From Wikipedia, the free encyclopedia
Jump to navigation Jump to search
Protein RAB1A PDB 2fol.png
Available structures
PDBOrtholog search: PDBe RCSB
AliasesRAB1A, RAB1, YPT1, member RAS oncogene family
External IDsMGI: 97842 HomoloGene: 36154 GeneCards: RAB1A
Gene location (Human)
Chromosome 2 (human)
Chr.Chromosome 2 (human)[1]
Chromosome 2 (human)
Genomic location for RAB1A
Genomic location for RAB1A
Band2p14Start65,070,696 bp[1]
End65,130,331 bp[1]
RNA expression pattern
PBB GE RAB1A 213440 at fs.png

PBB GE RAB1A 208724 s at fs.png

PBB GE RAB1A 207791 s at fs.png
More reference expression data
RefSeq (mRNA)



RefSeq (protein)



Location (UCSC)Chr 2: 65.07 – 65.13 MbChr 11: 20.2 – 20.23 Mb
PubMed search[3][4]
View/Edit HumanView/Edit Mouse

Ras-related protein Rab-1A is a protein that in humans is encoded by the RAB1A gene.[5][6]


RAB1A has been shown to interact with:


  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000138069 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000020149 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:".
  4. ^ "Mouse PubMed Reference:".
  5. ^ Zahraoui A, Touchot N, Chardin P, Tavitian A (Jul 1989). "The human Rab genes encode a family of GTP-binding proteins related to yeast YPT1 and SEC4 products involved in secretion". The Journal of Biological Chemistry. 264 (21): 12394–401. PMID 2501306.
  6. ^ "Entrez Gene: RAB1A RAB1A, member RAS oncogene family".
  7. ^ a b Cremers FP, Armstrong SA, Seabra MC, Brown MS, Goldstein JL (Jan 1994). "REP-2, a Rab escort protein encoded by the choroideremia-like gene". The Journal of Biological Chemistry. 269 (3): 2111–7. PMID 8294464.
  8. ^ Anant JS, Desnoyers L, Machius M, Demeler B, Hansen JC, Westover KD, Deisenhofer J, Seabra MC (Sep 1998). "Mechanism of Rab geranylgeranylation: formation of the catalytic ternary complex". Biochemistry. 37 (36): 12559–68. doi:10.1021/bi980881a. PMID 9730828.
  9. ^ a b Weide T, Teuber J, Bayer M, Barnekow A (Jun 2003). "MICAL-1 isoforms, novel rab1 interacting proteins". Biochemical and Biophysical Research Communications. 306 (1): 79–86. doi:10.1016/s0006-291x(03)00918-5. PMID 12788069.
  10. ^ Valsdottir R, Hashimoto H, Ashman K, Koda T, Storrie B, Nilsson T (Nov 2001). "Identification of rabaptin-5, rabex-5, and GM130 as putative effectors of rab33b, a regulator of retrograde traffic between the Golgi apparatus and ER". FEBS Letters. 508 (2): 201–9. doi:10.1016/s0014-5793(01)02993-3. PMID 11718716.
  11. ^ Short B, Preisinger C, Körner R, Kopajtich R, Byron O, Barr FA (Dec 2001). "A GRASP55-rab2 effector complex linking Golgi structure to membrane traffic". The Journal of Cell Biology. 155 (6): 877–83. doi:10.1083/jcb.200108079. PMC 2150909. PMID 11739401.
  12. ^ Satoh A, Wang Y, Malsam J, Beard MB, Warren G (Mar 2003). "Golgin-84 is a rab1 binding partner involved in Golgi structure". Traffic. 4 (3): 153–61. doi:10.1034/j.1600-0854.2003.00103.x. PMC 3282115. PMID 12656988.
  13. ^ Diao A, Rahman D, Pappin DJ, Lucocq J, Lowe M (Jan 2003). "The coiled-coil membrane protein golgin-84 is a novel rab effector required for Golgi ribbon formation". The Journal of Cell Biology. 160 (2): 201–12. doi:10.1083/jcb.200207045. PMC 2172652. PMID 12538640.
  14. ^ 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.
  15. ^ 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[edit]