PPIG (gene)

Peptidylprolyl isomerase G (cyclophilin G)
PDB rendering based on 2gw2.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 2GW2​, 2WFI​, 2WFJ​
Identifiers
Symbols	PPIG ; CARS-Cyp; CYP; SCAF10; SRCyp
External IDs	OMIM: 606093 MGI: 2445173 HomoloGene: 3520 GeneCards: PPIG Gene
EC number	5.2.1.8
Gene ontology Molecular function • peptidyl-prolyl cis-trans isomerase activity • protein binding • cyclosporin A binding • poly(A) RNA binding Cellular component • nucleus • nucleoplasm • cytoplasm • nuclear matrix • nuclear speck Biological process • protein peptidyl-prolyl isomerization • protein folding • RNA splicing Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	9360	228005
Ensembl	ENSG00000138398	ENSMUSG00000042133
UniProt	Q13427	A2AR02
RefSeq (mRNA)	NM_004792	NM_001081086
RefSeq (protein)	NP_004783	NP_001074555
Location (UCSC)	Chr 2: 169.58 – 169.64 Mb	Chr 2: 69.72 – 69.75 Mb
PubMed search

Peptidyl-prolyl cis-trans isomerase G is an enzyme that in humans is encoded by the PPIG gene.^[1][2][3]

Interactions

PPIG (gene) has been shown to interact with Pinin.^[4]

References

1. Nestel FP, Colwill K, Harper S, Pawson T, Anderson SK (Jan 1997). "RS cyclophilins: identification of an NK-TR1-related cyclophilin". Gene 180 (1-2): 151–5. doi:10.1016/S0378-1119(96)00436-2. PMID 8973360.
2. Bourquin JP, Stagljar I, Meier P, Moosmann P, Silke J, Baechi T, Georgiev O, Schaffner W (Jul 1997). "A serine/arginine-rich nuclear matrix cyclophilin interacts with the C-terminal domain of RNA polymerase II". Nucleic Acids Res 25 (11): 2055–61. doi:10.1093/nar/25.11.2055. PMC 146702. PMID 9153302.
3. "Entrez Gene: PPIG peptidylprolyl isomerase G (cyclophilin G)".
4. Lin, Chun Lun; Leu Steve; Lu Ming Chu; Ouyang Pin (Aug 2004). "Over-expression of SR-cyclophilin, an interaction partner of nuclear pinin, releases SR family splicing factors from nuclear speckles". Biochem. Biophys. Res. Commun. (United States) 321 (3): 638–47. doi:10.1016/j.bbrc.2004.07.013. ISSN 0006-291X. PMID 15358154.

Further reading

• 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.
• Dubourg B, Kamphausen T, Weiwad M, et al. (2004). "The human nuclear SRcyp is a cell cycle-regulated cyclophilin.". J. Biol. Chem. 279 (21): 22322–30. doi:10.1074/jbc.M400736200. PMID 15016823.
• Beausoleil SA, Jedrychowski M, Schwartz D, et al. (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins.". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
• Jin J, Smith FD, Stark C, et al. (2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization.". Curr. Biol. 14 (16): 1436–50. doi:10.1016/j.cub.2004.07.051. PMID 15324660.
• Lin CL, Leu S, Lu MC, Ouyang P (2004). "Over-expression of SR-cyclophilin, an interaction partner of nuclear pinin, releases SR family splicing factors from nuclear speckles.". Biochem. Biophys. Res. Commun. 321 (3): 638–47. doi:10.1016/j.bbrc.2004.07.013. PMID 15358154.
• 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.
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
• Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.". Cell 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.