Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Glycogen phosphorylase, muscle form  

UniProtKB / Swiss-Prot ID :  PYGM_HUMAN

Gene Name (Synonyms) : 
PYGM  

Species :  Homo sapiens (Human). 

Subcellular Localization :   

Protein 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. 

Protein Sequence MSRPLSDQEKRKQISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVATPRDYYFALAHTVRDHLVGRWIR...
Predicted Secondary Structure CCCCCCCHHHHHHHCCCCCCCCCCHHHHHHHHHHHHHHCCCCCHHHCCHHHHHHHHHHHHHHHHHHHHHH...
Protein Variant
LocationDescription
116L -> P (in GSD5). VAR_014002
194R -> W (in GSD5). VAR_014003
205G -> S (in GSD5). VAR_003431
292L -> P (in GSD5; rare mutation). VAR_014004
349E -> K (in GSD5). VAR_014005
397L -> P (in GSD5). VAR_003432
414R -> G (in dbSNP:rs11231866). VAR_061198
488T -> N (in GSD5). VAR_014006
543K -> T (in GSD5). VAR_003433
602R -> W (in GSD5). VAR_014007
655E -> K (in GSD5). VAR_003434
660A -> D (in GSD5). VAR_014008
666Q -> E (in GSD5). VAR_014009
685N -> Y (in GSD5). VAR_014010
686G -> R (in GSD5). VAR_014011
687A -> P (in GSD5). VAR_014012
704A -> V (in GSD5). VAR_014013
709Missing (in GSD5; common in Japanesepatients).
798W -> R (in GSD5). VAR_014015
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
15PhosphoserineRKQISVRGL
HHHHCCCCC
11.85HPRD
Link
15PhosphoserineRKQISVRGL
HHHHCCCCC
11.85Phosphositeplus
Link
15PhosphoserineRKQISVRGL
HHHHCCCCC
11.85SysPTM
Link
15Phosphoserine (PHK_group)RKQISVRGL
HHHHCCCCC
11.85PhosphoELM
Link
15Phosphoserine; by PHK; in formphosphorylase A.RKQISVRGL
HHHHCCCCC
11.85UniProtKB
Link
186PhosphotyrosineDWLRYGNPW
HHHHCCCCC
21.05Phosphositeplus
Link
290Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)FFEGKELRL
CCCHHHHHH
46.51Phosphositeplus
Link
316N6-acetyllysine.FKSSKFGCR
HHHCCCCCC
53.52UniProtKB
Link
537N6-acetyllysineRDVAKVKQE
HHHHHHHHH
50.22Phosphositeplus
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
M3K3_HUMANphysical interactionMINT-48500MINT14743216
S10A1_HUMANin vitro
in vivo
HPRD:01986HPRD12804600
PYGM_HUMANin vitroHPRD:01986HPRD10949035
GYS2_HUMANENSP00000164139STRING
GLGB_HUMANENSP00000164139STRING
CALM_HUMANENSP00000164139STRING
AGM1_HUMANENSP00000164139STRING
PHKG1_HUMANENSP00000164139STRING
AMYP_HUMANENSP00000164139STRING
GDE_HUMANENSP00000164139STRING
DYR1B_HUMANENSP00000164139STRING
KPBB_HUMANENSP00000164139STRING
GYS1_HUMANENSP00000164139STRING
FGF3_HUMANENSP00000164139STRING
MEN1_HUMANENSP00000164139STRING
UGPA_HUMANENSP00000164139STRING
GLYG_HUMANENSP00000164139STRING
ENPP3_HUMANENSP00000164139STRING
ENPP1_HUMANENSP00000164139STRING
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Disease Reference
Kegg disease
OMIM disease
232600Glycogen storage disease 5 (GSD5)
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-316, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Regulation of glycogen phosphorylase. Role of the peptide regionsurrounding the phosphoserine residue in determining enzymeproperties.";
Carty T.J., Tu J., Graves D.J.;
J. Biol. Chem. 250:4980-4985(1975).
Cited for: PHOSPHORYLATION AT SER-15.
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
Kim J.-E., Tannenbaum S.R., White F.M.;
J. Proteome Res. 4:1339-1346(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures