CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-038460
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Pyruvate kinase 
Protein Synonyms/Alias
  
Gene Name
 Pklr 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
127VAIALDTKGPEIRTGubiquitination[1]
159VLVTVDPKFRTRGDAubiquitination[1]
199LISLVVRKIGPEGLVubiquitination[1]
219GGFLGNRKGVNLPNAubiquitination[1]
317GIEIPAEKVFLAQKMacetylation[2, 3]
317GIEIPAEKVFLAQKMubiquitination[1]
323EKVFLAQKMMIGRCNacetylation[2, 4]
323EKVFLAQKMMIGRCNsuccinylation[4]
323EKVFLAQKMMIGRCNubiquitination[1]
388SFPVEAVKMQHAIARubiquitination[1]
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]
 [3] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [4] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Glycolysis; Kinase; Magnesium; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 543 AA 
Protein Sequence
MEGPAGYLRR ASVAQLTQEL GTAFFQQQQL PAAMADTFLE HLCLLDIDSE PVAARSTSII 60
ATIGPASRSV DRLKEMIKAG MNIARLNFSH GSHEYHAESI ANIREAAESF ATSPLSYRPV 120
AIALDTKGPE IRTGVLQGGP ESEVEIVKGS QVLVTVDPKF RTRGDAKTVW VDYHNITQVV 180
AVGGRIYIDD GLISLVVRKI GPEGLVTEVE HGGFLGNRKG VNLPNAEVDL PGLSEQDLLD 240
LRFGVEHNVD IIFASFVRKA SDVVAVRDAL GPEGRGIKII SKIENHEGVK KFDEILEVSD 300
GIMVARGDLG IEIPAEKVFL AQKMMIGRCN LAGKPVVCAT QMLESMITKA RPTRAETSDV 360
ANAVLDGADC IMLSGETAKG SFPVEAVKMQ HAIAREAEAA VYHRQLFEEL RRAAPLSRDP 420
TEVTAIGAVE ASFKCCAAAI IVLTKTGRSA QLLSRYRPRA AVIAVTRSAQ AARQVHLSRG 480
VFPLLYREPP EAVWADDVDR RVQFGIESGK LRGFLRVGDL VIVVTGWRPG SGYTNIMRVL 540
TIS 543 
Gene Ontology
 GO:0000287; F:magnesium ion binding; IEA:InterPro.
 GO:0030955; F:potassium ion binding; IEA:InterPro.
 GO:0004743; F:pyruvate kinase activity; IDA:MGI.
 GO:0006096; P:glycolysis; IEA:UniProtKB-UniPathway.
 GO:0051707; P:response to other organism; IMP:MGI. 
Interpro
 IPR001697; Pyr_Knase.
 IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
 IPR011037; Pyrv_Knase-like_insert_dom.
 IPR015794; Pyrv_Knase_a/b.
 IPR018209; Pyrv_Knase_AS.
 IPR015793; Pyrv_Knase_brl.
 IPR015795; Pyrv_Knase_C.
 IPR015806; Pyrv_Knase_insert_dom. 
Pfam
 PF00224; PK
 PF02887; PK_C 
SMART
  
PROSITE
 PS00110; PYRUVATE_KINASE 
PRINTS
 PR01050; PYRUVTKNASE.