CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003893
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Glycogen phosphorylase, muscle form 
Protein Synonyms/Alias
 Myophosphorylase 
Gene Name
 PYGM 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
537AFIRDVAKVKQENKLacetylation[1]
Reference
 [1] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786] 
Functional Description
 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. 
Sequence Annotation
 BINDING 76 76 AMP (By similarity).
 MOD_RES 2 2 N-acetylserine (By similarity).
 MOD_RES 15 15 Phosphoserine; by PHK; in form
 MOD_RES 473 473 Phosphotyrosine (By similarity).
 MOD_RES 681 681 N6-(pyridoxal phosphate)lysine (By  
Keyword
 3D-structure; Acetylation; Allosteric enzyme; Alternative splicing; Carbohydrate metabolism; Complete proteome; Disease mutation; Glycogen metabolism; Glycogen storage disease; Glycosyltransferase; Nucleotide-binding; Phosphoprotein; Polymorphism; Pyridoxal phosphate; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 842 AA 
Protein Sequence
MSRPLSDQEK RKQISVRGLA GVENVTELKK NFNRHLHFTL VKDRNVATPR DYYFALAHTV 60
RDHLVGRWIR TQQHYYEKDP KRIYYLSLEF YMGRTLQNTM VNLALENACD EATYQLGLDM 120
EELEEIEEDA GLGNGGLGRL AACFLDSMAT LGLAAYGYGI RYEFGIFNQK ISGGWQMEEA 180
DDWLRYGNPW EKARPEFTLP VHFYGHVEHT SQGAKWVDTQ VVLAMPYDTP VPGYRNNVVN 240
TMRLWSAKAP NDFNLKDFNV GGYIQAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV 300
VAATLQDIIR RFKSSKFGCR DPVRTNFDAF PDKVAIQLND THPSLAIPEL MRILVDLERM 360
DWDKAWDVTV RTCAYTNHTV LPEALERWPV HLLETLLPRH LQIIYEINQR FLNRVAAAFP 420
GDVDRLRRMS LVEEGAVKRI NMAHLCIAGS HAVNGVARIH SEILKKTIFK DFYELEPHKF 480
QNKTNGITPR RWLVLCNPGL AEVIAERIGE DFISDLDQLR KLLSFVDDEA FIRDVAKVKQ 540
ENKLKFAAYL EREYKVHINP NSLFDIQVKR IHEYKRQLLN CLHVITLYNR IKREPNKFFV 600
PRTVMIGGKA APGYHMAKMI IRLVTAIGDV VNHDPAVGDR LRVIFLENYR VSLAEKVIPA 660
ADLSEQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM AEEAGEENFF IFGMRVEDVD 720
KLDQRGYNAQ EYYDRIPELR QVIEQLSSGF FSPKQPDLFK DIVNMLMHHD RFKVFADYED 780
YIKCQEKVSA LYKNPREWTR MVIRNIATSG KFSSDRTIAQ YAREIWGVEP SRQRLPAPDE 840
AI 842 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0008184; F:glycogen phosphorylase activity; TAS:ProtInc.
 GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
 GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
 GO:0006006; P:glucose metabolic process; TAS:Reactome.
 GO:0005980; P:glycogen catabolic process; TAS:Reactome.
 GO:0044281; P:small molecule metabolic process; TAS:Reactome. 
Interpro
 IPR011833; Glycg_phsphrylas.
 IPR000811; Glyco_trans_35. 
Pfam
 PF00343; Phosphorylase 
SMART
  
PROSITE
 PS00102; PHOSPHORYLASE 
PRINTS