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RABAC1

From Wikipedia, the free encyclopedia

RABAC1
Identifiers
AliasesRABAC1, PRA1, PRAF1, YIP3, Rab acceptor 1
External IDsOMIM: 604925; MGI: 1201692; HomoloGene: 38182; GeneCards: RABAC1; OMA:RABAC1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_006423

NM_010261

RefSeq (protein)

NP_006414

NP_034391

Location (UCSC)Chr 19: 41.96 – 41.96 MbChr 7: 24.67 – 24.67 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

RABAC1 is a gene that in humans encodes the protein Prenylated Rab acceptor 1, also called PRA1, PRAF1, or RABAC1.[5][6][7] It is highly conserved in eukaryotes.[5] The protein is localized to Golgi[8] and late endosomes,[9] where it plays a role in vesicular trafficking, lipid transport and cell migration.[10]

Interactions

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RABAC1 has been shown to interact with numerous prenylated members of the Rab GTPase family[5][11][12] and VAMP2.[12]

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000105404Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000003380Ensembl, 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. ^ a b c 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.
  6. ^ 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.
  7. ^ "Entrez Gene: RABAC1 Rab acceptor 1 (prenylated)".
  8. ^ 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.
  9. ^ Sivars U, Aivazian D, Pfeffer SR (Oct 2003). "Yip3 catalyses the dissociation of endosomal Rab-GDI complexes". Nature. 425 (6960): 856–9. Bibcode:2003Natur.425..856S. doi:10.1038/nature02057. PMID 14574414. S2CID 4421009.
  10. ^ 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): M900641–MCP200. doi:10.1074/mcp.M900641-MCP200. PMC 3047168. PMID 20592422.
  11. ^ 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.
  12. ^ a b 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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