STRINGSTRING
STRING protein interaction network
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
secGPutative protein transport protein SEC61 subunit beta homolog; Involved in protein export. The function of the beta subunit is unknown, but it may be involved in stabilization of the trimeric complex. (54 aa)    
Predicted Functional Partners:
MCP_2874
Amidohydrolase family protein.
       0.581
MCP_2873
Putative universal stress protein.
       0.531
MCP_2872
Conserved hypothetical protein; Contains two CBS domains (IPR000644).
       0.495
secE
Protein transport protein SEC61 gamma subunit homolog; Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
    
 
 0.479
secY
Protein transport protein SEC61 subunit alpha homolog; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
    
 
 0.479
Your Current Organism:
Methanocella paludicola
NCBI taxonomy Id: 304371
Other names: M. paludicola SANAE, Methanocella paludicola SANAE, methanogenic archaeon SANAE, methanogenic archaeon str. SANAE, methanogenic archaeon strain SANAE
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.