PPIB
Sign in to saveAlso known as CYP-S1, CYPB, HEL-S-39, OI9, SCYLP, peptidylprolyl isomerase B, B
Peptidyl-prolyl cis-trans isomerase B is an enzyme that is encoded by the PPIB gene. As a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family, this protein catalyzes the cis-trans isomerization of proline imidic peptide bonds, which allows it to regulate protein folding of type I collagen. Generally, PPIases are found in all eubacteria and eukaryotes, as well as in a few archaebacteria, and thus are highly conserved.
Gene data
PPIB- Name
- peptidylprolyl isomerase B
- Type
- protein-coding
- Aliases
- CYP-S1, CYPB, HEL-S-39, OI9, SCYLP
The protein encoded by this gene is a cyclosporine-binding protein and is mainly located within the endoplasmic reticulum. It is associated with the secretory pathway and released in biological fluids. This protein can bind to cells derived from T- and B-lymphocytes, and may regulate cyclosporine A-mediated immunosuppression. Variants have been identified in this protein that give rise to recessive forms of osteogenesis imperfecta. [provided by RefSeq, Oct 2009].
via MyGene.info
Gene · Ensembl
peptidylprolyl isomerase B
- Symbol
- PPIB
- Biotype
- Protein coding
- Organism
- Homo sapiens
- Location
- 15:64,155,740-64,163,159
- Strand
- Reverse (−)
- Assembly
- GRCh38
via Ensembl · EMBL-EBI
Wikidata facts
- Image
- Protein PPIB PDB 1cyn.png
Show 6 more facts
- HomoloGene ID
- 726
- exact match
- identifiers.org/ncbigene/5479
- genomic end
- 64163134
- genomic start
- 64155740
- cytogenetic location
- 15q22.31
- Commons category
- Peptidyl-prolyl cis-trans isomerase B
Sources (3)
via Wikidata · CC0
~5 min read
Article
9 sectionsContents
- Structure
- Function
- Human PPIB
- Clinical significance
- Bacterial PPIB
- Interactions
- References
- Further reading
- External links
Peptidyl-prolyl cis-trans isomerase B is an enzyme that is encoded by the PPIB gene. As a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family, this protein catalyzes the cis-trans isomerization of proline imidic peptide bonds, which allows it to regulate protein folding of type I collagen. Generally, PPIases are found in all eubacteria and eukaryotes, as well as in a few archaebacteria, and thus are highly conserved.
== Structure ==