Pygl
entrez
110095
canonical
uniprot
Q9ET01
canonical
ensembl
ENSMUSG00000021069
resolver
ensp
ENSMUSP00000071231
resolver
enst
ENSMUST00000071250
resolver
genesymbol
Pygl
resolver
uniprot
Q3UKJ0
resolver
uniprot_entry
PYGL_MOUSE
resolver
uniprot_sec
Q3UKJ0
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 and acetylation. {ECO:0000250|UniProtKB:P06737}.
uniprot
proteins
amino_acid_sequence
MAKPLTDQEKRRQISIRGIVGVENVAELKKGFNRHLHFTLVKDRNVATPRDYYFALAHTVRDHLVGRWIRTQQHYYDKCPKRVYYLSLEFYMGRTLQNTMINLGLQNACDEAIYQLGLDMEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEYGIFNQKIREGWQVEEADDWLRHGNPWEKARPEFMLPVHFYGRVEHTQTGTKWVDTQVVLALPYDTPVPGYMNNTVNTMRLWSARAPNDFNLQDFNVGDYIQAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFVVAATLQDVIRRFKASKFGSKDGMGTVFDAFPDQVAIQLNDTHPALAIPELMRIFVDIEKLPWAKAWEITKKTFAYTNHTVLPEALERWPVELVEKLLPRHLEIIYEINQKHLDRIVALFPKDISRMRRMSLIEEEGGKRINMAHLCIVGCHAVNGVAKIHSDIVKTQVFKDFSELEPDKFQNKTNGITPRRWLLLCNPGLADLIAEKIGEDYVKDLSQLTKLHSFVSDDIFLREIAKVKQENKLKFSQFLEKEYKVKINPSSMFDVHVKRIHEYKRQLLNCLHVITMYNRIKKDPKKFFVPRTVIIGGKAAPGYHMAKMIIKLITSVAEVVNNDPMVGSKLKVIFLENYRVSLAEKVIPATDLSEQISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGEENLFIFGMRVDDVAALDKKGYEAKEYYEALPELKLVIDQIDNGFFSPNQPDLFKDIINMLFYHDRFKVFADYEAYVKCQEKVSQLYMNQKAWNTMVLKNIAASGKFSSDRTIKEYAKDIWNMEPSDLKISLSNESSNGVSANGK
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:0000250|UniProtKB:P06737}.
uniprot
proteins
mass_dalton
97463
uniprot
proteins
post_translational_modification
PTM: Acetylation, which is up-regulated by glucose and insulin and down-regulated by glucagon, inhibits the glycogen phosphorylase activity by promoting PPP1R3B-mediated recruitment of phosphatase PP1 and Ser-15 dephosphorylation. {ECO:0000250|UniProtKB:P06737}.; PTM: Phosphorylation at Ser-15 converts inactive phosphorylase b into active phosphorylase a. Dephosphorylation of Ser-15 by phosphatase PP1 inactivates the enzyme. {ECO:0000250|UniProtKB:P06737}.
uniprot
proteins
protein_family
Glycogen phosphorylase family
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23806337
uniprot
proteins
sequence_length
850
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P06737}.
uniprot
proteins