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AIP1 protein (Saccharomyces cerevisiae) - STRING interaction network
"AIP1" - Actin cortical patch component, interacts with the actin depolymerizing factor cofilin in Saccharomyces cerevisiae
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AIP1Actin cortical patch component, interacts with the actin depolymerizing factor cofilin; required to restrict cofilin localization to cortical patches; contains WD repeats; Involved in the depolymerization of actin filaments. Enhances the filament disassembly activity of cofilin and restricts cofilin localization to cortical actin patches (615 aa)    
Predicted Functional Partners:
COF1
Cofilin, promotes actin filament depolarization in a pH-dependent manner; binds both actin monomers and filaments and severs filaments; thought to be regulated by phosphorylation at SER4; ubiquitous and essential in eukaryotes; Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. It has the ability to bind G- and F-actin in a 1-1 ratio of cofilin to actin. Binding to F-actin is regulated by tropomyosin. It is the major component of intranuclear and cytoplasmic actin rods. Required for accumulation of actin at the cell division site via depolymerizing [...] (143 aa)
     
 
  0.988
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)
     
      0.968
ACT1
Actin, structural protein involved in cell polarization, endocytosis, and other cytoskeletal functions; Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells (375 aa)
     
 
  0.924
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)
     
 
  0.890
RIM20
Protein involved in proteolytic activation of Rim101p in response to alkaline pH; PalA/AIP1/Alix family member; interaction with the ESCRT-III subunit Snf7p suggests a relationship between pH response and multivesicular body formation; Required for the proteolytic cleavage of the transcriptional repressor RIM101 in response to alkaline ambient pH, which is necessary for sporulation and invasive growth. May act as a scaffold protein that recruits the calpain-like protease RIM13 via SNF7 to its substrate RIM101 (661 aa)
           
  0.836
BRO1
Cytoplasmic class E vacuolar protein sorting (VPS) factor; coordinates deubiquitination in the multivesicular body (MVB) pathway by recruiting Doa4p to endosomes; Class E VPS protein involved in concentration and sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles. Fusion between endosomes and the vacuole will then target the cargo proteins to the vacuolar lumen. Acts as an adapter that recruits the DOA4 deubiquitinase to the endosomes, leading to deubiquitination of cargo proteins prior to the lumenal sequestration. Its association t [...] (844 aa)
           
  0.808
SRV2
CAP (cyclase-associated protein) subunit of adenylyl cyclase complex; N-terminus binds adenylyl cyclase and facilitates activation by RAS; C-terminus binds ADP-actin monomers, facilitating regulation of actin dynamics and cell morphogenesis; The N-terminal domain binds to adenylyl cyclase, thereby enabling adenylyl cyclase to be activated by upstream regulatory signals, such as Ras. The C-terminal domain is required for normal cellular morphology and growth control (526 aa)
     
 
  0.771
UBC1
Ubiquitin-conjugating enzyme that mediates selective degradation of short-lived and abnormal proteins; plays a role in vesicle biogenesis and ER-associated protein degradation (ERAD); component of the cellular stress response; Catalyzes the covalent attachment of ubiquitin to other proteins. Functions in degradation of misfolded or regulated proteins localized in the endoplasmic reticulum (ER) lumen or membrane via the ubiquitin-proteasome system. Cognate E2 conjugating enzyme for the HRD1 ubiquitin ligase complex, which is part of the ERAD-L and ERAD-M pathways responsible for the rap [...] (215 aa)
     
      0.749
CDC21
Thymidylate synthase, required for de novo biosynthesis of pyrimidine deoxyribonucleotides; expression is induced at G1/S; Thymidylate synthase required for de novo biosynthesis of pyrimidine deoxyribonucleotides. Required for both nuclear and mitochondrial DNA synthesis (304 aa)
       
      0.749
DUG1
Cys-Gly metallo-di-peptidase; forms a complex with Dug2p and Dug3p to degrade glutathione (GSH) and other peptides containing a gamma-glu-X bond in an alternative pathway to GSH degradation by gamma-glutamyl transpeptidase (Ecm38p); Catalytic component of the GSH degradosomal complex involved in the degradation of glutathione (GSH) and other peptides containing a gamma-glu-X bond. Functions also in a DUG2- DUG3-independent manner as a dipeptidase with high specificity for Cys-Gly and no activity toward tri- or tetrapeptides (481 aa)
       
      0.747
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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