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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Actin-related protein 2/3 complex subunit 5''' is a [[protein]] that in humans is encoded by the ''ARPC5'' [[gene]].<ref name="pmid9359840">{{cite journal | vauthors = Machesky LM, Reeves E, Wientjes F, Mattheyse FJ, Grogan A, Totty NF, Burlingame AL, Hsuan JJ, Segal AW | title = Mammalian actin-related protein 2/3 complex localizes to regions of lamellipodial protrusion and is composed of evolutionarily conserved proteins | journal = Biochem. J. | volume = 328 ( Pt 1) | issue = 1 | pages = 105–12 | year = 1997 | pmid = 9359840 | pmc = 1218893 | doi =  }}</ref><ref name="pmid9230079">{{cite journal | vauthors = Welch MD, DePace AH, Verma S, Iwamatsu A, Mitchison TJ | title = The human Arp2/3 complex is composed of evolutionarily conserved subunits and is localized to cellular regions of dynamic actin filament assembly | journal = J. Cell Biol. | volume = 138 | issue = 2 | pages = 375–84  | date = August 1997 | pmid = 9230079 | pmc = 2138188 | doi = 10.1083/jcb.138.2.375 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ARPC5 actin related protein 2/3 complex, subunit 5, 16kDa| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10092| 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 = PBB_Protein_ARPC5_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1k8k.
| PDB = {{PDB2|1k8k}}, {{PDB2|1tyq}}, {{PDB2|1u2v}}, {{PDB2|2p9i}}, {{PDB2|2p9k}}, {{PDB2|2p9l}}, {{PDB2|2p9n}}, {{PDB2|2p9p}}, {{PDB2|2p9s}}, {{PDB2|2p9u}}
| Name = Actin related protein 2/3 complex, subunit 5, 16kDa
| HGNCid = 708
| Symbol = ARPC5
| AltSymbols =; ARC16; dJ127C7.3; p16-Arc
| OMIM = 604227
| ECnumber = 
| Homologene = 4176
| MGIid = 1915021
| GeneAtlas_image1 = PBB_GE_ARPC5_211963_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005200 |text = structural constituent of cytoskeleton}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005856 |text = cytoskeleton}} {{GNF_GO|id=GO:0005885 |text = Arp2/3 protein complex}}
| Process = {{GNF_GO|id=GO:0006928 |text = cell motility}} {{GNF_GO|id=GO:0030036 |text = actin cytoskeleton organization and biogenesis}} {{GNF_GO|id=GO:0030833 |text = regulation of actin filament polymerization}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 10092
    | Hs_Ensembl = ENSG00000162704
    | Hs_RefseqProtein = NP_005708
    | Hs_RefseqmRNA = NM_005717
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 181859024
    | Hs_GenLoc_end = 181871608
    | Hs_Uniprot = O15511
    | Mm_EntrezGene = 67771
    | Mm_Ensembl = ENSMUSG00000008475
    | Mm_RefseqmRNA = NM_026369
    | Mm_RefseqProtein = NP_080645
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 1
    | Mm_GenLoc_start = 154528943
    | Mm_GenLoc_end = 154537796
    | Mm_Uniprot = Q3TK56
  }}
}}
'''Actin related protein 2/3 complex, subunit 5, 16kDa''', also known as '''ARPC5''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ARPC5 actin related protein 2/3 complex, subunit 5, 16kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10092| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
This gene encodes one of seven subunits of the human Arp2/3 protein complex. The Arp2/3 protein complex has been implicated in the control of actin polymerization in cells and has been conserved through evolution. The exact role of the protein encoded by this gene, the p16 subunit, has yet to be determined.<ref name="entrez"/>
{{PBB_Summary
| section_title =
