CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002368
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Glycogen phosphorylase 
Protein Synonyms/Alias
  
Gene Name
 GPH1 
Gene Synonyms/Alias
 YPR160W; P9584.1 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
63HQVKKFNKAEDFQDRacetylation[1]
143DNALINMKIEDPEDPubiquitination[2]
322KFNNGDYKNSVAQQQubiquitination[2]
Reference
 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [2] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301] 
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
 MOD_RES 31 31 Phosphothreonine.
 MOD_RES 333 333 Phosphoserine.
 MOD_RES 751 751 N6-(pyridoxal phosphate)lysine.  
Keyword
 3D-structure; Carbohydrate metabolism; Complete proteome; Direct protein sequencing; Glycogen metabolism; Glycosyltransferase; Phosphoprotein; Pyridoxal phosphate; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 902 AA 
Protein Sequence
MPPASTSTTN DMITEEPTSP HQIPRLTRRL TGFLPQEIKS IDTMIPLKSR ALWNKHQVKK 60
FNKAEDFQDR FIDHVETTLA RSLYNCDDMA AYEAASMSIR DNLVIDWNKT QQKFTTRDPK 120
RVYYLSLEFL MGRALDNALI NMKIEDPEDP AASKGKPREM IKGALDDLGF KLEDVLDQEP 180
DAGLGNGGLG RLAACFVDSM ATEGIPAWGY GLRYEYGIFA QKIIDGYQVE TPDYWLNSGN 240
PWEIERNEVQ IPVTFYGYVD RPEGGKTTLS ASQWIGGERV LAVAYDFPVP GFKTSNVNNL 300
RLWQARPTTE FDFAKFNNGD YKNSVAQQQR AESITAVLYP NDNFAQGKEL RLKQQYFWCA 360
ASLHDILRRF KKSKRPWTEF PDQVAIQLND THPTLAIVEL QRVLVDLEKL DWHEAWDIVT 420
KTFAYTNHTV MQEALEKWPV GLFGHLLPRH LEIIYDINWF FLQDVAKKFP KDVDLLSRIS 480
IIEENSPERQ IRMAFLAIVG SHKVNGVAEL HSELIKTTIF KDFVKFYGPS KFVNVTNGIT 540
PRRWLKQANP SLAKLISETL NDPTEEYLLD MAKLTQLGKY VEDKEFLKKW NQVKLNNKIR 600
LVDLIKKEND GVDIINREYL DDTLFDMQVK RIHEYKRQQL NVFGIIYRYL AMKNMLKNGA 660
SIEEVAKKYP RKVSIFGGKS APGYYMAKLI IKLINCVADI VNNDESIEHL LKVVFVADYN 720
VSKAEIIIPA SDLSEHISTA GTEASGTSNM KFVMNGGLII GTVDGANVEI TREIGEDNVF 780
LFGNLSENVE ELRYNHQYHP QDLPSSLDSV LSYIESGQFS PENPNEFKPL VDSIKYHGDY 840
YLVSDDFESY LATHELVDQE FHNQRSEWLK KSVLSVANVG FFSSDRCIEE YSDTIWNVEP 900
VT 902 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:SGD.
 GO:0008184; F:glycogen phosphorylase activity; IMP:SGD.
 GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
 GO:0005980; P:glycogen catabolic process; IMP:SGD. 
Interpro
 IPR011833; Glycg_phsphrylas.
 IPR000811; Glyco_trans_35. 
Pfam
 PF00343; Phosphorylase 
SMART
  
PROSITE
 PS00102; PHOSPHORYLASE 
PRINTS