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EPS8 EPS8 CAPZA2 CAPZA2 CAPZB CAPZB GSN GSN CAPG CAPG TWF2 TWF2 CAPZA1 CAPZA1 ENSPCOP00000009506 ENSPCOP00000009506 SCIN SCIN ADD3 ADD3 ADD1 ADD1 AVIL AVIL TRIOBP TRIOBP NCK2 NCK2 NCK1 NCK1 VIL1 VIL1 SVIL SVIL ADD2 ADD2 VILL VILL ENSPCOP00000022537 ENSPCOP00000022537 FLII FLII
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:
EPS8Epidermal growth factor receptor pathway substrate 8. (711 aa)
CAPZA2F-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)
CAPZBF-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. (301 aa)
GSNGelsolin. (778 aa)
CAPGCapping actin protein, gelsolin like. (348 aa)
TWF2Twinfilin actin binding protein 2. (349 aa)
CAPZA1F-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. (286 aa)
ENSPCOP00000009506Uncharacterized protein. (103 aa)
SCINScinderin. (589 aa)
ADD3Adducin 3. (706 aa)
ADD1Adducin 1. (751 aa)
AVILAdvillin. (818 aa)
TRIOBPPH domain-containing protein. (647 aa)
NCK2Cytoplasmic protein. (380 aa)
NCK1Cytoplasmic protein. (377 aa)
VIL1Villin 1. (827 aa)
SVILSupervillin. (2078 aa)
ADD2Adducin 2. (725 aa)
VILLVillin like. (844 aa)
ENSPCOP00000022537F-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. (167 aa)
FLIIFLII actin remodeling protein. (1268 aa)
Your Current Organism:
Propithecus coquereli
NCBI taxonomy Id: 379532
Other names: P. coquereli, Propithecus verreauxi coquereli
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