CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006238
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 UTP--glucose-1-phosphate uridylyltransferase 
Protein Synonyms/Alias
 UDP-glucose pyrophosphorylase; UDPGP; UGPase 
Gene Name
 UGP1 
Gene Synonyms/Alias
 YKL035W; YKL248 
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
33QMRNALNKLADSSKLacetylation[1]
33QMRNALNKLADSSKLubiquitination[2]
39NKLADSSKLDDAARAacetylation[1]
39NKLADSSKLDDAARAubiquitination[2]
66FRRYLVEKSSRTTLEacetylation[1]
76RTTLEWDKIKSPNPDacetylation[1]
87PNPDEVVKYEIISQQacetylation[1]
280DKTRADVKGGTLISYubiquitination[2]
301LEVAQVPKEHIDEFKacetylation[1]
308KEHIDEFKNIRKFTNacetylation[1]
397CSDLLLVKSDLFRLEubiquitination[2]
409RLEHGSLKLDPSRFGacetylation[1]
409RLEHGSLKLDPSRFGubiquitination[2]
422FGPNPLIKLGSHFKKacetylation[1]
429KLGSHFKKVSGFNARubiquitination[2]
459TGNVFLGKDVTLRGTubiquitination[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
 Plays a central role as a glucosyl donor in cellular metabolic pathways. 
Sequence Annotation
 REGION 448 499 Oligomerization.
 ACT_SITE 388 388 Probable.
 METAL 123 123 Magnesium (Probable).
 METAL 246 246 Magnesium (Probable).
 MOD_RES 79 79 Phosphoserine.  
Keyword
 3D-structure; Complete proteome; Magnesium; Metal-binding; Nucleotidyltransferase; Phosphoprotein; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 499 AA 
Protein Sequence
MSTKKHTKTH STYAFESNTN SVAASQMRNA LNKLADSSKL DDAARAKFEN ELDSFFTLFR 60
RYLVEKSSRT TLEWDKIKSP NPDEVVKYEI ISQQPENVSN LSKLAVLKLN GGLGTSMGCV 120
GPKSVIEVRE GNTFLDLSVR QIEYLNRQYD SDVPLLLMNS FNTDKDTEHL IKKYSANRIR 180
IRSFNQSRFP RVYKDSLLPV PTEYDSPLDA WYPPGHGDLF ESLHVSGELD ALIAQGREIL 240
FVSNGDNLGA TVDLKILNHM IETGAEYIME LTDKTRADVK GGTLISYDGQ VRLLEVAQVP 300
KEHIDEFKNI RKFTNFNTNN LWINLKAVKR LIESSNLEME IIPNQKTITR DGHEINVLQL 360
ETACGAAIRH FDGAHGVVVP RSRFLPVKTC SDLLLVKSDL FRLEHGSLKL DPSRFGPNPL 420
IKLGSHFKKV SGFNARIPHI PKIVELDHLT ITGNVFLGKD VTLRGTVIIV CSDGHKIDIP 480
NGSILENVVV TGNLQILEH 499 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:SGD.
 GO:0005886; C:plasma membrane; IDA:SGD.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0003983; F:UTP:glucose-1-phosphate uridylyltransferase activity; IMP:SGD.
 GO:0006078; P:(1->6)-beta-D-glucan biosynthetic process; IMP:SGD.
 GO:0005978; P:glycogen biosynthetic process; IMP:SGD.
 GO:0005992; P:trehalose biosynthetic process; IGI:SGD.
 GO:0006011; P:UDP-glucose metabolic process; IMP:SGD. 
Interpro
 IPR002618; UDPGP_trans.
 IPR016267; UDPGP_trans_subgr. 
Pfam
 PF01704; UDPGP 
SMART
  
PROSITE
  
PRINTS