PPIB

Peptidylprolyl isomerase B (cyclophilin B)

PDB rendering based on 1cyn.

Available structures
PDB	1CYN, 3ICH, 3ICI

Identifiers

Symbols

PPIB; CYP-S1; CYPB; MGC14109; MGC2224; OI9; SCYLP

External IDs

OMIM: 123841 MGI: 97750 HomoloGene: 726 GeneCards: PPIB Gene

EC number

5.2.1.8

Gene Ontology
Molecular function	• peptidyl-prolyl cis-trans isomerase activity • protein binding • isomerase activity • peptide binding • unfolded protein binding
Cellular component	• endoplasmic reticulum • endoplasmic reticulum lumen • melanosome
Biological process	• protein peptidyl-prolyl isomerization • protein folding
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 15:
64.45 – 64.46 Mb

Chr 9:
65.91 – 65.91 Mb

PubMed search

[1]

[2]

Peptidyl-prolyl cis-trans isomerase B is an enzyme that in humans is encoded by the PPIB gene.^[1]

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.^[2]

Interactions

PPIB has been shown to interact with Apolipoprotein B.^[3]

References

^ Price ER, Zydowsky LD, Jin MJ, Baker CH, McKeon FD, Walsh CT (Apr 1991). "Human cyclophilin B: a second cyclophilin gene encodes a peptidyl-prolyl isomerase with a signal sequence". Proc Natl Acad Sci U S A 88 (5): 1903–7. doi:10.1073/pnas.88.5.1903. PMC 51134. PMID 2000394. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=51134.
^ "Entrez Gene: PPIB peptidylprolyl isomerase B (cyclophilin B)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5479.
^ Zhang, Jianying; Herscovitz Haya (Feb. 2003). "Nascent lipidated apolipoprotein B is transported to the Golgi as an incompletely folded intermediate as probed by its association with network of endoplasmic reticulum molecular chaperones, GRP94, ERp72, BiP, calreticulin, and cyclophilin B". J. Biol. Chem. (United States) 278 (9): 7459–68. doi:10.1074/jbc.M207976200. ISSN 0021-9258. PMID 12397072.

Rasmussen HH, van Damme J, Puype M, et al. (1993). "Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes.". Electrophoresis 13 (12): 960–9. doi:10.1002/elps.11501301199. PMID 1286667.
Peddada LB, McPherson JD, Law R, et al. (1992). "Somatic cell mapping of the human cyclophilin B gene (PPIB) to chromosome 15.". Cytogenet. Cell Genet. 60 (3–4): 219–21. doi:10.1159/000133343. PMID 1505219.
Arber S, Krause KH, Caroni P (1992). "s-cyclophilin is retained intracellularly via a unique COOH-terminal sequence and colocalizes with the calcium storage protein calreticulin". J. Cell Biol. 116 (1): 113–25. doi:10.1083/jcb.116.1.113. PMC 2289259. PMID 1530944. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2289259.
Hasel KW, Glass JR, Godbout M, Sutcliffe JG (1991). "An endoplasmic reticulum-specific cyclophilin". Mol. Cell. Biol. 11 (7): 3484–91. PMC 361082. PMID 1710767. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=361082.
Spik G, Haendler B, Delmas O, et al. (1991). "A novel secreted cyclophilin-like protein (SCYLP)". J. Biol. Chem. 266 (17): 10735–8. PMID 2040592.
Bram RJ, Crabtree GR (1994). "Calcium signalling in T cells stimulated by a cyclophilin B-binding protein". Nature 371 (6495): 355–8. doi:10.1038/371355a0. PMID 7522304.
Allain F, Boutillon C, Mariller C, Spik G (1995). "Selective assay for CyPA and CyPB in human blood using highly specific anti-peptide antibodies". J. Immunol. Methods 178 (1): 113–20. doi:10.1016/0022-1759(94)00249-V. PMID 7829860.
Price ER, Jin M, Lim D, et al. (1994). "Cyclophilin B trafficking through the secretory pathway is altered by binding of cyclosporin A". Proc. Natl. Acad. Sci. U.S.A. 91 (9): 3931–5. doi:10.1073/pnas.91.9.3931. PMC 43696. PMID 7909608. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=43696.
Mikol V, Kallen J, Walkinshaw MD (1994). "X-ray structure of a cyclophilin B/cyclosporin complex: comparison with cyclophilin A and delineation of its calcineurin-binding domain". Proc. Natl. Acad. Sci. U.S.A. 91 (11): 5183–6. doi:10.1073/pnas.91.11.5183. PMC 43956. PMID 8197205. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=43956.
Allain F, Denys A, Spik G (1994). "Characterization of surface binding sites for cyclophilin B on a human tumor T-cell line". J. Biol. Chem. 269 (24): 16537–40. PMID 8206968.
Luban J, Bossolt KL, Franke EK, et al. (1993). "Human immunodeficiency virus type 1 Gag protein binds to cyclophilins A and B". Cell 73 (6): 1067–78. doi:10.1016/0092-8674(93)90637-6. PMID 8513493.
Braaten D, Ansari H, Luban J (1997). "The hydrophobic pocket of cyclophilin is the binding site for the human immunodeficiency virus type 1 Gag polyprotein". J. Virol. 71 (3): 2107–13. PMC 191305. PMID 9032343. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=191305.
Montague JW, Hughes FM, Cidlowski JA (1997). "Native recombinant cyclophilins A, B, and C degrade DNA independently of peptidylprolyl cis-trans-isomerase activity. Potential roles of cyclophilins in apoptosis". J. Biol. Chem. 272 (10): 6677–84. doi:10.1074/jbc.272.10.6677. PMID 9045699.
Denys A, Allain F, Foxwell B, Spik G (1997). "Distribution of cyclophilin B-binding sites in the subsets of human peripheral blood lymphocytes". Immunology 91 (4): 609–17. doi:10.1046/j.1365-2567.1997.00296.x. PMC 1363883. PMID 9378502. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1363883.
Endrich MM, Gehring H (1998). "The V3 loop of human immunodeficiency virus type-1 envelope protein is a high-affinity ligand for immunophilins present in human blood". Eur. J. Biochem. 252 (3): 441–6. doi:10.1046/j.1432-1327.1998.2520441.x. PMID 9546659.
Endrich MM, Gehrig P, Gehring H (1999). "Maturation-induced conformational changes of HIV-1 capsid protein and identification of two high affinity sites for cyclophilins in the C-terminal domain". J. Biol. Chem. 274 (9): 5326–32. doi:10.1074/jbc.274.9.5326. PMID 10026140.
Bristow R, Byrne J, Squirell J, et al. (1999). "Human cyclophilin has a significantly higher affinity for HIV-1 recombinant p55 than p24". J. Acquir. Immune Defic. Syndr. Hum. Retrovirol. 20 (4): 334–6. PMID 10096576.
Rycyzyn MA, Reilly SC, O'Malley K, Clevenger CV (2001). "Role of cyclophilin B in prolactin signal transduction and nuclear retrotranslocation". Mol. Endocrinol. 14 (8): 1175–86. doi:10.1210/me.14.8.1175. PMID 10935542.
Yurchenko V, O'Connor M, Dai WW, et al. (2001). "CD147 is a signaling receptor for cyclophilin B". Biochem. Biophys. Res. Commun. 288 (4): 786–8. doi:10.1006/bbrc.2001.5847. PMID 11688976.

PDB gallery

1cyn: CYCLOPHILIN B COMPLEXED WITH [D-(CHOLINYLESTER)SER8]-CYCLOSPORIN

PPIB

Interactions

References

Further reading