O00469.2
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UniProt Primary Accession #
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UniProt Secondary Accession #
UniProt Related Accession #
Molecular Weight
49,142 Da
NCBI Official Full Name
Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2
NCBI Official Synonym Full Names
procollagen-lysine,2-oxoglutarate 5-dioxygenase 2
NCBI Protein Information
procollagen-lysine,2-oxoglutarate 5-dioxygenase 2
UniProt Protein Name
Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2
UniProt Synonym Protein Names
Lysyl hydroxylase 2; LH2
UniProt Synonym Gene Names
UniProt Entry Name
PLOD2_HUMAN
NCBI Summary for PLOD2
The protein encoded by this gene is a membrane-bound homodimeric enzyme that is localized to the cisternae of the rough endoplasmic reticulum. The enzyme (cofactors iron and ascorbate) catalyzes the hydroxylation of lysyl residues in collagen-like peptides. The resultant hydroxylysyl groups are attachment sites for carbohydrates in collagen and thus are critical for the stability of intermolecular crosslinks. Some patients with Ehlers-Danlos syndrome type VIB have deficiencies in lysyl hydroxylase activity. Mutations in the coding region of this gene are associated with Bruck syndrome. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Jul 2008]
UniProt Comments for PLOD2
PLOD2: 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. Defects in PLOD2 are the cause of Bruck syndrome type 2 (BRKS2). Bruck syndrome, also known as osteogenesis imperfecta with congenital joint contractures, is an autosomal recessive disease characterized by generalized osteopenia, joint contractures at birth, fragile bones and short stature. It can be distinguished from osteogenesis imperfecta by the absence of hearing loss and dentinogenesis imperfecta, and by the presence of clubfoot and congenital joint limitations. The molecular defect is an aberrant cross-linking of bone collagen, due to underhydroxylation of lysine residues within the telopeptides of type I collagen, whereas the lysine residues in the triple helix are normal. 2 isoforms of the human protein are produced by alternative splicing.
Protein type: Amino Acid Metabolism - lysine degradation; Oxidoreductase; EC 1.14.11.4; Endoplasmic reticulum
Chromosomal Location of Human Ortholog: 3q24
Cellular Component: endoplasmic reticulum; endoplasmic reticulum membrane
Molecular Function: procollagen-lysine 5-dioxygenase activity
Biological Process: protein modification process; response to hypoxia
Disease: Bruck Syndrome 2
Research Articles on PLOD2
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Pathways associated with PLOD2 blocking peptide
Diseases associated with PLOD2 blocking peptide
Organs/Tissues associated with PLOD2 blocking peptide
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