Ran-binding protein 10 (RANBP10)
The protein contains 620 amino acids for an estimated molecular weight of 67257 Da.
May act as an adapter protein to couple membrane receptors to intracellular signaling pathways (Probable). Core component of the CTLH E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin from UBE2H and mediates ubiquitination and subsequent proteasomal degradation of the transcription factor HBP1 (PubMed:29911972). Enhances dihydrotestosterone-induced transactivation activity of AR, as well as dexamethasone-induced transactivation activity of NR3C1, but does not affect estrogen-induced transactivation (PubMed:18222118). Acts as a guanine nucleotide exchange factor (GEF) for RAN GTPase. May play an essential role in hemostasis and in maintaining microtubule dynamics with respect to both platelet shape and function (By similarity). (updated: Sept. 12, 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.
- 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.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- 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.
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The reference OMIM entry for this protein is 614031
Ran-binding protein 10; ranbp10
Kiaa1464
CLONING
By sequencing clones obtained from a size-fractionated fetal brain cDNA library, Nagase et al. (2000) cloned RANBP10, which they designated KIAA1464. The deduced 621-amino acid protein shares significant similarity with RANBPM (RANBP9; 603854). RT-PCR ELISA detected low RANBP10 expression in all adult and fetal tissues and specific adult brain regions examined. By searching databases for sequences similar to RANBP9, followed by PCR and RACE, Wang et al. (2004) cloned human RANBP10. The deduced 620-amino acid protein has a calculated molecular mass of 67 kD. RANBP10 contains a SPRY domain in its N-terminal half, but it lacks the proline- and glutamine-rich region present in RANBP9. RANBP10 shares 68% amino acid identity with RANBP9 and 95% identity with mouse Ranbp10. Northern blot analysis detected a 5.3-kb RANBP10 transcript in several human tissues, with highest expression in skeletal muscle. EST database analysis revealed widespread RANBP10 expression. Schulze et al. (2008) determined that mouse Ranbp10 contains a consensus guanine nucleotide exchange factor (GEF) domain that is most similar to the GEF domain of Sos2 (601247). Northern blot analysis detected Ranbp10 expression in adult mouse liver, spleen, and bone marrow, with lower levels in other tissues examined. In fetal liver cultures, Ranbp10 was highly expressed in mature megakaryocytes. Immunofluorescence analysis showed that Ranbp10 localized to cytoplasmic microtubules in megakaryocytes and platelets.GENE FUNCTION
Using protein pull-down and coimmunoprecipitation analyses, Wang et al. (2004) showed that, like RANBP9, RANBP10 interacted directly with RAN (601179), a small nuclear GTPase, and MET (164860), a receptor protein tyrosine kinase for hepatocyte growth factor (HGF; 142409). Pull-down experiments revealed that RANBP9 and RANBP10 competed for MET binding. RANBP9, but not RANBP10, induced ERK (MAPK3; 601795) phosphorylation and expression from a serum response element (SRE) reporter gene. RANBP10 inhibited RANBP9-mediated reporter gene activation. Megakaryocytes are large polyploid cells that conclude their maturation by assembling nascent blood platelets within a complex reticular network of microtubules. Using a yeast 2-hybrid assay, Schulze et al. (2008) showed that mouse Ranbp10 bound beta-tubulins, including the platelet- and megakaryocyte-specific beta-1 tubulin (TUBB1; 612901). The N-terminal domain of Ranbp10 showed Ran-specific GEF activity. Depletion of endogenous Ranbp10 from megakaryocytes via small interfering RNA disrupted the reticular array of microtubule filaments, resulting in scattered tubulin filaments, short fragments, and punctate foci. Knockdown of Ranbp10 had no effect on intranuclear Ran localization. Schulze et al. (2008) concluded that Ranbp10 regulates the microtubule network of megakaryocytes and coordinates platelet assembly and release. Kunert et al. (2009) found that overexpression of Ranbp10 in mouse megakaryocytes resulted in exceptionally thick microtubules and increased cytoplasmic Ran localization, likely due to elevated Ran-specific GEF activity and accumulation of cytoplasmic Ran-GTP. Harada et al. (2008) showed that both RANBP9 and RANBP10 enhanced dihydrotestosterone (DHT)-induced transactivation activity of androgen receptor (AR; 313700). Simultaneous overexpression of RANBP10 and RANBP9 had an additive effect on AR transactivation. Both RANBP10 and RANBP9 enhanced glucocorticoid receptor (GCCR; ... More on the omim web site
Oct. 2, 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 614031 was added.