PYGM
entrez
5837
canonical
uniprot
P11217
canonical
ensembl
ENSG00000068976
resolver
ensp
ENSP00000164139
resolver
ensp
ENSP00000366650
resolver
genesymbol
PYGM
resolver
hgnc
HGNC:9726
resolver
uniprot
A0AVK1
resolver
uniprot
A6NDY6
resolver
uniprot_entry
PYGM_HUMAN
resolver
uniprot_sec
A0AVK1
resolver
uniprot_sec
A6NDY6
resolver
activity_regulation
ACTIVITY REGULATION: Allosterically regulated through the non-covalent binding of metabolites, being activated by AMP and inhibited by ATP, ADP, and glucose-6-phosphate. The activity is also controlled by post-translational modifications including phosphorylation. {ECO:0000269|PubMed:1150650}.
uniprot
proteins
amino_acid_sequence
MSRPLSDQEKRKQISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVATPRDYYFALAHTVRDHLVGRWIRTQQHYYEKDPKRIYYLSLEFYMGRTLQNTMVNLALENACDEATYQLGLDMEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIFNQKISGGWQMEEADDWLRYGNPWEKARPEFTLPVHFYGHVEHTSQGAKWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSAKAPNDFNLKDFNVGGYIQAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFVVAATLQDIIRRFKSSKFGCRDPVRTNFDAFPDKVAIQLNDTHPSLAIPELMRILVDLERMDWDKAWDVTVRTCAYTNHTVLPEALERWPVHLLETLLPRHLQIIYEINQRFLNRVAAAFPGDVDRLRRMSLVEEGAVKRINMAHLCIAGSHAVNGVARIHSEILKKTIFKDFYELEPHKFQNKTNGITPRRWLVLCNPGLAEVIAERIGEDFISDLDQLRKLLSFVDDEAFIRDVAKVKQENKLKFAAYLEREYKVHINPNSLFDIQVKRIHEYKRQLLNCLHVITLYNRIKREPNKFFVPRTVMIGGKAAPGYHMAKMIIRLVTAIGDVVNHDPAVGDRLRVIFLENYRVSLAEKVIPAADLSEQISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGEENFFIFGMRVEDVDKLDQRGYNAQEYYDRIPELRQVIEQLSSGFFSPKQPDLFKDIVNMLMHHDRFKVFADYEDYIKCQEKVSALYKNPREWTRMVIRNIATSGKFSSDRTIAQYAREIWGVEPSRQRLPAPDEAI
uniprot
proteins
disease_involvement
DISEASE: Glycogen storage disease 5 (GSD5) [MIM:232600]: A metabolic disorder resulting in myopathy characterized by exercise intolerance, cramps, muscle weakness and recurrent myoglobinuria. {ECO:0000269|PubMed:10382911, ECO:0000269|PubMed:10382912, ECO:0000269|PubMed:10417800, ECO:0000269|PubMed:10590419, ECO:0000269|PubMed:10681080, ECO:0000269|PubMed:10714589, ECO:0000269|PubMed:10899452, ECO:0000269|PubMed:11706962, ECO:0000269|PubMed:12031624, ECO:0000269|PubMed:7603523, ECO:0000269|PubMed:8316268, ECO:0000269|PubMed:8535454, ECO:0000269|PubMed:9506549}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.4.1.1
uniprot
proteins
function
FUNCTION: Allosteric enzyme that catalyzes the rate-limiting step in glycogen catabolism, the phosphorolytic cleavage of glycogen to produce glucose-1-phosphate, and plays a central role in maintaining cellular and organismal glucose homeostasis. {ECO:0000269|PubMed:8316268}.
uniprot
proteins
mass_dalton
97092
uniprot
proteins
post_translational_modification
PTM: Phosphorylation of Ser-15 converts phosphorylase B (unphosphorylated) to phosphorylase A. {ECO:0000269|PubMed:1150650}.
uniprot
proteins
protein_family
Glycogen phosphorylase family
uniprot
proteins
pubmed
10382911
uniprot
proteins
pubmed
10382912
uniprot
proteins
pubmed
10417800
uniprot
proteins
pubmed
10590419
uniprot
proteins
pubmed
10681080
uniprot
proteins
pubmed
10714589
uniprot
proteins
pubmed
10899452
uniprot
proteins
pubmed
1150650
uniprot
proteins
pubmed
11706962
uniprot
proteins
pubmed
12031624
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16523484
uniprot
proteins
pubmed
16554811
uniprot
proteins
pubmed
3447177
uniprot
proteins
pubmed
3466902
uniprot
proteins
pubmed
3840433
uniprot
proteins
pubmed
7603523
uniprot
proteins
pubmed
8316268
uniprot
proteins
pubmed
8535454
uniprot
proteins
pubmed
9506549
uniprot
proteins
pubmed
9633816
uniprot
proteins
sequence_length
842
uniprot
proteins