Version 5.4
Mus musculus Protein: Pigu
Summary
InnateDB Protein IDBP-622617.2
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Pigu
Protein Name phosphatidylinositol glycan anchor biosynthesis, class U
Synonyms
Species Mus musculus
Ensembl Protein ENSMUSP00000126236
InnateDB Gene IDBG-210539 (Pigu)
Protein Structure
UniProt Annotation
Function Component of the GPI transamidase complex. May be involved in the recognition of either the GPI attachment signal or the lipid portion of GPI (By similarity). {ECO:0000250}.
Subcellular Localization Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
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
Biological Process
GO:0006506 GPI anchor biosynthetic process
Cellular Component
GO:0005789 endoplasmic reticulum membrane
GO:0016021 integral component of membrane
GO:0042765 GPI-anchor transamidase complex
Protein Structure and Domains
PDB ID MGI:3039607
InterPro IPR009600 GPI transamidase subunit PIG-U
PFAM PF06728
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q8K358
PhosphoSite PhosphoSite-Q8K358
TrEMBL
UniProt Splice Variant
Entrez Gene 228812
UniGene Mm.5434
RefSeq
MGI ID
MGI Symbol Pigu
OMIM
CCDS
HPRD
IMGT
EMBL AL845325 AL929588 BC028278
GenPept AAH28278

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