ARFRP1

{{Short description|Protein-coding gene in the species Homo sapiens}}

{{Infobox_gene}}

ADP-ribosylation factor-related protein 1 is a protein that in humans is encoded by the ARFRP1 gene.{{cite journal | vauthors = Schurmann A, Massmann S, Joost HG | title = ARP is a plasma membrane-associated Ras-related GTPase with remote similarity to the family of ADP-ribosylation factors | journal = J Biol Chem | volume = 270 | issue = 51 | pages = 30657–63 |date=Jan 1996 | pmid = 8530503 | doi =10.1074/jbc.270.51.30657 | doi-access = free }}{{cite web | title = Entrez Gene: ARFRP1 ADP-ribosylation factor related protein 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10139}}

Function

The protein encoded by this gene is a membrane-associated GTP-ase and localizes to the plasma membrane. It is related to the ADP-ribosylation factor (ARF) and ARF-like (ARL) genes. The gene is located in a gene cluster that includes the a gene (M68) that is overexpressed in some tumors.

Interactions

ARFRP1 has been shown to interact with PSCD1.{{cite journal | vauthors = Schürmann A, Schmidt M, Asmus M, Bayer S, Fliegert F, Koling S, Massmann S, Schilf C, Subauste MC, Voss M, Jakobs KH, Joost HG | title = The ADP-ribosylation factor (ARF)-related GTPase ARF-related protein binds to the ARF-specific guanine nucleotide exchange factor cytohesin and inhibits the ARF-dependent activation of phospholipase D | journal = J. Biol. Chem. | volume = 274 | issue = 14 | pages = 9744–51 |date=April 1999 | pmid = 10092663 | doi = 10.1074/jbc.274.14.9744 | doi-access = free }}

References

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Further reading

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  • {{cite journal | vauthors=Zahn C, Hommel A, Lu L |title=Knockout of Arfrp1 leads to disruption of ARF-like1 (ARL1) targeting to the trans-Golgi in mouse embryos and HeLa cells. |journal=Mol. Membr. Biol. |volume=23 |issue= 6 |pages= 475–85 |year= 2007 |pmid= 17127620 |doi= 10.1080/09687860600840100 |s2cid=22778359 |display-authors=etal}}
  • {{cite journal | vauthors=Shin HW, Kobayashi H, Kitamura M |title=Roles of ARFRP1 (ADP-ribosylation factor-related protein 1) in post-Golgi membrane trafficking. |journal=J. Cell Sci. |volume=118 |issue= Pt 17 |pages= 4039–48 |year= 2005 |pmid= 16129887 |doi= 10.1242/jcs.02524 |display-authors=etal|doi-access=free }}
  • {{cite journal | vauthors=Barrios-Rodiles M, Brown KR, Ozdamar B |title=High-throughput mapping of a dynamic signaling network in mammalian cells. |journal=Science |volume=307 |issue= 5715 |pages= 1621–5 |year= 2005 |pmid= 15761153 |doi= 10.1126/science.1105776 |bibcode=2005Sci...307.1621B |s2cid=39457788 |display-authors=etal}}
  • {{cite journal | vauthors=Gerhard DS, Wagner L, Feingold EA |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 | pmc=528928 |display-authors=etal}}
  • {{cite journal | vauthors=Behnia R, Panic B, Whyte JR, Munro S |title=Targeting of the Arf-like GTPase Arl3p to the Golgi requires N-terminal acetylation and the membrane protein Sys1p. |journal=Nat. Cell Biol. |volume=6 |issue= 5 |pages= 405–13 |year= 2004 |pmid= 15077113 |doi= 10.1038/ncb1120 |s2cid=22954283 }}
  • {{cite journal | vauthors=Ota T, Suzuki Y, Nishikawa T |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 |display-authors=etal|doi-access=free }}
  • {{cite journal | vauthors=Strausberg RL, Feingold EA, Grouse LH |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 | pmc=139241 |bibcode=2002PNAS...9916899M |display-authors=etal|doi-access=free }}
  • {{cite journal | vauthors=Deloukas P, Matthews LH, Ashurst J |title=The DNA sequence and comparative analysis of human chromosome 20. |journal=Nature |volume=414 |issue= 6866 |pages= 865–71 |year= 2002 |pmid= 11780052 |doi= 10.1038/414865a |bibcode=2001Natur.414..865D |display-authors=etal|doi-access=free }}
  • {{cite journal | vauthors=Coppola T, Magnin-Luthi S, Perret-Menoud V |title=Direct interaction of the Rab3 effector RIM with Ca2+ channels, SNAP-25, and synaptotagmin. |journal=J. Biol. Chem. |volume=276 |issue= 35 |pages= 32756–62 |year= 2001 |pmid= 11438518 |doi= 10.1074/jbc.M100929200 |display-authors=etal|doi-access=free }}
  • {{cite journal | vauthors=Bai C, Connolly B, Metzker ML |title=Overexpression of M68/DcR3 in human gastrointestinal tract tumors independent of gene amplification and its location in a four-gene cluster. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 3 |pages= 1230–5 |year= 2000 |pmid= 10655513 |doi=10.1073/pnas.97.3.1230 | pmc=15578 |bibcode=2000PNAS...97.1230B |display-authors=etal|doi-access=free }}
  • {{cite journal | vauthors=Schürmann A, Schmidt M, Asmus M |title=The ADP-ribosylation factor (ARF)-related GTPase ARF-related protein binds to the ARF-specific guanine nucleotide exchange factor cytohesin and inhibits the ARF-dependent activation of phospholipase D. |journal=J. Biol. Chem. |volume=274 |issue= 14 |pages= 9744–51 |year= 1999 |pmid= 10092663 |doi=10.1074/jbc.274.14.9744 |display-authors=etal|doi-access=free }}

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