STRINGSTRING
T1HCK5_RHOPR T1HCK5_RHOPR T1HA14_RHOPR T1HA14_RHOPR T1I943_RHOPR T1I943_RHOPR R4G887_RHOPR R4G887_RHOPR R4G5G6_RHOPR R4G5G6_RHOPR T1HIQ8_RHOPR T1HIQ8_RHOPR T1HGL5_RHOPR T1HGL5_RHOPR T1HN74_RHOPR T1HN74_RHOPR T1HN75_RHOPR T1HN75_RHOPR T1HP17_RHOPR T1HP17_RHOPR T1HE43_RHOPR T1HE43_RHOPR T1I949_RHOPR T1I949_RHOPR T1IEI6_RHOPR T1IEI6_RHOPR T1IF32_RHOPR T1IF32_RHOPR T1HDJ5_RHOPR T1HDJ5_RHOPR T1HD86_RHOPR T1HD86_RHOPR T1HCP5_RHOPR T1HCP5_RHOPR T1HZF3_RHOPR T1HZF3_RHOPR T1HUR3_RHOPR T1HUR3_RHOPR
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:
T1HCK5_RHOPRWD_REPEATS_REGION domain-containing protein. (388 aa)
T1HA14_RHOPRSAC domain-containing protein. (601 aa)
T1I943_RHOPRSerine/threonine-protein phosphatase. (309 aa)
R4G887_RHOPRPutative phosphoglucosamine acetyltransferase. (200 aa)
R4G5G6_RHOPRF-actin-capping protein subunit alpha; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. (287 aa)
T1HIQ8_RHOPRF-actin-capping protein subunit beta; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. (275 aa)
T1HGL5_RHOPRUncharacterized protein. (285 aa)
T1HN74_RHOPRUncharacterized protein. (201 aa)
T1HN75_RHOPRJmjC domain-containing protein. (373 aa)
T1HP17_RHOPRUncharacterized protein. (499 aa)
T1HE43_RHOPRUncharacterized protein. (798 aa)
T1I949_RHOPRUncharacterized protein. (787 aa)
T1IEI6_RHOPRUncharacterized protein. (149 aa)
T1IF32_RHOPRUncharacterized protein. (348 aa)
T1HDJ5_RHOPRUncharacterized protein. (414 aa)
T1HD86_RHOPRUncharacterized protein. (709 aa)
T1HCP5_RHOPRRING-type domain-containing protein. (373 aa)
T1HZF3_RHOPRUncharacterized protein. (612 aa)
T1HUR3_RHOPRUncharacterized protein. (432 aa)
Your Current Organism:
Rhodnius prolixus
NCBI taxonomy Id: 13249
Other names: R. prolixus
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