PPIB PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding. 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: 15q22.31
Cellular Component:  endoplasmic reticulum; endoplasmic reticulum chaperone complex; endoplasmic reticulum lumen; melanosome; nucleus; perinuclear region of cytoplasm; protein-containing complex; smooth endoplasmic reticulum
Molecular Function:  cyclosporin A binding; peptidyl-prolyl cis-trans isomerase activity; protein binding; RNA polymerase binding
Biological Process:  bone development; chaperone-mediated protein folding; positive regulation by host of viral genome replication; positive regulation by host of viral process; positive regulation of multicellular organism growth; protein peptidyl-prolyl isomerization; protein stabilization
Disease: Osteogenesis Imperfecta, Type Ix
Reference #:  P23284 (UniProtKB)
Alt. Names/Synonyms: B; Cyclophilin B; cyclophilin-like protein; CYP-S1; CYPB; epididymis secretory protein Li 39; HEL-S-39; 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, siRNAs or Recombinant Proteins from Cell Signaling Technology® Total Proteins
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PPIB

Protein Structure Not Found.


Cross-references to other databases:  STRING  |  cBioPortal  |  Wikipedia  |  Reactome  |  neXtProt  |  Protein Atlas  |  BioGPS  |  Pfam  |  RCSB PDB  |  ENZYME  |  Phospho3D  |  Phospho.ELM  |  NetworKIN  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene  |  InnateDB