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
LCN15Lipocalin-15; Lipocalin 15. (184 aa)    
Predicted Functional Partners:
LCN9
Epididymal-specific lipocalin-9; Lipocalin 9.
   
 
0.682
LCN12
Epididymal-specific lipocalin-12; Binds all-trans retinoic acid and may act as a retinoid carrier protein within the epididymis. May play a role in male fertility (By similarity).
   
 
 0.671
LCN1
Lipocalin-1; Could play a role in taste reception. Could be necessary for the concentration and delivery of sapid molecules in the gustatory system. Can bind various ligands, with chemical structures ranging from lipids and retinoids to the macrocyclic antibiotic rifampicin and even to microbial siderophores. Exhibits an extremely wide ligand pocket; Belongs to the calycin superfamily. Lipocalin family.
   
 
 0.650
NUDT15
Nucleotide triphosphate diphosphatase NUDT15; May catalyze the hydrolysis of nucleoside triphosphates including dGTP, dTTP, dCTP, their oxidized forms like 8-oxo-dGTP and the prodrug thiopurine derivatives 6-thio-dGTP and 6-thio-GTP. Could also catalyze the hydrolysis of some nucleoside diphosphate derivatives. Hydrolyzes oxidized nucleosides triphosphates like 8-oxo-dGTP in vitro, but the specificity and efficiency towards these substrates are low. Therefore, the potential in vivo sanitizing role of this enzyme, that would consist in removing oxidatively damaged forms of nucleosides t [...]
    
   0.609
ALKBH2
DNA oxidative demethylase ALKBH2; Dioxygenase that repairs alkylated DNA and RNA containing 1- methyladenine and 3-methylcytosine by oxidative demethylation. Can also repair alkylated DNA containing 1-ethenoadenine (in vitro). Has strong preference for double-stranded DNA. Has low efficiency with single- stranded substrates. Requires molecular oxygen, alpha-ketoglutarate and iron.
    
   0.603
APOD
Apolipoprotein D; APOD occurs in the macromolecular complex with lecithin- cholesterol acyltransferase. It is probably involved in the transport and binding of bilin. Appears to be able to transport a variety of ligands in a number of different contexts.
     
 0.602
OBP2A
Odorant binding protein 2A; Belongs to the calycin superfamily. Lipocalin family.
   
  
 0.583
OBP2B
Odorant-binding protein 2b; Probably binds and transports small hydrophobic volatile molecules; Belongs to the calycin superfamily. Lipocalin family.
      
 0.560
LCN8
Epididymal-specific lipocalin-8; May play a role in male fertility. May act as a retinoid carrier protein within the epididymis.
   
  
 0.559
ATG4A
Cysteine protease ATG4A; Cysteine protease required for the cytoplasm to vacuole transport (Cvt) and autophagy. Cleaves the C-terminal amino acid of ATG8 family proteins to reveal a C-terminal glycine. Exposure of the glycine at the C-terminus is essential for ATG8 proteins conjugation to phosphatidylethanolamine (PE) and insertion to membranes, which is necessary for autophagy. Preferred substrate is GABARAPL2 followed by MAP1LC3A and GABARAP. Has also an activity of delipidating enzyme for the PE-conjugated forms.
    
   0.493
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, human, man
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