Version 5.4
Homo sapiens Protein: PPIL4
Summary
InnateDB Protein IDBP-97731.5
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol PPIL4
Protein Name peptidylprolyl isomerase (cyclophilin)-like 4
Synonyms
Species Homo sapiens
Ensembl Protein ENSP00000253329
InnateDB Gene IDBG-97729 (PPIL4)
Protein Structure
UniProt Annotation
Function PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity). {ECO:0000250}.
Subcellular Localization Nucleus {ECO:0000305}.
Disease Associations
Tissue Specificity Abundantly expressed in kidney but has a ubiquitously low expression pattern in other adult tissues. {ECO:0000269PubMed:11978968}.
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 10 experimentally validated interaction(s) in this database.
Experimentally validated
Total 10 [view]
Protein-Protein 10 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Gene Ontology

Molecular Function
Accession GO Term
GO:0000166 nucleotide binding
GO:0003676 nucleic acid binding
GO:0003755 peptidyl-prolyl cis-trans isomerase activity
GO:0044822 poly(A) RNA binding
Biological Process
GO:0000413 protein peptidyl-prolyl isomerization
GO:0006457 protein folding
Cellular Component
GO:0005634 nucleus
Protein Structure and Domains
PDB ID
InterPro IPR000504 RNA recognition motif domain
IPR002130 Cyclophilin-type peptidyl-prolyl cis-trans isomerase domain
IPR029000 Cyclophilin-like domain
PFAM PF00076
PF00160
PRINTS PR00153
PIRSF
SMART SM00360
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q8WUA2
PhosphoSite PhosphoSite-Q8WUA2
TrEMBL Q9P1R3
UniProt Splice Variant
Entrez Gene 85313
UniGene Hs.743579
RefSeq NP_624311
HUGO HGNC:15702
OMIM 607609
CCDS CCDS34550
HPRD 07606
IMGT
EMBL AF068298 AF308286 AF357880 AK315388 AL078581 AL357619 BC016984 BC020986 BX537536 CH471051
GenPept AAF65187 AAG48254 AAH16984 AAH20986 AAM63961 BAG37781 CAD97776 CAI16471 CAI19508 EAW47799

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