RALBP1

RalA binding protein 1

Rendering based on PDB 2KWH.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
SymbolsRALBP1 ; RIP1; RLIP1; RLIP76
External IDsOMIM: 605801 MGI: 108466 HomoloGene: 4940 GeneCards: RALBP1 Gene
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez1092819765
EnsemblENSG00000017797ENSMUSG00000024096
UniProtQ15311Q62172
RefSeq (mRNA)NM_006788NM_001198949
RefSeq (protein)NP_006779NP_001185878
Location (UCSC)Chr 18:
9.48 – 9.54 Mb		Chr 17:
65.85 – 65.89 Mb
PubMed search

RalA-binding protein 1 is a protein that in humans is encoded by the RALBP1 gene.[1][2]

Interactions

RALBP1 has been shown to interact with:

References

  1. ↑ 1.0 1.1 1.2 Jullien-Flores V, Dorseuil O, Romero F, Letourneur F, Saragosti S, Berger R et al. (Oct 1995). "Bridging Ral GTPase to Rho pathways. RLIP76, a Ral effector with CDC42/Rac GTPase-activating protein activity". J Biol Chem 270 (38): 22473–7. doi:10.1074/jbc.270.38.22473. PMID 7673236.
  2. ↑ "Entrez Gene: RALBP1 ralA binding protein 1".
  3. ↑ Rossé C, L'Hoste S, Offner N, Picard A, Camonis J (Aug 2003). "RLIP, an effector of the Ral GTPases, is a platform for Cdk1 to phosphorylate epsin during the switch off of endocytosis in mitosis". J. Biol. Chem. 278 (33): 30597–604. doi:10.1074/jbc.M302191200. PMID 12775724. Vancouver style error (help)
  4. ↑ Hu Y, Mivechi NF (May 2003). "HSF-1 interacts with Ral-binding protein 1 in a stress-responsive, multiprotein complex with HSP90 in vivo". J. Biol. Chem. 278 (19): 17299–306. doi:10.1074/jbc.M300788200. PMID 12621024.
  5. ↑ 5.0 5.1 Moskalenko S, Tong C, Rosse C, Mirey G, Formstecher E, Daviet L et al. (Dec 2003). "Ral GTPases regulate exocyst assembly through dual subunit interactions". J. Biol. Chem. 278 (51): 51743–8. doi:10.1074/jbc.M308702200. PMID 14525976.
  6. ↑ Cantor SB, Urano T, Feig LA (Aug 1995). "Identification and characterization of Ral-binding protein 1, a potential downstream target of Ral GTPases". Mol. Cell. Biol. 15 (8): 4578–84. PMC 230698. PMID 7623849.
  7. ↑ 7.0 7.1 Ikeda M, Ishida O, Hinoi T, Kishida S, Kikuchi A (Jan 1998). "Identification and characterization of a novel protein interacting with Ral-binding protein 1, a putative effector protein of Ral". J. Biol. Chem. 273 (2): 814–21. doi:10.1074/jbc.273.2.814. PMID 9422736.
  8. ↑ Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N et al. (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.

