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Protein Page:
PPIB (human)

Overview
PPIB PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Defects in PPIB are the cause of osteogenesis imperfecta type 9 (OI9). OI9 is a connective tissue disorder characterized by bone fragility, low bone mass and bowing of limbs due to multiple fractures. Short limb dwarfism and blue sclerae are observed in some but not all patients. Belongs to the cyclophilin-type PPIase family. PPIase B subfamily. Note: This description may include information from UniProtKB.
Protein type: Chaperone; Cyclophilin; EC 5.2.1.8; Isomerase; RNA-binding; Secreted; Secreted, signal peptide
Chromosomal Location of Human Ortholog: 15q21-q22
Cellular Component: endoplasmic reticulum; endoplasmic reticulum lumen; focal adhesion; membrane; nucleus; perinuclear region of cytoplasm
Molecular Function: collagen binding; peptidyl-prolyl cis-trans isomerase activity; protein binding; protein complex binding; unfolded protein binding
Biological Process: positive regulation of multicellular organism growth; protein peptidyl-prolyl isomerization; protein stabilization
Disease: Osteogenesis Imperfecta, Type Ix
Reference #:  P23284 (UniProtKB)
Alt. Names/Synonyms: Cyclophilin B; cyclophilin-like protein; CYP-S1; CYPB; MGC14109; MGC2224; OI9; Peptidyl-prolyl cis-trans isomerase B; peptidylprolyl isomerase B; peptidylprolyl isomerase B (cyclophilin B); PPIase B; PPIB; Rotamase B; S-cyclophilin; SCYLP
Gene Symbols: PPIB
Molecular weight: 23,743 Da
Basal Isoelectric point: 9.42  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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PPIB

Protein Structure Not Found.
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