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Protein ARF5 PDB 1z6x.png
Available structures
PDB Ortholog search: PDBe RCSB
Aliases ARF5, ADP ribosylation factor 5
External IDs MGI: 99434 HomoloGene: 129625 GeneCards: ARF5
Gene location (Human)
Chromosome 7 (human)
Chr. Chromosome 7 (human)[1]
Chromosome 7 (human)
Genomic location for ARF5
Genomic location for ARF5
Band 7q32.1 Start 127,588,345 bp[1]
End 127,591,705 bp[1]
RNA expression pattern
PBB GE ARF5 201526 at fs.png
More reference expression data
Species Human Mouse
RefSeq (mRNA)



RefSeq (protein)



Location (UCSC) Chr 7: 127.59 – 127.59 Mb Chr 6: 28.42 – 28.43 Mb
PubMed search [3] [4]
View/Edit Human View/Edit Mouse

ADP-ribosylation factor 5 is a protein that in humans is encoded by the ARF5 gene.[5][6]

ADP-ribosylation factor 5 (ARF5) is a member of the human ARF gene family. These genes encode small guanine nucleotide-binding proteins that stimulate the ADP-ribosyltransferase activity of cholera toxin and play a role in vesicular trafficking and as activators of phospholipase D. The gene products include 6 ARF proteins and 11 ARF-like proteins and constitute 1 family of the RAS superfamily. The ARF proteins are categorized as class I (ARF1, ARF2,and ARF3), class II (ARF4 and ARF5) and class III (ARF6). The members of each class share a common gene organization. The ARF5 gene spans approximately 3.2kb of genomic DNA and contains six exons and five introns.[6]


ARF5 has been shown to interact with ARFIP2.[7][8]


  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000004059 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000020440 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". 
  4. ^ "Mouse PubMed Reference:". 
  5. ^ Tsuchiya M, Price SR, Tsai SC, Moss J, Vaughan M (March 1991). "Molecular identification of ADP-ribosylation factor mRNAs and their expression in mammalian cells". J Biol Chem. 266 (5): 2772–7. PMID 1993656. 
  6. ^ a b "Entrez Gene: ARF5 ADP-ribosylation factor 5". 
  7. ^ Kanoh, H; Williger B T; Exton J H (February 1997). "Arfaptin 1, a putative cytosolic target protein of ADP-ribosylation factor, is recruited to Golgi membranes". J. Biol. Chem. UNITED STATES. 272 (9): 5421–9. doi:10.1074/jbc.272.9.5421. ISSN 0021-9258. PMID 9038142. 
  8. ^ Shin, O H; Exton J H (August 2001). "Differential binding of arfaptin 2/POR1 to ADP-ribosylation factors and Rac1". Biochem. Biophys. Res. Commun. United States. 285 (5): 1267–73. doi:10.1006/bbrc.2001.5330. ISSN 0006-291X. PMID 11478794. 

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