STRINGSTRING
A0A182R3K2 A0A182R3K2 A0A182R5F4 A0A182R5F4 A0A182R7N3 A0A182R7N3 A0A182R918 A0A182R918 A0A182RD03 A0A182RD03 A0A182RF40 A0A182RF40 A0A182RFS2 A0A182RFS2 A0A182RHL3 A0A182RHL3 A0A182RNL3 A0A182RNL3 A0A182RQU3 A0A182RQU3 A0A182RRG9 A0A182RRG9 A0A182RSP5 A0A182RSP5 A0A182RV04 A0A182RV04 A0A182RYY4 A0A182RYY4 A0A1I8JU33 A0A1I8JU33 A0A1Y9HDE3 A0A1Y9HDE3 A0A1Y9HDJ7 A0A1Y9HDJ7 A0A453YNP6 A0A453YNP6 A0A4Y0B0G2 A0A4Y0B0G2 A0A4Y0BE07 A0A4Y0BE07 A0A4Y0BEI2 A0A4Y0BEI2 A0A4Y0BMB1 A0A4Y0BMB1 A0A4Y0BQS2 A0A4Y0BQS2 A0A4Y0BQZ6 A0A4Y0BQZ6 A0A4Y0BRV3 A0A4Y0BRV3 A0A4Y0BVE0 A0A4Y0BVE0
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:
A0A182R3K2Thioredoxin; Belongs to the thioredoxin family. (139 aa)
A0A182R5F4Uncharacterized protein. (582 aa)
A0A182R7N3Uncharacterized protein. (180 aa)
A0A182R918Superoxide dismutase [Cu-Zn]; Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Belongs to the Cu-Zn superoxide dismutase family. (153 aa)
A0A182RD03Uncharacterized protein. (73 aa)
A0A182RF40Superoxide dismutase; Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Belongs to the iron/manganese superoxide dismutase family. (118 aa)
A0A182RFS2Catalase; Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide. (504 aa)
A0A182RHL3Thioredoxin peroxidase 1. (229 aa)
A0A182RNL3Peroxiredoxin; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides; Belongs to the peroxiredoxin family. Prx5 subfamily. (194 aa)
A0A182RQU3Thioredoxin peroxidase 3. (258 aa)
A0A182RRG9Thioredoxin; Belongs to the thioredoxin family. (107 aa)
A0A182RSP5Copper-zinc superoxide dismutase 1. (223 aa)
A0A182RV04Superoxide dismutase [Cu-Zn]; Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Belongs to the Cu-Zn superoxide dismutase family. (208 aa)
A0A182RYY4Thioredoxin peroxidase 4. (221 aa)
A0A1I8JU33Copper-zinc superoxide dismutase 3. (164 aa)
A0A1Y9HDE3Superoxide dismutase [Cu-Zn]; Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Belongs to the Cu-Zn superoxide dismutase family. (172 aa)
A0A1Y9HDJ7Endoplasmic reticulum resident protein 44 precursor. (405 aa)
A0A453YNP6Thioredoxin; Belongs to the thioredoxin family. (136 aa)
A0A4Y0B0G2Thioredoxin domain-containing protein. (2031 aa)
A0A4Y0BE07Glutaredoxin domain-containing protein. (112 aa)
A0A4Y0BEI2PMSR domain-containing protein. (236 aa)
A0A4Y0BMB1CHK domain-containing protein. (488 aa)
A0A4Y0BQS2Uncharacterized protein. (667 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)
A0A4Y0BRV3DJ-1_PfpI domain-containing protein. (211 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)
Your Current Organism:
Anopheles funestus
NCBI taxonomy Id: 62324
Other names: A. funestus
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