STRINGSTRING
RALB RALB EXOC2 EXOC2 EXOC8 EXOC8 RALBP1 RALBP1 RALGDS RALGDS RGL2 RGL2 PLD1 PLD1 RGL1 RGL1 RALA RALA PLD2 PLD2 RAC2 RAC2
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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RALBRas-related protein Ral-B; Multifunctional GTPase involved in a variety of cellular processes including gene expression, cell migration, cell proliferation, oncogenic transformation and membrane trafficking. Accomplishes its multiple functions by interacting with distinct downstream effectors. Acts as a GTP sensor for GTP-dependent exocytosis of dense core vesicles (By similarity). Required both to stabilize the assembly of the exocyst complex and to localize functional exocyst complexes to the leading edge of migrating cells (By similarity). Required for suppression of apoptosis. In l [...] (206 aa)    
Predicted Functional Partners:
EXOC2
Exocyst complex component 2; Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane; Belongs to the SEC5 family.
   
 0.999
EXOC8
Exocyst complex component 8; Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane; Belongs to the EXO84 family.
   
 
 0.999
RALBP1
RalA-binding protein 1; Can activate specifically hydrolysis of GTP bound to RAC1 and CDC42, but not RALA. Mediates ATP-dependent transport of S-(2,4- dinitrophenyl)-glutathione (DNP-SG) and doxorubicin (DOX) and is the major ATP-dependent transporter of glutathione conjugates of electrophiles (GS-E) and DOX in erythrocytes. Can catalyze transport of glutathione conjugates and xenobiotics, and may contribute to the multidrug resistance phenomenon. Serves as a scaffold protein that brings together proteins forming an endocytotic complex during interphase and also with CDK1 to switch off [...]
   
 0.999
RALGDS
Ral guanine nucleotide dissociation stimulator; Stimulates the dissociation of GDP from the Ras-related RalA and RalB GTPases which allows GTP binding and activation of the GTPases. Interacts and acts as an effector molecule for R-Ras, H-Ras, K-Ras, and Rap.
   
 0.996
RGL2
Ral guanine nucleotide dissociation stimulator-like 2; Probable guanine nucleotide exchange factor. Putative effector of Ras and/or Rap. Associates with the GTP-bound form of Rap 1A and H-Ras in vitro (By similarity).
   
 0.972
PLD1
Phospholipase D1; Implicated as a critical step in numerous cellular pathways, including signal transduction, membrane trafficking, and the regulation of mitosis. May be involved in the regulation of perinuclear intravesicular membrane traffic (By similarity).
   
 0.964
RGL1
Ral guanine nucleotide dissociation stimulator-like 1; Probable guanine nucleotide exchange factor.
   
 0.960
RALA
Ras-related protein Ral-A; Multifunctional GTPase involved in a variety of cellular processes including gene expression, cell migration, cell proliferation, oncogenic transformation and membrane trafficking. Accomplishes its multiple functions by interacting with distinct downstream effectors. Acts as a GTP sensor for GTP-dependent exocytosis of dense core vesicles. The RALA-exocyst complex regulates integrin- dependent membrane raft exocytosis and growth signaling. Key regulator of LPAR1 signaling and competes with GRK2 for binding to LPAR1 thus affecting the signaling properties of t [...]
  
 
0.938
PLD2
Phospholipase D2; May have a role in signal-induced cytoskeletal regulation and/or endocytosis.
    
 0.926
RAC2
Ras-related C3 botulinum toxin substrate 2; Plasma membrane-associated small GTPase which cycles between an active GTP-bound and inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses, such as secretory processes, phagocytose of apoptotic cells and epithelial cell polarization. Augments the production of reactive oxygen species (ROS) by NADPH oxidase.
   
0.924
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, human, man
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