Ran-specific GTPase-activating protein (RANBP1)
The protein contains 201 amino acids for an estimated molecular weight of 23310 Da.
Plays a role in RAN-dependent nucleocytoplasmic transport. Alleviates the TNPO1-dependent inhibition of RAN GTPase activity and mediates the dissociation of RAN from proteins involved in transport into the nucleus (By similarity). Induces a conformation change in the complex formed by XPO1 and RAN that triggers the release of the nuclear export signal of cargo proteins (PubMed:20485264). Promotes the disassembly of the complex formed by RAN and importin beta. Promotes dissociation of RAN from a complex with KPNA2 and CSE1L (By similarity). Required for normal mitotic spindle assembly and normal progress through mitosis via its effect on RAN (PubMed:17671426). Does not increase the RAN GTPase activity by itself, but increases GTP hydrolysis mediated by RANGAP1 (PubMed:7882974). Inhibits RCC1-dependent exchange of RAN-bound GDP by GTP (PubMed:7882974, PubMed:7616957). (updated: March 28, 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.
- Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.
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.
(right-click above to access to more options from the contextual menu)
| Variant | Description |
|---|---|
| a breast cancer sample; somatic mutation | |
| dbSNP:rs5746863 |
Biological Process
G1/S transition of mitotic cell cycle
Intracellular transport
Positive regulation of GTPase activity
Positive regulation of mitotic centrosome separation
Protein import into nucleus
Regulation of catalytic activity
RNA export from nucleus
Signal transduction
Spindle organization
Ubiquitin-dependent protein catabolic process
Viral process
The reference OMIM entry for this protein is 601180
Ran-binding protein 1; ranbp1
Hpaii tiny fragments locus 9a; htf9a
CLONING
Coutavas et al. (1993) isolated a Ran/TC4-binding protein, RanBP1, that interacts specifically with GTP-charged RAN (601179). The authors cloned the mouse RanBP1 cDNA by screening an expression library containing cDNAs from 16-day mouse embryos. Bischoff et al. (1995) identified a 23-kD protein, RANBP1, that binds to RAN complexed with GTP but not GDP. Based on partial peptide sequence of the purified protein, primers were designed to amplify a cDNA encoding the protein. They also showed that RANBP1 does not activate GTPase activity of RAN but does markedly increase GTP hydrolysis by the RanGTPase-activating protein (RanGAP1). Hayashi et al. (1995) isolated human RANBP1 using the 2-hybrid method with either RAN or RCC1 (179710) as targets. The RANBP1 cDNA encodes a 201-amino acid protein that is 92% identical to its mouse homolog. Hayashi et al. (1995) showed that, in both mammalian cells and in yeast, RANBP1 acts as a negative regulator of RCC1 by inhibiting RCC1-stimulated guanine nucleotide release from RAN. See also 601181.BIOCHEMICAL FEATURES
- Crystal Structure Seewald et al. (2002) presented the 3-dimensional structure of a Ran-RanBP1-RanGAP ternary complex in the ground state and in a transition-state mimic. The structure and biochemical experiments showed that RanGAP does not act through an arginine finger, that the basic machinery for fast GTP hydrolysis is provided exclusively by Ran, and that correct positioning of the catalytic glutamine is essential for catalysis.GENE FUNCTION
Guarguaglini et al. (1997) found that mouse Htf9c (611151) and Ranbp1 were divergently transcribed from a bidirectional promoter. Expression of both genes was activated upon entry into the cell cycle, peaked in S phase, and was downregulated during completion of the cell cycle. The bidirectional promoter was downregulated in both orientations in arrested cells. Activation of the promoter was specific, resulting in more restricted Htf9c expression and a sharper peak of Htf9c expression in S phase compared with Ranbp1 expression. A region containing an E2f (189971) site was important for cell cycle control of Htf9c, and a common region containing sites for Sp1 (189906) and E2f contributed to activation in both orientations. ... More on the omim web site
April 12, 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
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 601180 was added.