STRINGSTRING
XP_505126.1 protein (Yarrowia lipolytica) - STRING interaction network
"XP_505126.1" - YALI0F07601p in Yarrowia lipolytica
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:
some 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 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:
Neighborhood
Gene Fusion
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
XP_505126.1YALI0F07601p (616 aa)    
Predicted Functional Partners:
XP_504759.1
YALI0E34111p (152 aa)
       
  0.977
XP_503497.2
YALI0E03388p (147 aa)
       
  0.936
ACT1
YALI0D08272p; Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells (375 aa)
       
  0.919
XP_503580.1
YALI0E05335p (394 aa)
       
  0.912
XP_500739.1
YALI0B10934p (464 aa)
       
  0.902
COF1
YALI0F20856p; Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. It has the ability to bind G- and F-actin in a 1-1 ratio of cofilin to actin. Binding to F-actin is regulated by tropomyosin. It is the major component of intranuclear and cytoplasmic actin rods. Required for accumulation of actin at the cell division site via depolymerizing actin at the cell ends. In association with myosin II has a role in the assembly of the contractile ring via severing actin filaments. Involved in the maintenance of the contractile ring once formed. In association [...] (153 aa)
 
 
 
  0.896
XP_505931.2
YALI0F27049p (161 aa)
     
  0.844
XP_503362.1
YALI0E00176p (1594 aa)
     
  0.831
XP_505369.1
YALI0F13343p (2084 aa)
     
  0.828
CAP2
YALI0C20735p; 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 (By similarity) (260 aa)
       
 
  0.817
Your Current Organism:
Yarrowia lipolytica
NCBI taxonomy Id: 4952
Other names: Candida lipolytica, Dipodascaceae, Mycotorula lipolytica, Y. lipolytica, Yarrowia, Yarrowia lipolytica
Server load: low (4%) [HD]