proteins and that RAN-GDP is the species bound and transported by NTF2. ... More on the omim web site
Feb. 10, 2018: Protein entry updated
Automatic update: Entry updated from uniprot information.
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 605813 was added.
Jan. 28, 2016: Protein entry updated
Automatic update: model status changed
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed