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  • 11.0 [archived version]
STRINGSTRING
LEPREL2 LEPREL2 PPIB PPIB COL11A2 COL11A2 COL24A1 COL24A1 COL16A1 COL16A1 COL5A1 COL5A1 COL1A2 COL1A2 COL27A1 COL27A1 COL1A1 COL1A1 CRTAP CRTAP P4HB P4HB
"LEPREL2" - Prolyl 3-hydroxylase 3 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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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
LEPREL2Prolyl 3-hydroxylase 3; Part of a complex composed of PLOD1, P3H3 and P3H4 that catalyzes hydroxylation of lysine residues in collagen alpha chains and is required for normal assembly and cross-linkling of collagen fibrils. Required for normal hydroxylation of lysine residues in type I collagen chains in skin, bone, tendon, aorta and cornea. Required for normal skin stability via its role in hydroxylation of lysine residues in collagen alpha chains and in collagen fibril assembly. Apparently not required for normal prolyl 3-hydroxylation on collagen chains, possibly because it function [...] (736 aa)    
Predicted Functional Partners:
PPIB
Peptidyl-prolyl cis-trans isomerase B; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Cyclophilin peptidylprolyl isomerases (216 aa)
      
  0.932
CRTAP
Cartilage-associated protein; Necessary for efficient 3-hydroxylation of fibrillar collagen prolyl residues; Belongs to the leprecan family (401 aa)
      
0.929
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 (1860 aa)
      
 
  0.921
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; Collagens (1838 aa)
      
 
  0.916
COL11A2
Collagen alpha-2(XI) chain; May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils; Collagens (1650 aa)
      
 
  0.911
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 (1366 aa)
      
 
  0.911
P4HB
Protein disulfide-isomerase; This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chape [...] (508 aa)
          
  0.910
COL16A1
Collagen alpha-1(XVI) chain; Involved in mediating cell attachment and inducing integrin-mediated cellular reactions, such as cell spreading and alterations in cell morphology; Collagens (1604 aa)
      
 
  0.910
COL1A1
Collagen alpha-1(I) chain; Type I collagen is a member of group I collagen (fibrillar forming collagen); Collagens (1464 aa)
      
 
  0.910
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 (1714 aa)
          
  0.909
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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