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
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Your Input:
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 | COL1A1 | collagen, type I, alpha 1 (1464 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) | ||
 | LEPRE1 | leucine proline-enriched proteoglycan (leprecan) 1 (736 aa) | ||
 | COL1A2 | collagen, type I, alpha 2 (1366 aa) | ||
 | COL3A1 | collagen, type III, alpha 1 (1466 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) | ||
 | CRTAP | cartilage associated protein; Necessary for efficient 3-hydroxylation of fibrillar collagen prolyl residues (401 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) | ||
 | UBC | ubiquitin C (685 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
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