STRINGSTRING
STRING protein interaction network
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:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
ttll-5Tubulin polyglutamylase ttll-5; Polyglutamylase which preferentially modifies alpha-tubulin (By similarity). Involved in the side-chain initiation step of the polyglutamylation reaction rather than in the elongation step (By similarity). Together with ttll-4 and ttll-11, required for male mating. Probably by regulating microtubule stability via the glutamylation of tubulin, negatively regulates axon regrowth after injury in PLM neurons. (730 aa)    
Predicted Functional Partners:
ccpp-1
Cytosolic carboxypeptidase 1; Catalyzes the deglutamylation of polyglutamate side chains generated by post-translational polyglutamylation of proteins such as tubulins (Probable). Via the deglutamylation of tubulin, regulates the localization and velocity of kinesin motors and the structural integrity of microtubules in sensory cilia. In male CEM sensory neurons, regulates the cilia release of bioactive extracellular vesicles. Also regulates microtubule dynamics in uterine muscle cells.
  
  
 0.945
ttll-12
Tubulin--tyrosine ligase-like protein 12; Regulates microtubule dynamics in uterine muscle cells. Belongs to the tubulin--tyrosine ligase family.
      
 0.905
dcap-1
mRNA_decap_C domain-containing protein.
    
 
 0.899
dcap-2
mRNA-decapping enzyme 2; RNA-decapping enzyme although it does not bind cap. May contribute to gene regulation in multiple RNA pathways including monomethylguanosine- and trimethylguanosine-capped RNAs. Belongs to the Nudix hydrolase family. DCP2 subfamily.
   
 
 0.888
ccpp-6
Cytosolic carboxypeptidase 6; Metallocarboxypeptidase that catalyzes the removing of polyglutamate side chains that are present on the gamma-carboxyl group of glutamate residues of tubulin in sensory cilia. Probably via the deglutamylation of tubulin, promotes microtubule stability required for axon regrowth after injury. Also regulates microtubule dynamics in uterine muscle cells. Belongs to the peptidase M14 family.
      
 0.882
spas-1
Probable spastin homolog spas-1; Severs microtubules, probably in an ATP-dependent fashion. Belongs to the AAA ATPase family. Spastin subfamily.
   
  
 0.842
ttll-11
Tubulin polyglutamylase ttll-11; Polyglutamylase which preferentially modifies tubulin. Involved in the side-chain initiation step of the polyglutamylation reaction. By controlling tubulin glutamylation, regulates ciliary specialization and motor-based transport. Promotes the formation of A and B tubule singlets by splaying microtubule doublets in cilia. Together with ttll-4 and 5, required for male mating. [Isoform b]: Specifically promotes tubulin glutamylation in male ciliated CEM, HOB and RnB neurons that release bioactive extracellular vesicles. Regulates the localization of TRP c [...]
  
  
0.769
mec-17
Alpha-tubulin N-acetyltransferase 1; Specifically acetylates 'Lys-40' in alpha-tubulin/mec-12 on the lumenal side of microtubules. Promotes microtubule destabilization and accelerates microtubule dynamics; this activity may be independent of acetylation activity. Acetylates alpha-tubulin with a slow enzymatic rate, due to a catalytic site that is not optimized for acetyl transfer. Enters the microtubule through each end and diffuses quickly throughout the lumen of microtubules. Acetylates only long/old microtubules because of its slow acetylation rate since it does not have time to act [...]
   
  
 0.759
T04C12.8
Uncharacterized protein.
    
 
 0.756
Y18D10A.3
NAD(P)H-hydrate epimerase; Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX; Belongs to the NnrE/AIBP family.
    
 
 0.756
Your Current Organism:
Caenorhabditis elegans
NCBI taxonomy Id: 6239
Other names: C. elegans, Rhabditis elegans, roundworm
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