CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004065
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Pyruvate kinase PKLR 
Protein Synonyms/Alias
 L-PK; Pyruvate kinase isozymes L/R 
Gene Name
 Pklr 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
190VLVTVDPKFQTRGDAacetylation[1]
541QFGIESGKLRGFLRVacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405
Functional Description
 Plays a key role in glycolysis (By similarity). 
Sequence Annotation
 REGION 475 480 Allosteric activator binding (By
 REGION 559 564 Allosteric activator binding (By
 METAL 118 118 Potassium (By similarity).
 METAL 120 120 Potassium (By similarity).
 METAL 156 156 Potassium (By similarity).
 METAL 157 157 Potassium; via carbonyl oxygen (By
 METAL 315 315 Magnesium (By similarity).
 METAL 339 339 Magnesium (By similarity).
 BINDING 116 116 Substrate (By similarity).
 BINDING 338 338 Substrate; via amide nitrogen (By
 BINDING 339 339 Substrate; via amide nitrogen (By
 BINDING 371 371 Substrate (By similarity).
 BINDING 525 525 Allosteric activator (By similarity).
 BINDING 532 532 Allosteric activator (By similarity).  
Keyword
 Allosteric enzyme; Alternative splicing; ATP-binding; Complete proteome; Glycolysis; Kinase; Magnesium; Metal-binding; Nucleotide-binding; Potassium; Pyruvate; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 574 AA 
Protein Sequence
MSVQENTLPQ QLWPWIFRSQ KDLAKSALSG APGGPAGYLR RASVAQLTQE LGTAFFQQQQ 60
LPAAMADTFL EHLCLLDIDS QPVAARSTSI IATIGPASRS VDRLKEMIKA GMNIARLNFS 120
HGSHEYHAES IANIREATES FATSPLSYRP VAIALDTKGP EIRTGVLQGG PESEVEIVKG 180
SQVLVTVDPK FQTRGDAKTV WVDYHNITRV VAVGGRIYID DGLISLVVQK IGPEGLVTEV 240
EHGGILGSRK GVNLPNTEVD LPGLSEQDLL DLRFGVQHNV DIIFASFVRK ASDVLAVRDA 300
LGPEGQNIKI ISKIENHEGV KKFDEILEVS DGIMVARGDL GIEIPAEKVF LAQKMMIGRC 360
NLAGKPVVCA TQMLESMITK ARPTRAETSD VANAVLDGAD CIMLSGETAK GSFPVEAVMM 420
QHAIAREAEA AVYHRQLFEE LRRAAPLSRD PTEVTAIGAV EASFKCCAAA IIVLTKTGRS 480
AQLLSQYRPR AAVIAVTRSA QAARQVHLSR GVFPLLYREP PEAIWADDVD RRVQFGIESG 540
KLRGFLRVGD LVIVVTGWRP GSGYTNIMRV LSVS 574 
Gene Ontology
 GO:0005829; C:cytosol; IDA:RGD.
 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; IDA:RGD.
 GO:0006754; P:ATP biosynthetic process; IDA:RGD.
 GO:0032869; P:cellular response to insulin stimulus; IDA:RGD.
 GO:0006096; P:glycolysis; IDA:RGD.
 GO:0042866; P:pyruvate biosynthetic process; IDA:RGD.
 GO:0033198; P:response to ATP; IDA:RGD.
 GO:0051591; P:response to cAMP; IDA:RGD.
 GO:0009749; P:response to glucose stimulus; IEP:RGD.
 GO:0009408; P:response to heat; IDA:RGD.
 GO:0001666; P:response to hypoxia; IEP:RGD.
 GO:0010226; P:response to lithium ion; IDA:RGD.
 GO:0007584; P:response to nutrient; IEP:RGD.
 GO:0051707; P:response to other organism; IEA:Compara. 
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.