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TIM22 protein (Saccharomyces cerevisiae) - STRING interaction network
"TIM22" - Essential core component of the mitochondrial TIM22 complex involved in insertion of polytopic proteins into the inner membrane in Saccharomyces cerevisiae
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TIM22Essential core component of the mitochondrial TIM22 complex involved in insertion of polytopic proteins into the inner membrane; forms the channel through which proteins are imported; Essential core component of the TIM22 complex, a complex that mediates the import and insertion of multi-pass transmembrane proteins, such as mitochondrial carrier family members, into the mitochondrial inner membrane. In the TIM22 complex, it constitutes the voltage-activated and signal-gated channel. Forms a twin-pore translocase that uses the membrane potential as external driving force in 2 voltage-de [...] (207 aa)    
Predicted Functional Partners:
TIM54
Component of the mitochondrial TIM22 complex involved in insertion of polytopic proteins into the inner membrane; Essential component of the TIM22 complex, a complex that mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. The TIM22 complex forms a twin-pore translocase that uses the membrane potential as external driving force. Its precise function within the TIM22 complex is unclear (478 aa)
     
  0.999
TIM23
Essential component of the Translocase of the Inner Mitochondrial membrane (TIM23 complex); involved in protein import into mitochondrial matrix and inner membrane; with Tim17p, contributes to architecture and function of the import channel; Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane (222 aa)
     
  0.999
TIM10
Essential protein of the mitochondrial intermembrane space, forms a complex with Tim9p (TIM10 complex) that delivers hydrophobic proteins to the TIM22 complex for insertion into the inner membrane; Mitochondrial intermembrane chaperone that participates in the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from ag [...] (93 aa)
     
  0.999
TIM12
Essential protein of the inner mitochondrial membrane, peripherally localized; component of the TIM22 complex, which is a twin-pore translocase that mediates insertion of numerous multispanning inner membrane proteins; Essential component of the TIM22 complex, a complex that mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. The TIM22 complex forms a twin-pore translocase that uses the membrane potential as external driving force. In the TIM22 complex, it acts as a docking point for the soluble TIM9-TIM10 heterohexamer that gui [...] (109 aa)
     
  0.998
TOM22
Component of the TOM (Translocase of Outer Membrane) complex; responsible for initial import of mitochondrially directed proteins; mediates interaction between TOM and TIM complexes and acts as a receptor for precursor proteins; Central component of the TOM (translocase of outer membrane) receptor complex responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins. Together with TOM20 and TOM70 functions as the transit peptide receptor at the surface of the mitochondrion outer membrane and facilitates the movement of preproteins into the TOM [...] (152 aa)
     
  0.998
TIM18
Component of the mitochondrial TIM22 complex involved in insertion of polytopic proteins into the inner membrane; may mediate assembly or stability of the complex; Component of the TIM22 complex, a complex that mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. The TIM22 complex forms a twin- pore translocase that uses the membrane potential as external driving force. Its role in the complex is unclear but it may be involved in the assembly and stabilization of the TIM22 complex (192 aa)
       
  0.998
TIM13
Mitochondrial intermembrane space protein, forms a complex with Tim8p that delivers a subset of hydrophobic proteins to the TIM22 complex for insertion into the inner membrane; Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and gu [...] (105 aa)
     
  0.998
TIM9
Essential protein of the mitochondrial intermembrane space, forms a complex with Tim10p (TIM10 complex) that delivers hydrophobic proteins to the TIM22 complex for insertion into the inner membrane; Mitochondrial intermembrane chaperone that participates in the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from a [...] (87 aa)
     
  0.998
TOM40
Component of the TOM (translocase of outer membrane) complex responsible for recognition and initial import steps for all mitochondrially directed proteins; constitutes the core element of the protein conducting pore; Channel-forming protein essential for import of protein precursors into mitochondria (387 aa)
     
 
  0.995
TIM44
Essential component of the Translocase of the Inner Mitochondrial membrane (TIM23 complex); tethers the import motor and regulatory factors (PAM complex) to the translocation channel (Tim23p-Tim17p core complex); Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. Recruits mitochondrial HSP70 and its co- chaperone (MGE1) to drive protein translocation into the matrix using ATP as an energy source (431 aa)
     
  0.995
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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