Ranbp1

RAN binding protein 1

PDB rendering based on 1k5d.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
1K5D, 1K5G

Identifiers

Symbols

RANBP1; HTF9A

External IDs

OMIM: 601180 MGI: 96269 HomoloGene: 21600 GeneCards: RANBP1 Gene

Gene Ontology
Molecular function	• GDP-dissociation inhibitor activity • GTPase activator activity • Ran GTPase binding
Cellular component	• nucleus • nuclear envelope • cytoplasm • centrosome
Biological process	• spindle organization • signal transduction • viral reproduction • positive regulation of mitotic centrosome separation • intracellular transport
Sources: Amigo / QuickGO

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 22:
20.1 – 20.11 Mb

Chr 16:
18.24 – 18.25 Mb

PubMed search

[1]

[2]

Ran-specific binding protein 1 is an enzyme that in humans is encoded by the RANBP1 gene.^[1]^[2]^[3]

Ran/TC4-binding protein, RanBP1, interacts specifically with GTP-charged RAN. RANBP1 encodes a 23-kD protein that binds to RAN complexed with GTP but not GDP. RANBP1 does not activate GTPase activity of RAN but does markedly increase GTP hydrolysis by the RanGTPase-activating protein (RanGAP1). The RANBP1 cDNA encodes a 201-amino acid protein that is 92% similar to its mouse homolog. In both mammalian cells and in yeast, RANBP1 acts as a negative regulator of RCC1 by inhibiting RCC1-stimulated guanine nucleotide release from RAN.^[3]

Interactions [link]

RANBP1 has been shown to interact with XPO1,^[4]^[5] KPNB1^[5]^[6] and Ran.^[5]^[7]^[8]

References [link]

^ Hayashi N, Yokoyama N, Seki T, Azuma Y, Ohba T, Nishimoto T (August 1995). "RanBP1, a Ras-like nuclear G protein binding to Ran/TC4, inhibits RCC1 via Ran/TC4". Mol Gen Genet 247 (6): 661–9. DOI:10.1007/BF00290397. PMID 7616957.
^ Kehlenbach RH, Dickmanns A, Kehlenbach A, Guan T, Gerace L (July 1999). "A Role for RanBP1 in the Release of CRM1 from the Nuclear Pore Complex in a Terminal Step of Nuclear Export". J Cell Biol 145 (4): 645–57. DOI:10.1083/jcb.145.4.645. PMC 2133185. PMID 10330396. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2133185.
^ ^a ^b "Entrez Gene: RANBP1 RAN binding protein 1". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5902.
^ Singh, B B; Patel H H, Roepman R, Schick D, Ferreira P A (December 1999). "The zinc finger cluster domain of RanBP2 is a specific docking site for the nuclear export factor, exportin-1". J. Biol. Chem. (United States) 274 (52): 37370–8. DOI:10.1074/jbc.274.52.37370. ISSN 0021-9258. PMID 10601307.
^ ^a ^b ^c Plafker, K; Macara I G (May. 2000). "Facilitated Nucleocytoplasmic Shuttling of the Ran Binding Protein RanBP1". Mol. Cell. Biol. (United States) 20 (10): 3510–21. DOI:10.1128/MCB.20.10.3510-3521.2000. ISSN 0270-7306. PMC 85643. PMID 10779340. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=85643.
^ 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.
^ Ren, M; Villamarin A, Shih A, Coutavas E, Moore M S, LoCurcio M, Clarke V, Oppenheim J D, D'Eustachio P, Rush M G (April 1995). "Separate domains of the Ran GTPase interact with different factors to regulate nuclear protein import and RNA processing". Mol. Cell. Biol. (United States) 15 (4): 2117–24. ISSN 0270-7306. PMC 230439. PMID 7891706. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=230439.
^ Steggerda, S M; Paschal B M (July 2000). "The mammalian Mog1 protein is a guanine nucleotide release factor for Ran". J. Biol. Chem. (United States) 275 (30): 23175–80. DOI:10.1074/jbc.C000252200. ISSN 0021-9258. PMID 10811801.

