ARF5

ADP-ribosylation factor 5, also known as ARF5, is a human gene.cite web | title = Entrez Gene: ARF5 ADP-ribosylation factor 5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=381| accessdate = ]

PBB_Summary
section_title =
summary_text = 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.cite web | title = Entrez Gene: ARF5 ADP-ribosylation factor 5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=381| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Lee FJ, Moss J, Vaughan M |title=Human and Giardia ADP-ribosylation factors (ARFs) complement ARF function in Saccharomyces cerevisiae. |journal=J. Biol. Chem. |volume=267 |issue= 34 |pages= 24441–5 |year= 1992 |pmid= 1447192 |doi=
*cite journal | author=Tsuchiya M, Price SR, Tsai SC, "et al." |title=Molecular identification of ADP-ribosylation factor mRNAs and their expression in mammalian cells. |journal=J. Biol. Chem. |volume=266 |issue= 5 |pages= 2772–7 |year= 1991 |pmid= 1993656 |doi=
*cite journal | author=Stearns T, Willingham MC, Botstein D, Kahn RA |title=ADP-ribosylation factor is functionally and physically associated with the Golgi complex. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 3 |pages= 1238–42 |year= 1990 |pmid= 2105501 |doi=
*cite journal | author=Orcl L, Palmer DJ, Amherdt M, Rothman JE |title=Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins from the cytosol. |journal=Nature |volume=364 |issue= 6439 |pages= 732–4 |year= 1993 |pmid= 8355790 |doi= 10.1038/364732a0
*cite journal | author=Helms JB, Palmer DJ, Rothman JE |title=Two distinct populations of ARF bound to Golgi membranes. |journal=J. Cell Biol. |volume=121 |issue= 4 |pages= 751–60 |year= 1993 |pmid= 8491770 |doi=
*cite journal | author=Kanoh H, Williger BT, Exton JH |title=Arfaptin 1, a putative cytosolic target protein of ADP-ribosylation factor, is recruited to Golgi membranes. |journal=J. Biol. Chem. |volume=272 |issue= 9 |pages= 5421–9 |year= 1997 |pmid= 9038142 |doi=
*cite journal | author=McGuire RE, Daiger SP, Green ED |title=Localization and characterization of the human ADP-ribosylation factor 5 (ARF5) gene. |journal=Genomics |volume=41 |issue= 3 |pages= 481–4 |year= 1997 |pmid= 9169151 |doi= 10.1006/geno.1997.4689
*cite journal | author=Andreev J, Simon JP, Sabatini DD, "et al." |title=Identification of a new Pyk2 target protein with Arf-GAP activity. |journal=Mol. Cell. Biol. |volume=19 |issue= 3 |pages= 2338–50 |year= 1999 |pmid= 10022920 |doi=
*cite journal | author=Honda A, Nogami M, Yokozeki T, "et al." |title=Phosphatidylinositol 4-phosphate 5-kinase alpha is a downstream effector of the small G protein ARF6 in membrane ruffle formation. |journal=Cell |volume=99 |issue= 5 |pages= 521–32 |year= 1999 |pmid= 10589680 |doi=
*cite journal | author=Shin OH, Ross AH, Mihai I, Exton JH |title=Identification of arfophilin, a target protein for GTP-bound class II ADP-ribosylation factors. |journal=J. Biol. Chem. |volume=274 |issue= 51 |pages= 36609–15 |year= 2000 |pmid= 10593962 |doi=
*cite journal | author=Kondo A, Hashimoto S, Yano H, "et al." |title=A new paxillin-binding protein, PAG3/Papalpha/KIAA0400, bearing an ADP-ribosylation factor GTPase-activating protein activity, is involved in paxillin recruitment to focal adhesions and cell migration. |journal=Mol. Biol. Cell |volume=11 |issue= 4 |pages= 1315–27 |year= 2000 |pmid= 10749932 |doi=
*cite journal | author=Nevrivy DJ, Peterson VJ, Avram D, "et al." |title=Interaction of GRASP, a protein encoded by a novel retinoic acid-induced gene, with members of the cytohesin family of guanine nucleotide exchange factors. |journal=J. Biol. Chem. |volume=275 |issue= 22 |pages= 16827–36 |year= 2000 |pmid= 10828067 |doi=
*cite journal | author=Shin OH, Couvillon AD, Exton JH |title=Arfophilin is a common target of both class II and class III ADP-ribosylation factors. |journal=Biochemistry |volume=40 |issue= 36 |pages= 10846–52 |year= 2001 |pmid= 11535061 |doi=
*cite journal | author=Austin C, Boehm M, Tooze SA |title=Site-specific cross-linking reveals a differential direct interaction of class 1, 2, and 3 ADP-ribosylation factors with adaptor protein complexes 1 and 3. |journal=Biochemistry |volume=41 |issue= 14 |pages= 4669–77 |year= 2002 |pmid= 11926829 |doi=
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Scherer SW, Cheung J, MacDonald JR, "et al." |title=Human chromosome 7: DNA sequence and biology. |journal=Science |volume=300 |issue= 5620 |pages= 767–72 |year= 2003 |pmid= 12690205 |doi= 10.1126/science.1083423
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Rual JF, Venkatesan K, Hao T, "et al." |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173–8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209

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