STRINGSTRING
C5167_032345 C5167_032345 C5167_017437 C5167_017437 C5167_012849 C5167_012849 C5167_013128 C5167_013128 C5167_013804 C5167_013804 C5167_004372 C5167_004372 C5167_006028 C5167_006028 C5167_005253 C5167_005253 C5167_024256 C5167_024256 C5167_024361 C5167_024361 C5167_023525 C5167_023525 C5167_024530 C5167_024530 C5167_025782 C5167_025782 C5167_008633 C5167_008633 C5167_008959 C5167_008959 C5167_032111 C5167_032111 C5167_048822 C5167_048822 C5167_050939 C5167_050939 C5167_050082 C5167_050082 C5167_049899 C5167_049899 C5167_000397 C5167_000397 C5167_001387 C5167_001387 C5167_039535 C5167_039535 C5167_001611 C5167_001611 C5167_045632 C5167_045632 C5167_043299 C5167_043299 C5167_043607 C5167_043607 C5167_044930 C5167_044930 C5167_045863 C5167_045863 C5167_043747 C5167_043747 C5167_045630 C5167_045630
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:
C5167_032345Elongation factor G, mitochondrial; Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. (812 aa)
C5167_017437Tr-type G domain-containing protein. (1111 aa)
C5167_012849Elongation factor G, chloroplastic; Chloroplast-localized elongation factor EF-G involved in protein synthesis in plastids. Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl- tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. (704 aa)
C5167_013128Translation factor GUF1 homolog, mitochondrial; Promotes mitochondrial protein synthesis. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Binds to mitochondrial ribosomes in a GTP-dependent manner. (722 aa)
C5167_013804EFG_C domain-containing protein. (61 aa)
C5167_004372Tr-type G domain-containing protein. (1014 aa)
C5167_006028Uncharacterized protein. (195 aa)
C5167_005253Tr-type G domain-containing protein. (843 aa)
C5167_024256Tr-type G domain-containing protein. (991 aa)
C5167_024361Translation factor GUF1 homolog, mitochondrial; Promotes mitochondrial protein synthesis. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Binds to mitochondrial ribosomes in a GTP-dependent manner. (620 aa)
C5167_023525Tr-type G domain-containing protein. (843 aa)
C5167_024530Uncharacterized protein. (159 aa)
C5167_025782EFG_C domain-containing protein. (140 aa)
C5167_008633Uncharacterized protein. (144 aa)
C5167_008959Tr-type G domain-containing protein. (677 aa)
C5167_032111Tr-type G domain-containing protein. (991 aa)
C5167_048822Elongation factor G, chloroplastic; Chloroplast-localized elongation factor EF-G involved in protein synthesis in plastids. Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl- tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. (704 aa)
C5167_050939Tr-type G domain-containing protein. (843 aa)
C5167_050082EFG_II domain-containing protein. (212 aa)
C5167_049899Elongation factor G, mitochondrial; Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. (802 aa)
C5167_000397Tr-type G domain-containing protein. (843 aa)
C5167_001387EFG_C domain-containing protein. (612 aa)
C5167_039535Tr-type G domain-containing protein. (677 aa)
C5167_001611Tr-type G domain-containing protein. (684 aa)
C5167_045632Uncharacterized protein. (261 aa)
C5167_043299EFG_IV domain-containing protein. (594 aa)
C5167_043607Tr-type G domain-containing protein. (843 aa)
C5167_044930Tr-type G domain-containing protein. (843 aa)
C5167_045863Tr-type G domain-containing protein. (684 aa)
C5167_043747Uncharacterized protein. (147 aa)
C5167_045630Uncharacterized protein. (478 aa)
Your Current Organism:
Papaver somniferum
NCBI taxonomy Id: 3469
Other names: P. somniferum, Papaver somniferum L., Papaver somniferum convar. nigrum (Hayne) Alef., opium poppy
Server load: low (30%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.