Ran-specific binding protein 1 is an enzyme that in humans is encoded by the RANBP1 gene.[5][6][7]

RANBP1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesRANBP1, HTF9A, RAN binding protein 1
External IDsOMIM: 601180; MGI: 96269; HomoloGene: 21600; GeneCards: RANBP1; OMA:RANBP1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001278639
NM_001278640
NM_001278641
NM_002882

NM_011239

RefSeq (protein)

NP_001265568
NP_001265569
NP_001265570
NP_002873

NP_035369

Location (UCSC)Chr 22: 20.12 – 20.13 MbChr 16: 18.06 – 18.07 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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.[7]

Interactions

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RANBP1 has been shown to interact with XPO1,[8][9] KPNB1[9][10] and Ran.[9][11][12]

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000099901Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000005732Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ 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. S2CID 24266692.
  6. ^ 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.
  7. ^ a b "Entrez Gene: RANBP1 RAN binding protein 1".
  8. ^ 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. 274 (52): 37370–8. doi:10.1074/jbc.274.52.37370. hdl:2066/120791. ISSN 0021-9258. PMID 10601307.
  9. ^ a b c Plafker, K; Macara I G (May 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. ISSN 0270-7306. PMC 85643. PMID 10779340.
  10. ^ Yaseen, N R; Blobel G (September 1999). "GTP hydrolysis links initiation and termination of nuclear import on the nucleoporin nup358". J. Biol. Chem. 274 (37): 26493–502. doi:10.1074/jbc.274.37.26493. ISSN 0021-9258. PMID 10473610.
  11. ^ 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. 15 (4): 2117–24. doi:10.1128/MCB.15.4.2117. ISSN 0270-7306. PMC 230439. PMID 7891706.
  12. ^ Steggerda, S M; Paschal B M (July 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. ISSN 0021-9258. PMID 10811801.

Further reading

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