| summary_text = This gene encodes one of seven subunits of the human Arp2/3 protein complex. The Arp2/3 protein complex has been implicated in the control of actin polymerization in cells and has been conserved through evolution. The exact role of the protein encoded by this gene, the p16 subunit, has yet to be determined.<ref name="entrez">{{cite web | title = Entrez Gene: ARPC5 actin related protein 2/3 complex, subunit 5, 16kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10092| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal  | author=Welch MD, Iwamatsu A, Mitchison TJ |title=Actin polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes. |journal=Nature |volume=385 |issue= 6613 |pages= 265-9 |year= 1997 |pmid= 9000076 |doi= 10.1038/385265a0 }}
*{{cite journal  | author=Welch MD, DePace AH, Verma S, ''et al.'' |title=The human Arp2/3 complex is composed of evolutionarily conserved subunits and is localized to cellular regions of dynamic actin filament assembly. |journal=J. Cell Biol. |volume=138 |issue= 2 |pages= 375-84 |year= 1997 |pmid= 9230079 |doi=  }}
*{{cite journal  | author=Machesky LM, Reeves E, Wientjes F, ''et al.'' |title=Mammalian actin-related protein 2/3 complex localizes to regions of lamellipodial protrusion and is composed of evolutionarily conserved proteins. |journal=Biochem. J. |volume=328 ( Pt 1) |issue=  |pages= 105-12 |year= 1998 |pmid= 9359840 |doi=  }}
*{{cite journal  | author=Zhao X, Yang Z, Qian M, Zhu X |title=Interactions among subunits of human Arp2/3 complex: p20-Arc as the hub. |journal=Biochem. Biophys. Res. Commun. |volume=280 |issue= 2 |pages= 513-7 |year= 2001 |pmid= 11162547 |doi= 10.1006/bbrc.2000.4151 }}
*{{cite journal  | author=Robinson RC, Turbedsky K, Kaiser DA, ''et al.'' |title=Crystal structure of Arp2/3 complex. |journal=Science |volume=294 |issue= 5547 |pages= 1679-84 |year= 2001 |pmid= 11721045 |doi= 10.1126/science.1066333 }}
*{{cite journal  | author=Gournier H, Goley ED, Niederstrasser H, ''et al.'' |title=Reconstitution of human Arp2/3 complex reveals critical roles of individual subunits in complex structure and activity. |journal=Mol. Cell |volume=8 |issue= 5 |pages= 1041-52 |year= 2002 |pmid= 11741539 |doi=  }}
*{{cite journal  | author=Millard TH, Behrendt B, Launay S, ''et al.'' |title=Identification and characterisation of a novel human isoform of Arp2/3 complex subunit p16-ARC/ARPC5. |journal=Cell Motil. Cytoskeleton |volume=54 |issue= 1 |pages= 81-90 |year= 2003 |pmid= 12451597 |doi= 10.1002/cm.10087 }}
*{{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=Gevaert K, Goethals M, Martens L, ''et al.'' |title=Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. |journal=Nat. Biotechnol. |volume=21 |issue= 5 |pages= 566-9 |year= 2004 |pmid= 12665801 |doi= 10.1038/nbt810 }}
*{{cite journal  | author=Singh S, Powell DW, Rane MJ, ''et al.'' |title=Identification of the p16-Arc subunit of the Arp 2/3 complex as a substrate of MAPK-activated protein kinase 2 by proteomic analysis. |journal=J. Biol. Chem. |volume=278 |issue= 38 |pages= 36410-7 |year= 2003 |pmid= 12829704 |doi= 10.1074/jbc.M306428200 }}
*{{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  | 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=Gregory SG, Barlow KF, McLay KE, ''et al.'' |title=The DNA sequence and biological annotation of human chromosome 1. |journal=Nature |volume=441 |issue= 7091 |pages= 315-21 |year= 2006 |pmid= 16710414 |doi= 10.1038/nature04727 }}
*{{cite journal  | author=Ewing RM, Chu P, Elisma F, ''et al.'' |title=Large-scale mapping of human protein-protein interactions by mass spectrometry. |journal=Mol. Syst. Biol. |volume=3 |issue=  |pages= 89 |year= 2007 |pmid= 17353931 |doi= 10.1038/msb4100134 }}
}}
{{refend}}


