RABAC1

Rab acceptor 1 (prenylated)
Identifiers
Symbols RABAC1 ; PRA1; PRAF1; YIP3
External IDs OMIM: 604925 MGI: 1201692 HomoloGene: 38182 GeneCards: RABAC1 Gene
RNA expression pattern
More reference expression data
Orthologs
Species Human Mouse
Entrez 10567 14470
Ensembl ENSG00000105404 ENSMUSG00000003380
UniProt Q9UI14 Q9Z0S9
RefSeq (mRNA) NM_006423 NM_010261
RefSeq (protein) NP_006414 NP_034391
Location (UCSC) Chr 19:
41.96 – 41.96 Mb
Chr 7:
24.97 – 24.97 Mb
PubMed search

RABAC1 is a gene that in humans encodes the protein Prenylated Rab acceptor 1, also called PRA1, PRAF1, or RABAC1.[1][2][3] It is highly conserved in eukaryotes.[1] The protein is localized to Golgi[4] and late endosomes,[5] where it plays a role in vesicular trafficking, lipid transport and cell migration.[6]

Interactions

RABAC1 has been shown to interact with numerous prenylated members of the Rab GTPase family[1][7][8] and VAMP2.[8]

References

  1. 1 2 3 Bucci C, Chiariello M, Lattero D, Maiorano M, Bruni CB (May 1999). "Interaction cloning and characterization of the cDNA encoding the human prenylated rab acceptor (PRA1)". Biochemical and Biophysical Research Communications 258 (3): 657–62. doi:10.1006/bbrc.1999.0651. PMID 10329441.
  2. Hutt DM, Da-Silva LF, Chang LH, Prosser DC, Ngsee JK (Jun 2000). "PRA1 inhibits the extraction of membrane-bound rab GTPase by GDI1". The Journal of Biological Chemistry 275 (24): 18511–9. doi:10.1074/jbc.M909309199. PMID 10751420.
  3. "Entrez Gene: RABAC1 Rab acceptor 1 (prenylated)".
  4. Abdul-Ghani M, Gougeon PY, Prosser DC, Da-Silva LF, Ngsee JK (Mar 2001). "PRA isoforms are targeted to distinct membrane compartments". The Journal of Biological Chemistry 276 (9): 6225–33. doi:10.1074/jbc.M009073200. PMID 11096102.
  5. Sivars U, Aivazian D, Pfeffer SR (Oct 2003). "Yip3 catalyses the dissociation of endosomal Rab-GDI complexes". Nature 425 (6960): 856–9. doi:10.1038/nature02057. PMID 14574414.
  6. Liu HP, Wu CC, Kao HY, Huang YC, Liang Y, Chen CC, Yu JS, Chang YS (Mar 2011). "Proteome-wide dysregulation by PRA1 depletion delineates a role of PRA1 in lipid transport and cell migration". Molecular & Cellular Proteomics 10 (3): M900641MCP200. doi:10.1074/mcp.M900641-MCP200. PMC 3047168. PMID 20592422.
  7. 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.
  8. 1 2 Martincic I, Peralta ME, Ngsee JK (Oct 1997). "Isolation and characterization of a dual prenylated Rab and VAMP2 receptor". The Journal of Biological Chemistry 272 (43): 26991–8. doi:10.1074/jbc.272.43.26991. PMID 9341137.

Further reading

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