Peptidyl-prolyl cis-trans isomerase B (PPIB)
The protein contains 216 amino acids for an estimated molecular weight of 23743 Da.
PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding. (updated: June 20, 2018)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
- Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
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| Variant | Description |
|---|---|
| OI9 | |
| dbSNP:rs11558595 |
Biological Process
Bone development
Chaperone-mediated protein folding
Collagen fibril organization
Extracellular matrix organization
Neutrophil chemotaxis
Positive regulation by host of viral genome replication
Positive regulation by host of viral process
Positive regulation of multicellular organism growth
Protein folding
Protein peptidyl-prolyl isomerization
Protein refolding
Protein stabilization
Cellular Component
Cytoplasm
Endoplasmic reticulum
Endoplasmic reticulum chaperone complex
Endoplasmic reticulum lumen
Extracellular exosome
Focal adhesion
Intracellular membrane-bounded organelle
Melanosome
Membrane
Nucleoplasm
Nucleus
Perinuclear region of cytoplasm
Protein-containing complex
Smooth endoplasmic reticulum
The reference OMIM entry for this protein is 123841
Peptidyl-prolyl isomerase b; ppib
Cyclophilin b; cypb
DESCRIPTION
Cyclophilins, such as CYPB, bind the immunosuppressive drug cyclosporin A (CsA) with high affinity. CsA blocks helper T-cell activation at a step between T-cell receptor stimulation and the transcriptional activation of cytokine genes. Cyclophilins from many species possess peptidyl-prolyl cis-trans isomerase (PPIase) activity that is blocked by CsA and therefore may be relevant in CsA-mediated immunosuppression (Price et al., 1991).CLONING
Probing with the cyclophilin A (CYPA; 123840) cDNA under reduced stringencies, Price et al. (1991) identified the CYPB gene. The deduced protein is 64% identical to CYPA and is distinguished from it by a signal sequence that probably directs it to the endoplasmic reticulum (ER). CYPB shows even stronger similarity to yeast CYPB, which also has an ER-directed signal sequence.MAPPING
Peddada et al. (1992) used the PCR technique to generate a unique probe complementary to the hydrophobic 5-prime end of the human cyclophilin B gene. Using this probe in an analysis of human/hamster hybrid somatic cell lines, they assigned the CYPB gene to chromosome 15.GENE FUNCTION
Price et al. (1991) found that the signal sequence was removed from CYPB upon expression in E. coli, and the processed protein possessed PPIase activity that was inhibited by CsA. Yurchenko et al. (2001) determined that CD147 (BSG; 109480) serves as a receptor for CYPB. CYPB induced Ca(2+) flux, ERK (see MAPK3; 601795) phosphorylation, and chemotaxis in CD147-transfected Chinese hamster ovary cells, but not in control cells. The chemotactic response of primary human neutrophils to CYPB was blocked by antibodies to CD147. FHOD1 (606881) regulates gene transcription, actin-cytoskeleton structure, and cell migration. Using a yeast 2-hybrid screen with a human bone marrow cDNA expression library, Westendorf and Koka (2004) found that FHOD1 interacted with cyclophilin B, as well as with the central portion of PRKCBP1 (ZMYND8; 615713) and the B isoform of WISH (NCKIPSD; 606671). Using CsA as a bioprobe to identify cellular factors involved in hepatitis C virus (HCV) genome replication, Watashi et al. (2005) showed that CYPB interacts with HCV RNA polymerase NS5B to directly stimulate its RNA binding activity. HCV replication could be reduced by RNA interference-mediated reduction of endogenous CYPB expression or by the induced loss of NS5B binding to CYPB. Watashi et al. (2005) concluded that CYPB functions as a stimulatory regulator of NS5B in the HCV replication machinery and suggested that CYPB could be a target for antiviral therapy.MOLECULAR GENETICS
CRTAP (605497), P3H1 (LEPRE1; 610339), and CYPB (PPIB) form an intracellular collagen-modifying complex that 3-hydroxylates proline at position 986 (P986) in the alpha-1 chains of collagen type I (120150), and deficiency of CRTAP or P3H1 has been reported in autosomal recessive lethal or severe osteogenesis imperfecta (OI; see 610682 and 610915). In 4 patients with osteogenesis imperfecta type IX (OI9; 259440) from 2 unrelated families, van Dijk et al. (2009) analyzed the PPIB gene and identified homozygosity for a 4-bp deletion (123841.0001) and a nonsense mutation (123841.0002), respectively. The percentage of 3-hydroxylated P986 residues in patients with PPIB mutations was decreased in comparison to controls, but it was higher than in patients with CRTAP or LEPRE1 mutations. In addition, in bone tissue from patients with CRTA ... More on the omim web site
July 2, 2018: Protein entry updated
Automatic update: Entry updated from uniprot information.
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
June 20, 2017: Protein entry updated
Automatic update: comparative model was added.
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 123841 was added.
Jan. 28, 2016: Protein entry updated
Automatic update: model status changed
Jan. 25, 2016: Protein entry updated
Automatic update: model status changed