• Version:
  • 11.0 [archived version]
STRINGSTRING
PAK4 PAK4 CAPZA2 CAPZA2 TMOD4 TMOD4 CAPZA1 CAPZA1 CAPZB CAPZB LRRC16A LRRC16A SLC16A9 SLC16A9 CD2AP CD2AP MYO1C MYO1C SLC2A9 SLC2A9 MYO1A MYO1A
"LRRC16A" - F-actin-uncapping protein LRRC16A in Homo sapiens
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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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:
some 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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LRRC16AF-actin-uncapping protein LRRC16A; Cell membrane-cytoskeleton-associated protein that plays a role in the regulation of actin polymerization at the barbed end of actin filaments. Prevents F-actin heterodimeric capping protein (CP) activity at the leading edges of migrating cells, and hence generates uncapped barbed ends and enhances actin polymerization, however, seems unable to nucleate filaments. Plays a role in lamellipodial protrusion formations and cell migration; Belongs to the CARMIL family (1371 aa)    
Predicted Functional Partners:
CAPZA2
F-actin-capping protein subunit alpha-2; 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)
     
  0.991
CAPZB
F-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. Plays a role in the regulation of cell morphology and cytoskeletal organization (301 aa)
       
  0.989
CAPZA1
F-actin-capping protein subunit alpha-1; 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. May play a role in the formation of epithelial cell junctions (286 aa)
     
  0.913
TMOD4
Tropomodulin-4; Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton; Tropomodulins (345 aa)
           
  0.903
CD2AP
CD2-associated protein; Seems to act as an adapter protein between membrane proteins and the actin cytoskeleton. In collaboration with CBLC, modulates the rate of RET turnover and may act as regulatory checkpoint that limits the potency of GDNF on neuronal survival. Controls CBLC function, converting it from an inhibitor to a promoter of RET degradation (By similarity). May play a role in receptor clustering and cytoskeletal polarity in the junction between T-cell and antigen-presenting cell (By similarity). May anchor the podocyte slit diaphragm to the actin cytoskeleton in renal glom [...] (639 aa)
     
 
  0.844
SLC16A9
Monocarboxylate transporter 9; Proton-linked monocarboxylate transporter. May catalyze the transport of monocarboxylates across the plasma membrane; Solute carriers (509 aa)
           
  0.839
MYO1C
Unconventional myosin-Ic; Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments. Involved in glucose transporter recycling in response to insulin by regulating movement of intracellular GLUT4-containing vesicles to the plasma membrane. Component of the hair cell’s (the sensory cells of the inner ear) adaptation-motor complex. Acts as a mediator of adaptation of mechanoelectrical transduction in st [...] (1063 aa)
         
  0.830
MYO1A
Unconventional myosin-Ia; Involved in directing the movement of organelles along actin filaments; Myosins, class I (1043 aa)
         
  0.822
PAK4
Serine/threonine-protein kinase PAK 4; Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell migration, growth, proliferation or cell survival. Activation by various effectors including growth factor receptors or active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Phosphorylates and inactivates the protein phosphatase SSH1, leading to increased inhibitory phosphorylation of the actin binding/depolymerizing factor cofilin [...] (591 aa)
       
 
  0.815
SLC2A9
Solute carrier family 2, facilitated glucose transporter member 9; Transport urate and fructose. May have a role in the urate reabsorption by proximal tubules. Also transports glucose at low rate; Solute carriers (540 aa)
           
  0.760
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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