CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021144
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Glycogen phosphorylase, liver form 
Protein Synonyms/Alias
  
Gene Name
 Pygl 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
3*****MAKPLTDQEKubiquitination[1]
29VENVAELKKGFNRHLacetylation[2, 3, 4, 5]
29VENVAELKKGFNRHLubiquitination[1]
78TQQHYYDKCPKRVYYacetylation[2, 3]
78TQQHYYDKCPKRVYYubiquitination[1]
170EYGIFNQKIREGWQVubiquitination[1]
295EGKELRLKQEYFVVAubiquitination[1]
320KASKFGSKDGMGTVFubiquitination[1]
359RIFVDIEKLPWAKAWubiquitination[1]
364IEKLPWAKAWEITKKubiquitination[1]
370AKAWEITKKTFAYTNubiquitination[1]
371KAWEITKKTFAYTNHubiquitination[1]
395WPVELVEKLLPRHLEubiquitination[1]
410IIYEINQKHLDRIVAubiquitination[1]
421RIVALFPKDISRMRRubiquitination[1]
438LIEEEGGKRINMAHLubiquitination[1]
465KIHSDIVKTQVFKDFubiquitination[1]
470IVKTQVFKDFSELEPubiquitination[1]
479FSELEPDKFQNKTNGubiquitination[1]
483EPDKFQNKTNGITPRubiquitination[1]
514KIGEDYVKDLSQLTKubiquitination[1]
521KDLSQLTKLHSFVSDubiquitination[1]
545VKQENKLKFSQFLEKubiquitination[1]
552KFSQFLEKEYKVKINubiquitination[1]
557LEKEYKVKINPSSMFubiquitination[1]
609RTVIIGGKAAPGYHMubiquitination[1]
618APGYHMAKMIIKLITubiquitination[1]
640NDPMVGSKLKVIFLEubiquitination[1]
642PMVGSKLKVIFLENYubiquitination[1]
656YRVSLAEKVIPATDLubiquitination[1]
724DDVAALDKKGYEAKEacetylation[3]
724DDVAALDKKGYEAKEubiquitination[1]
730DKKGYEAKEYYEALPubiquitination[1]
773LFYHDRFKVFADYEAubiquitination[1]
796SQLYMNQKAWNTMVLubiquitination[1]
804AWNTMVLKNIAASGKubiquitination[1]
811KNIAASGKFSSDRTIubiquitination[1]
823RTIKEYAKDIWNMEPubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [3] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [4] Circadian acetylome reveals regulation of mitochondrial metabolic pathways.
 Masri S, Patel VR, Eckel-Mahan KL, Peleg S, Forne I, Ladurner AG, Baldi P, Imhof A, Sassone-Corsi P.
 Proc Natl Acad Sci U S A. 2013 Feb 26;110(9):3339-44. [PMID: 23341599]
 [5] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654] 
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 (By similarity). 
Sequence Annotation
 BINDING 76 76 AMP (By similarity).
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 15 15 Phosphoserine; by PHK; in form
 MOD_RES 527 527 Phosphoserine.
 MOD_RES 681 681 N6-(pyridoxal phosphate)lysine (By  
Keyword
 Acetylation; Allosteric enzyme; Carbohydrate metabolism; Complete proteome; Direct protein sequencing; Glycogen metabolism; Glycosyltransferase; Nucleotide-binding; Phosphoprotein; Pyridoxal phosphate; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 850 AA 
Protein Sequence
MAKPLTDQEK RRQISIRGIV GVENVAELKK GFNRHLHFTL VKDRNVATPR DYYFALAHTV 60
RDHLVGRWIR TQQHYYDKCP KRVYYLSLEF YMGRTLQNTM INLGLQNACD EAIYQLGLDM 120
EELEEIEEDA GLGNGGLGRL AACFLDSMAT LGLAAYGYGI RYEYGIFNQK IREGWQVEEA 180
DDWLRHGNPW EKARPEFMLP VHFYGRVEHT QTGTKWVDTQ VVLALPYDTP VPGYMNNTVN 240
TMRLWSARAP NDFNLQDFNV GDYIQAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV 300
VAATLQDVIR RFKASKFGSK DGMGTVFDAF PDQVAIQLND THPALAIPEL MRIFVDIEKL 360
PWAKAWEITK KTFAYTNHTV LPEALERWPV ELVEKLLPRH LEIIYEINQK HLDRIVALFP 420
KDISRMRRMS LIEEEGGKRI NMAHLCIVGC HAVNGVAKIH SDIVKTQVFK DFSELEPDKF 480
QNKTNGITPR RWLLLCNPGL ADLIAEKIGE DYVKDLSQLT KLHSFVSDDI FLREIAKVKQ 540
ENKLKFSQFL EKEYKVKINP SSMFDVHVKR IHEYKRQLLN CLHVITMYNR IKKDPKKFFV 600
PRTVIIGGKA APGYHMAKMI IKLITSVAEV VNNDPMVGSK LKVIFLENYR VSLAEKVIPA 660
TDLSEQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM AEEAGEENLF IFGMRVDDVA 720
ALDKKGYEAK EYYEALPELK LVIDQIDNGF FSPNQPDLFK DIINMLFYHD RFKVFADYEA 780
YVKCQEKVSQ LYMNQKAWNT MVLKNIAASG KFSSDRTIKE YAKDIWNMEP SDLKISLSNE 840
SSNGVSANGK 850 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:Compara.
 GO:0005886; C:plasma membrane; IEA:Compara.
 GO:0016208; F:AMP binding; IEA:Compara.
 GO:0005524; F:ATP binding; IEA:Compara.
 GO:0032052; F:bile acid binding; IEA:Compara.
 GO:0030246; F:carbohydrate binding; IEA:Compara.
 GO:0008144; F:drug binding; IEA:Compara.
 GO:0008184; F:glycogen phosphorylase activity; IDA:MGI.
 GO:0002060; F:purine nucleobase binding; IEA:Compara.
 GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
 GO:0019842; F:vitamin binding; IEA:Compara.
 GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IEA:Compara.
 GO:0042593; P:glucose homeostasis; IEA:Compara.
 GO:0005980; P:glycogen catabolic process; IEA:Compara.
 GO:0005977; P:glycogen metabolic process; IDA:MGI. 
Interpro
 IPR011833; Glycg_phsphrylas.
 IPR000811; Glyco_trans_35. 
Pfam
 PF00343; Phosphorylase 
SMART
  
PROSITE
 PS00102; PHOSPHORYLASE 
PRINTS