Version 5.4
Mus musculus Protein: Ppil4
Summary
InnateDB Protein IDBP-132687.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Ppil4
Protein Name peptidylprolyl isomerase (cyclophilin)-like 4
Synonyms 3732410E19Rik; 3830425H19Rik; AI788954; AW146233; PPIase;
Species Mus musculus
Ensembl Protein ENSMUSP00000015901
InnateDB Gene IDBG-132685 (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:0000250}.
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 0 experimentally validated interaction(s) in this database.
They are also associated with 5 interaction(s) predicted by orthology.
Predicted by orthology
Total 5 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0000166 nucleotide binding
GO:0003676 nucleic acid binding
GO:0003723 RNA 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
GO:0008150 biological_process
Cellular Component
GO:0005575 cellular_component
GO:0005634 nucleus
Protein Structure and Domains
PDB ID MGI:1914668
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 Q9CXG3
PhosphoSite PhosphoSite-Q9CXG3
TrEMBL Q9D3J1
UniProt Splice Variant
Entrez Gene 67418
UniGene Mm.421918
RefSeq NP_080417
MGI ID
MGI Symbol Ppil4
OMIM
CCDS CCDS23690
HPRD
IMGT
EMBL AC159137 AK011443 AK012371 AK013377 AK014406 AK017370 AK167258 BC079912
GenPept AAH79912 BAB27623 BAB28194 BAB28818 BAB29330 BAB30711 BAE39374

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