STRINGSTRING
EIF2S3 EIF2S3 EEF1A2 EEF1A2 GFM1 GFM1 EEF2 EEF2 GFM2 GFM2 EFTUD2 EFTUD2 GUF1 GUF1 EEF1A1 EEF1A1 GSPT1 GSPT1 LOC108636537 LOC108636537 ENSCHIP00000003677 ENSCHIP00000003677 EIF5B EIF5B TUFM TUFM LOC108634721 LOC108634721
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:
EIF2S3Tr-type G domain-containing protein. (472 aa)
EEF1A2Elongation factor 1-alpha; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis. (463 aa)
GFM1Elongation 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. Does not mediate the disassembly of ribosomes from messenger RNA at the termination of mito [...] (753 aa)
EEF2Tr-type G domain-containing protein. (858 aa)
GFM2Ribosome-releasing factor 2, mitochondrial; Mitochondrial GTPase that mediates the disassembly of ribosomes from messenger RNA at the termination of mitochondrial protein biosynthesis. Acts in collaboration with MRRF. GTP hydrolysis follows the ribosome disassembly and probably occurs on the ribosome large subunit. Not involved in the GTP-dependent ribosomal translocation step during translation elongation; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily. (777 aa)
EFTUD2Elongation factor Tu GTP binding domain containing 2. (972 aa)
GUF1Translation factor GUF1, 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. (669 aa)
EEF1A1Elongation factor 1-alpha; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis. (462 aa)
GSPT1G1 to S phase transition 1. (638 aa)
LOC108636537Elongation factor 1-alpha; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis. (441 aa)
ENSCHIP00000003677Tr-type G domain-containing protein. (438 aa)
EIF5BEukaryotic translation initiation factor 5B. (1220 aa)
TUFMElongation factor Tu; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis. (452 aa)
LOC108634721Tr-type G domain-containing protein. (473 aa)
Your Current Organism:
Capra hircus
NCBI taxonomy Id: 9925
Other names: African dwarf goat, African dwarf goats, C. hircus, Capra aegagrus hircus, domestic goat, goat, goats
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