Further reading [link]

Bischoff FR, Krebber H, Smirnova E et al. (1995). "Co-activation of RanGTPase and inhibition of GTP dissociation by Ran-GTP binding protein RanBP1". EMBO J. 14 (4): 705–15. PMC 398135. PMID 7882974. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=398135.
Ren M, Villamarin A, Shih A et al. (1995). "Separate domains of the Ran GTPase interact with different factors to regulate nuclear protein import and RNA processing". Mol. Cell. Biol. 15 (4): 2117–24. PMC 230439. PMID 7891706. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=230439.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4. DOI:10.1016/0378-1119(94)90802-8. PMID 8125298.
Coutavas E, Ren M, Oppenheim JD et al. (1994). "Characterization of proteins that interact with the cell-cycle regulatory protein Ran/TC4". Nature 366 (6455): 585–7. DOI:10.1038/366585a0. PMID 8255297.
Zolotukhin AS, Felber BK (1997). "Mutations in the nuclear export signal of human ran-binding protein RanBP1 block the Rev-mediated posttranscriptional regulation of human immunodeficiency virus type 1". J. Biol. Chem. 272 (17): 11356–60. DOI:10.1074/jbc.272.17.11356. PMID 9111043.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. DOI:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Plafker K, Macara IG (2000). "Facilitated Nucleocytoplasmic Shuttling of the Ran Binding Protein RanBP1". Mol. Cell. Biol. 20 (10): 3510–21. DOI:10.1128/MCB.20.10.3510-3521.2000. PMC 85643. PMID 10779340. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=85643.
Steggerda SM, Paschal BM (2000). "The mammalian Mog1 protein is a guanine nucleotide release factor for Ran". J. Biol. Chem. 275 (30): 23175–80. DOI:10.1074/jbc.C000252200. PMID 10811801.
Maynard TM, Haskell GT, Bhasin N et al. (2002). "RanBP1, a velocardiofacial/DiGeorge syndrome candidate gene, is expressed at sites of mesenchymal/epithelial induction". Mech. Dev. 111 (1–2): 177–80. DOI:10.1016/S0925-4773(01)00616-5. PMID 11804793.
Strausberg RL, Feingold EA, Grouse LH et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. DOI:10.1073/pnas.242603899. PMC 139241. PMID 12477932. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
Di Fiore B, Ciciarello M, Mangiacasale R et al. (2004). "Mammalian RanBP1 regulates centrosome cohesion during mitosis". J. Cell. Sci. 116 (Pt 16): 3399–411. DOI:10.1242/jcs.00624. PMID 12840069.
Seewald MJ, Kraemer A, Farkasovsky M et al. (2003). "Biochemical Characterization of the Ran-RanBP1-RanGAP System: Are RanBP Proteins and the Acidic Tail of RanGAP Required for the Ran-RanGAP GTPase Reaction?". Mol. Cell. Biol. 23 (22): 8124–36. DOI:10.1128/MCB.23.22.8124-8136.2003. PMC 262373. PMID 14585972. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=262373.
Ota T, Suzuki Y, Nishikawa T et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. DOI:10.1038/ng1285. PMID 14702039.
Bohlson SS, Zhang M, Ortiz CE, Tenner AJ (2005). "CD93 interacts with the PDZ domain-containing adaptor protein GIPC: implications in the modulation of phagocytosis". J. Leukoc. Biol. 77 (1): 80–9. DOI:10.1189/jlb.0504305. PMID 15459234.
Collins JE, Wright CL, Edwards CA et al. (2005). "A genome annotation-driven approach to cloning the human ORFeome". Genome Biol. 5 (10): R84. DOI:10.1186/gb-2004-5-10-r84. PMC 545604. PMID 15461802. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=545604.
Bruneel A, Labas V, Mailloux A et al. (2006). "Proteomics of human umbilical vein endothelial cells applied to etoposide-induced apoptosis". Proteomics 5 (15): 3876–84. DOI:10.1002/pmic.200401239. PMID 16130169.
Takeda E, Hieda M, Katahira J, Yoneda Y (2006). "Phosphorylation of RanGAP1 stabilizes its interaction with Ran and RanBP1". Cell Struct. Funct. 30 (2): 69–80. DOI:10.1247/csf.30.69. PMID 16428860.
Ewing RM, Chu P, Elisma F et al. (2007). "Large-scale mapping of human protein–protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. DOI:10.1038/msb4100134. PMC 1847948. PMID 17353931. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1847948.

PDB gallery

1k5d: Crystal structure of Ran-GPPNHP-RanBP1-RanGAP complex

1k5g: Crystal structure of Ran-GDP-AlFx-RanBP1-RanGAP complex

This protein-related article is a stub. You can help Wikipedia by expanding it.

https://wn.com/RANBP1

Podcasts:

Email this Page Play all in Full Screen Show More Related Videos

Most Related
Most Recent
Most Popular
Top Rated

PLAYLIST TIME:

Interactions [link]

References [link]

Further reading [link]

https://wn.com/RANBP1

Podcasts:

EXPLORE WN.com