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  • 11.0 [archived version]
STRINGSTRING
CRTAP CRTAP LEPRE1 LEPRE1 PPIB PPIB COL21A1 COL21A1 COL13A1 COL13A1 COL1A2 COL1A2 COL5A3 COL5A3 COL6A5 COL6A5 COL14A1 COL14A1 COL7A1 COL7A1 COL6A3 COL6A3 COL26A1 COL26A1 COL1A1 COL1A1 COL6A2 COL6A2 COL8A1 COL8A1 COL10A1 COL10A1 COL4A5 COL4A5 COL17A1 COL17A1 COL3A1 COL3A1 COL12A1 COL12A1 COL18A1 COL18A1 COL9A3 COL9A3 LEPREL1 LEPREL1 P4HB P4HB P4HA1 P4HA1 COLGALT1 COLGALT1
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:
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:
COL1A1Collagen alpha-1(I) chain; Type I collagen is a member of group I collagen (fibrillar forming collagen); Collagens (1464 aa)
LEPRE1Prolyl 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)
COL21A1Collagen type XXI alpha 1 chain; Collagens (957 aa)
COLGALT1Procollagen 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; Belongs to the glycosyltransferase 25 family (622 aa)
COL8A1Collagen alpha-1(VIII) chain; 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; Collagens (744 aa)
P4HA1Prolyl 4-hydroxylase subunit alpha-1; Catalyzes the post-translational formation of 4- hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins; Belongs to the P4HA family (534 aa)
COL5A3Collagen 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)
COL6A5Collagen alpha-5(VI) chain; Collagen VI acts as a cell-binding protein; Collagens (2611 aa)
COL6A3Collagen alpha-3(VI) chain; Collagen VI acts as a cell-binding protein; Collagens (3177 aa)
COL1A2Collagen 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)
COL14A1Collagen alpha-1(XIV) chain; Plays an adhesive role by integrating collagen bundles. It is probably associated with the surface of interstitial collagen fibrils via COL1. The COL2 domain may then serve as a rigid arm which sticks out from the fibril and protrudes the large N-terminal globular domain into the extracellular space, where it might interact with other matrix molecules or cell surface receptors (By similarity); Collagens (1796 aa)
PPIBPeptidyl-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)
COL6A2Collagen alpha-2(VI) chain; Collagen VI acts as a cell-binding protein; Collagens (1019 aa)
COL3A1Collagen 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)
LEPREL1Prolyl 3-hydroxylase 2; Prolyl 3-hydroxylase that catalyzes the post- translational formation of 3-hydroxyproline on collagens. Contributes to proline 3-hydroxylation of collagen COL4A1 and COL1A1 in tendons, the eye sclera and in the eye lens capsule (By similarity). Has high activity with the type IV collagen COL4A1, and lower activity with COL1A1. Catalyzes hydroxylation of the first Pro in Gly-Pro-Hyp sequences where Hyp is 4-hydroxyproline. Has no activity on substrates that lack 4- hydroxyproline in the third position; Belongs to the leprecan family (708 aa)
COL26A1Collagen type XXVI alpha 1 chain; Collagens (441 aa)
CRTAPCartilage-associated protein; Necessary for efficient 3-hydroxylation of fibrillar collagen prolyl residues; Belongs to the leprecan family (401 aa)
COL12A1Collagen 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)
COL10A1Collagen alpha-1(X) chain; Type X collagen is a product of hypertrophic chondrocytes and has been localized to presumptive mineralization zones of hyaline cartilage; Collagens (680 aa)
P4HBProtein 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)
COL4A5Collagen alpha-5(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; Collagens (1691 aa)
COL7A1Collagen alpha-1(VII) chain; 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; Collagens (2944 aa)
COL17A1Collagen alpha-1(XVII) chain; May play a role in the integrity of hemidesmosome and the attachment of basal keratinocytes to the underlying basement membrane; Collagens (1497 aa)
COL9A3Collagen alpha-3(IX) chain; Structural component of hyaline cartilage and vitreous of the eye; Collagen proteoglycans (684 aa)
COL18A1Collagen alpha-1(XVIII) chain; Probably plays a major role in determining the retinal structure as well as in the closure of the neural tube; Belongs to the multiplexin collagen family (1519 aa)
COL13A1Collagen alpha-1(XIII) chain; Involved in cell-matrix and cell-cell adhesion interactions that are required for normal development. May participate in the linkage between muscle fiber and basement membrane. May play a role in endochondral ossification of bone and branching morphogenesis of lung. Binds heparin. At neuromuscular junctions, may play a role in acetylcholine receptor clustering; Collagens (717 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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