Version 5.4
Mus musculus Protein: Pigh
Summary
InnateDB Protein IDBP-152584.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Pigh
Protein Name phosphatidylinositol glycan anchor biosynthesis, class H
Synonyms 2210416H01Rik; A930028P05Rik;
Species Mus musculus
Ensembl Protein ENSMUSP00000072018
InnateDB Gene IDBG-152582 (Pigh)
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. {ECO:0000250}.
Subcellular Localization Cytoplasm {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 4 interaction(s) predicted by orthology.
Predicted by orthology
Total 4 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0003674 molecular_function
GO:0017176 phosphatidylinositol N-acetylglucosaminyltransferase activity
Biological Process
GO:0006506 GPI anchor biosynthetic process
GO:0008150 biological_process
Cellular Component
GO:0000506 glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex
GO:0005730 nucleolus
GO:0005739 mitochondrion
Protein Structure and Domains
PDB ID MGI:99463
InterPro IPR019328 GPI-GlcNAc transferase complex, PIG-H component, conserved domain
PFAM PF10181
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q5M9N4
PhosphoSite PhosphoSite-
TrEMBL
UniProt Splice Variant
Entrez Gene 110417
UniGene Mm.268317
RefSeq NP_084264
MGI ID
MGI Symbol Pigh
OMIM
CCDS CCDS26006
HPRD
IMGT
EMBL AK167892 BC086806
GenPept AAH86806 BAE39904

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