STRINGSTRING
gfm2 gfm2 EFL1 EFL1 gtpbp1 gtpbp1 EEF1A1-2 EEF1A1-2 LOC103480295 LOC103480295 EEF1A1 EEF1A1 mtif2 mtif2 LOC103468154 LOC103468154 LOC103472994 LOC103472994 EFTUD2 EFTUD2 eif2s3 eif2s3 hbs1l hbs1l tufm tufm gfm1 gfm1 LOC103470876 LOC103470876 GTPBP2 GTPBP2 gspt1 gspt1
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:
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. (771 aa)
EFL1Elongation factor like GTPase 1. (1106 aa)
gtpbp1GTP binding protein 1. (710 aa)
EEF1A1-2Elongation factor 1-alpha; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis. (492 aa)
LOC103480295GTP binding protein 1, like. (666 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)
mtif2Mitochondrial translational initiation factor 2. (705 aa)
LOC103468154G1 to S phase transition 1, like. (639 aa)
LOC103472994Elongation factor 1-alpha; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis. (462 aa)
EFTUD2Elongation factor Tu GTP binding domain containing 2. (389 aa)
eif2s3Eukaryotic translation initiation factor 2, subunit 3 gamma. (472 aa)
hbs1lHBS1-like translational GTPase. (721 aa)
tufmElongation factor Tu; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis. (446 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 [...] (788 aa)
LOC103470876GTP binding protein 2b. (606 aa)
GTPBP2GTP binding protein 2. (610 aa)
gspt1G1 to S phase transition 1. (486 aa)
Your Current Organism:
Poecilia reticulata
NCBI taxonomy Id: 8081
Other names: Acanthophacelus reticulata, P. reticulata, Poecilia (Acanthophacelus) reticulata, Poecilia latipinna reticulata, guppy
Server load: low (22%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.