Constists of 14 exons.

The coding region of the gene starts from exon 1 to exon 14 (60^th bps to 2249^th bps). The length of the transcript is 2190 bps.

No known pseudogenes.

RanBPM was originally identified as a centrosomal 55 kDa protein and is involved in microtubule nucleation at the centrosome (Nakamura et al., 1998). A later work by the same group revealed that the full-length RanBPM encodes for 729 amino acids and its molecular weight is 90 kDa (Nishitani et al., 2001).
RanBPM protein contains multiple conserved domains which provide potential protein-protein interaction sites such as an N-terminus proline rich domain (PRD), a splA and Ryr (SPRY) domain (212-333 aa), a lissencephaly type-I-like homology (LisH) motif (365-397 aa), a carboxy terminal to LisH (CTLH) motif (403-460 aa), and a CT11-RanBPM (CRA) motif (615-717 aa) at the C terminus of RanBPM (Murrin and Talbot, 2007). These domains play a significant role in interaction of RanBPM with a wide range of transmembrane and intracellular proteins.

RanBPM is ubiquitously expressed in human and murine cell lines and tissues of kidney, uterus, ovary, bladder, spleen, thymus, brain, skeletal muscle, lung, prostate, testes, small intestine, colon and peripheral blood lymphocytes (Rao et al., 2002; Wang et al., 2002). In contrast, reduced expression was observed in cancer cells and in several human tumor tissues.

RanBPM is localized in the nucleus, cytoplasm, plasma membrane and cell juctions (Nishitani et al., 2001; Umeda et al., 2003; Denti et al., 2004; Chang et al., 2010).

The direct binding of RanBPM with p73α, results in the nuclear translocation of cytoplasmic RanBPM. RanBPM is involved in the stabilization of p73 protein by preventing its degradation through the ubiquitin-proteasomal pathway and increases its proapoptotic function (Kramer et al., 2005). Expression of RanBPM augments T-type Ca2+ currents in HEK293/Cav3.1 cells (Kim et al., 2009). RanBPM was found to abolish the inhibitory effect of PKC on Cav3.1 currents, suggesting a key role of RanBPM in Cav3.1 channel-mediated signaling pathways. RanBPM interacts with brain-specific protein p42IP4, and modulates the p42IP4 function to regulate synaptic plasticity, actin cytoskeleton remodeling and mitogen-activated protein kinase cascade (Haase et al., 2008).
RanBPM also exhibits negative regulation. It binds with Mu opioid receptor (MOP), and inhibits the agonist-induced receptor internalization without altering MOP signaling through adenylyl cyclase, suggesting the regulatory effect of RanBPM on MOP activity in mammalian cells (Talbot et al., 2009). CD39, a prototypic member of the NTPDase family, forms a complex with RanBPM (Wu et al., 2006). This association substantially down-regulates the NTPDase activity of CD39.
RanBPM also acts as a ligand for the Rho-GEF domain (Bowman et al., 2008). RanBPM along with Rho-GEF domain of obscurin regulates the assembly of titin during the formation of the Z-disk and A/I junction, showing a vital role of RanBPM in myofibrillogenesis.
RanBPM stimulates the transcriptional activity of different proteins. RanBPM interacts with androgen receptor (AR) (Rao et al., 2002). AR belongs to a large steroid receptor family which also includes glucocorticoid (GR), progesterone, and mineralocorticoid receptors. RanBPM was found to enhance AR transactivation in a ligand-dependent fashion. Similar results were observed with GR activity, whereas the estrogen receptor activity remains unaffected. Furthermore, RanBPM was found to enhance the activity of thyroid hormone receptors (TRs), a member of nuclear receptor superfamily in a ligand-independent manner (Poirier et al., 2006), which confirms the selective action of RanBPM on receptors activity.
Expression of RanBPM influences the activity of Rta, which activates the transcription of Epstein-Barr virus (EBV) lytic genes and the lytic cycle, indicating a new role of RanBPM as a viral protein regulator. Sumoylation of Rta enhances its activity to complete the EBV lytic development in an efficient way (Chang et al., 2008). RanBPM promotes Rta sumoylation by interacting with Ubc9, which states the participation of RanBPM in EBV lytic activation.
RanBPM interacts with several proteins which are involved in neurological function. By interacting with PlexinA receptor, RanBPM mediates Semaphorin 3A signaling which is involved in axonal growth (Togashi et al., 2006). It also interacts with calbindin D28K (Lutz et al., 2003) and TAF4 to regulate neuritogenesis in neural stem cells (Brunkhorst et al., 2005). Expression of RanBPM in primary neurons decreased L1-dependent neurite outgrowth and extension (Cheng et al., 2005). RanBPM showed high expression in the Kenyon cells of the larval mushroom body (MB), and its expression is sufficient to rescue all behavioral phenotypes (Scantlebury et al., 2010). By performing genetic epistasis experiments, authors observed the participation of RanBPM with the FMRP (Fragile X Mental Retardation Protein) in the development of neuromuscular junction. Citron kinase (CITK) plays an important role in neurogenic mitoses. RanBPM potentially interacts with CITK and plays a novel role in the progression of neocortical precursors through M-phase at the ventricular surface (Chang et al., 2010).

Human RanBPM shows 90% nucleotide homology with mouse RanBPM.