CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-016897
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Glycogen phosphorylase, brain form 
Protein Synonyms/Alias
  
Gene Name
 Pygb 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
359RILVDVEKVDWDKAWubiquitination[1]
364VEKVDWDKAWEITKKubiquitination[1]
521TDLSQLKKLLSLVDDubiquitination[1]
725DVEALDQKGYNAREFubiquitination[1]
811RNIACSGKFSSDRTIacetylation[2]
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 acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441] 
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 (By similarity).
 MOD_RES 15 15 Phosphoserine; by PHK; in form
 MOD_RES 197 197 Phosphotyrosine.
 MOD_RES 473 473 Phosphotyrosine.
 MOD_RES 681 681 N6-(pyridoxal phosphate)lysine (By  
Keyword
 Acetylation; Allosteric enzyme; Carbohydrate metabolism; Complete proteome; Glycogen metabolism; Glycosyltransferase; Phosphoprotein; Pyridoxal phosphate; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 843 AA 
Protein Sequence
MAKPLTDSER QKQISVRGIA GLGDVAEVRK SFNRHLHFTL VKDRNVATPR DYFFALAHTV 60
RDHLVGRWIR TQQHYYERDP KRIYYLSLEF YMGRTLQNTM VNLGLQTACD EATYQLGLDL 120
EELEEIEEDA GLGNGGLGRL AACFLDSMAT LGLAAYGYGI RYEFGIFNQK IVNGWQVEEA 180
DDWLRYGNPW EKARPEYMLP VHFYGRVEHT PDGVLWLDTQ VVLAMPYDTP VPGYKNNTVN 240
TMRLWSAKAP NDFKLKDFNV GDYIEAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV 300
VAATLQDIIR RFKSSRFGCR DPVRTCFETF PDKVAIQLND THPALSIPEL MRILVDVEKV 360
DWDKAWEITK KTCAYTNHTV LPEALERWPV SMFEKLLPRH LEIIYAINQR HLDHVAALFP 420
GDVDRLRRMS VIEEGDCKRI NMAHLCVIGS HAVNGVARIH SEIVKQSVFK DFYELEPEKF 480
QNKTNGITPR RWLLLCNPGL AEIIVERIGE GFLTDLSQLK KLLSLVDDEA FIRDVAKVKQ 540
ENKLKFSAQL EKEYKVKINP ASMFDVHVKR IHEYKRQLLN CLHIITLYNR IKKDPAKAFV 600
PRTVMIGGKA APGYHMAKMI IKLVTSIGDV VNHDPVVGDR LRVIFLENYR VSLAEKVIPA 660
ADLSQQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM AEEAGEENLF IFGMRVEDVE 720
ALDQKGYNAR EFYERLPELR QAVDQISSGF FSPKDPDCFK DVVNMLMYHD RFKVFADYEA 780
YIQCQAQVDR LYRNSKEWTK KVIRNIACSG KFSSDRTITE YAREIWGVEP SDLQIPPPNL 840
PKD 843 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:Compara.
 GO:0008184; F:glycogen phosphorylase activity; IEA:InterPro.
 GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
 GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW. 
Interpro
 IPR011833; Glycg_phsphrylas.
 IPR000811; Glyco_trans_35. 
Pfam
 PF00343; Phosphorylase 
SMART
  
PROSITE
 PS00102; PHOSPHORYLASE 
PRINTS