CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001790
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Phosphoglycerate kinase 
Protein Synonyms/Alias
  
Gene Name
 PGK1 
Gene Synonyms/Alias
 YCR012W; YCR12W 
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
6**MSLSSKLSVQDLDacetylation[1]
15SVQDLDLKDKRVFIRacetylation[1]
32FNVPLDGKKITSNQRacetylation[1]
48VAALPTIKYVLEHHPacetylation[1]
48VAALPTIKYVLEHHPubiquitination[2]
74PNGERNEKYSLAPVAacetylation[1]
74PNGERNEKYSLAPVAubiquitination[2]
82YSLAPVAKELQSLLGacetylation[1]
82YSLAPVAKELQSLLGubiquitination[3]
142GQKVKASKEDVQKFRacetylation[1]
147ASKEDVQKFRHELSSacetylation[1]
190AAGFLLEKELKYFGKacetylation[1]
190AAGFLLEKELKYFGKubiquitination[2]
193FLLEKELKYFGKALEacetylation[1]
193FLLEKELKYFGKALEubiquitination[2]
197KELKYFGKALENPTRacetylation[1]
197KELKYFGKALENPTRubiquitination[2, 3]
214LAILGGAKVADKIQLacetylation[1]
214LAILGGAKVADKIQLubiquitination[2]
218GGAKVADKIQLIDNLacetylation[1]
258IGDSIFDKAGAEIVPacetylation[1]
258IGDSIFDKAGAEIVPubiquitination[2, 3, 4]
266AGAEIVPKLMEKAKAacetylation[1]
266AGAEIVPKLMEKAKAubiquitination[2]
274LMEKAKAKGVEVVLPubiquitination[3]
302NTKTVTDKEGIPAGWacetylation[1, 5]
302NTKTVTDKEGIPAGWubiquitination[2, 3]
320DNGPESRKLFAATVAacetylation[1]
320DNGPESRKLFAATVAubiquitination[2]
345PGVFEFEKFAAGTKAubiquitination[2]
351EKFAAGTKALLDEVVacetylation[1]
351EKFAAGTKALLDEVVubiquitination[2]
359ALLDEVVKSSAAGNTacetylation[1]
379GDTATVAKKYGVTDKacetylation[1]
379GDTATVAKKYGVTDKubiquitination[3]
380DTATVAKKYGVTDKIacetylation[1]
380DTATVAKKYGVTDKIubiquitination[2]
386KKYGVTDKISHVSTGacetylation[1]
415GVAFLSEKK******acetylation[1]
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, VillĂ©n J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301]
 [3] Sites of ubiquitin attachment in Saccharomyces cerevisiae.
 Starita LM, Lo RS, Eng JK, von Haller PD, Fields S.
 Proteomics. 2012 Jan;12(2):236-40. [PMID: 22106047]
 [4] A perturbed ubiquitin landscape distinguishes between ubiquitin in trafficking and in proteolysis.
 Ziv I, Matiuhin Y, Kirkpatrick DS, Erpapazoglou Z, Leon S, Pantazopoulou M, Kim W, Gygi SP, Haguenauer-Tsapis R, Reis N, Glickman MH, Kleifeld O.
 Mol Cell Proteomics. 2011 May;10(5):M111.009753. [PMID: 21427232]
 [5] Preparative peptide isoelectric focusing as a tool for improving the identification of lysine-acetylated peptides from complex mixtures.
 Xie H, Bandhakavi S, Roe MR, Griffin TJ.
 J Proteome Res. 2007 May;6(5):2019-26. [PMID: 17397211
Functional Description
  
Sequence Annotation
 NP_BIND 371 374 ATP.
 REGION 24 26 Substrate binding.
 REGION 63 66 Substrate binding.
 BINDING 39 39 Substrate.
 BINDING 122 122 Substrate.
 BINDING 169 169 Substrate.
 BINDING 218 218 ATP.
 BINDING 311 311 ATP; via carbonyl oxygen.
 BINDING 335 335 ATP.
 BINDING 342 342 ATP.
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 93 93 Phosphothreonine.
 MOD_RES 110 110 Phosphoserine.
 MOD_RES 130 130 Phosphoserine.
 MOD_RES 154 154 Phosphoserine.
 MOD_RES 172 172 Phosphoserine.
 MOD_RES 203 203 Phosphothreonine.
 MOD_RES 241 241 Phosphothreonine.
 MOD_RES 298 298 Phosphothreonine.
 MOD_RES 318 318 Phosphoserine.
 MOD_RES 331 331 Phosphothreonine.
 MOD_RES 392 392 Phosphothreonine.  
Keyword
 3D-structure; Acetylation; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Glycolysis; Kinase; Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 416 AA 
Protein Sequence
MSLSSKLSVQ DLDLKDKRVF IRVDFNVPLD GKKITSNQRI VAALPTIKYV LEHHPRYVVL 60
ASHLGRPNGE RNEKYSLAPV AKELQSLLGK DVTFLNDCVG PEVEAAVKAS APGSVILLEN 120
LRYHIEEEGS RKVDGQKVKA SKEDVQKFRH ELSSLADVYI NDAFGTAHRA HSSMVGFDLP 180
QRAAGFLLEK ELKYFGKALE NPTRPFLAIL GGAKVADKIQ LIDNLLDKVD SIIIGGGMAF 240
TFKKVLENTE IGDSIFDKAG AEIVPKLMEK AKAKGVEVVL PVDFIIADAF SADANTKTVT 300
DKEGIPAGWQ GLDNGPESRK LFAATVAKAK TIVWNGPPGV FEFEKFAAGT KALLDEVVKS 360
SAAGNTVIIG GGDTATVAKK YGVTDKISHV STGGGASLEL LEGKELPGVA FLSEKK 416 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:SGD.
 GO:0005886; C:plasma membrane; IDA:SGD.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004618; F:phosphoglycerate kinase activity; IDA:SGD.
 GO:0006094; P:gluconeogenesis; IMP:SGD.
 GO:0006096; P:glycolysis; IMP:SGD. 
Interpro
 IPR001576; Phosphoglycerate_kinase.
 IPR015901; Phosphoglycerate_kinase_C.
 IPR015911; Phosphoglycerate_kinase_CS.
 IPR015824; Phosphoglycerate_kinase_N. 
Pfam
 PF00162; PGK 
SMART
  
PROSITE
 PS00111; PGLYCERATE_KINASE 
PRINTS
 PR00477; PHGLYCKINASE.