Version 5.4
Homo sapiens Protein: GYG2
Summary
InnateDB Protein IDBP-40984.5
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol GYG2
Protein Name glycogenin 2
Synonyms GN-2; GN2;
Species Homo sapiens
Ensembl Protein ENSP00000370555
InnateDB Gene IDBG-40982 (GYG2)
Protein Structure
UniProt Annotation
Function Self-glucosylates, via an inter-subunit mechanism, to form an oligosaccharide primer that serves as substrate for glycogen synthase.
Subcellular Localization
Disease Associations
Tissue Specificity Expressed preferentially in liver, heart, and pancreas.
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 10 experimentally validated interaction(s) in this database.
Experimentally validated
Total 10 [view]
Protein-Protein 10 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Gene Ontology

Molecular Function
Accession GO Term
GO:0008466 glycogenin glucosyltransferase activity
GO:0016757 transferase activity, transferring glycosyl groups
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0005978 glycogen biosynthetic process
GO:0005980 glycogen catabolic process
GO:0006006 glucose metabolic process
GO:0044281 small molecule metabolic process
Cellular Component
GO:0005829 cytosol
Protein Structure and Domains
PDB ID
InterPro IPR002495 Glycosyl transferase, family 8
IPR029044 Nucleotide-diphospho-sugar transferases
PFAM PF01501
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt O15488
PhosphoSite PhosphoSite-O15488
TrEMBL
UniProt Splice Variant
Entrez Gene 8908
UniGene Hs.701629
RefSeq NP_003909
HUGO HGNC:4700
OMIM 300198
CCDS CCDS14121
HPRD 02185
IMGT
EMBL AC138085 AF179615 AF179616 AF179617 AF179618 AF179619 AF179620 AF179621 AF179622 AF179623 AF179624 BC023152 U94357 U94358 U94360 U94361 U94362 U94363 U94364
GenPept AAB84373 AAB84374 AAB84375 AAB84376 AAB84377 AAB84378 AAB84379 AAF61855 AAH23152

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