ARFRP1: Difference between revisions
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{{ | '''ADP-ribosylation factor-related protein 1''' is a [[protein]] that in humans is encoded by the ''ARFRP1'' [[gene]].<ref name="pmid8530503">{{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 | pmc = | doi =10.1074/jbc.270.51.30657 }}</ref><ref name="entrez">{{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| accessdate = }}</ref> | ||
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== 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 ([[ADP ribosylation factor|ARF]]) and ARF-like (ARL) genes. The gene is located in a gene cluster that includes the a gene ([[TNFRSF6B|M68]]) that is overexpressed in some tumors.<ref name="entrez"/> | |||
== Interactions == | |||
ARFRP1 has been shown to [[Protein-protein interaction|interact]] with [[PSCD1]].<ref name="pmid10092663">{{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 }}</ref> | |||
==References== | ==References== | ||
{{reflist | {{reflist}} | ||
==Further reading== | ==Further reading== | ||
{{refbegin | 2}} | {{refbegin | 2}} | ||
*{{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 |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}} | |||
*{{cite journal | | *{{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 |display-authors=etal}} | ||
*{{cite journal | | *{{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 | | *{{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 }} | ||
*{{cite journal | | *{{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}} | ||
*{{cite journal | | *{{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 |display-authors=etal}} | ||
*{{cite journal | | *{{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 |display-authors=etal}} | ||
*{{cite journal | | *{{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}} | ||
*{{cite journal | | *{{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 |display-authors=etal}} | ||
*{{cite journal | | *{{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}} | ||
*{{cite journal | | |||
*{{cite journal | | |||
}} | |||
{{refend}} | {{refend}} | ||
{{ | ==External links== | ||
{{ | * {{UCSC genome browser|ARFRP1}} | ||
* {{UCSC gene details|ARFRP1}} | |||
{{gene-20-stub}} |
Latest revision as of 19:18, 8 November 2017
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External IDs | GeneCards: [1] | ||||||
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Species | Human | Mouse | |||||
Entrez |
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Ensembl |
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UniProt |
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RefSeq (mRNA) |
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RefSeq (protein) |
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Location (UCSC) | n/a | n/a | |||||
PubMed search | n/a | n/a | |||||
Wikidata | |||||||
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ADP-ribosylation factor-related protein 1 is a protein that in humans is encoded by the ARFRP1 gene.[1][2]
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.[2]
Interactions
ARFRP1 has been shown to interact with PSCD1.[3]
References
- ↑ Schurmann A, Massmann S, Joost HG (Jan 1996). "ARP is a plasma membrane-associated Ras-related GTPase with remote similarity to the family of ADP-ribosylation factors". J Biol Chem. 270 (51): 30657–63. doi:10.1074/jbc.270.51.30657. PMID 8530503.
- ↑ 2.0 2.1 "Entrez Gene: ARFRP1 ADP-ribosylation factor related protein 1".
- ↑ Schürmann A, Schmidt M, Asmus M, Bayer S, Fliegert F, Koling S, Massmann S, Schilf C, Subauste MC, Voss M, Jakobs KH, Joost HG (April 1999). "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". J. Biol. Chem. 274 (14): 9744–51. doi:10.1074/jbc.274.14.9744. PMID 10092663.
Further reading
- Zahn C, Hommel A, Lu L, et al. (2007). "Knockout of Arfrp1 leads to disruption of ARF-like1 (ARL1) targeting to the trans-Golgi in mouse embryos and HeLa cells". Mol. Membr. Biol. 23 (6): 475–85. doi:10.1080/09687860600840100. PMID 17127620.
- Shin HW, Kobayashi H, Kitamura M, et al. (2005). "Roles of ARFRP1 (ADP-ribosylation factor-related protein 1) in post-Golgi membrane trafficking". J. Cell Sci. 118 (Pt 17): 4039–48. doi:10.1242/jcs.02524. PMID 16129887.
- Barrios-Rodiles M, Brown KR, Ozdamar B, et al. (2005). "High-throughput mapping of a dynamic signaling network in mammalian cells". Science. 307 (5715): 1621–5. doi:10.1126/science.1105776. PMID 15761153.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
- Behnia R, Panic B, Whyte JR, Munro S (2004). "Targeting of the Arf-like GTPase Arl3p to the Golgi requires N-terminal acetylation and the membrane protein Sys1p". Nat. Cell Biol. 6 (5): 405–13. doi:10.1038/ncb1120. PMID 15077113.
- Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Deloukas P, Matthews LH, Ashurst J, et al. (2002). "The DNA sequence and comparative analysis of human chromosome 20". Nature. 414 (6866): 865–71. doi:10.1038/414865a. PMID 11780052.
- Coppola T, Magnin-Luthi S, Perret-Menoud V, et al. (2001). "Direct interaction of the Rab3 effector RIM with Ca2+ channels, SNAP-25, and synaptotagmin". J. Biol. Chem. 276 (35): 32756–62. doi:10.1074/jbc.M100929200. PMID 11438518.
- Bai C, Connolly B, Metzker ML, et al. (2000). "Overexpression of M68/DcR3 in human gastrointestinal tract tumors independent of gene amplification and its location in a four-gene cluster". Proc. Natl. Acad. Sci. U.S.A. 97 (3): 1230–5. doi:10.1073/pnas.97.3.1230. PMC 15578. PMID 10655513.
- Schürmann A, Schmidt M, Asmus M, et al. (1999). "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.". J. Biol. Chem. 274 (14): 9744–51. doi:10.1074/jbc.274.14.9744. PMID 10092663.
External links
- ARFRP1 human gene location in the UCSC Genome Browser.
- ARFRP1 human gene details in the UCSC Genome Browser.
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