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MTC5 protein (Saccharomyces cerevisiae) - STRING interaction network
"MTC5" - Subunit of the SEA in Saccharomyces cerevisiae
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Predicted Interactions
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protein homology
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MTC5Subunit of the SEA (Seh1-associated) complex, a coatomer-related complex that associates dynamically with the vacuole; has N-terminal WD-40 repeats and a C-terminal RING motif; mtc5 is synthetically sick with cdc13-1; Component of the SEA complex which coats the vacuolar membrane and is involved in intracellular trafficking, autophagy, response to nitrogen starvation, and amino acid biogenesis. May be involved in telomere capping (1148 aa)    
Predicted Functional Partners:
RTC1
Subunit of the SEA (Seh1-associated) complex, a coatomer-related complex that associates dynamically with the vacuole; null mutation suppresses cdc13-1 temperature sensitivity; has N-terminal WD-40 repeats and a C-terminal RING motif; Component of the SEA complex which coats the vacuolar membrane and is involved in intracellular trafficking, autophagy, response to nitrogen starvation, and amino acid biogenesis. May be involved in a process influencing telomere capping (1341 aa)
       
  0.994
SEA4
Subunit of the SEA (Seh1-associated) complex, a coatomer-related complex that associates dynamically with the vacuole; has an N-terminal beta-propeller fold and a C-terminal RING motif; promoter contains multiple GCN4 binding sites; Component of the SEA complex which coats the vacuolar membrane and is involved in intracellular trafficking, autophagy, response to nitrogen starvation, and amino acid biogenesis (1038 aa)
       
  0.994
IML1
Subunit of both the SEA (Seh1-associated) and Iml1p complexes; SEA complex is a coatomer-related complex that associates dynamically with the vacuole; Iml1p complex (Iml1p-Npr2p-Npr3p) is required for non-nitrogen-starvation (NNS)-induced autophagy; /.../ized to either pre-autophagosomal structures (PAS) or non-PAS structures during NNS-induced autophagy; has an N-terminal CDC48-like domain (RANS) required for NNS-induced autophagy and a C-terminal DEP domain; Component of the SEA complex which coats the vacuolar membrane and is involved in intracellular trafficking, autophagy, respons [...] (1584 aa)
     
  0.994
SEH1
Nuclear pore protein of the conserved Nup84p complex (Nup84p, Nup85p, Nup120p, Nup145p, and Seh1p); part of the SEA (Seh1-associated) complex, a coatamer-related complex that associates dynamically with the vacuole; homologous to Sec13p; the Nup84 s /.../lex has a role in transcription elongation; Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Involved in nuclear pol [...] (349 aa)
       
  0.977
SEC13
Component of the Nup84 nuclear pore sub-complex, the Sec13p-Sec31p complex of the COPII vesicle coat, and the SEA (Seh1-associated) complex; required for vesicle formation in ER to Golgi transport and nuclear pore complex organization; the Nup84 sub /.../x has a role in transcription elongation; Functions as a component of the nuclear pore complex (NPC) and the COPII coat. It is one of 5 proteins constituting the COPII coat, which is involved in anterograde (ER to Golgi) double- membrane transport vesicle formation. First the small GTPase SAR1, activated by and binding to the integral [...] (297 aa)
       
  0.959
NPR2
Subunit of SEA (Seh1-associated), Npr2/3, and Iml1p complexes; Npr2/3 complex mediates downregulation of TORC1 activity upon amino acid limitation; SEA complex is a coatomer-related complex that associates dynamically with the vacuole; Iml1p complex /.../p-Npr2p-Npr3p) is required for non-nitrogen-starvation (NNS)-induced autophagy; Iml1p interacts primarily with phosphorylated Npr2p; homolog of human NPRL2; target of Grr1p; required for growth on urea and proline; Component of the SEA complex which coats the vacuolar membrane and is involved in intracellular trafficking, autophagy, re [...] (615 aa)
       
  0.954
NPR3
Subunit of SEA (Seh1-associated), Npr2/3, and Iml1p complexes; Npr2/3 complex mediates downregulation of TORC1 activity upon amino acid limitation; SEA complex is a coatomer-related complex that associates dynamically with the vacuole; Iml1p complex /.../p-Npr2p-Npr3p) is required for non-nitrogen-starvation (NNS)-induced autophagy; required for Npr2p phosphorylation and Iml1p-Npr2p interaction; null mutant shows delayed meiotic DNA replication and double-strand break repair; Component of the SEA complex which coats the vacuolar membrane and is involved in intracellular trafficking, au [...] (1146 aa)
       
  0.927
TRP1
Phosphoribosylanthranilate isomerase that catalyzes the third step in tryptophan biosynthesis; in 2004, the sequence of TRP1 from strain S228C was updated by changing the previously annotated internal STOP (TAA) to serine (TCA) (224 aa)
       
      0.454
SLM4
Component of the EGO complex, which is involved in the regulation of microautophagy, and of the GSE complex, which is required for proper sorting of amino acid permease Gap1p; gene exhibits synthetic genetic interaction with MSS4; Component of the GSE complex, a GTPase complex required for intracellular sorting of GAP1 out of the endosome. Component of the EGO complex, a complex involved in the regulation of microautophagy (162 aa)
       
 
  0.441
VAM6
Vacuolar protein that plays a critical role in the tethering steps of vacuolar membrane fusion by facilitating guanine nucleotide exchange on small guanosine triphosphatase Ypt7p; Required for vacuolar assembly. Acts as component of the HOPS complex that acts during the docking stage of vacuole fusion. HOPS is an effector for the vacuolar Rab GTPase YPT7 and is required for vacuolar SNARE complex assembly. It remains bound to SNARE complexes after vacuole fusion (1049 aa)
       
 
  0.402
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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