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  • 11.0 [archived version]
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LEPREL1 LEPREL1 COL15A1 COL15A1 COL9A2 COL9A2 PPIB PPIB COL27A1 COL27A1 COL28A1 COL28A1 CRTAP CRTAP P4HB P4HB COL1A1 COL1A1 COL11A2 COL11A2 COL9A3 COL9A3
"LEPREL1" - Prolyl 3-hydroxylase 2 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
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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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LEPREL1Prolyl 3-hydroxylase 2; Prolyl 3-hydroxylase that catalyzes the post- translational formation of 3-hydroxyproline on collagens. Contributes to proline 3-hydroxylation of collagen COL4A1 and COL1A1 in tendons, the eye sclera and in the eye lens capsule (By similarity). Has high activity with the type IV collagen COL4A1, and lower activity with COL1A1. Catalyzes hydroxylation of the first Pro in Gly-Pro-Hyp sequences where Hyp is 4-hydroxyproline. Has no activity on substrates that lack 4- hydroxyproline in the third position; Belongs to the leprecan family (708 aa)    
Predicted Functional Partners:
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)
         
  0.961
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)
     
  0.943
CRTAP
Cartilage-associated protein; Necessary for efficient 3-hydroxylation of fibrillar collagen prolyl residues; Belongs to the leprecan family (401 aa)
     
0.925
COL9A2
Collagen alpha-2(IX) chain; Structural component of hyaline cartilage and vitreous of the eye; Collagen proteoglycans (689 aa)
         
  0.921
COL1A1
Collagen alpha-1(I) chain; Type I collagen is a member of group I collagen (fibrillar forming collagen); Collagens (1464 aa)
     
 
  0.919
COL28A1
Collagen alpha-1(XXVIII) chain; May act as a cell-binding protein; Belongs to the VWA-containing collagen family (1125 aa)
         
  0.918
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)
         
  0.916
COL11A2
Collagen alpha-2(XI) chain; May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils; Collagens (1650 aa)
     
 
  0.916
COL9A3
Collagen alpha-3(IX) chain; Structural component of hyaline cartilage and vitreous of the eye; Collagen proteoglycans (684 aa)
         
  0.915
COL15A1
Collagen alpha-1(XV) chain; Structural protein that stabilizes microvessels and muscle cells, both in heart and in skeletal muscle; Collagen proteoglycans (1388 aa)
     
 
  0.914
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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