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PPIG
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2GW2, 2WFI, 2WFJ
Identifiers
Aliases	PPIG, CARS-Cyp, CYP, SCAF10, SRCyp, peptidylprolyl isomerase G
External IDs	OMIM: 606093; MGI: 2445173; HomoloGene: 3520; GeneCards: PPIG; OMA:PPIG - orthologs
Gene location (Human) Chr. Chromosome 2 (human) Band 2q31.1 Start 169,584,342 bp End 169,641,406 bp
Gene location (Mouse) Chr. Chromosome 2 (mouse) Band 2|2 C2 Start 69,552,889 bp End 69,584,356 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in sural nerve secondary oocyte Achilles tendon internal globus pallidus tendon of biceps brachii superficial temporal artery caput epididymis pylorus lactiferous duct tail of epididymis Top expressed in zygote genital tubercle morula tail of embryo saccule otic placode otic vesicle secondary oocyte blastocyst embryo More reference expression data BioGPS More reference expression data
Gene ontology Molecular function cyclosporin A binding protein binding isomerase activity RNA binding peptidyl-prolyl cis-trans isomerase activity unfolded protein binding Cellular component nuclear matrix nucleus nucleoplasm cytosol nuclear speck Biological process protein folding RNA splicing protein peptidyl-prolyl isomerization protein refolding Sources:Amigo / QuickGO
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 NP_001394390 NP_001394391 NP_001394392 NP_001394393 NP_001394394 NP_001394395 NP_001394397 NP_001394402 NP_001394403 NP_001394404 NP_001394405 NP_001394406 NP_001394407 NP_001394408 NP_001394409 NP_001394410 NP_001394411 NP_001394412 NP_001394413 Location (UCSC) Chr 2: 169.58 – 169.64 Mb Chr 2: 69.55 – 69.58 Mb PubMed search
Wikidata
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Peptidyl-prolyl cis-trans isomerase G is an enzyme that in humans is encoded by the PPIG gene.

Interactions

PPIG (gene) has been shown to interact with Pinin.

References

1. ^ GRCh38: Ensembl release 89: ENSG00000138398 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000042133 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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.
6. 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.
7. "Entrez Gene: PPIG peptidylprolyl isomerase G (cyclophilin G)".
8. Lin CL, 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. 321 (3). United States: 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. Bibcode:2002PNAS...9916899M. 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. Bibcode:2004PNAS..10112130B. 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. Bibcode:2004CBio...14.1436J. doi:10.1016/j.cub.2004.07.051. PMID 15324660. S2CID 2371325.
• 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. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
• 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. S2CID 7827573.
• Davis TL, Walker JR, Campagna-Slater V, et al. (2010). "Structural and biochemical characterization of the human cyclophilin family of peptidyl-prolyl isomerases". PLOS Biol. 8 (7): e1000439. doi:10.1371/journal.pbio.1000439. PMC 2911226. PMID 20676357.

External links

• Overview of all the structural information available in the PDB for UniProt: Q13427 (Peptidyl-prolyl cis-trans isomerase G) at the PDBe-KB.

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