RANBP2

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RAN binding protein 2
Protein RANBP2 PDB 1rrp.png
PDB rendering based on 1rrp.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols RANBP2 ; ANE1; IIAE3; NUP358; TRP1; TRP2
External IDs OMIM601181 MGI894323 HomoloGene68510 GeneCards: RANBP2 Gene
EC number 5.2.1.8
RNA expression pattern
PBB GE RANBP2 201713 s at tn.png
PBB GE RANBP2 201711 x at tn.png
PBB GE RANBP2 201712 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 5903 19386
Ensembl ENSG00000153201 ENSMUSG00000003226
UniProt P49792 Q9ERU9
RefSeq (mRNA) NM_006267 NM_011240
RefSeq (protein) NP_006258 NP_035370
Location (UCSC) Chr 2:
109.34 – 109.4 Mb
Chr 10:
58.45 – 58.49 Mb
PubMed search [1] [2]

RAN binding protein 2, also known as RANBP2 is protein which in humans is encoded by the RANBP2 gene.[1]

RanBP2 is also known as Nup358 since it is a member nucleoporin family that makes-up the nuclear pore complex. RanBP2 has a 358 KDa molecular weight.

Function[edit]

RAN is a small GTP-binding protein of the RAS superfamily. Ran GTPase is a master regulatory switch, which among other functions, controls the shuttling of proteins between the nuclear and cytoplasm compartments of the cell. Ran GTPase controls a variety of cellular functions through its interactions with other proteins. The RanBP2 gene encodes a very large RAN-binding protein that localizes to cytoplasmic filaments emanating from the nuclear pore complex. RanBP2/Nup358 is a giant scaffold and mosaic cyclophilin-related nucleoporin implicated in controlling selective processes of the Ran-GTPase cycle. RanBP2 is composed of multiple domains. Each domain of RanBP2 selectively and directly interacts with distinct proteins such as Ran GTPase, importin-beta, exportin-1/CRM1, red opsin, subunits of the proteasome, cox11 and the kinesin-1 isoforms, KIF5B and KIF5C. Another partner of RanBP2 is the E2 enzyme UBC9. RanBP2 strongly enhances SUMO1 transfer from UBC9 to the SUMO1 target SP100. Another target for SUMOylation is RanGAP which is the GTPase activating protein for Ran. SUMO-RanGAP interacts with a domain near the carboxyl terminus of RanBP2. These findings place sumoylation at the cytoplasmic filaments of the nuclear pore complex and suggest that, for some substrates, modification and nuclear import are linked events. The pleiotropic (multifunctional) role of RanBP2 reflects its interaction with multiple partners, each presenting distinct cellular or molecular functions. This gene is partially duplicated in a gene cluster that lies in a hot spot for recombination on human chromosome 2q.

Clinical significance[edit]

Insufficiency of RanBP2 is directly linked to carcinogenesis, aneuploidy, and neuroprotection of photoreceptor neurons to light-elicited stress and aging. Human missense mutations in RanBP2 were identified in its leucine-rich domain and they cause autosomal dominant necrotizing encephalopathy (ADNE).[2]

Interactions[edit]

RANBP2 has been shown to interact with KPNB1[3][4][5] and UBE2I.[6][7]

References[edit]

  1. ^ Beddow AL, Richards SA, Orem NR, Macara IG (April 1995). "The Ran/TC4 GTPase-binding domain: identification by expression cloning and characterization of a conserved sequence motif". Proceedings of the National Academy of Sciences of the United States of America 92 (8): 3328–32. doi:10.1073/pnas.92.8.3328. PMC 42159. PMID 7724562. 
  2. ^ "Entrez Gene: RANBP2 RAN binding protein 2". 
  3. ^ Yaseen, N R; Blobel G (September 1999). "GTP hydrolysis links initiation and termination of nuclear import on the nucleoporin nup358". J. Biol. Chem. (UNITED STATES) 274 (37): 26493–502. doi:10.1074/jbc.274.37.26493. ISSN 0021-9258. PMID 10473610. 
  4. ^ Delphin, C; Guan T, Melchior F, Gerace L (Dec 1997). "RanGTP Targets p97 to RanBP2, a Filamentous Protein Localized at the Cytoplasmic Periphery of the Nuclear Pore Complex". Mol. Biol. Cell (UNITED STATES) 8 (12): 2379–90. doi:10.1091/mbc.8.12.2379. ISSN 1059-1524. PMC 25714. PMID 9398662. 
  5. ^ Ben-Efraim, I; Gerace L (January 2001). "Gradient of Increasing Affinity of Importin β for Nucleoporins along the Pathway of Nuclear Import". J. Cell Biol. (United States) 152 (2): 411–7. doi:10.1083/jcb.152.2.411. ISSN 0021-9525. PMC 2199621. PMID 11266456. 
  6. ^ Ewing, Rob M; Chu Peter, Elisma Fred, Li Hongyan, Taylor Paul, Climie Shane, McBroom-Cerajewski Linda, Robinson Mark D, O'Connor Liam, Li Michael, Taylor Rod, Dharsee Moyez, Ho Yuen, Heilbut Adrian, Moore Lynda, Zhang Shudong, Ornatsky Olga, Bukhman Yury V, Ethier Martin, Sheng Yinglun, Vasilescu Julian, Abu-Farha Mohamed, Lambert Jean-Philippe, Duewel Henry S, Stewart Ian I, Kuehl Bonnie, Hogue Kelly, Colwill Karen, Gladwish Katharine, Muskat Brenda, Kinach Robert, Adams Sally-Lin, Moran Michael F, Morin Gregg B, Topaloglou Thodoros, Figeys Daniel (2007). "Large-scale mapping of human protein–protein interactions by mass spectrometry". Mol. Syst. Biol. (England) 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931. 
  7. ^ Zhang, Hong; Saitoh Hisato, Matunis Michael J (September 2002). "Enzymes of the SUMO Modification Pathway Localize to Filaments of the Nuclear Pore Complex". Mol. Cell. Biol. (United States) 22 (18): 6498–508. doi:10.1128/MCB.22.18.6498-6508.2002. ISSN 0270-7306. PMC 135644. PMID 12192048. 

Further reading[edit]