RALBP1

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

RALBP1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesRALBP1, RIP1, RLIP1, RLIP76, ralA binding protein 1
External IDsOMIM: 605801 MGI: 108466 HomoloGene: 4940 GeneCards: RALBP1
Gene location (Human)
Chr.Chromosome 18 (human)[1]
Band18p11.22Start9,475,009 bp[1]
End9,538,114 bp[1]
RNA expression pattern


More reference expression data
Orthologs
SpeciesHumanMouse
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 MbChr 17: 65.85 – 65.89 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Interactions

RALBP1 has been shown to interact with:

gollark: 1, 2, 3, 4, 7, 8, 9, 0 and derivatives.
gollark: 3 is not permissible.
gollark: On each diagram show clearly the coordinates of the maximum and minimum points.The graph of y = f(x) + a has a minimum at (3, 0), where a is a constant. you.
gollark: Quarantine initiated. None are safe.
gollark: Wait, .0? Are you sure?

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. doi:10.1038/nature04209. PMID 16189514.

Further reading


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