PPIH

Peptidylprolyl isomerase H (cyclophilin H), also known as PPIH, is a human gene.cite web | title = Entrez Gene: PPIH peptidylprolyl isomerase H (cyclophilin H)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10465| accessdate = ]

PBB_Summary
section_title =
summary_text = The protein encoded by this gene is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. This protein is a specific component of the complex that includes pre-mRNA processing factors PRPF3, PRPF4, and PRPF18, as well as U4/U5/U6 tri-snRNP. This protein has been shown to possess PPIase activity and may act as a protein chaperone that mediates the interactions between different proteins inside the spliceosome.cite web | title = Entrez Gene: PPIH peptidylprolyl isomerase H (cyclophilin H)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10465| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Horowitz DS, Kobayashi R, Krainer AR |title=A new cyclophilin and the human homologues of yeast Prp3 and Prp4 form a complex associated with U4/U6 snRNPs. |journal=RNA |volume=3 |issue= 12 |pages= 1374–87 |year= 1997 |pmid= 9404889 |doi=
*cite journal | author=Teigelkamp S, Achsel T, Mundt C, "et al." |title=The 20kD protein of human [U4/U6.U5] tri-snRNPs is a novel cyclophilin that forms a complex with the U4/U6-specific 60kD and 90kD proteins. |journal=RNA |volume=4 |issue= 2 |pages= 127–41 |year= 1998 |pmid= 9570313 |doi=
*cite journal | author=Reidt U, Reuter K, Achsel T, "et al." |title=Crystal structure of the human U4/U6 small nuclear ribonucleoprotein particle-specific SnuCyp-20, a nuclear cyclophilin. |journal=J. Biol. Chem. |volume=275 |issue= 11 |pages= 7439–42 |year= 2000 |pmid= 10713041 |doi=
*cite journal | author=Horowitz DS, Lee EJ, Mabon SA, Misteli T |title=A cyclophilin functions in pre-mRNA splicing. |journal=EMBO J. |volume=21 |issue= 3 |pages= 470–80 |year= 2002 |pmid= 11823439 |doi=
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Reidt U, Wahl MC, Fasshauer D, "et al." |title=Crystal structure of a complex between human spliceosomal cyclophilin H and a U4/U6 snRNP-60K peptide. |journal=J. Mol. Biol. |volume=331 |issue= 1 |pages= 45–56 |year= 2003 |pmid= 12875835 |doi=
*cite journal | author=Ingelfinger D, Göthel SF, Marahiel MA, "et al." |title=Two protein-protein interaction sites on the spliceosome-associated human cyclophilin CypH. |journal=Nucleic Acids Res. |volume=31 |issue= 16 |pages= 4791–6 |year= 2004 |pmid= 12907720 |doi=
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Andersen JS, Lam YW, Leung AK, "et al." |title=Nucleolar proteome dynamics. |journal=Nature |volume=433 |issue= 7021 |pages= 77–83 |year= 2005 |pmid= 15635413 |doi= 10.1038/nature03207
*cite journal | author=Rual JF, Venkatesan K, Hao T, "et al." |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173–8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209

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