• Version:
  • 11.0 [archived version]
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ADAMTS10 ADAMTS10 ADAMTS20 ADAMTS20 THSD4 THSD4 ADAMTS14 ADAMTS14 ADAMTSL1 ADAMTSL1 ADAMTS12 ADAMTS12 ADAMTS17 ADAMTS17 THSD1 THSD1 ADAMTSL2 ADAMTSL2 B3GALTL B3GALTL POFUT2 POFUT2
"THSD4" - Thrombospondin type-1 domain-containing protein 4 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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Edges represent protein-protein associations
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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]
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THSD4Thrombospondin type-1 domain-containing protein 4; Promotes FBN1 matrix assembly. Attenuates TGFB signaling, possibly by accelerating the sequestration of large latent complexes of TGFB or active TGFB by FBN1 microfibril assembly, thereby negatively regulating the expression of TGFB regulatory targets, such as POSTN (By similarity); ADAMTS like (1018 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)
     
 
  0.948
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)
     
 
  0.930
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)
     
 
0.926
ADAMTS17
ADAM metallopeptidase with thrombospondin type 1 motif 17 (1095 aa)
         
0.925
THSD1
Thrombospondin type-1 domain-containing protein 1; Thrombospondin type 1 domain containing 1 (852 aa)
         
  0.925
ADAMTSL1
ADAMTS-like protein 1; I-set domain containing; ADAMTS like (1762 aa)
     
 
0.924
ADAMTSL2
ADAMTS-like protein 2; ADAMTS like 2 (951 aa)
         
0.920
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)
     
 
0.920
ADAMTS12
A disintegrin and metalloproteinase with thrombospondin motifs 12; Metalloprotease that may play a role in the degradation of COMP. Cleaves also alpha-2 macroglobulin and aggregan. Has anti-tumorigenic properties; ADAM metallopeptidases with thrombospondin type 1 motif (1594 aa)
     
 
0.918
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)
         
0.918
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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