Pygl
entrez
64035
canonical
uniprot
P09811
canonical
ensembl
ENSRNOG00000006388
resolver
ensembl
ENSRNOG00055008990
resolver
ensembl
ENSRNOG00060006655
resolver
ensembl
ENSRNOG00065006991
resolver
ensp
ENSRNOP00000009183
resolver
ensp
ENSRNOP00055012157
resolver
ensp
ENSRNOP00060008125
resolver
ensp
ENSRNOP00065008023
resolver
enst
ENSRNOT00000009183
resolver
enst
ENSRNOT00055015198
resolver
enst
ENSRNOT00060010914
resolver
enst
ENSRNOT00065010917
resolver
genesymbol
Pygl
resolver
genesymbol_syn
Lgp
resolver
uniprot_entry
PYGL_RAT
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
MAKPLTDQEKRRQISIRGIVGVENVAELKKGFNRHLHFTLVKDRNVATPRDYYFALAHTVRDHLVGRWIRTQQHYYDKCPKRVYYLSLEFYMGRTLQNTMINLGLQNACDEAIYQLGLDMEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEYGIFNQKIREGWQVEEADDWLRHGNPWEKARPEFMLPVHFYGRVEHTQAGTKWVDTQVVLALPYDTPVPGYMNNTVNTMRLWSARAPNDFNLQDFNVGDYIQAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFVVAATLQDVIRRFKASKFGSKDGVGTVFDAFPDQVAIQLNDTHPALAIPELMRIFVDIEKLPWSKAWEITKKTFAYTNHTVLPEALERWPVDLVEKLLPRHLQIIYEINQKHLDRIVALFPKDIDRMRRMSLIEEEGGKRINMAHLCIVGCHAVNGVAKIHSDIVKTQVFKDFSELEPDKFQNKTNGITPRRWLLLCNPGLADLIAEKIGEDYVKDLSQLTKLHSFVGDDIFLREIAKVKQENKLKFSQFLEKEYKVKINPSSMFDVHVKRIHEYKRQLLNCLHVITMYNRIKKDPKKFFVPRTVIIGGKAAPGYHMAKMIIKLVTSVAEVVNNDPMVGSKLKVIFLENYRVSLAEKVIPATDLSEQISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGEENLFIFGMRVDDVAALDKKGYEAKEYYEALPELKLVIDQIDNGFFSPNQPDLFKDIINMLFYHDRFKVFADYEAYVKCQEKVSQLYMNQKAWNTMVLRNIAASGKFSSDRTIREYAKDIWNMEPSDLKISLSKESSNGVNANGK
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
97483
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
1339293
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1765272
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
2424788
uniprot
proteins
pubmed
2575583
uniprot
proteins
pubmed
7498521
uniprot
proteins
pubmed
7720853
uniprot
proteins
pubmed
8482535
uniprot
proteins
pubmed
9841883
uniprot
proteins
sequence_length
850
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P06737}.
uniprot
proteins