PPIL2

Peptidylprolyl isomerase (cyclophilin)-like 2
PDB rendering based on 1zkc.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1ZKC​
Identifiers
Symbols	PPIL2 ; CYC4; CYP60; Cyp-60; UBOX7; hCyP-60
External IDs	OMIM: 607588 MGI: 2447857 HomoloGene: 8643 GeneCards: PPIL2 Gene
EC number	5.2.1.8
Gene ontology Molecular function • peptidyl-prolyl cis-trans isomerase activity • protein binding • ligase activity • ubiquitin-ubiquitin ligase activity • ubiquitin protein ligase activity Cellular component • nucleus • nucleoplasm • cytoplasm • Golgi lumen • plasma membrane Biological process • protein polyubiquitination • protein peptidyl-prolyl isomerization • protein folding • blood coagulation • leukocyte migration • protein localization to plasma membrane Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	23759	66053
Ensembl	ENSG00000100023	ENSMUSG00000022771
UniProt	Q13356	Q9D787
RefSeq (mRNA)	NM_014337	NM_001252444
RefSeq (protein)	NP_055152	NP_001239373
Location (UCSC)	Chr 22: 21.65 – 21.7 Mb	Chr 16: 17.09 – 17.11 Mb
PubMed search

Peptidyl-prolyl cis-trans isomerase-like 2 is an enzyme that in humans is encoded by the PPIL2 gene.^[1][2]

This gene is a member of the cyclophilin family of peptidylprolyl isomerases. The cyclophilins are a highly conserved ubiquitous family, members of which play an important role in protein folding, immunosuppression by cyclosporin A, and infection of HIV-1 virions. This protein interacts with the proteinase inhibitor eglin c and is localized in the nucleus. Multiple transcript variants encoding different isoforms have been found for this gene.^[2]

References

1. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP; et al. (Dec 1999). "The DNA sequence of human chromosome 22". Nature 402 (6761): 489–95. doi:10.1038/990031. PMID 10591208.
2. "Entrez Gene: PPIL2 peptidylprolyl isomerase (cyclophilin)-like 2".

Further reading

• Wang BB, Hayenga KJ, Payan DG, Fisher JM (1996). "Identification of a nuclear-specific cyclophilin which interacts with the proteinase inhibitor eglin c". Biochem. J. 314 (1): 313–9. PMC 1217042. PMID 8660300.
• Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• Collins JE, Wright CL, Edwards CA, et al. (2005). "A genome annotation-driven approach to cloning the human ORFeome". Genome Biol. 5 (10): R84. doi:10.1186/gb-2004-5-10-r84. PMC 545604. PMID 15461802.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Pushkarsky T, Yurchenko V, Vanpouille C, et al. (2005). "Cell surface expression of CD147/EMMPRIN is regulated by cyclophilin 60". J. Biol. Chem. 280 (30): 27866–71. doi:10.1074/jbc.M503770200. PMID 15946952.
• Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.