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FLASH GENE
Symbol P3H2 contributors: mct - updated : 02-01-2019
HGNC name prolyl 3-hydroxylase 2
HGNC id 19317
PROTEIN
PHYSICAL PROPERTIES
STRUCTURE
motifs/domains
  • a signal sequence
  • four tetratricopeptide repeats (TPRs)
  • a leucine zipper
  • a P-loop
  • a prolyl 4-hydroxylase alpha domain (P4Halpha)
  • and a C-terminal KDEL ER-retention motif
  • HOMOLOGY
    Homologene
    FAMILY
  • leprecan family of proteoglycans, P3H family
  • prolyl 3-hydroxylases family
  • CATEGORY enzyme , structural protein
    SUBCELLULAR LOCALIZATION extracellular
        intracellular
    intracellular,cytoplasm,organelle,lumen
    intracellular,cytoplasm,organelle,endoplasmic reticulum
    intracellular,cytoplasm,organelle,Golgi
    basic FUNCTION
  • catalyzing the posttranslational formation of 4- hydroxyproline in -Xaa-Pro-Gly- sequences
  • in collagens and other proteins
  • P3H2 is responsible for the hydroxylation of collagen IV, which has the highest 3-hydroxyproline content of all collagens (PMUID: 18487197)
  • tissue specific P3H1, P3H2, P3H3 gene expression in both fetal and adult tissues indicating a developmental role for prolyl 3-hydroxylase activity
  • role for P3H2 in post-translational modification of fibril-forming collagens
  • P3H1 preferentially 3-hydroxylates proline at a single site in collagen type I chains, whereas P3H2 is responsible for 3-hydroxylating multiple proline sites in collagen types I, II, IV, and V
  • is involved in the post-translational modification of fibrillar collagens
  • role for the Leprecans in the post-translational modification of collagens expressed in the stroma of the reproductive organs
  • CELLULAR PROCESS
    PHYSIOLOGICAL PROCESS
    PATHWAY
    metabolism
    signaling
    a component
    INTERACTION
    DNA
    RNA
    small molecule cofactor,
    iron and ascorbate
    protein
    cell & other
    REGULATION
    ASSOCIATED DISORDERS
    corresponding disease(s) MCVD
    Other morbid association(s)
    TypeGene ModificationChromosome rearrangementProtein expressionProtein Function
    constitutional       loss of function
    altered collagen prolyl 3-hydroxylation is caused by loss of P3H2
    tumoral     --low  
    in human hepatocellular carcinoma
    Susceptibility
    Variant & Polymorphism
    Candidate gene
    Marker
    Therapy target
    ANIMAL & CELL MODELS
  • P3h2-null mice are embryonic-lethal by embryonic day 8.5