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Plod3 Plod3 Plod1 Plod1 Col8a2 Col8a2 Col19a1 Col19a1 Col24a1 Col24a1 Col4a3 Col4a3 P3h3 P3h3 Colgalt1 Colgalt1 Col22a1 Col22a1 Colgalt2 Colgalt2 Col4a4 Col4a4 Col28a1 Col28a1 Col18a1 Col18a1 P4ha2 P4ha2 Col20a1 Col20a1 P4ha3 P4ha3 P4hb P4hb Col6a6 Col6a6 Plod2 Plod2 Col4a1 Col4a1 Col4a2 Col4a2 Col26a1 Col26a1 Col8a1 Col8a1 Col4a5 Col4a5 LOC103693323 LOC103693323 Col14a1 Col14a1 P4ha1 P4ha1 Col25a1 Col25a1 Col6a5 Col6a5 LOC100909752 LOC100909752 Col13a1 Col13a1 Col4a6 Col4a6 Col10a1 Col10a1 P3h2 P3h2
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:
a 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 to 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:
Plod3Multifunctional procollagen lysine hydroxylase and glycosyltransferase LH3; Multifunctional enzyme that catalyzes a series of post- translational modifications on Lys residues in procollagen. Plays a redundant role in catalyzing the formation of hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens (By similarity). Plays a redundant role in catalyzing the transfer of galactose onto hydroxylysine groups, giving rise to galactosyl 5-hydroxylysine (By similarity). Has an essential role by catalyzing the subsequent transfer of glucose moieties, giving rise to 1,2-glucosylgalactosy [...] (741 aa)
Plod1Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1; 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 (By similarity). 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 (By similarity). (728 aa)
Col8a2Collagen type VIII alpha 2 chain. (699 aa)
Col19a1Collagen type XIX alpha 1 chain. (1129 aa)
Col24a1Collagen type XXIV alpha 1 chain. (1352 aa)
Col4a3Collagen type IV alpha 3 chain. (1671 aa)
P3h3Leprecan-like 2 (Predicted), isoform CRA_b. (548 aa)
Colgalt1Glycosyltransferase 25 domain containing 1 (Predicted). (617 aa)
Col22a1Collagen type XXII alpha 1 chain. (1613 aa)
Colgalt2Collagen beta(1-O)galactosyltransferase 2. (624 aa)
Col4a4Collagen type IV alpha 4 chain. (159 aa)
Col28a1Collagen type XXVIII alpha 1 chain. (1142 aa)
Col18a1Procollagen, type XVIII, alpha 1, isoform CRA_a. (1311 aa)
P4ha2Prolyl 4-hydroxylase subunit alpha 2. (535 aa)
Col20a1Collagen type XX alpha 1 chain. (1362 aa)
P4ha3Prolyl 4-hydroxylase subunit alpha-3; Catalyzes the post-translational formation of 4- hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins. (544 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 [...] (509 aa)
Col6a6Collagen type VI alpha 6 chain. (2264 aa)
Plod2Procollagen-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)
Col4a1Collagen type IV alpha 1 chain. (1669 aa)
Col4a2Collagen type IV alpha 2 chain. (1645 aa)
Col26a1Collagen type XXVI alpha 1 chain. (440 aa)
Col8a1Collagen type VIII alpha 1 chain. (744 aa)
Col4a5Collagen type IV alpha 5 chain. (1691 aa)
LOC103693323Collagen alpha-1(XXIII) chain. (532 aa)
Col14a1Collagen type XIV alpha 1 chain. (1794 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)
Col25a1Collagen type XXV alpha 1 chain. (503 aa)
Col6a5Collagen type VI alpha 5 chain. (2632 aa)
LOC100909752Procollagen, type XV, isoform CRA_a. (1345 aa)
Col13a1Similar to alpha 1 type XIII collagen isoform 17, isoform CRA_a. (739 aa)
Col4a6Collagen type IV alpha 6 chain. (1638 aa)
Col10a1Collagen type X alpha 1 chain. (680 aa)
P3h2Prolyl 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 (By similarity). Belongs to the leprecan family. (702 aa)
Your Current Organism:
Rattus norvegicus
NCBI taxonomy Id: 10116
Other names: Buffalo rat, Norway rat, R. norvegicus, Rattus PC12 clone IS, Rattus sp. strain Wistar, Sprague-Dawley rat, Wistar rats, brown rat, laboratory rat, rat, rats, zitter rats
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