ARFRP1: Difference between revisions

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{{Infobox_gene}}
{{PBB_Controls
'''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>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = ADP-ribosylation factor related protein 1
| HGNCid = 662
| Symbol = ARFRP1
| AltSymbols =; ARP; ARL18; Arp1
| OMIM = 604699
| ECnumber = 
| Homologene = 2425
| MGIid = 1923938
| GeneAtlas_image1 = PBB_GE_ARFRP1_203174_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_ARFRP1_215984_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003924 |text = GTPase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005525 |text = GTP binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005624 |text = membrane fraction}}
| Process = {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007264 |text = small GTPase mediated signal transduction}} {{GNF_GO|id=GO:0007369 |text = gastrulation}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 10139
    | Hs_Ensembl = ENSG00000101246
    | Hs_RefseqProtein = NP_003215
    | Hs_RefseqmRNA = NM_003224
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 20
    | Hs_GenLoc_start = 61800447
    | Hs_GenLoc_end = 61809634
    | Hs_Uniprot = Q13795
    | Mm_EntrezGene = 76688
    | Mm_Ensembl = ENSMUSG00000038671
    | Mm_RefseqmRNA = NM_029702
    | Mm_RefseqProtein = NP_083978
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 2
    | Mm_GenLoc_start = 181287240
    | Mm_GenLoc_end = 181294768
    | Mm_Uniprot = Q80SX7
  }}
}}
'''ADP-ribosylation factor related protein 1''', also known as '''ARFRP1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ARFRP1 ADP-ribosylation factor related protein 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10139| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
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"/>
{{PBB_Summary
 
| section_title =
== Interactions ==
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: ARFRP1 ADP-ribosylation factor related protein 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10139| accessdate = }}</ref>
 
}}
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|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
*{{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}}
| citations =
*{{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  | author=Zahn C, Hommel A, Lu L, ''et al.'' |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 }}
*{{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  | author=Shin HW, Kobayashi H, Kitamura M, ''et al.'' |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 }}
*{{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  | author=Barrios-Rodiles M, Brown KR, Ozdamar B, ''et al.'' |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 }}
*{{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  | 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  | 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  | author=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  | 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  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |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 }}
*{{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  | 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  | 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  | author=Deloukas P, Matthews LH, Ashurst J, ''et al.'' |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 }}
*{{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  | author=Coppola T, Magnin-Luthi S, Perret-Menoud V, ''et al.'' |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 }}
*{{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  | author=Bai C, Connolly B, Metzker ML, ''et al.'' |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=  }}
*{{cite journal  | author=Schürmann A, Schmidt M, Asmus M, ''et al.'' |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= }}
*{{cite journal  | author=Schürmann 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 |year= 1996 |pmid= 8530503 |doi=  }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
==External links==
{{WikiDoc Sources}}
* {{UCSC genome browser|ARFRP1}}
* {{UCSC gene details|ARFRP1}}
 
 
{{gene-20-stub}}

Latest revision as of 19:18, 8 November 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
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/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

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

  1. ↑ 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. ↑ 2.0 2.1 "Entrez Gene: ARFRP1 ADP-ribosylation factor related protein 1".
  3. ↑ 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

External links


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