STRINGSTRING
A0EDT0_PARTE A0EDT0_PARTE A0EFI6_PARTE A0EFI6_PARTE A0BL60_PARTE A0BL60_PARTE A0BN83_PARTE A0BN83_PARTE A0C641_PARTE A0C641_PARTE A0C9U4_PARTE A0C9U4_PARTE A0CAG8_PARTE A0CAG8_PARTE A0CDU0_PARTE A0CDU0_PARTE A0CEH0_PARTE A0CEH0_PARTE A0CT20_PARTE A0CT20_PARTE A0CTP4_PARTE A0CTP4_PARTE A0D5J3_PARTE A0D5J3_PARTE A0DF70_PARTE A0DF70_PARTE A0DGW7_PARTE A0DGW7_PARTE A0DJ56_PARTE A0DJ56_PARTE A0DPV3_PARTE A0DPV3_PARTE EF-1a EF-1a A0DRB1_PARTE A0DRB1_PARTE A0DW80_PARTE A0DW80_PARTE A0ED84_PARTE A0ED84_PARTE
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:
A0EDT0_PARTEElongation factor 1-alpha; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis. (438 aa)
A0EFI6_PARTEElongation factor Tu; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis. (471 aa)
A0BL60_PARTEElongation factor 1-alpha; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis. (433 aa)
A0BN83_PARTETr-type G domain-containing protein. (357 aa)
A0C641_PARTETr-type G domain-containing protein. (836 aa)
A0C9U4_PARTEElongation 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. (721 aa)
A0CAG8_PARTETr-type G domain-containing protein. (836 aa)
A0CDU0_PARTETr-type G domain-containing protein. (646 aa)
A0CEH0_PARTETr-type G domain-containing protein. (830 aa)
A0CT20_PARTETr-type G domain-containing protein. (265 aa)
A0CTP4_PARTETr-type G domain-containing protein. (211 aa)
A0D5J3_PARTETr-type G domain-containing protein. (784 aa)
A0DF70_PARTETr-type G domain-containing protein. (646 aa)
A0DGW7_PARTEElongation 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. (721 aa)
A0DJ56_PARTETr-type G domain-containing protein. (324 aa)
A0DPV3_PARTEElongation factor 1-alpha; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis. (437 aa)
EF-1aElongation factor 1-alpha; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis. (437 aa)
A0DRB1_PARTEUncharacterized protein. (1348 aa)
A0DW80_PARTETr-type G domain-containing protein. (185 aa)
A0ED84_PARTETranslation 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. (606 aa)
Your Current Organism:
Paramecium tetraurelia
NCBI taxonomy Id: 5888
Other names: P. tetraurelia, Paramecium aurelia syngen 4
Server load: low (24%) [HD]