PPIH

PPIH
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1MZW, 1QOI
Identifiers
Aliases	PPIH , CYP-20, CYPH, SnuCyp-20, USA-CYP, peptidylprolyl isomerase H
External IDs	OMIM: 606095 MGI: 106499 HomoloGene: 38172 GeneCards: PPIH
Gene location (Human) Chr. Chromosome 1 (human) [1] Band 1p34.2 Start 42,658,335 bp [1] End 42,676,758 bp [1]
Gene location (Mouse) Chr. Chromosome 4 (mouse) [2] Band 4 D2.1|4 55.34 cM Start 119,157,207 bp [2] End 119,177,743 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in embryo ganglionic eminence secondary oocyte rectum lymph node left lobe of thyroid gland monocyte islet of Langerhans spleen right lobe of thyroid gland Top expressed in spermatocyte yolk sac morula spermatid lip neural tube thymus primitive streak duodenum mirror More reference expression data BioGPS More reference expression data
Gene ontology Molecular function ribonucleoprotein complex binding isomerase activity protein binding peptidyl-prolyl cis-trans isomerase activity cyclosporin A binding unfolded protein binding Cellular component cytoplasm nuclear speck U4/U6 x U5 tri-snRNP complex spliceosomal complex nucleus nucleoplasm U4/U6 snRNP Biological process mRNA splicing, via spliceosome mRNA processing positive regulation of viral genome replication protein folding RNA splicing protein-containing complex assembly protein peptidyl-prolyl isomerization angiogenesis protein refolding Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 10465 66101 Ensembl ENSG00000171960 ENSMUSG00000060288 UniProt O43447 Q9D868 RefSeq (mRNA) NM_006347 NM_001330510 NM_001110129 NM_001110130 NM_028677 RefSeq (protein) NP_001317439 NP_006338 NP_001103599 NP_001103600 NP_082953 Location (UCSC) Chr 1: 42.66 – 42.68 Mb Chr 4: 119.16 – 119.18 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Peptidyl-prolyl cis-trans isomerase H is an enzyme that in humans is encoded by the PPIH gene. ^{[5] [6] [7]}

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. ^[7]

References

1. GRCh38: Ensembl release 89: ENSG00000171960 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000060288 - 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. Horowitz DS, Kobayashi R, Krainer AR (Dec 1997). "A new cyclophilin and the human homologues of yeast Prp3 and Prp4 form a complex associated with U4/U6 snRNPs". RNA. 3 (12): 1374–87. PMC   1369579 . PMID   9404889.
6. Teigelkamp S, Achsel T, Mundt C, Gothel SF, Cronshagen U, Lane WS, Marahiel M, Luhrmann R (May 1998). "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". RNA. 4 (2): 127–41. PMC   1369602 . PMID   9570313.
7. "Entrez Gene: PPIH peptidylprolyl isomerase H (cyclophilin H)".

Further reading

• Reidt U, Reuter K, Achsel T, et al. (2000). "Crystal structure of the human U4/U6 small nuclear ribonucleoprotein particle-specific SnuCyp-20, a nuclear cyclophilin" (PDF). J. Biol. Chem. 275 (11): 7439–42. doi: 10.1074/jbc.275.11.7439 . PMID   10713041. S2CID   20261807.
• Horowitz DS, Lee EJ, Mabon SA, Misteli T (2002). "A cyclophilin functions in pre-mRNA splicing". EMBO J. 21 (3): 470–80. doi:10.1093/emboj/21.3.470. PMC   125845 . PMID   11823439.
• 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.
• Reidt U, Wahl MC, Fasshauer D, et al. (2003). "Crystal structure of a complex between human spliceosomal cyclophilin H and a U4/U6 snRNP-60K peptide". J. Mol. Biol. 331 (1): 45–56. doi:10.1016/S0022-2836(03)00684-3. hdl: 11858/00-001M-0000-0012-F238-B . PMID   12875835.
• Ingelfinger D, Göthel SF, Marahiel MA, et al. (2004). "Two protein–protein interaction sites on the spliceosome-associated human cyclophilin CypH". Nucleic Acids Res. 31 (16): 4791–6. doi:10.1093/nar/gkg660. PMC   169899 . PMID   12907720.
• 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.
• Andersen JS, Lam YW, Leung AK, et al. (2005). "Nucleolar proteome dynamics". Nature. 433 (7021): 77–83. Bibcode:2005Natur.433...77A. doi:10.1038/nature03207. PMID   15635413. S2CID   4344740.
• 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.