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  • 11.0 [archived version]
STRINGSTRING
COL12A1 COL12A1 COL4A4 COL4A4 COL11A2 COL11A2 COL5A2 COL5A2 COL4A1 COL4A1 COL28A1 COL28A1 COL22A1 COL22A1 COL5A3 COL5A3 COL5A1 COL5A1 COL11A1 COL11A1 COL4A2 COL4A2
"COL22A1" - Collagen alpha-1(XXII) chain in Homo sapiens
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.
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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:
some 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 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
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
COL22A1Collagen alpha-1(XXII) chain; Acts as a cell adhesion ligand for skin epithelial cells and fibroblasts; Belongs to the fibril-associated collagens with interrupted helices (FACIT) family (1626 aa)    
Predicted Functional Partners:
COL12A1
Collagen alpha-1(XII) chain; Type XII collagen interacts with type I collagen- containing fibrils, the COL1 domain could be associated with the surface of the fibrils, and the COL2 and NC3 domains may be localized in the perifibrillar matrix; Belongs to the fibril-associated collagens with interrupted helices (FACIT) family (3063 aa)
      
0.931
COL11A1
Collagen alpha-1(XI) chain; May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils; Collagens (1806 aa)
    
0.927
COL11A2
Collagen alpha-2(XI) chain; May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils; Collagens (1650 aa)
    
0.926
COL28A1
Collagen alpha-1(XXVIII) chain; May act as a cell-binding protein; Belongs to the VWA-containing collagen family (1125 aa)
      
0.923
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)
    
0.922
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)
    
0.921
COL4A2
Collagen alpha-2(IV) chain; 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 (1712 aa)
    
0.920
COL4A1
Collagen alpha-1(IV) chain; 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 (1669 aa)
    
0.920
COL5A3
Collagen alpha-3(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 (1745 aa)
    
0.920
COL4A4
Collagen alpha-4(IV) chain; 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)
    
0.920
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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