STRINGSTRING
L798_10587 L798_10587 L798_14801 L798_14801 L798_15788 L798_15788 L798_01277 L798_01277 L798_11753 L798_11753 L798_14802 L798_14802 L798_05096 L798_05096 L798_05129 L798_05129 L798_03981 L798_03981 L798_07817 L798_07817 L798_12386 L798_12386 L798_07586 L798_07586 L798_03699 L798_03699 L798_01310 L798_01310 L798_00629 L798_00629 L798_07111 L798_07111 L798_14598 L798_14598 L798_05054 L798_05054 L798_05044 L798_05044 L798_05548 L798_05548 L798_11237 L798_11237 L798_06489 L798_06489 L798_11828 L798_11828 L798_11228 L798_11228 L798_12353 L798_12353
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:
L798_10587F-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. (294 aa)
L798_14801Apoptosis 1 inhibitor. (109 aa)
L798_15788Dual specificity protein phosphatase 12. (339 aa)
L798_01277Apoptosis inhibitor IAP. (392 aa)
L798_11753Serine/threonine-protein phosphatase 6 regulatory subunit 3. (938 aa)
L798_14802Apoptosis inhibitor 3. (96 aa)
L798_05096E3 ubiquitin-protein ligase HUWE1. (3312 aa)
L798_05129E3 ubiquitin-protein ligase HUWE1. (713 aa)
L798_03981F-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. (276 aa)
L798_07817Serine/threonine-protein phosphatase. (303 aa)
L798_12386Tyrosine-protein phosphatase non-receptor type 2. (476 aa)
L798_07586Menin. (637 aa)
L798_03699Striatin-3. (731 aa)
L798_01310E3 ubiquitin-protein ligase parkin; Functions within a multiprotein E3 ubiquitin ligase complex, catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins. (475 aa)
L798_00629Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6. (390 aa)
L798_07111Ubiquitin carboxyl-terminal hydrolase. (810 aa)
L798_14598Ras suppressor protein 1. (286 aa)
L798_05054Phosphatidylinositide phosphatase SAC1-B. (589 aa)
L798_05044Ras-responsive element-binding protein 1. (2119 aa)
L798_05548LIM domain-containing protein. (341 aa)
L798_11237Uncharacterized protein. (792 aa)
L798_06489Apoptosis 1 inhibitor. (396 aa)
L798_11828F-box-like/WD repeat-containing protein TBL1XR1. (495 aa)
L798_11228N-acetyltransferase 9. (199 aa)
L798_12353EF-hand domain-containing protein. (501 aa)
Your Current Organism:
Zootermopsis nevadensis
NCBI taxonomy Id: 136037
Other names: Z. nevadensis
Server load: low (14%) [HD]