Human Gene PPIB (uc002and.3) Description and Page Index
Description: Homo sapiens peptidylprolyl isomerase B (cyclophilin B) (PPIB), mRNA. RefSeq Summary (NM_000942): 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]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: EU794651.1, SRR1163658.412242.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968189, SAMEA1968540 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Transcript (Including UTRs) Position: hg19 chr15:64,448,014-64,455,354 Size: 7,341 Total Exon Count: 5 Strand: - Coding Region Position: hg19 chr15:64,448,222-64,455,185 Size: 6,964 Coding Exon Count: 5
ID:PPIB_HUMAN DESCRIPTION: RecName: Full=Peptidyl-prolyl cis-trans isomerase B; Short=PPIase B; EC=18.104.22.168; AltName: Full=CYP-S1; AltName: Full=Cyclophilin B; AltName: Full=Rotamase B; AltName: Full=S-cyclophilin; Short=SCYLP; Flags: Precursor; 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: Cyclosporin A (CsA) inhibits CYPB. SUBUNIT: Interacts with DYM. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Melanosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. DISEASE: Defects in PPIB are the cause of osteogenesis imperfecta type 9 (OI9) [MIM:259440]. 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. SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase B subfamily. SIMILARITY: Contains 1 PPIase cyclophilin-type domain. CAUTION: It is uncertain whether Met-1 or Met-9 is the initiator. SEQUENCE CAUTION: Sequence=AAA52150.1; Type=Erroneous initiation; WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/ppib/"; WEB RESOURCE: Name=Osteogenesis imperfecta variant database; Note=Peptidyl-prolyl cis-trans isomerase B (PPIB); URL="http://oi.gene.le.ac.uk/home.php?select_db=PPIB";
Genetic Association Studies of Complex Diseases and Disorders
Genetic Association Database (archive): PPIB CDC HuGE Published Literature: PPIB
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on P23284
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
Biological Process: GO:0000413 protein peptidyl-prolyl isomerization GO:0006457 protein folding GO:0040018 positive regulation of multicellular organism growth GO:0044794 positive regulation by host of viral process GO:0044829 positive regulation by host of viral genome replication GO:0050821 protein stabilization GO:0060348 bone development GO:0061077 chaperone-mediated protein folding GO:1901873 regulation of post-translational protein modification