Version 5.4
Mus musculus Protein: Pigq
Summary
InnateDB Protein IDBP-154073.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Pigq
Protein Name phosphatidylinositol glycan anchor biosynthesis, class Q
Synonyms Gpi1; Gpi1h; Gpi1p; Gpih;
Species Mus musculus
Ensembl Protein ENSMUSP00000026823
InnateDB Gene IDBG-154069 (Pigq)
Protein Structure
UniProt Annotation
Function Part of the complex catalyzing the transfer of N- acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI biosynthesis.
Subcellular Localization 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 7 interaction(s) predicted by orthology.
Predicted by orthology
Total 7 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0017176 phosphatidylinositol N-acetylglucosaminyltransferase activity
Biological Process
GO:0006506 GPI anchor biosynthetic process
Cellular Component
GO:0000506 glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex
GO:0016021 integral component of membrane
Protein Structure and Domains
PDB ID MGI:1333114
InterPro IPR007720 N-acetylglucosaminyl transferase component
PFAM PF05024
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q9QYT7
PhosphoSite PhosphoSite-Q9QYT7
TrEMBL Q3TF56
UniProt Splice Variant
Entrez Gene 14755
UniGene Mm.407751
RefSeq NP_035952
MGI ID
MGI Symbol Pigq
OMIM
CCDS CCDS28538
HPRD
IMGT
EMBL AB008895 AB008921 AC159277 AF030178 AK163680 AK169284 BC003917 BC014287 CH466606
GenPept AAC79574 AAH03917 AAH14287 BAA23615 BAA84658 BAE37455 BAE41042 EDL22475

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