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 nodes:
protein of unknown 3D structure
protein of unknown 3D structure
large nodes:
some 3D structure is known or predicted
some 3D structure is known or predicted
Node Color
colored nodes:
query proteins and first shell of interactors
query proteins and first shell of interactors
white nodes:
second shell of interactors
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
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
|
Your Input:
|
||||
 | P4HA2 | prolyl 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) | ||
 | COL10A1 | collagen, type X, alpha 1; Type X collagen is a product of hypertrophic chondrocytes and has been localized to presumptive mineralization zones of hyaline cartilage (680 aa) | ||
 | COL21A1 | collagen, type XXI, alpha 1 (957 aa) | ||
 | P4HA1 | prolyl 4-hydroxylase, alpha polypeptide I; Catalyzes the post-translational formation of 4- hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins (534 aa) | ||
 | COL5A3 | collagen, 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) | ||
 | ITGA1 | integrin, alpha 1; Integrin alpha-1/beta-1 is a receptor for laminin and collagen. It recognizes the proline-hydroxylated sequence G-F-P-G- E-R in collagen (1179 aa) | ||
 | PLOD2 | procollagen-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) | ||
 | COL6A3 | collagen, type VI, alpha 3; Collagen VI acts as a cell-binding protein (3177 aa) | ||
 | LEPRE1 | leucine proline-enriched proteoglycan (leprecan) 1 (736 aa) | ||
 | COL6A2 | collagen, type VI, alpha 2 (1019 aa) | ||
 | ITGB1 | integrin, beta 1 (fibronectin receptor, beta polypeptide, antigen CD29 includes MDF2, MSK12) (798 aa) | ||
 | COL3A1 | collagen, type III, alpha 1 (1466 aa) | ||
 | COL8A2 | collagen, 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) | ||
 | LEPREL1 | leprecan-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) | ||
 | P4HB | prolyl 4-hydroxylase, beta polypeptide; 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 [...] (508 aa) | ||
 | COL9A3 | collagen, type IX, alpha 3; Structural component of hyaline cartilage and vitreous of the eye (684 aa) | ||
 | COL18A1 | collagen, type XVIII, alpha 1 (1519 aa) | ||
 | COL20A1 | collagen, type XX, alpha 1; Probable collagen protein (1284 aa) | ||
 | COL4A2 | collagen, type IV, alpha 2; 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) | ||
 | COL6A1 | collagen, type VI, alpha 1; Collagen VI acts as a cell-binding protein (1028 aa) | ||
 | COL11A1 | collagen, type XI, alpha 1 (1806 aa) | ||
 | COL24A1 | collagen, type XXIV, alpha 1; May participate in regulating type I collagen fibrillogenesis at specific anatomical locations during fetal development (1714 aa) | ||
 | COL16A1 | collagen, type XVI, alpha 1; Involved in mediating cell attachment and inducing integrin-mediated cellular reactions, such as cell spreading and alterations in cell morphology (1604 aa) | ||
 | COL5A2 | collagen, type V, alpha 2 (1499 aa) | ||
 | LEPREL2 | leprecan-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) | ||
 | COL25A1 | collagen, type XXV, alpha 1; Inhibits fibrillization of beta amyloid peptide during the elongation phase. Has also been shown to assemble amyloid fibrils into protease-resistant aggregates. Binds heparin (654 aa) | ||
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
Other names: H. sapiens, Homo, Homo sapiens, human, man
Share
