Alternative titles; symbols
HGNC Approved Gene Symbol: RANBP1
Cytogenetic location: 22q11.21 Genomic coordinates (GRCh38) : 22:20,116,104-20,127,355 (from NCBI)
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.
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.
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.
Bischoff, F. R., Krebber, H., Smirnova, E., Dong, W., Ponstingl, H. Co-activation of RanGTPase and inhibition of GTP dissociation by Ran-GTP binding protein RanBP1. EMBO J. 14: 705-715, 1995. [PubMed: 7882974] [Full Text: https://doi.org/10.1002/j.1460-2075.1995.tb07049.x]
Coutavas, E., Ren, M., Oppenheim, J. D., D'Eustachio, P., Rush, M. G. Characterization of proteins that interact with the cell-cycle regulatory protein Ran/TC4. Nature 366: 585-587, 1993. [PubMed: 8255297] [Full Text: https://doi.org/10.1038/366585a0]
Guarguaglini, G., Battistoni, A., Pittoggi, C., Di Matteo, G., Di Fiore, B., Lavia, P. Expression of the murine RanBP1 and Htf9-c genes is regulated from a shared bidirectional promoter during cell cycle progression. Biochem. J. 325: 277-286, 1997. [PubMed: 9224656] [Full Text: https://doi.org/10.1042/bj3250277]
Hayashi, N., Yokoyama, N., Seki, T., Azuma, Y., Ohba, T., Nishimoto, T. RanBP1, a Ras-like nuclear G protein binding to Ran/TC4, inhibits RCC1 via Ran/TC4. Molec. Gen. Genet. 247: 661-669, 1995. [PubMed: 7616957] [Full Text: https://doi.org/10.1007/BF00290397]
Seewald, M. J., Korner, C., Wittinghofer, A., Vetter, I. R. RanGAP mediates GTP hydrolysis without an arginine finger. Nature 415: 662-666, 2002. [PubMed: 11832950] [Full Text: https://doi.org/10.1038/415662a]