CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-037657
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Phosphorylase 
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
3*****MAKPLTDQEKacetylation[1]
29VENVAELKKSFNRHLacetylation[1]
29VENVAELKKSFNRHLubiquitination[2, 3, 4]
42HLHFTLVKDRNVATTubiquitination[2, 3, 4]
78TQQHYYDKCPKRVYYubiquitination[3]
170EYGIFNQKIRDGWQVubiquitination[2, 3, 4, 5, 6]
192RYGNPWEKSRPEFMLubiquitination[2, 3, 4, 5]
206LPVHFYGKVEHTNTGubiquitination[2, 3, 4]
290NDNFFEGKELRLKQEubiquitination[2, 3, 4, 7, 8]
295EGKELRLKQEYFVVAubiquitination[3, 4]
359RIFVDIEKLPWSKAWubiquitination[2, 4]
364IEKLPWSKAWELTQKubiquitination[2, 4, 5]
371KAWELTQKTFAYTNHubiquitination[2, 3, 4]
395WPVDLVEKLLPRHLEubiquitination[2, 4, 5]
410IIYEINQKHLDRIVAubiquitination[2, 3, 4]
421RIVALFPKDVDRLRRacetylation[1]
421RIVALFPKDVDRLRRubiquitination[2, 4, 5]
438LIEEEGSKRINMAHLubiquitination[2, 4]
465KIHSDIVKTKVFKDFubiquitination[2]
470IVKTKVFKDFSELEPubiquitination[2, 4]
479FSELEPDKFQNKTNGubiquitination[2]
483EPDKFQNKTNGITPRubiquitination[2, 4, 5]
514KIGEDYVKDLSQLTKubiquitination[2, 4]
521KDLSQLTKLHSFLGDubiquitination[2, 3, 4]
545VKQENKLKFSQFLETubiquitination[2, 4]
555QFLETEYKVKINPSSubiquitination[2, 4, 5]
557LETEYKVKINPSSMFubiquitination[2]
569SMFDVQVKRIHEYKRubiquitination[2, 4]
609RTVIIGGKAAPGYHMubiquitination[2, 4]
640NDPMVGSKLKVIFLEubiquitination[2, 4]
642PMVGSKLKVIFLENYubiquitination[7]
656YRVSLAEKVIPATDLubiquitination[2, 4]
724DDVAALDKKGYEAKEubiquitination[2, 4]
725DVAALDKKGYEAKEYubiquitination[2]
730DKKGYEAKEYYEALPubiquitination[2, 4]
754DNGFFSPKQPDLFKDubiquitination[2, 4]
Reference
 [1] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [7] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [8] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 
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
  
Keyword
 Carbohydrate metabolism; Complete proteome; Glycosyltransferase; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 819 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 LYMKSDAVRP KHWPGKDSVQ TGPLRETVR 819 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005886; C:plasma membrane; IDA:HPA.
 GO:0008184; F:glycogen phosphorylase activity; IEA:InterPro.
 GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
 GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW. 
Interpro
 IPR011833; Glycg_phsphrylas.
 IPR000811; Glyco_trans_35. 
Pfam
 PF00343; Phosphorylase 
SMART
  
PROSITE
 PS00102; PHOSPHORYLASE 
PRINTS