CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005898
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Pyruvate kinase PKLR 
Protein Synonyms/Alias
 Pyruvate kinase 1; Pyruvate kinase isozymes L/R; R-type/L-type pyruvate kinase; Red cell/liver pyruvate kinase 
Gene Name
 PKLR 
Gene Synonyms/Alias
 PK1; PKL 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
348GIEIPAEKVFLAQKMubiquitination[1, 2]
354EKVFLAQKMMIGRCNubiquitination[1, 2]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983
Functional Description
 Plays a key role in glycolysis (By similarity). 
Sequence Annotation
 REGION 475 480 Allosteric activator binding.
 REGION 559 564 Allosteric activator binding.
 METAL 118 118 Potassium.
 METAL 120 120 Potassium.
 METAL 156 156 Potassium.
 METAL 157 157 Potassium; via carbonyl oxygen.
 METAL 315 315 Magnesium.
 METAL 339 339 Magnesium.
 BINDING 116 116 Substrate.
 BINDING 338 338 Substrate; via amide nitrogen.
 BINDING 339 339 Substrate; via amide nitrogen.
 BINDING 371 371 Substrate.
 BINDING 525 525 Allosteric activator.
 BINDING 532 532 Allosteric activator.  
Keyword
 3D-structure; Allosteric enzyme; Alternative splicing; ATP-binding; Complete proteome; Disease mutation; Glycolysis; Hereditary hemolytic anemia; Kinase; Magnesium; Metal-binding; Nucleotide-binding; Polymorphism; Potassium; Pyruvate; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 574 AA 
Protein Sequence
MSIQENISSL QLRSWVSKSQ RDLAKSILIG APGGPAGYLR RASVAQLTQE LGTAFFQQQQ 60
LPAAMADTFL EHLCLLDIDS EPVAARSTSI IATIGPASRS VERLKEMIKA GMNIARLNFS 120
HGSHEYHAES IANVREAVES FAGSPLSYRP VAIALDTKGP EIRTGILQGG PESEVELVKG 180
SQVLVTVDPA FRTRGNANTV WVDYPNIVRV VPVGGRIYID DGLISLVVQK IGPEGLVTQV 240
ENGGVLGSRK GVNLPGAQVD LPGLSEQDVR DLRFGVEHGV DIVFASFVRK ASDVAAVRAA 300
LGPEGHGIKI ISKIENHEGV KRFDEILEVS DGIMVARGDL GIEIPAEKVF LAQKMMIGRC 360
NLAGKPVVCA TQMLESMITK PRPTRAETSD VANAVLDGAD CIMLSGETAK GNFPVEAVKM 420
QHAIAREAEA AVYHRQLFEE LRRAAPLSRD PTEVTAIGAV EAAFKCCAAA IIVLTTTGRS 480
AQLLSRYRPR AAVIAVTRSA QAARQVHLCR GVFPLLYREP PEAIWADDVD RRVQFGIESG 540
KLRGFLRVGD LVIVVTGWRP GSGYTNIMRV LSIS 574 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0000287; F:magnesium ion binding; IEA:InterPro.
 GO:0030955; F:potassium ion binding; IEA:InterPro.
 GO:0004743; F:pyruvate kinase activity; TAS:ProtInc.
 GO:0006754; P:ATP biosynthetic process; IEA:Compara.
 GO:0032869; P:cellular response to insulin stimulus; IEA:Compara.
 GO:0031018; P:endocrine pancreas development; TAS:Reactome.
 GO:0006112; P:energy reserve metabolic process; TAS:Reactome.
 GO:0006096; P:glycolysis; TAS:Reactome.
 GO:0031325; P:positive regulation of cellular metabolic process; TAS:Reactome.
 GO:0042866; P:pyruvate biosynthetic process; IEA:Compara.
 GO:0033198; P:response to ATP; IEA:Compara.
 GO:0051591; P:response to cAMP; IEA:Compara.
 GO:0009749; P:response to glucose stimulus; IEA:Compara.
 GO:0009408; P:response to heat; IEA:Compara.
 GO:0001666; P:response to hypoxia; IEA:Compara.
 GO:0010226; P:response to lithium ion; IEA:Compara.
 GO:0007584; P:response to nutrient; IEA:Compara.
 GO:0051707; P:response to other organism; IEA:Compara.
 GO:0044281; P:small molecule metabolic process; TAS:Reactome. 
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.