ARPC3: Difference between revisions

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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
{{Infobox protein family
| update_page = yes
| Symbol = P21-Arc
| require_manual_inspection = no
| Name = ARP2/3 complex ARPC3 (21 kDa) subunit
| update_protein_box = yes
| image = PDB 1u2v EBI.jpg
| update_summary = yes
| width =
| update_citations = yes
| caption = crystal structure of arp2/3 complex with bound adp and calcium
| Pfam = PF04062
| Pfam_clan = 
| InterPro = IPR007204
| SMART =
| PROSITE =
| MEROPS =
| SCOP =
| TCDB =  
| OPM family =  
| OPM protein =  
| CAZy =  
| CDD =  
}}
}}
 
'''Actin-related protein 2/3 complex subunit 3''' is a [[protein]] that in humans is encoded by the ''ARPC3'' [[gene]].<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=Aug 1997 | pmid = 9230079 | pmc = 2138188 | doi =10.1083/jcb.138.2.375 }}</ref><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 | issue =  1| pages = 105–12 |date=Jan 1998 | pmid = 9359840 | pmc = 1218893 | doi =  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ARPC3 actin related protein 2/3 complex, subunit 3, 21kDa| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10094| accessdate = }}</ref>
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_ARPC3_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 3, 21kDa
| HGNCid = 706
| Symbol = ARPC3
| AltSymbols =; ARC21; p21-Arc
| OMIM = 604225
| ECnumber =
| Homologene = 4178
| MGIid = 1928375
| GeneAtlas_image1 = PBB_GE_ARPC3_208736_at_tn.png
  | Function = {{GNF_GO|id=GO:0005200 |text = structural constituent of cytoskeleton}}  
| Component = {{GNF_GO|id=GO:0005885 |text = Arp2/3 protein complex}} {{GNF_GO|id=GO:0030027 |text = lamellipodium}}
| Process = {{GNF_GO|id=GO:0006928 |text = cell motility}} {{GNF_GO|id=GO:0030833 |text = regulation of actin filament polymerization}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 10094
    | Hs_Ensembl = ENSG00000111229
    | Hs_RefseqProtein = NP_005710
    | Hs_RefseqmRNA = NM_005719
    | Hs_GenLoc_db =   
    | Hs_GenLoc_chr = 12
    | Hs_GenLoc_start = 109357090
    | Hs_GenLoc_end = 109372541
    | Hs_Uniprot = O15145
    | Mm_EntrezGene = 56378
    | Mm_Ensembl = ENSMUSG00000029465
    | Mm_RefseqmRNA = NM_019824
    | Mm_RefseqProtein = NP_062798
    | Mm_GenLoc_db =   
    | Mm_GenLoc_chr = 5
    | Mm_GenLoc_start = 122652495
    | Mm_GenLoc_end = 122666796
    | Mm_Uniprot = Q9JM76
  }}
}}
'''Actin related protein 2/3 complex, subunit 3, 21kDa''', also known as '''ARPC3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ARPC3 actin related protein 2/3 complex, subunit 3, 21kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10094| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
{{PBB_Summary
| section_title =  
| 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 p21 subunit, has yet to be determined.<ref name="entrez">{{cite web | title = Entrez Gene: ARPC3 actin related protein 2/3 complex, subunit 3, 21kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10094| accessdate = }}</ref>
| summary_text = This gene encodes one of seven subunits of the [[Arp2/3 complex|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 p21 subunit, has yet to be determined.<ref name="entrez"/>
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| 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  | 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  | 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  | vauthors=Marchand JB, Kaiser DA, Pollard TD, Higgs HN |title=Interaction of WASP/Scar proteins with actin and vertebrate Arp2/3 complex. |journal=Nat. Cell Biol. |volume=3 |issue= 1 |pages= 76–82 |year= 2001 |pmid= 11146629 |doi= 10.1038/35050590 }}
*{{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  | 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 }}
*{{cite journal  | author=Marchand JB, Kaiser DA, Pollard TD, Higgs HN |title=Interaction of WASP/Scar proteins with actin and vertebrate Arp2/3 complex. |journal=Nat. Cell Biol. |volume=3 |issue= 1 |pages= 76-82 |year= 2001 |pmid= 11146629 |doi= 10.1038/35050590 }}
*{{cite journal  | vauthors=Robinson RC, Turbedsky K, Kaiser DA |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 |display-authors=etal}}
*{{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  | vauthors=Gournier H, Goley ED, Niederstrasser H |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=10.1016/S1097-2765(01)00393-8 |display-authors=etal}}
*{{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  | vauthors=Andersen JS, Lyon CE, Fox AH |title=Directed proteomic analysis of the human nucleolus. |journal=Curr. Biol. |volume=12 |issue= 1 |pages= 1–11 |year= 2002 |pmid= 11790298 |doi=10.1016/S0960-9822(01)00650-9 |display-authors=etal}}
*{{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  | 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=Andersen JS, Lyon CE, Fox AH, ''et al.'' |title=Directed proteomic analysis of the human nucleolus. |journal=Curr. Biol. |volume=12 |issue= 1 |pages= 1-11 |year= 2002 |pmid= 11790298 |doi=  }}
*{{cite journal  | vauthors=Gevaert K, Goethals M, Martens L |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 |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=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=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  | vauthors=Andersen JS, Lam YW, Leung AK |title=Nucleolar proteome dynamics. |journal=Nature |volume=433 |issue= 7021 |pages= 77–83 |year= 2005 |pmid= 15635413 |doi= 10.1038/nature03207 |display-authors=etal}}
*{{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=Dubois T, Paléotti O, Mironov AA |title=Golgi-localized GAP for Cdc42 functions downstream of ARF1 to control Arp2/3 complex and F-actin dynamics. |journal=Nat. Cell Biol. |volume=7 |issue= 4 |pages= 353–64 |year= 2005 |pmid= 15793564 |doi= 10.1038/ncb1244 |display-authors=etal}}
*{{cite journal  | author=Andersen JS, Lam YW, Leung AK, ''et al.'' |title=Nucleolar proteome dynamics. |journal=Nature |volume=433 |issue= 7021 |pages= 77-83 |year= 2005 |pmid= 15635413 |doi= 10.1038/nature03207 }}
*{{cite journal  | vauthors=Stelzl U, Worm U, Lalowski M |title=A human protein-protein interaction network: a resource for annotating the proteome. |journal=Cell |volume=122 |issue= 6 |pages= 957–68 |year= 2005 |pmid= 16169070 |doi= 10.1016/j.cell.2005.08.029 |display-authors=etal}}
*{{cite journal  | author=Dubois T, Paléotti O, Mironov AA, ''et al.'' |title=Golgi-localized GAP for Cdc42 functions downstream of ARF1 to control Arp2/3 complex and F-actin dynamics. |journal=Nat. Cell Biol. |volume=7 |issue= 4 |pages= 353-64 |year= 2005 |pmid= 15793564 |doi= 10.1038/ncb1244 }}
*{{cite journal  | vauthors=Ewing RM, Chu P, Elisma F |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 |doi= 10.1038/msb4100134 | pmc=1847948 |display-authors=etal}}
*{{cite journal  | author=Stelzl U, Worm U, Lalowski M, ''et al.'' |title=A human protein-protein interaction network: a resource for annotating the proteome. |journal=Cell |volume=122 |issue= 6 |pages= 957-68 |year= 2005 |pmid= 16169070 |doi= 10.1016/j.cell.2005.08.029 }}
*{{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}}
{{refend}}


