CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002824
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Glycogen phosphorylase, liver form 
Protein Synonyms/Alias
  
Gene Name
 Pygl 
Gene Synonyms/Alias
 Lgp 
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
3*****MAKPLTDQEKacetylation[1]
29VENVAELKKGFNRHLacetylation[1]
192RHGNPWEKARPEFMLacetylation[1]
364IEKLPWSKAWEITKKacetylation[1]
410IIYEINQKHLDRIVAacetylation[1]
421RIVALFPKDIDRMRRacetylation[1]
470IVKTQVFKDFSELEPacetylation[1]
521KDLSQLTKLHSFVGDacetylation[1]
545VKQENKLKFSQFLEKacetylation[1]
552KFSQFLEKEYKVKINacetylation[1]
597RIKKDPKKFFVPRTVacetylation[1]
730DKKGYEAKEYYEALPacetylation[1]
811RNIAASGKFSSDRTIacetylation[1]
823RTIREYAKDIWNMEPacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405] 
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 (By similarity).
 MOD_RES 15 15 Phosphoserine; by PHK; in form
 MOD_RES 681 681 N6-(pyridoxal phosphate)lysine (By  
Keyword
 Acetylation; Allosteric enzyme; Carbohydrate metabolism; Complete proteome; 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 QAGTKWVDTQ VVLALPYDTP VPGYMNNTVN 240
TMRLWSARAP NDFNLQDFNV GDYIQAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV 300
VAATLQDVIR RFKASKFGSK DGVGTVFDAF PDQVAIQLND THPALAIPEL MRIFVDIEKL 360
PWSKAWEITK KTFAYTNHTV LPEALERWPV DLVEKLLPRH LQIIYEINQK HLDRIVALFP 420
KDIDRMRRMS LIEEEGGKRI NMAHLCIVGC HAVNGVAKIH SDIVKTQVFK DFSELEPDKF 480
QNKTNGITPR RWLLLCNPGL ADLIAEKIGE DYVKDLSQLT KLHSFVGDDI FLREIAKVKQ 540
ENKLKFSQFL EKEYKVKINP SSMFDVHVKR IHEYKRQLLN CLHVITMYNR IKKDPKKFFV 600
PRTVIIGGKA APGYHMAKMI IKLVTSVAEV VNNDPMVGSK LKVIFLENYR VSLAEKVIPA 660
TDLSEQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM AEEAGEENLF IFGMRVDDVA 720
ALDKKGYEAK EYYEALPELK LVIDQIDNGF FSPNQPDLFK DIINMLFYHD RFKVFADYEA 780
YVKCQEKVSQ LYMNQKAWNT MVLRNIAASG KFSSDRTIRE YAKDIWNMEP SDLKISLSKE 840
SSNGVNANGK 850 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:RGD.
 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; IDA:RGD.
 GO:0008144; F:drug binding; IDA:RGD.
 GO:0008184; F:glycogen phosphorylase activity; IDA:RGD.
 GO:0042803; F:protein homodimerization activity; IDA:RGD.
 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; IMP:RGD.
 GO:0042593; P:glucose homeostasis; IEA:Compara.
 GO:0005980; P:glycogen catabolic process; IDA:RGD. 
Interpro
 IPR011833; Glycg_phsphrylas.
 IPR000811; Glyco_trans_35. 
Pfam
 PF00343; Phosphorylase 
SMART
  
PROSITE
 PS00102; PHOSPHORYLASE 
PRINTS