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A0A2I2F0H4 A0A2I2F0H4 A0A2I2F0H8 A0A2I2F0H8 A0A2I2F4N9 A0A2I2F4N9 A0A2I2F952 A0A2I2F952 A0A2I2F9J6 A0A2I2F9J6 A0A2I2FBB9 A0A2I2FBB9 A0A2I2FDR1 A0A2I2FDR1 A0A2I2FG21 A0A2I2FG21 A0A2I2FLF8 A0A2I2FLF8 A0A2I2FLI7 A0A2I2FLI7 A0A2I2FMY1 A0A2I2FMY1 A0A2I2FN57 A0A2I2FN57 A0A2I2FNP8 A0A2I2FNP8
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:
A0A2I2F0H4Component of IIS longevity pathway SMK-1-domain-containing protein. (683 aa)
A0A2I2F0H8Leucine carboxyl methyltransferase 1; Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha- leucine ester residues; Belongs to the methyltransferase superfamily. LCMT family. (386 aa)
A0A2I2F4N9Serine/threonine-protein phosphatase. (329 aa)
A0A2I2F952Protein phosphatase PP2A regulatory subunit B; Belongs to the phosphatase 2A regulatory subunit B family. (473 aa)
A0A2I2F9J6Serine/threonine-protein phosphatase 2A activator; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. (424 aa)
A0A2I2FBB9Metallo-dependent phosphatase. (336 aa)
A0A2I2FDR1Uncharacterized protein. (447 aa)
A0A2I2FG21Serine/threonine-protein phosphatase 2A activator; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. (474 aa)
A0A2I2FLF8SET domain-containing protein. (574 aa)
A0A2I2FLI7Protein phosphatase methylesterase 1; Demethylates proteins that have been reversibly carboxymethylated. (463 aa)
A0A2I2FMY1Protein phosphatase PP2A regulatory subunit A. (616 aa)
A0A2I2FN57Serine/threonine-protein phosphatase. (432 aa)
A0A2I2FNP8Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit; The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment. (651 aa)
Your Current Organism:
Aspergillus candidus
NCBI taxonomy Id: 41067
Other names: A. candidus, CBS 566.65
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