STRINGSTRING
STRING protein interaction network
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.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
Plod2Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2; Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links. (758 aa)    
Predicted Functional Partners:
Plod1
Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1; 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. Forms hydroxylysine residues in -Xaa-Lys- Gly- sequences in collagens (By similarity). These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links.
  
0.964
Colgalt1
Procollagen galactosyltransferase 1; Beta-galactosyltransferase that transfers beta-galactose to hydroxylysine residues of type I collagen. By acting on collagen glycosylation, facilitates the formation of collagen triple helix. Also involved in the biosynthesis of collagen type IV. Belongs to the glycosyltransferase 25 family.
   
0.938
Colgalt2
Procollagen galactosyltransferase 2; Beta-galactosyltransferase that transfers beta-galactose to hydroxylysine residues of collagen.
   
0.930
Plod3
Multifunctional procollagen lysine hydroxylase and glycosyltransferase LH3; Multifunctional enzyme that catalyzes a series of post- translational modifications on Lys residues in procollagen. Plays a redundant role in catalyzing the formation of hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. Plays a redundant role in catalyzing the transfer of galactose onto hydroxylysine groups, giving rise to galactosyl 5- hydroxylysine (By similarity). Has an essential role by catalyzing the subsequent transfer of glucose moieties, giving rise to 1,2- glucosylgalactosyl-5-hydroxylys [...]
  
0.915
Camkmt
Calmodulin-lysine N-methyltransferase; Catalyzes the trimethylation of 'Lys-116' in calmodulin.
     
  0.900
Fkbp10
Peptidyl-prolyl cis-trans isomerase FKBP10; PPIases accelerate the folding of proteins during protein synthesis.
   
  
 0.864
P4ha1
Prolyl 4-hydroxylase subunit alpha-1; Catalyzes the post-translational formation of 4- hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins.
   
  
 0.861
P4ha2
Prolyl 4-hydroxylase subunit alpha-2; Catalyzes the post-translational formation of 4- hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins.
   
  
 0.861
Col1a1
Collagen alpha-1(I) chain; Type I collagen is a member of group I collagen (fibrillar forming collagen); Belongs to the fibrillar collagen family.
   
 0.793
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.
   
 0.776
Your Current Organism:
Mus musculus
NCBI taxonomy Id: 10090
Other names: LK3 transgenic mice, M. musculus, Mus sp. 129SV, house mouse, mouse, nude mice, transgenic mice
Server load: low (36%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.