Version 5.4
Homo sapiens Protein: FPGT
Summary
InnateDB Protein IDBP-99718.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol FPGT
Protein Name fucose-1-phosphate guanylyltransferase
Synonyms GFPP;
Species Homo sapiens
Ensembl Protein ENSP00000359935
InnateDB Gene IDBG-545534 (FPGT)
Protein Structure
UniProt Annotation
Function Catalyzes the formation of GDP-L-fucose from GTP and L- fucose-1-phosphate. Functions as a salvage pathway to reutilize L- fucose arising from the turnover of glycoproteins and glycolipids.
Subcellular Localization Cytoplasm.
Disease Associations
Tissue Specificity Expressed in many tissues.
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 3 experimentally validated interaction(s) in this database.
They are also associated with 1 interaction(s) predicted by orthology.
Experimentally validated
Total 3 [view]
Protein-Protein 1 [view]
Protein-DNA 2 [view]
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Predicted by orthology
Total 1 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0003824 catalytic activity
GO:0005525 GTP binding
GO:0016772 transferase activity, transferring phosphorus-containing groups
GO:0047341 fucose-1-phosphate guanylyltransferase activity
Biological Process
GO:0006004 fucose metabolic process
Cellular Component
GO:0005737 cytoplasm
Protein Structure and Domains
PDB ID
InterPro IPR011004 Trimeric LpxA-like
IPR012120 Fucose-1-phosphate guanylyltransferase
IPR012887 L-fucokinase
PFAM PF07959
PRINTS
PIRSF PIRSF036640
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt
PhosphoSite PhosphoSite-O14772
TrEMBL
UniProt Splice Variant
Entrez Gene 8790
UniGene Hs.480085
RefSeq NP_003829
HUGO HGNC:3825
OMIM 603609
CCDS CCDS663
HPRD 06790
IMGT
EMBL AC098692 AF017445 AF017446 AK299468 AK304490 BC032308
GenPept AAC73005 AAC82511 AAH32308 BAG61434 BAG65299

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