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  • 11.0 [archived version]
STRINGSTRING
P4HB P4HB COL1A2 COL1A2 SERPINH1 SERPINH1 COL3A1 COL3A1 LEPREL2 LEPREL2 COL5A2 COL5A2 COL1A1 COL1A1 COL5A1 COL5A1 LEPRE1 LEPRE1 PPIB PPIB CRTAP CRTAP
"CRTAP" - Cartilage-associated protein in Homo sapiens
Nodes:
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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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colored nodes:
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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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
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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Score
CRTAPCartilage-associated protein; Necessary for efficient 3-hydroxylation of fibrillar collagen prolyl residues; Belongs to the leprecan family (401 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)
     
  0.995
LEPRE1
Prolyl 3-hydroxylase 1; Basement membrane-associated chondroitin sulfate proteoglycan (CSPG). 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. May be involved in the secretory pathway of cells. Has growth suppressive activity in fibroblasts (804 aa)
     
0.994
COL1A1
Collagen alpha-1(I) chain; Type I collagen is a member of group I collagen (fibrillar forming collagen); Collagens (1464 aa)
     
 
  0.975
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)
     
 
  0.974
SERPINH1
Serpin H1; Binds specifically to collagen. Could be involved as a chaperone in the biosynthetic pathway of collagen; Serpin peptidase inhibitors (418 aa)
     
 
  0.974
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) (1499 aa)
     
 
  0.954
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)
     
 
  0.942
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)
     
 
  0.942
COL3A1
Collagen alpha-1(III) chain; Collagen type III occurs in most soft connective tissues along with type I collagen. Involved in regulation of cortical development. Is the major ligand of ADGRG1 in the developing brain and binding to ADGRG1 inhibits neuronal migration and activates the RhoA pathway by coupling ADGRG1 to GNA13 and possibly GNA12 (1466 aa)
     
 
  0.941
LEPREL2
Prolyl 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)
     
0.929
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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