RALBP1

RALBP1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2KWH, 2KWI, 2MBG
Identifiers
Aliases	RALBP1, RIP1, RLIP1, RLIP76, ralA binding protein 1
External IDs	OMIM: 605801; MGI: 108466; HomoloGene: 4940; GeneCards: RALBP1; OMA:RALBP1 - orthologs
Gene location (Human) Chr. Chromosome 18 (human)[1] Band 18p11.22 Start 9,475,009 bp[1] End 9,538,114 bp[1]
Gene location (Mouse) Chr. Chromosome 17 (mouse)[2] Band 17 E1.1|17 35.26 cM Start 66,155,413 bp[2] End 66,192,793 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in renal medulla nipple spinal ganglia buccal mucosa cell pylorus trigeminal ganglion human penis external globus pallidus mucosa of pharynx pars reticulata Top expressed in zygote primary oocyte Rostral migratory stream secondary oocyte lactiferous gland genital tubercle lacrimal gland tail of embryo esophagus seminal vesicula More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein binding transmembrane transporter activity GTPase activator activity xenobiotic transmembrane transporter activity ATPase-coupled transmembrane transporter activity Cellular component cytosol membrane Biological process endocytosis regulation of small GTPase mediated signal transduction transmembrane transport regulation of GTPase activity chemotaxis positive regulation of GTPase activity signal transduction small GTPase mediated signal transduction xenobiotic transmembrane transport doxorubicin transport xenobiotic detoxification by transmembrane export across the plasma membrane Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 10928 19765 Ensembl ENSG00000017797 ENSMUSG00000024096 UniProt Q15311 Q62172 RefSeq (mRNA) NM_006788 NM_001198949 NM_009067 RefSeq (protein) NP_006779 NP_001185878 NP_033093 Location (UCSC) Chr 18: 9.48 – 9.54 Mb Chr 17: 66.16 – 66.19 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

RalA-binding protein 1 is a protein that in humans is encoded by the RALBP1 gene.[5][6]

Interactions

RALBP1 has been shown to interact with:

• Cyclin B1,[7]
• HSF1,[8]
• RALA,[5][9][10][11]
• RALB,[5][9][12] and
• REPS2.[11]

References

1. GRCh38: Ensembl release 89: ENSG00000017797 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000024096 – Ensembl, 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. Jullien-Flores V, Dorseuil O, Romero F, Letourneur F, Saragosti S, Berger R, Tavitian A, Gacon G, Camonis JH (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.
6. "Entrez Gene: RALBP1 ralA binding protein 1".
7. 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.
8. 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.
9. Moskalenko S, Tong C, Rosse C, Mirey G, Formstecher E, Daviet L, Camonis J, White MA (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.
10. 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. doi:10.1128/mcb.15.8.4578. PMC 230698. PMID 7623849.
11. 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.
12. Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.

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. S2CID 623242.
• 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, Camonis JH (2000). "RLIP76, an effector of the GTPase Ral, interacts with the AP2 complex: involvement of the Ral pathway in receptor endocytosis" (PDF). J. Cell Sci. 113 (16): 2837–44. doi:10.1242/jcs.113.16.2837. PMID 10910768.
• Awasthi S, Cheng J, Singhal SS, Saini MK, Pandya U, Pikula S, Bandorowicz-Pikula J, Singh SV, Zimniak P, Awasthi YC (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, Awasthi S, Awasthi YC (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, Awasthi YC, Awasthi S (2002). "Purification and functional reconstitution of intact ral-binding Gtpase activating protein, RLIP76, in artificial liposomes". Acta Biochim. Pol. 48 (2): 551–62. doi:10.18388/abp.2001_3938. PMID 11732624.
• Matsuzaki T, Hanai S, Kishi H, Liu Z, Bao Y, Kikuchi A, Tsuchida K, Sugino H (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, Awasthi S (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.
• Moskalenko S, Tong C, Rosse C, Mirey G, Formstecher E, Daviet L, Camonis J, White MA (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, Cheung A, Prince A (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. S2CID 1851441.
• 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.