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ARC35 protein (Saccharomyces cerevisiae) - STRING interaction network
"ARC35" - Subunit of the ARP2/3 complex, which is required for the motility and integrity of cortical actin patches in Saccharomyces cerevisiae
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Predicted Interactions
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ARC35Subunit of the ARP2/3 complex, which is required for the motility and integrity of cortical actin patches; required for cortical localization of calmodulin; Functions as actin-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the mother actin filament (By similarity) (342 aa)    
Predicted Functional Partners:
ARC18
Subunit of the ARP2/3 complex, which is required for the motility and integrity of cortical actin patches; Functions as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks (178 aa)
     
  0.999
ARC19
Subunit of the ARP2/3 complex, which is required for the motility and integrity of cortical actin patches; Functions as actin-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the mother actin filament (By similarity) (171 aa)
     
  0.999
ARC15
Subunit of the ARP2/3 complex, which is required for the motility and integrity of cortical actin patches; has mRNA binding activity; Functions as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks (154 aa)
     
  0.999
ARP2
Essential component of the Arp2/3 complex, which is a highly conserved actin nucleation center required for the motility and integrity of actin patches; involved in endocytosis and membrane growth and polarity; Functions as ATP-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the pointed end of the daughter actin filament (By similarity) (391 aa)
     
  0.999
ARP3
Essential component of the Arp2/3 complex, which is a highly conserved actin nucleation center required for the motility and integrity of actin patches; involved in endocytosis and membrane growth and polarity; Functions as ATP-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the pointed end of the daughter actin filament (By similarity) (449 aa)
     
  0.999
ARC40
Subunit of the ARP2/3 complex, which is required for the motility and integrity of cortical actin patches; Functions as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks (384 aa)
     
  0.994
CAP1
Alpha subunit of the capping protein (CP) heterodimer (Cap1p and Cap2p) which binds to the barbed ends of actin filaments preventing further polymerization; localized predominantly to cortical actin patches; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments (268 aa)
     
 
  0.967
LAS17
Actin assembly factor, activates the Arp2/3 protein complex that nucleates branched actin filaments; localizes with the Arp2/3 complex to actin patches; homolog of the human Wiskott-Aldrich syndrome protein (WASP) (633 aa)
       
  0.955
CAP2
Beta subunit of the capping protein (CP) heterodimer (Cap1p and Cap2p) which binds to the barbed ends of actin filaments preventing further polymerization; localized predominantly to cortical actin patches; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments (287 aa)
     
 
  0.952
MYO5
One of two type I myosins; contains proline-rich tail homology 2 (TH2) and SH3 domains; MYO5 deletion has little effect on growth, but myo3 myo5 double deletion causes severe defects in growth and actin cytoskeleton organization; One of two redundant type-I myosins implicated in the organization of the actin cytoskeleton. Required for proper actin cytoskeleton polarization and for the internalization step in endocytosis. At the cell cortex, assembles in patch-like structures together with proteins from the actin-polymerizing machinery and promotes actin assembly. Functions redundantly [...] (1219 aa)
       
 
  0.936
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: Candida robusta, Pachytichospora, S. cerevisiae, Saccharomyces, Saccharomyces capensis, Saccharomyces cerevisiae, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, lager beer yeast, yeast
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