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STRINGSTRING
CRTAP CRTAP PPIB PPIB LEPREL2 LEPREL2 COL5A3 COL5A3 COL4A5 COL4A5 COL5A2 COL5A2 COL8A2 COL8A2 LEPREL1 LEPREL1 COL28A1 COL28A1 COL1A1 COL1A1 P4HA3 P4HA3 COL19A1 COL19A1 COL4A3 COL4A3 COL4A4 COL4A4 COL9A1 COL9A1 GLT25D2 GLT25D2 COL2A1 COL2A1 COL9A2 COL9A2 COL7A1 COL7A1 ADAMTS2 ADAMTS2 P4HA2 P4HA2 COL6A6 COL6A6 GLT25D1 GLT25D1 PCOLCE2 PCOLCE2 ADAMTS3 ADAMTS3 ADAMTS14 ADAMTS14
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 Size
small protein node
small nodes:
protein of unknown 3D structure
large protein node
large nodes:
some 3D structure is known or predicted
Node Color
colored protein node
colored nodes:
query proteins and first shell of interactors
non-colored protein node
white nodes:
second shell of interactors
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 each other.
Known Interactions
database edge
from curated databases
experiment edge
experimentally determined
Predicted Interactions
neighborhood edge
gene neighborhood
fusion edge
gene fusions
cooccurrence edge
gene co-occurrence
Others
textmining edge
textmining
coexpression edge
co-expression
homology edge
protein homology
Your Input:
P4HA2prolyl 4-hydroxylase, alpha polypeptide II; Catalyzes the post-translational formation of 4- hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins (535 aa)
COL1A1collagen, type I, alpha 1 (1464 aa)
ADAMTS2ADAM metallopeptidase with thrombospondin type 1 motif, 2; Cleaves the propeptides of type I and II collagen prior to fibril assembly. Does not act on type III collagen. May also play a role in development that is independent of its role in collagen biosynthesis (1211 aa)
GLT25D1glycosyltransferase 25 domain containing 1; Has a beta-galactosyltransferase activity; transfers beta-galactose to hydroxylysine residues of collagen (622 aa)
COL5A3collagen, type V, alpha 3; 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 (1745 aa)
ADAMTS3ADAM metallopeptidase with thrombospondin type 1 motif, 3; Cleaves the propeptides of type II collagen prior to fibril assembly. Does not act on types I and III collagens (1205 aa)
PCOLCE2procollagen C-endopeptidase enhancer 2; Binds to the C-terminal propeptide of types I and II procollagens and may enhance the cleavage of that propeptide by BMP1 (415 aa)
PPIBpeptidylprolyl isomerase B (cyclophilin B); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (216 aa)
COL8A2collagen, type VIII, alpha 2; Macromolecular component of the subendothelium. Major component of the Descemet’s membrane (basement membrane) of corneal endothelial cells. Also component of the endothelia of blood vessels. Necessary for migration and proliferation of vascular smooth muscle cells and thus, has a potential role in the maintenance of vessel wall integrity and structure, in particular in atherogenesis (By similarity) (703 aa)
COL19A1collagen, type XIX, alpha 1 (1142 aa)
LEPREL1leprecan-like 1; Shows prolyl 3-hydroxylase activity catalyzing the post- translational formation of 3-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens, especially types II, IV and V (By similarity) (708 aa)
CRTAPcartilage associated protein; Necessary for efficient 3-hydroxylation of fibrillar collagen prolyl residues (401 aa)
COL4A5collagen, type IV, alpha 5; Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a ’chicken-wire’ meshwork together with laminins, proteoglycans and entactin/nidogen (1691 aa)
P4HA3prolyl 4-hydroxylase, alpha polypeptide III; Catalyzes the post-translational formation of 4- hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins (544 aa)
COL7A1collagen, type VII, alpha 1; Stratified squamous epithelial basement membrane protein that forms anchoring fibrils which may contribute to epithelial basement membrane organization and adherence by interacting with extracellular matrix (ECM) proteins such as type IV collagen (2944 aa)
COL9A1collagen, type IX, alpha 1 (921 aa)
COL6A6collagen, type VI, alpha 6; Collagen VI acts as a cell-binding protein (By similarity) (2263 aa)
GLT25D2glycosyltransferase 25 domain containing 2; Has a beta-galactosyltransferase activity; transfers beta-galactose to hydroxylysine residues on collagen (626 aa)
COL9A2collagen, type IX, alpha 2; Structural component of hyaline cartilage and vitreous of the eye (689 aa)
ADAMTS14ADAM metallopeptidase with thrombospondin type 1 motif, 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 (1226 aa)
COL5A2collagen, type V, alpha 2 (1499 aa)
COL2A1collagen, type II, alpha 1 (1487 aa)
COL4A3collagen, type IV, alpha 3 (Goodpasture antigen) (1670 aa)
COL4A4collagen, type IV, alpha 4; Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a ’chicken-wire’ meshwork together with laminins, proteoglycans and entactin/nidogen (1690 aa)
LEPREL2leprecan-like 2; Has prolyl 3-hydroxylase activity catalyzing the post- translational formation of 3-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens, especially types IV and V (By similarity) (735 aa)
COL28A1collagen, type XXVIII, alpha 1; May act as a cell-binding protein (1125 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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