Version 5.4
Homo sapiens Protein: PPIH
Summary
InnateDB Protein IDBP-97226.5
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol PPIH
Protein Name peptidylprolyl isomerase H (cyclophilin H)
Synonyms
Species Homo sapiens
Ensembl Protein ENSP00000306614
InnateDB Gene IDBG-97224 (PPIH)
Protein Structure
UniProt Annotation
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, one of the building blocks of the spliceosome. May act as a chaperone. {ECO:0000269PubMed:11823439, ECO:0000269PubMed:12875835, ECO:0000269PubMed:9570313}.
Subcellular Localization Nucleus speckle {ECO:0000269PubMed:9570313}. Cytoplasm {ECO:0000269PubMed:9570313}. Note=Colocalizes with spliceosomal snRNPs. A small proportion may also be cytoplasmic.
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 26 experimentally validated interaction(s) in this database.
Experimentally validated
Total 26 [view]
Protein-Protein 25 [view]
Protein-DNA 1 [view]
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Gene Ontology

Molecular Function
Accession GO Term
GO:0003755 peptidyl-prolyl cis-trans isomerase activity
GO:0005515 protein binding
GO:0016018 cyclosporin A binding
GO:0043021 ribonucleoprotein complex binding
Biological Process
GO:0000398 mRNA splicing, via spliceosome
GO:0000413 protein peptidyl-prolyl isomerization
GO:0006457 protein folding
GO:0006461 protein complex assembly
GO:0045070 positive regulation of viral genome replication
Cellular Component
GO:0005681 spliceosomal complex
GO:0005737 cytoplasm
GO:0016607 nuclear speck
GO:0046540 U4/U6 x U5 tri-snRNP complex
GO:0071001 U4/U6 snRNP
Protein Structure and Domains
PDB ID
InterPro IPR002130 Cyclophilin-type peptidyl-prolyl cis-trans isomerase domain
IPR029000 Cyclophilin-like domain
PFAM PF00160
PRINTS PR00153
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt O43447
PhosphoSite PhosphoSite-O43447
TrEMBL Q6FH36
UniProt Splice Variant
Entrez Gene 10465
UniGene Hs.256639
RefSeq NP_006338
HUGO HGNC:14651
OMIM 606095
CCDS CCDS469
HPRD 12084
IMGT
EMBL AC098484 AF016371 AF036331 AK311979 BC003412 BT019343 CH471059 CR541920
GenPept AAC51927 AAC60793 AAH03412 AAV38150 BAG34918 CAG46718 EAX07153 EAX07156

If you use InnateDB for your research, please cite the following publication:

Breuer et al., InnateDB: systems biology of innate immunity and beyond - recent updates and continuing curation. Nucl. Acids Res. (2013) 41 (D1) 

InnateDB is being developed jointly by the Brinkman Laboratory (Simon Fraser University, British Columbia, Canada), the Hancock Laboratory (University of British Columbia, Vancouver, British Columbia) and the Lynn EMBL Australia Group (South Australian Health & Medical Research Institute and Flinders University, Adelaide, Australia).

Funding is currently provided by Allergen and EMBL Australia. Previous funding has been provided by Genome Canada, the Foundation for the National Institutes of Health through the Grand Challenges in Global Health initiative and by Teagasc. InnateDB curated interactions are licensed under the Design Science License. All other data is licensed under the terms of the originating database. Contact: innatedb-mail@sfu.ca