Names & Taxonomy

Uniprot ID:
P23284
Entry Name:
PPIB_HUMAN
Status:
reviewed
Protein Names:
Peptidyl-prolyl cis-trans isomerase B (PPIase B) (EC 5.2.1.8) (CYP-S1) (Cyclophilin B) (Rotamase B) (S-cyclophilin) (SCYLP)
Gene Names:
PPIB CYPB
Gene Names Primary:
PPIB
Organism:
Homo sapiens (Human)

Structure

Length:
216
Sequence:
MLRLSERNMKVLLAAALIAGSVFFLLLPGPSAADEKKKGPKVTVKVYFDLRIGDEDVGRVIFGLFGKTVPKTVDNFVALATGEKGFGYKNSKFHRVIKDFMIQGGDFTRGDGTGGKSIYGERFPDENFKLKHYGPGWVSMANAGKDTNGSQFFITTVKTAWLDGKHVVFGKVLEGMEVVRKVESTKTDSRDKPLKDVIIADCGKIEVEKPFAIAKE
Proteomes:
UP000005640

Subcellular location

Subcellular Location:
Endoplasmic reticulum lumen

Function

Function:
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Catalytic Activity:
Peptidylproline (omega=180) = peptidylproline (omega=0).
Enzyme Regulation:
ENZYME REGULATION: Cyclosporin A (CsA) inhibits CYPB.
Cross Reference Drug Bank:
DB00172
Gene Ontology Go:
endoplasmic reticulum
endoplasmic reticulum chaperone complex
endoplasmic reticulum lumen
extracellular exosome
focal adhesion
macromolecular complex
melanosome
membrane
nucleus
perinuclear region of cytoplasm
smooth endoplasmic reticulum
peptide binding
peptidyl-prolyl cis-trans isomerase activity
poly(A) RNA binding
protein complex binding
RNA polymerase binding
unfolded protein binding
bone development
chaperone-mediated protein folding
extracellular matrix organization
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
Gene Ontology Biological Process:
bone development
chaperone-mediated protein folding
extracellular matrix organization
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
Gene Ontology Molecular Function:
peptide binding
peptidyl-prolyl cis-trans isomerase activity
poly(A) RNA binding
protein complex binding
RNA polymerase binding
unfolded protein binding
Gene Ontology Cellular Component:
endoplasmic reticulum
endoplasmic reticulum chaperone complex
endoplasmic reticulum lumen
extracellular exosome
focal adhesion
macromolecular complex
melanosome
membrane
nucleus
perinuclear region of cytoplasm
smooth endoplasmic reticulum
Keywords:
3D-structure
Acetylation
Complete proteome
Cyclosporin
Direct protein sequencing
Disease mutation
Dwarfism
Endoplasmic reticulum
Glycoprotein
Isomerase
Osteogenesis imperfecta
Polymorphism
Reference proteome
Rotamase
Signal
Interacts With:
Q9WMX2; Q8N9N5; P13667; P40855; O43765; Q9UMX0; Q9UMX0-2

Publication

PubMed ID:
2040592 14702039 16572171 15489334 2000394 1710767 1286667 1530944 17081065 19781681 21269460 21280149 24275569 25944712 8197205 20801878 20089953