Version 5.4
Homo sapiens Protein: PYGB
Summary
InnateDB Protein IDBP-61443.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol PYGB
Protein Name phosphorylase, glycogen; brain
Synonyms GPBB;
Species Homo sapiens
Ensembl Protein ENSP00000216962
InnateDB Gene IDBG-61441 (PYGB)
Protein Structure
UniProt Annotation
Function Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.
Subcellular Localization
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 20 experimentally validated interaction(s) in this database.
Experimentally validated
Total 20 [view]
Protein-Protein 20 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Gene Ontology

Molecular Function
Accession GO Term
GO:0004645 phosphorylase activity
GO:0008184 glycogen phosphorylase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0005980 glycogen catabolic process
GO:0006006 glucose metabolic process
GO:0044281 small molecule metabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0016020 membrane
Protein Structure and Domains
PDB ID
InterPro IPR000811 Glycosyl transferase, family 35
IPR011833 Glycogen/starch/alpha-glucan phosphorylase
PFAM PF00343
PRINTS
PIRSF PIRSF000460
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt P11216
PhosphoSite PhosphoSite-P11216
TrEMBL Q8TDG6
UniProt Splice Variant
Entrez Gene 5834
UniGene Hs.730268
RefSeq NP_002853
HUGO HGNC:9723
OMIM 138550
CCDS CCDS13171
HPRD 00720
IMGT
EMBL AF432222 AL121772 BC017045 BC030795 J03544 U47025
GenPept AAA59597 AAB60395 AAH17045 AAH30795 AAL99928 CAC00661

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