CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005585
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Glycogen [starch] synthase isoform 2 
Protein Synonyms/Alias
  
Gene Name
 GSY2 
Gene Synonyms/Alias
 YLR258W; L8479.8 
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
31IYSVLKSKAPITVAQubiquitination[1]
40PITVAQYKDHYHLIGacetylation[2]
260FEAEHLLKRKPDGILubiquitination[1]
289FQNLHALKKEKINDFacetylation[2]
Reference
 [1] 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, VillĂ©n J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301]
 [2] 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
Functional Description
 Transfers the glycosyl residue from UDP-Glc to the non- reducing end of alpha-1,4-glucan. Is believed to regulate the synthesis of glycogen. 
Sequence Annotation
 BINDING 20 20 UDP-glucose (By similarity).
 MOD_RES 159 159 Phosphoserine (Potential).
 MOD_RES 363 363 Phosphoserine (Potential).
 MOD_RES 467 467 Phosphoserine.
 MOD_RES 651 651 Phosphoserine.
 MOD_RES 655 655 Phosphoserine; by PHO85.
 MOD_RES 661 661 Phosphoserine; by PKA (Potential).
 MOD_RES 663 663 Phosphoserine; by PKA (Potential).
 MOD_RES 668 668 Phosphothreonine; by PHO85.  
Keyword
 3D-structure; Allosteric enzyme; Complete proteome; Direct protein sequencing; Glycogen biosynthesis; Glycosyltransferase; Phosphoprotein; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 705 AA 
Protein Sequence
MSRDLQNHLL FETATEVANR VGGIYSVLKS KAPITVAQYK DHYHLIGPLN KATYQNEVDI 60
LDWKKPEAFS DEMRPVQHAL QTMESRGVHF VYGRWLIEGA PKVILFDLDS VRGYSNEWKG 120
DLWSLVGIPS PENDFETNDA ILLGYTVAWF LGEVAHLDSQ HAIVAHFHEW LAGVALPLCR 180
KRRIDVVTIF TTHATLLGRY LCASGSFDFY NCLESVDVDH EAGRFGIYHR YCIERAAAHS 240
ADVFTTVSQI TAFEAEHLLK RKPDGILPNG LNVIKFQAFH EFQNLHALKK EKINDFVRGH 300
FHGCFDFDLD NTLYFFIAGR YEYKNKGADM FIEALARLNY RLKVSGSKKT VVAFIVMPAK 360
NNSFTVEALK GQAEVRALEN TVHEVTTSIG KRIFDHAIRY PHNGLTTELP TDLGELLKSS 420
DKVMLKRRIL ALRRPEGQLP PIVTHNMVDD ANDLILNKIR QVQLFNSPSD RVKMIFHPEF 480
LNANNPILGL DYDEFVRGCH LGVFPSYYEP WGYTPAECTV MGVPSITTNV SGFGAYMEDL 540
IETNQAKDYG IYIVDRRFKA PDESVEQLVD YMEEFVKKTR RQRINQRNRT ERLSDLLDWK 600
RMGLEYVKAR QLALRRGYPD QFRELVGEEL NDSNMDALAG GKKLKVARPL SVPGSPRDLR 660
SNSTVYMTPG DLGTLQEVNN ADDYFSLGVN PAADDDDDGP YADDS 705 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:SGD.
 GO:0005634; C:nucleus; IDA:SGD.
 GO:0004373; F:glycogen (starch) synthase activity; IDA:SGD.
 GO:0005978; P:glycogen biosynthetic process; IMP:SGD. 
Interpro
 IPR008631; Glycogen_synth. 
Pfam
 PF05693; Glycogen_syn 
SMART
  
PROSITE
  
PRINTS