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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
ADAMTS14A disintegrin and metalloproteinase with thrombospondin motifs 14; Has aminoprocollagen type I processing activity in the absence of ADAMTS2. Seems to be synthesized as a latent enzyme that requires activation to display aminoprocollagen peptidase activity. Cleaves lysyl oxidase LOX at a site downstream of its propeptide cleavage site to produce a short LOX form. (1226 aa)    
Predicted Functional Partners:
SGPL1
Sphingosine-1-phosphate lyase 1; Cleaves phosphorylated sphingoid bases (PSBs), such as sphingosine-1-phosphate, into fatty aldehydes and phosphoethanolamine. Elevates stress-induced ceramide production and apoptosis. Required for global lipid homeostasis in liver and cholesterol homeostasis in fibroblasts. Involved in the regulation of pro- inflammatory response and neutrophil trafficking. Modulates neuronal autophagy via phosphoethanolamine production which regulates accumulation of aggregate-prone proteins such as APP (By similarity). Seems to play a role in establishing neuronal co [...]
      
 0.850
COL24A1
Collagen alpha-1(XXIV) chain; May participate in regulating type I collagen fibrillogenesis at specific anatomical locations during fetal development. Belongs to the fibrillar collagen family.
   
 0.638
COL5A1
Collagen alpha-1(V) chain; Type V collagen is a member of group I collagen (fibrillar forming collagen). It is a minor connective tissue component of nearly ubiquitous distribution. Type V collagen binds to DNA, heparan sulfate, thrombospondin, heparin, and insulin.
   
 0.631
COL27A1
Collagen alpha-1(XXVII) chain; Plays a role during the calcification of cartilage and the transition of cartilage to bone; Belongs to the fibrillar collagen family.
   
 0.627
COL1A2
Collagen alpha-2(I) chain; Type I collagen is a member of group I collagen (fibrillar forming collagen); Belongs to the fibrillar collagen family.
   
 0.604
COL5A3
Collagen alpha-3(V) chain; Type V collagen is a member of group I collagen (fibrillar forming collagen). It is a minor connective tissue component of nearly ubiquitous distribution. Type V collagen binds to DNA, heparan sulfate, thrombospondin, heparin, and insulin.
   
 0.597
COL1A1
Collagen alpha-1(I) chain; Type I collagen is a member of group I collagen (fibrillar forming collagen).
   
 0.589
COL5A2
Collagen alpha-2(V) chain; Type V collagen is a member of group I collagen (fibrillar forming collagen). It is a minor connective tissue component of nearly ubiquitous distribution. Type V collagen binds to DNA, heparan sulfate, thrombospondin, heparin, and insulin. Type V collagen is a key determinant in the assembly of tissue-specific matrices (By similarity).
   
 0.589
COL11A1
Collagen alpha-1(XI) chain; May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils.
   
 0.587
FURIN
Furin; Ubiquitous endoprotease within constitutive secretory pathways capable of cleavage at the RX(K/R)R consensus motif. Mediates processing of TGFB1, an essential step in TGF-beta-1 activation. (Microbial infection) Required for H7N1 and H5N1 influenza virus infection probably by cleaving hemagglutinin.
   
  
 0.585
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, human, man
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