Reactome: A Curated Pathway Database
Results 1 to 10 of 39
Pathways (7) Reactions (8) Proteins (1) Others (23)
Protein: UniProt:P08123 COL1A2 (Homo sapiens)
Last changed: 2015-03-10 08:59:22

Pathway: Vesicle-mediated transport (Homo sapiens)
Last changed: 2015-03-06 23:15:47

Pathway: Extracellular matrix organization (Homo sapiens)
The extracellular matrix is a component of all mammalian tissues, a network consisting largely of the fibrous proteins collagen, elastin and associated-microfibrils, fibronectin and laminins embedded in a viscoelastic gel of anionic proteoglycan polymers. It performs many functions in addition to its structural role; as a major component of the cellular microenvironment it influences cell behaviours su
Last changed: 2015-03-06 18:40:03

Pathway: Assembly of collagen fibrils and other multimeric structures (Homo sapiens)
Collagen trimers in triple-helical form, referred to as procollagen or collagen molecules, are exported from the ER and trafficked through the Golgi network before secretion into the extracellular space. For fibrillar collagens namely types I, II, III, V, XI, XXIV and XXVII (Gordon & Hahn 2010, Ricard-Blum 2011) secretion is concomitant with processing of the N and C terminal collagen propeptides. Thes
Last changed: 2015-03-06 18:40:03

Pathway: Collagen biosynthesis and modifying enzymes (Homo sapiens)
The biosynthesis of collagen is a multistep process. Collagen propeptides are cotranslationally translocated into the ER lumen. Propeptides undergo a number of post-translational modifications. Proline and lysine residues may be hydroxylated by prolyl 3-, prolyl 4- and lysyl hydroxylases. 4-hydroxyproline is essential for intramolecular hydrogen bonding and stability of the triple helical collagenous d
Last changed: 2015-03-06 18:40:03

Pathway: Binding and Uptake of Ligands by Scavenger Receptors (Homo sapiens)
Scavenger receptors bind free extracellular ligands as the initial step in clearance of the ligands from the body (reviewed in Ascenzi et al. 2005, Areschoug and Gordon 2009, Nielsen et al. 2010). Some scavenger receptors, such as the CD163-haptoglobin system, are specific for only one ligand. Others, such as the SCARA receptors (SR-A receptors) are less specific, binding several ligands which share a
Last changed: 2015-03-06 18:40:03

Pathway: Collagen formation (Homo sapiens)
Collagen is a family of at least 29 structural proteins derived from over 40 human genes (Myllyharju & Kivirikko 2004). It is the main component of connective tissue, and the most abundant protein in mammals making up about 25% to 35% of whole-body protein content. A defining feature of collagens is the formation of trimeric left-handed polyproline II-type helical collagenous regions. The packing withi
Last changed: 2015-03-06 18:40:03

Pathway: Scavenging by Class A Receptors (Homo sapiens)
Class A scavenger receptors contain an intracellular domain, a transmembrane region, a coiled-coil domain, a collagenous domain, and the SR cysteine-rich domain (reviewed in Areschoug and Gordon 2009, Bowdish and Gordon 2009). The coiled coil domains interact to form trimers. The collagenous domain (Rohrer et al. 1990, Acton et al. 1993) and/or the SR cysteine-rich domain (Brannstrom et al. 2002) bind
Last changed: 2015-03-06 10:40:16

Reaction: Collagen prolyl 4-hydroxylase converts proline to 4-hydroxyproline (Homo sapiens)
Collagen was for many years considered the only source of 4-hydroxyproline (4-Hyp) in animals. Though it is now known that other proteins such as C1q and elastin also contain 4-Hyp, collagen is by far the major source (Adams & Frank 1980). 4-Hyp is required for collagen stability at physiological temperatures. The abundance of Hyp in animal proteins is ~4%, making it more abundant than the amino-acids
Last changed: 2015-03-06 10:40:16

Reaction: Removal of fibrillar collagen N-propeptides (Homo sapiens)
Fibrillar collagen is synthesized in the ER as procollagen with N- and C-terminal propeptides flanking the collagenous domain (Bellamy & Bornstein 1971). These propeptides, particularly the C-propeptide, inhibit fibril formation (Kadler et al. 1987). Propeptide removal and self-assembly of collagen into fibrils can be studied in vitro (Kadler et al. 1987). Early studies of propeptide processing identif
Last changed: 2015-03-06 10:40:16

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