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Identification
HMDB Protein ID HMDBP10695
Secondary Accession Numbers
  • 16956
Name Peptidyl-prolyl cis-trans isomerase H
Synonyms
  1. CypH
  2. PPIase H
  3. Rotamase H
  4. Small nuclear ribonucleoprotein particle-specific cyclophilin H
  5. U-snRNP-associated cyclophilin SnuCyp-20
  6. USA-CYP
Gene Name PPIH
Protein Type Enzyme
Biological Properties
General Function Involved in peptidyl-prolyl cis-trans isomerase activity
Specific Function PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Participates in pre-mRNA splicing. May play a role in the assembly of the U4/U5/U6 tri-snRNP complex. May act as a chaperone
Pathways Not Available
Reactions Not Available
GO Classification
Function
catalytic activity
cis-trans isomerase activity
peptidyl-prolyl cis-trans isomerase activity
isomerase activity
Process
metabolic process
macromolecule metabolic process
cellular protein metabolic process
protein folding
protein metabolic process
Cellular Location
  1. Cytoplasm
  2. Nucleus speckle
Gene Properties
Chromosome Location Chromosome:1
Locus 1p34.1
SNPs PPIH
Gene Sequence
>534 bp
ATGGCGGTGGCAAATTCAAGTCCTGTTAACCCCGTGGTGTTCTTTGATGTCAGTATTGGC
GGTCAGGAAGTTGGCCGCATGAAGATCGAGCTCTTTGCAGACGTTGTGCCTAAGACGGCC
GAGAACTTTAGGCAGTTCTGCACCGGAGAATTCAGGAAAGATGGGGTTCCAATAGGATAC
AAAGGAAGCACCTTCCACAGGGTCATAAAGGATTTCATGATTCAGGGTGGAGATTTTGTT
AATGGAGATGGTACTGGAGTCGCCAGTATTTACCGGGGGCCATTTGCAGATGAAAATTTT
AAACTTAGACACTCAGCTCCAGGCCTGCTTTCCATGGCGAACAGTGGTCCAAGTACAAAT
GGCTGTCAGTTCTTTATCACCTGCTCTAAGTGCGATTGGCTGGATGGGAAGCATGTGGTG
TTTGGAAAAATCATCGATGGACTTCTAGTGATGAGAAAGATTGAGAATGTTCCCACAGGC
CCCAACAATAAGCCCAAGCTACCTGTGGTGATCTCGCAGTGTGGGGAGATGTAG
Protein Properties
Number of Residues 177
Molecular Weight 19208.0
Theoretical pI 8.22
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence
>Peptidyl-prolyl cis-trans isomerase H
MAVANSSPVNPVVFFDVSIGGQEVGRMKIELFADVVPKTAENFRQFCTGEFRKDGVPIGY
KGSTFHRVIKDFMIQGGDFVNGDGTGVASIYRGPFADENFKLRHSAPGLLSMANSGPSTN
GCQFFITCSKCDWLDGKHVVFGKIIDGLLVMRKIENVPTGPNNKPKLPVVISQCGEM
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID O43447
UniProtKB/Swiss-Prot Entry Name PPIH_HUMAN
PDB IDs
GenBank Gene ID AF016371
GeneCard ID PPIH
GenAtlas ID PPIH
HGNC ID HGNC:14651
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  3. Horowitz DS, Kobayashi R, Krainer AR: A new cyclophilin and the human homologues of yeast Prp3 and Prp4 form a complex associated with U4/U6 snRNPs. RNA. 1997 Dec;3(12):1374-87. [PubMed:9404889 ]
  4. Reidt U, Wahl MC, Fasshauer D, Horowitz DS, Luhrmann R, Ficner R: Crystal structure of a complex between human spliceosomal cyclophilin H and a U4/U6 snRNP-60K peptide. J Mol Biol. 2003 Aug 1;331(1):45-56. [PubMed:12875835 ]
  5. Teigelkamp S, Achsel T, Mundt C, Gothel SF, Cronshagen U, Lane WS, Marahiel M, Luhrmann R: 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. 1998 Feb;4(2):127-41. [PubMed:9570313 ]
  6. Horowitz DS, Lee EJ, Mabon SA, Misteli T: A cyclophilin functions in pre-mRNA splicing. EMBO J. 2002 Feb 1;21(3):470-80. [PubMed:11823439 ]
  7. Reidt U, Reuter K, Achsel T, Ingelfinger D, Luhrmann R, Ficner R: Crystal structure of the human U4/U6 small nuclear ribonucleoprotein particle-specific SnuCyp-20, a nuclear cyclophilin. J Biol Chem. 2000 Mar 17;275(11):7439-42. [PubMed:10713041 ]