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  • 11.0 [archived version]
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ADAMTSL3 ADAMTSL3 ADAMTS14 ADAMTS14 ADAMTSL2 ADAMTSL2 ADAMTSL4 ADAMTSL4 ADAMTS13 ADAMTS13 ADAMTS20 ADAMTS20 ADAMTS10 ADAMTS10 ADAMTS17 ADAMTS17 B3GALTL B3GALTL POFUT2 POFUT2 ADAMTSL5 ADAMTSL5
"ADAMTSL5" - ADAMTS-like protein 5 in Homo sapiens
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.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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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
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[Homology]
Score
ADAMTSL5ADAMTS-like protein 5; May play a role in modulation of fibrillin microfibrils in the extracellular matrix (ECM); ADAMTS like (471 aa)    
Predicted Functional Partners:
POFUT2
GDP-fucose protein O-fucosyltransferase 2; Catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue in the consensus sequence C1-X(2,3)-S/T-C2-X(2)-G of thrombospondin type 1 repeats where C1 and C2 are the first and second cysteines, respectively. O-fucosylates members of several protein families including the ADAMTS family, the thrombosporin (TSP) and spondin families. The O-fucosylation of TSRs is also required for restricting epithelial to mesenchymal transition (EMT), maintaining the correct patterning of mesoderm and l [...] (429 aa)
     
 
  0.940
B3GALTL
Beta-1,3-glucosyltransferase; O-glucosyltransferase that transfers glucose toward fucose with a beta-1,3 linkage. Specifically glucosylates O-linked fucosylglycan on TSP type-1 domains of proteins, thereby contributing to elongation of O-fucosylglycan (498 aa)
         
  0.924
ADAMTSL4
ADAMTS-like protein 4; Positive regulation of apoptosis. May facilitate FBN1 microfibril biogenesis; ADAMTS like (1097 aa)
     
0.924
ADAMTSL2
ADAMTS-like protein 2; ADAMTS like 2 (951 aa)
     
 
0.920
ADAMTS17
ADAM metallopeptidase with thrombospondin type 1 motif 17 (1095 aa)
         
0.919
ADAMTS20
A disintegrin and metalloproteinase with thrombospondin motifs 20; May play a role in tissue-remodeling process occurring in both normal and pathological conditions. May have a protease- independent function in the transport from the endoplasmic reticulum to the Golgi apparatus of secretory cargos, mediated by the GON domain; ADAM metallopeptidases with thrombospondin type 1 motif (1910 aa)
         
0.917
ADAMTS14
A disintegrin and metalloproteinase with thrombospondin motifs 14; Has a aminoprocollagen type I activity processing activity in the absence of ADAMTS2. Seems to be synthesized as a latent enzyme that requires activation to display aminoprocollagen peptidase activity; ADAM metallopeptidases with thrombospondin type 1 motif (1226 aa)
         
0.916
ADAMTS13
A disintegrin and metalloproteinase with thrombospondin motifs 13; Cleaves the vWF multimers in plasma into smaller forms thereby controlling vWF-mediated platelet thrombus formation; ADAM metallopeptidases with thrombospondin type 1 motif (1427 aa)
         
0.916
ADAMTS10
A disintegrin and metalloproteinase with thrombospondin motifs 10; Metalloprotease that participate in microfibrils assembly. Microfibrils are extracellular matrix components occurring independently or along with elastin in the formation of elastic tissues; ADAM metallopeptidases with thrombospondin type 1 motif (1103 aa)
     
 
0.915
ADAMTSL3
ADAMTS-like protein 3; Immunoglobulin like domain containing (1691 aa)
     
 
0.915
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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