|
gptkbp:instanceOf
|
gptkb:protein
gptkb:collagen
|
|
gptkbp:alternativeName
|
gptkb:fibrillar_collagen
gptkb:collagen_type_I
collagen I
|
|
gptkbp:aminoAcidContent
|
rich in glycine
rich in hydroxyproline
rich in proline
|
|
gptkbp:associatedWith
|
gptkb:Ehlers-Danlos_syndrome
gptkb:osteogenesis_imperfecta
dermatosparaxis
|
|
gptkbp:biosynthesized_from
|
fibroblasts
osteoblasts
|
|
gptkbp:composedOf
|
one alpha-2 chain
two alpha-1 chains
|
|
gptkbp:crosslinking
|
forms fibrils
stabilized by covalent bonds
|
|
gptkbp:degradedBy
|
collagenase
|
|
gptkbp:discoveredBy
|
Gustav von Bunge
|
|
gptkbp:discoveredIn
|
late 19th century
|
|
gptkbp:encodedBy
|
gptkb:COL1A1_gene
gptkb:COL1A2_gene
|
|
gptkbp:foundIn
|
gptkb:ligament
gptkb:bone
gptkb:skin
gptkb:tendon
cornea
blood vessels
organs
|
|
gptkbp:function
|
structural support
provides tensile strength
|
|
gptkbp:majorComponentOf
|
gptkb:extracellular_matrix
|
|
gptkbp:molecularWeight
|
~300 kDa
|
|
gptkbp:percentageOfTotalCollagen
|
~90% in bone
|
|
gptkbp:postTranslationalModification
|
glycosylation
hydroxylation of lysine
hydroxylation of proline
|
|
gptkbp:solubility
|
insoluble in water
|
|
gptkbp:structure
|
triple helix
|
|
gptkbp:usedIn
|
tissue engineering
medical devices
wound healing
cosmetic products
|
|
gptkbp:bfsParent
|
gptkb:Col1a1
gptkb:collagen_alpha-1(I)_chain
gptkb:collagen_type_I_alpha_1_chain
gptkb:collagen_type_I
gptkb:collagen_type_I_alpha_chain
gptkb:matrix_metallopeptidase_13
gptkb:CTX_(C-terminal_telopeptide)
|
|
gptkbp:bfsLayer
|
8
|
|
https://www.w3.org/2000/01/rdf-schema#label
|
type I collagen
|