CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002367
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
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
29VENVAELKKSFNRHLubiquitination[1, 2, 3]
30ENVAELKKSFNRHLHubiquitination[1]
42HLHFTLVKDRNVATTubiquitination[1, 3]
170EYGIFNQKIRDGWQVubiquitination[1, 2, 3, 4, 5, 6]
192RYGNPWEKSRPEFMLubiquitination[1, 3, 4, 6]
206LPVHFYGKVEHTNTGubiquitination[1, 3]
290NDNFFEGKELRLKQEubiquitination[1, 3, 5]
295EGKELRLKQEYFVVAubiquitination[3]
316IRRFKASKFGSTRGAubiquitination[1]
359RIFVDIEKLPWSKAWubiquitination[1, 3]
364IEKLPWSKAWELTQKubiquitination[1, 3, 4, 6]
371KAWELTQKTFAYTNHubiquitination[1, 3]
395WPVDLVEKLLPRHLEubiquitination[1, 3, 4, 6]
410IIYEINQKHLDRIVAubiquitination[1, 3]
421RIVALFPKDVDRLRRubiquitination[1, 3, 4, 5, 6]
438LIEEEGSKRINMAHLubiquitination[1, 3]
465KIHSDIVKTKVFKDFubiquitination[1]
470IVKTKVFKDFSELEPacetylation[7]
470IVKTKVFKDFSELEPubiquitination[1, 3]
479FSELEPDKFQNKTNGubiquitination[1]
483EPDKFQNKTNGITPRubiquitination[1, 3, 6]
514KIGEDYVKDLSQLTKubiquitination[1, 3, 5]
521KDLSQLTKLHSFLGDubiquitination[1, 3]
545VKQENKLKFSQFLETubiquitination[1, 3]
555QFLETEYKVKINPSSubiquitination[1, 3, 4, 6]
557LETEYKVKINPSSMFubiquitination[1]
569SMFDVQVKRIHEYKRubiquitination[1, 3]
609RTVIIGGKAAPGYHMubiquitination[1, 3]
640NDPMVGSKLKVIFLEubiquitination[1, 3]
656YRVSLAEKVIPATDLubiquitination[1, 3]
724DDVAALDKKGYEAKEubiquitination[1, 3]
725DVAALDKKGYEAKEYubiquitination[1]
730DKKGYEAKEYYEALPubiquitination[1, 3]
754DNGFFSPKQPDLFKDubiquitination[1, 3]
796SQLYMNPKAWNTMVLubiquitination[1]
804AWNTMVLKNIAASGKubiquitination[1, 3, 4, 5, 6, 8]
811KNIAASGKFSSDRTIubiquitination[1, 3, 4, 6]
819FSSDRTIKEYAQNIWubiquitination[1, 3]
834NVEPSDLKISLSNESubiquitination[1, 3]
843SLSNESNKVNGN***ubiquitination[1]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [3] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [5] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [6] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [7] 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]
 [8] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094] 
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-acetylalanine.
 MOD_RES 15 15 Phosphoserine; by PHK; in form
 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
 847 AA 
Protein Sequence
MAKPLTDQEK RRQISIRGIV GVENVAELKK SFNRHLHFTL VKDRNVATTR DYYFALAHTV 60
RDHLVGRWIR TQQHYYDKCP KRVYYLSLEF YMGRTLQNTM INLGLQNACD EAIYQLGLDI 120
EELEEIEEDA GLGNGGLGRL AACFLDSMAT LGLAAYGYGI RYEYGIFNQK IRDGWQVEEA 180
DDWLRYGNPW EKSRPEFMLP VHFYGKVEHT NTGTKWIDTQ VVLALPYDTP VPGYMNNTVN 240
TMRLWSARAP NDFNLRDFNV GDYIQAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV 300
VAATLQDIIR RFKASKFGST RGAGTVFDAF PDQVAIQLND THPALAIPEL MRIFVDIEKL 360
PWSKAWELTQ KTFAYTNHTV LPEALERWPV DLVEKLLPRH LEIIYEINQK HLDRIVALFP 420
KDVDRLRRMS LIEEEGSKRI NMAHLCIVGS HAVNGVAKIH SDIVKTKVFK DFSELEPDKF 480
QNKTNGITPR RWLLLCNPGL AELIAEKIGE DYVKDLSQLT KLHSFLGDDV FLRELAKVKQ 540
ENKLKFSQFL ETEYKVKINP SSMFDVQVKR IHEYKRQLLN CLHVITMYNR IKKDPKKLFV 600
PRTVIIGGKA APGYHMAKMI IKLITSVADV VNNDPMVGSK LKVIFLENYR VSLAEKVIPA 660
TDLSEQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM AEEAGEENLF IFGMRIDDVA 720
ALDKKGYEAK EYYEALPELK LVIDQIDNGF FSPKQPDLFK DIINMLFYHD RFKVFADYEA 780
YVKCQDKVSQ LYMNPKAWNT MVLKNIAASG KFSSDRTIKE YAQNIWNVEP SDLKISLSNE 840
SNKVNGN 847 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005886; C:plasma membrane; IDA:HPA.
 GO:0016208; F:AMP binding; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IDA:UniProtKB.
 GO:0032052; F:bile acid binding; IDA:UniProtKB.
 GO:0008144; F:drug binding; IDA:UniProtKB.
 GO:0005536; F:glucose binding; NAS:UniProtKB.
 GO:0008184; F:glycogen phosphorylase activity; IMP:UniProtKB.
 GO:0042803; F:protein homodimerization activity; NAS:UniProtKB.
 GO:0002060; F:purine nucleobase binding; IDA:UniProtKB.
 GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
 GO:0019842; F:vitamin binding; IDA:UniProtKB.
 GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IEA:Compara.
 GO:0042593; P:glucose homeostasis; IMP:UniProtKB.
 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