STRINGSTRING
A0A4Y0BW35 A0A4Y0BW35 A0A4Y0BVE0 A0A4Y0BVE0 A0A4Y0BQZ6 A0A4Y0BQZ6 A0A4Y0BQM9 A0A4Y0BQM9 A0A4Y0BPE6 A0A4Y0BPE6 A0A4Y0BMH2 A0A4Y0BMH2 A0A4Y0BLS7 A0A4Y0BLS7 A0A4Y0BHB0 A0A4Y0BHB0 A0A182RUX2 A0A182RUX2 A0A182RST5 A0A182RST5 A0A182RIZ2 A0A182RIZ2 A0A182RHF1 A0A182RHF1 A0A182RGP4 A0A182RGP4 A0A182R344 A0A182R344
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:
A0A4Y0BW35Uncharacterized protein. (739 aa)
A0A4Y0BVE0Peptide-methionine (R)-S-oxide reductase; Methionine-sulfoxide reductase that specifically reduces methionine (R)-sulfoxide back to methionine. While in many cases methionine oxidation is the result of random oxidation following oxidative stress, methionine oxidation is also a post-translational modification that takes place on specific residues. (147 aa)
A0A4Y0BQZ6Peptide-methionine (R)-S-oxide reductase; Methionine-sulfoxide reductase that specifically reduces methionine (R)-sulfoxide back to methionine. While in many cases methionine oxidation is the result of random oxidation following oxidative stress, methionine oxidation is also a post-translational modification that takes place on specific residues. (242 aa)
A0A4Y0BQM9Gelsolin-like domain-containing protein. (201 aa)
A0A4Y0BPE6BRO1 domain-containing protein. (850 aa)
A0A4Y0BMH2Uncharacterized protein. (393 aa)
A0A4Y0BLS7TPR_REGION domain-containing protein. (416 aa)
A0A4Y0BHB0Uncharacterized protein. (393 aa)
A0A182RUX2Uncharacterized protein. (163 aa)
A0A182RST5ADF-H domain-containing protein; Belongs to the actin-binding proteins ADF family. (148 aa)
A0A182RIZ2Arp2/3 complex 34 kDa subunit; Functions as actin-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. (304 aa)
A0A182RHF1Profilin; Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. (126 aa)
A0A182RGP4Uncharacterized protein. (1121 aa)
A0A182R344Uncharacterized protein. (1184 aa)
Your Current Organism:
Anopheles funestus
NCBI taxonomy Id: 62324
Other names: A. funestus
Server load: low (14%) [HD]