Further reading

  • Awasthi S, Sharma R, Singhal SS, Zimniak P, Awasthi YC (2003). "RLIP76, a novel transporter catalyzing ATP-dependent efflux of xenobiotics". Drug Metab. Dispos. 30 (12): 1300–10. doi:10.1124/dmd.30.12.1300. PMID 12433796.
  • Yamaguchi A, Urano T, Goi T, Feig LA (1998). "An Eps homology (EH) domain protein that binds to the Ral-GTPase target, RalBP1". J. Biol. Chem. 272 (50): 31230–4. doi:10.1074/jbc.272.50.31230. PMID 9395447.
  • Ikeda M, Ishida O, Hinoi T, Kishida S, Kikuchi A (1998). "Identification and characterization of a novel protein interacting with Ral-binding protein 1, a putative effector protein of Ral". J. Biol. Chem. 273 (2): 814–21. doi:10.1074/jbc.273.2.814. PMID 9422736.
  • Iouzalen N, Camonis J, Moreau J (1998). "Identification and characterization in Xenopus of XsmgGDS, a RalB binding protein". Biochem. Biophys. Res. Commun. 250 (2): 359–63. doi:10.1006/bbrc.1998.9336. PMID 9753634.
  • Suzuki J, Yamazaki Y, Li G, Kaziro Y, Koide H, Guang L (2000). "Involvement of Ras and Ral in Chemotactic Migration of Skeletal Myoblasts". Mol. Cell. Biol. 20 (13): 4658–65. doi:10.1128/MCB.20.13.4658-4665.2000. PMC 85875. PMID 10848592.
  • Jullien-Flores V, Mahé Y, Mirey G, Leprince C, Meunier-Bisceuil B, Sorkin A et al. (2000). "RLIP76, an effector of the GTPase Ral, interacts with the AP2 complex: involvement of the Ral pathway in receptor endocytosis". J. Cell. Sci. 113 (16): 2837–44. PMID 10910768. Vancouver style error (help)
  • Awasthi S, Cheng J, Singhal SS, Saini MK, Pandya U, Pikula S et al. (2000). "Novel function of human RLIP76: ATP-dependent transport of glutathione conjugates and doxorubicin". Biochemistry 39 (31): 9327–34. doi:10.1021/bi992964c. PMID 10924126.
  • Sharma R, Singhal SS, Cheng J, Yang Y, Sharma A, Zimniak P et al. (2001). "RLIP76 is the major ATP-dependent transporter of glutathione-conjugates and doxorubicin in human erythrocytes". Arch. Biochem. Biophys. 391 (2): 171–9. doi:10.1006/abbi.2001.2395. PMID 11437348.
  • Singhal SS, Singhal J, Cheng J, Pikuła S, Sharma R, Zimniak P et al. (2002). "Purification and functional reconstitution of intact ral-binding Gtpase activating protein, RLIP76, in artificial liposomes". Acta Biochim. Pol. 48 (2): 551–62. PMID 11732624. Vancouver style error (help)
  • Matsuzaki T, Hanai S, Kishi H, Liu Z, Bao Y, Kikuchi A et al. (2002). "Regulation of endocytosis of activin type II receptors by a novel PDZ protein through Ral/Ral-binding protein 1-dependent pathway". J. Biol. Chem. 277 (21): 19008–18. doi:10.1074/jbc.M112472200. PMID 11882656.
  • Singhal SS, Singhal J, Sharma R, Singh SV, Zimniak P, Awasthi YC et al. (2003). "Role of RLIP76 in lung cancer doxorubicin resistance: I. The ATPase activity of RLIP76 correlates with doxorubicin and 4-hydroxynonenal resistance in lung cancer cells". Int. J. Oncol. 22 (2): 365–75. doi:10.3892/ijo.22.2.365. PMID 12527936.
  • Awasthi S, Singhal SS, Singhal J, Cheng J, Zimniak P, Awasthi YC (2003). "Role of RLIP76 in lung cancer doxorubicin resistance: II. Doxorubicin transport in lung cancer by RLIP76". Int. J. Oncol. 22 (4): 713–20. doi:10.3892/ijo.22.4.713. PMID 12632060.
  • Awasthi S, Singhal SS, Singhal J, Yang Y, Zimniak P, Awasthi YC (2003). "Role of RLIP76 in lung cancer doxorubicin resistance: III. Anti-RLIP76 antibodies trigger apoptosis in lung cancer cells and synergistically increase doxorubicin cytotoxicity". Int. J. Oncol. 22 (4): 721–32. doi:10.3892/ijo.22.4.721. PMID 12632061.
  • Rossé C, L'Hoste S, Offner N, Picard A, Camonis J (2003). "RLIP, an effector of the Ral GTPases, is a platform for Cdk1 to phosphorylate epsin during the switch off of endocytosis in mitosis". J. Biol. Chem. 278 (33): 30597–604. doi:10.1074/jbc.M302191200. PMID 12775724. Vancouver style error (help)
  • Moskalenko S, Tong C, Rosse C, Mirey G, Formstecher E, Daviet L et al. (2004). "Ral GTPases regulate exocyst assembly through dual subunit interactions". J. Biol. Chem. 278 (51): 51743–8. doi:10.1074/jbc.M308702200. PMID 14525976.
  • Gómez MI, Lee A, Reddy B, Muir A, Soong G, Pitt A et al. (2004). "Staphylococcus aureus protein A induces airway epithelial inflammatory responses by activating TNFR1". Nat. Med. 10 (8): 842–8. doi:10.1038/nm1079. PMID 15247912. Vancouver style error (help)
  • Zhang H, Zhang R, Luo Y, D'Alessio A, Pober JS, Min W (2004). "AIP1/DAB2IP, a novel member of the Ras-GAP family, transduces TRAF2-induced ASK1-JNK activation". J. Biol. Chem. 279 (43): 44955–65. doi:10.1074/jbc.M407617200. PMID 15310755.