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    RAN

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    Anti-RAN Recombinant Antibody Products

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    For Research Use Only. Not For Clinical Use.


    RAN (ras-related nuclear protein) is a small GTP binding protein belonging to the RAS superfamily that is essential for the translocation of RNA and proteins through the nuclear pore complex. The RAN protein is also involved in control of DNA synthesis and cell cycle progression. Nuclear localization of RAN requires the presence of regulator of chromosome condensation 1 (RCC1). Mutations in RAN disrupt DNA synthesis. Because of its many functions, it is likely that RAN interacts with several other proteins. RAN regulates formation and organization of the microtubule network independently of its role in the nucleus-cytosol exchange of macromolecules. RAN could be a key signaling molecule regulating microtubule polymerization during mitosis. RCC1 generates a high local concentration of RAN-GTP around chromatin which, in turn, induces the local nucleation of microtubules. RAN is an androgen receptor (AR) coactivator that binds differentially with different lengths of polyglutamine within the androgen receptor. Polyglutamine repeat expansion in the AR is linked to Kennedy's disease (X-linked spinal and bulbar muscular atrophy). RAN coactivation of the AR diminishes with polyglutamine expansion within the AR, and this weak coactivation may lead to partial androgen insensitivity during the development of Kennedy's disease.
    Protein class

    Plasma proteins, Transporters

    Predicted location

    Intracellular

    Single cell type specificity

    Low cell type specificity

    Immune cell specificity

    Low immune cell specificity

    Cell line specificity

    Low cell line specificity

    Interaction

    Monomer. Interacts with RANGAP1, which promotes RAN-mediated GTP hydrolysis (PubMed:7819259, PubMed:9428644). Interacts with KPNB1 (PubMed:8896452, PubMed:9428644, PubMed:10367892). Interaction with KPNB1 inhibits RANGAP1-mediated stimulation of GTPase activity (PubMed:9428644). Interacts with RCC1 which promotes the exchange of RAN-bound GDP by GTP (PubMed:1961752, PubMed:7819259, PubMed:12194828, PubMed:11336674). Interaction with KPNB1 inhibits RCC1-mediated exchange of RAN-bound GDP by GTP (PubMed:8896452). Interacts (GTP-bound form) with TNPO1; the interaction is direct (PubMed:9351834). Interacts (GTP-bound form) with TNPO3; the interaction is direct (PubMed:23878195, PubMed:24915079, PubMed:24449914). Interacts with KPNB1 and with TNPO1; both inhibit RAN GTPase activity (PubMed:8896452, PubMed:9428644). Interacts (via C-terminus) with RANBP1, which alleviates the inhibition of RAN GTPase activity (PubMed:7891706, PubMed:8896452, PubMed:9428644, PubMed:11832950). Interacts with RANGRF, which promotes the release of bound guanine nucleotide (PubMed:29040603). RANGRF and RCC1 compete for an overlapping binding site on RAN (PubMed:29040603). Identified in a complex with KPNA2 and CSE1L; interaction with RANBP1 mediates dissociation of RAN from this complex (PubMed:9428644). Interaction with both RANBP1 and KPNA2 promotes dissociation of the complex between RAN and KPNB1 (PubMed:9428644). Identified in a complex composed of RAN, RANGAP1 and RANBP1 (PubMed:16428860). Identified in a complex that contains TNPO1, RAN and RANBP1 (PubMed:9428644). Identified in a nuclear export complex with XPO1 (PubMed:9323133, PubMed:15574331, PubMed:10209022). Found in a nuclear export complex with RANBP3 and XPO1 (PubMed:11571268, PubMed:11425870). Interacts with RANBP2/NUP358 (PubMed:10078529, PubMed:26272610). Interaction with RANBP1 or RANBP2 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). Component of a nuclear export receptor complex composed of KPNB1, RAN, SNUPN and XPO1 (PubMed:10209022, PubMed:19389996). Found in a nuclear export complex with RAN, XPO5 and pre-miRNA (By similarity). Interacts (GTP-bound form) with XPO5 (By similarity). Part of a complex consisting of RANBP9, RAN, DYRK1B and COPS5 (PubMed:14500717). Interacts with RANBP9 and RANBP10 (PubMed:14684163). Interacts in its GTP-bound form with BIRC5/survivin at S and M phases of the cell cycle (PubMed:18591255). Interacts with TERT; the interaction requires hydrogen peroxide-mediated phosphorylation of TERT and transports TERT to the nucleus (PubMed:12808100). Interacts with MAD2L2 (PubMed:19753112). Interacts with VRK1 and VRK3 (PubMed:18617507). Interacts with isoform 1 and isoform 2 of VRK2 (PubMed:18617507). Interacts with NEMP1 and KPNB1 (By similarity). Interacts (GDP-bound form) with NUTF2; regulates RAN nuclear import (PubMed:9822603, PubMed:10679025, PubMed:18266911). Interacts with CAPG; mediates CAPG nuclear import (PubMed:10679025, PubMed:18266911). Interacts with NUP153 (PubMed:18611384, PubMed:19505478). Interacts with the AR N-terminal poly-Gln region; the interaction with AR is inversely correlated with the poly-Gln length (PubMed:10400640). Interacts with MYCBP2, which promotes RAN-mediated GTP hydrolysis (PubMed:26304119). Interacts with EPG5 (PubMed:29130391). (Microbial infection) In case of HIV-1 infection, found in a complex with HIV-1 Rev, RNAs containing a Rev response element (RRE) and XPO1. (Microbial infection) Found in a complex with HTLV-1 Rex, RANBP3 and XPO1. (Microbial infection) Interacts with Mengo encephalomyocarditis virus Leader protein; the complex L-RAN recruits cellular kinases responsible for the L-induced nucleocytoplasmic trafficking inhibition.

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