{{protein-stub}}
ARPC5 has been shown to [[Protein-protein interaction|interact]] with [[ARPC4]].<ref name="pmid12451597">{{cite journal | vauthors = Millard TH, Behrendt B, Launay S, Fütterer K, Machesky LM | title = Identification and characterisation of a novel human isoform of Arp2/3 complex subunit p16-ARC/ARPC5 | journal = Cell Motil. Cytoskeleton | volume = 54 | issue = 1 | pages = 81–90 | year = 2003 | pmid = 12451597 | doi = 10.1002/cm.10087 }}</ref><ref name="pmid11162547">{{cite journal | vauthors = Zhao X, Yang Z, Qian M, Zhu X | title = Interactions among subunits of human Arp2/3 complex: p20-Arc as the hub | journal = Biochem. Biophys. Res. Commun. | volume = 280 | issue = 2 | pages = 513–7 | year = 2001 | pmid = 11162547 | doi = 10.1006/bbrc.2000.4151 }}</ref>
{{WikiDoc Sources}}
 
== References ==
{{Reflist}}
 
== Further reading ==
{{Refbegin | 2}}
* {{cite journal | vauthors = Welch MD, Iwamatsu A, Mitchison TJ | title = Actin polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes | journal = Nature | volume = 385 | issue = 6613 | pages = 265–9 | year = 1997 | pmid = 9000076 | doi = 10.1038/385265a0 }}
* {{cite journal | vauthors = Robinson RC, Turbedsky K, Kaiser DA, Marchand JB, Higgs HN, Choe S, Pollard TD | title = Crystal structure of Arp2/3 complex | journal = Science | volume = 294 | issue = 5547 | pages = 1679–84 | year = 2001 | pmid = 11721045 | doi = 10.1126/science.1066333 }}
* {{cite journal | vauthors = Gournier H, Goley ED, Niederstrasser H, Trinh T, Welch MD | title = Reconstitution of human Arp2/3 complex reveals critical roles of individual subunits in complex structure and activity | journal = Mol. Cell | volume = 8 | issue = 5 | pages = 1041–52 | year = 2001 | pmid = 11741539 | doi = 10.1016/S1097-2765(01)00393-8 }}
* {{cite journal | vauthors = Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J | title = Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides | journal = Nat. Biotechnol. | volume = 21 | issue = 5 | pages = 566–9 | year = 2003 | pmid = 12665801 | doi = 10.1038/nbt810 }}
* {{cite journal | vauthors = Singh S, Powell DW, Rane MJ, Millard TH, Trent JO, Pierce WM, Klein JB, Machesky LM, McLeish KR | title = Identification of the p16-Arc subunit of the Arp 2/3 complex as a substrate of MAPK-activated protein kinase 2 by proteomic analysis | journal = J. Biol. Chem. | volume = 278 | issue = 38 | pages = 36410–7 | year = 2003 | pmid = 12829704 | doi = 10.1074/jbc.M306428200 }}
* {{cite journal | vauthors = Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D | title = Large-scale mapping of human protein-protein interactions by mass spectrometry | journal = Mol. Syst. Biol. | volume = 3 | issue = 1 | pages = 89 | year = 2007 | pmid = 17353931 | pmc = 1847948 | doi = 10.1038/msb4100134 }}
{{Refend}}
 
== External links ==
* {{UCSC genome browser|ARPC5}}
* {{UCSC gene details|ARPC5}}
 
{{PDB Gallery|geneid=10092}}
 
 
{{Gene-1-stub}}

Latest revision as of 15:24, 26 January 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Actin-related protein 2/3 complex subunit 5 is a protein that in humans is encoded by the ARPC5 gene.[1][2][3]

Function

This gene encodes one of seven subunits of the human Arp2/3 protein complex. The Arp2/3 protein complex has been implicated in the control of actin polymerization in cells and has been conserved through evolution. The exact role of the protein encoded by this gene, the p16 subunit, has yet to be determined.[3]

Interactions

ARPC5 has been shown to interact with ARPC4.[4][5]

References

  1. ↑ Machesky LM, Reeves E, Wientjes F, Mattheyse FJ, Grogan A, Totty NF, Burlingame AL, Hsuan JJ, Segal AW (1997). "Mammalian actin-related protein 2/3 complex localizes to regions of lamellipodial protrusion and is composed of evolutionarily conserved proteins". Biochem. J. 328 ( Pt 1) (1): 105–12. PMC 1218893. PMID 9359840.
  2. ↑ Welch MD, DePace AH, Verma S, Iwamatsu A, Mitchison TJ (August 1997). "The human Arp2/3 complex is composed of evolutionarily conserved subunits and is localized to cellular regions of dynamic actin filament assembly". J. Cell Biol. 138 (2): 375–84. doi:10.1083/jcb.138.2.375. PMC 2138188. PMID 9230079.
  3. ↑ 3.0 3.1 "Entrez Gene: ARPC5 actin related protein 2/3 complex, subunit 5, 16kDa".
  4. ↑ Millard TH, Behrendt B, Launay S, Fütterer K, Machesky LM (2003). "Identification and characterisation of a novel human isoform of Arp2/3 complex subunit p16-ARC/ARPC5". Cell Motil. Cytoskeleton. 54 (1): 81–90. doi:10.1002/cm.10087. PMID 12451597.
  5. ↑ Zhao X, Yang Z, Qian M, Zhu X (2001). "Interactions among subunits of human Arp2/3 complex: p20-Arc as the hub". Biochem. Biophys. Res. Commun. 280 (2): 513–7. doi:10.1006/bbrc.2000.4151. PMID 11162547.

Further reading

  • Welch MD, Iwamatsu A, Mitchison TJ (1997). "Actin polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes". Nature. 385 (6613): 265–9. doi:10.1038/385265a0. PMID 9000076.
  • Robinson RC, Turbedsky K, Kaiser DA, Marchand JB, Higgs HN, Choe S, Pollard TD (2001). "Crystal structure of Arp2/3 complex". Science. 294 (5547): 1679–84. doi:10.1126/science.1066333. PMID 11721045.
  • Gournier H, Goley ED, Niederstrasser H, Trinh T, Welch MD (2001). "Reconstitution of human Arp2/3 complex reveals critical roles of individual subunits in complex structure and activity". Mol. Cell. 8 (5): 1041–52. doi:10.1016/S1097-2765(01)00393-8. PMID 11741539.
  • Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J (2003). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801.
  • Singh S, Powell DW, Rane MJ, Millard TH, Trent JO, Pierce WM, Klein JB, Machesky LM, McLeish KR (2003). "Identification of the p16-Arc subunit of the Arp 2/3 complex as a substrate of MAPK-activated protein kinase 2 by proteomic analysis". J. Biol. Chem. 278 (38): 36410–7. doi:10.1074/jbc.M306428200. PMID 12829704.
  • Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.

External links


Retrieved from "https://www.wikidoc.org/index.php?title=ARPC5&oldid=1530745"