{{protein-stub}}
==External links==
{{WikiDoc Sources}}
* {{UCSC genome browser|ARPC3}}
* {{UCSC gene details|ARPC3}}
 
{{PDB Gallery|geneid=10094}}
 
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{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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{{gene-12-stub}}

Latest revision as of 18:17, 29 August 2017

VALUE_ERROR (nil)
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
ARP2/3 complex ARPC3 (21 kDa) subunit
File:PDB 1u2v EBI.jpg
crystal structure of arp2/3 complex with bound adp and calcium
Identifiers
SymbolP21-Arc
PfamPF04062
InterProIPR007204

Actin-related protein 2/3 complex subunit 3 is a protein that in humans is encoded by the ARPC3 gene.[1][2][3]

This gene encodes one of seven subunits of the 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 p21 subunit, has yet to be determined.[3]

References

  1. ↑ Welch MD, DePace AH, Verma S, Iwamatsu A, Mitchison TJ (Aug 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.
  2. ↑ Machesky LM, Reeves E, Wientjes F, Mattheyse FJ, Grogan A, Totty NF, Burlingame AL, Hsuan JJ, Segal AW (Jan 1998). "Mammalian actin-related protein 2/3 complex localizes to regions of lamellipodial protrusion and is composed of evolutionarily conserved proteins". Biochem J. 328 (1): 105–12. PMC 1218893. PMID 9359840.
  3. ↑ 3.0 3.1 "Entrez Gene: ARPC3 actin related protein 2/3 complex, subunit 3, 21kDa".

Further reading

External links



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