CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008499
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Pyruvate kinase PKM 
Protein Synonyms/Alias
 Pyruvate kinase muscle isozyme 
Gene Name
 Pkm 
Gene Synonyms/Alias
 Pk3; Pkm2; Pykm 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
3*****MPKPHSEAGTubiquitination[1]
62SRSVEMLKEMIKSGMubiquitination[1]
66EMLKEMIKSGMNVARubiquitination[1]
89EYHAETIKNVREATEubiquitination[1]
115VAVALDTKGPEIRTGubiquitination[1]
125EIRTGLIKGSGTAEVubiquitination[1]
135GTAEVELKKGATLKIubiquitination[1]
141LKKGATLKITLDNAYubiquitination[1]
162NILWLDYKNICKVVEubiquitination[1]
166LDYKNICKVVEVGSKubiquitination[1]
186GLISLQVKEKGADFLubiquitination[1]
188ISLQVKEKGADFLVTubiquitination[1]
206NGGSLGSKKGVNLPGubiquitination[1]
207GGSLGSKKGVNLPGAubiquitination[1]
305GIEIPAEKVFLAQKMubiquitination[1]
311EKVFLAQKMMIGRCNubiquitination[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
Functional Description
 Glycolytic enzyme that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. Stimulates POU5F1-mediated transcriptional activation (By similarity). 
Sequence Annotation
 REGION 307 531 Interaction with POU5F1 (By similarity).
 REGION 389 433 Intersubunit contact.
 REGION 432 437 D-fructose 1,6-bisphosphate binding; part
 REGION 514 521 D-fructose 1,6-bisphosphate binding; part
 METAL 75 75 Potassium (By similarity).
 METAL 77 77 Potassium (By similarity).
 METAL 113 113 Potassium (By similarity).
 METAL 114 114 Potassium; via carbonyl oxygen (By
 METAL 272 272 Magnesium (By similarity).
 METAL 296 296 Magnesium (By similarity).
 BINDING 70 70 Serine (By similarity).
 BINDING 73 73 Substrate (By similarity).
 BINDING 106 106 Serine (By similarity).
 BINDING 295 295 Substrate; via amide nitrogen (By
 BINDING 296 296 Substrate; via amide nitrogen (By
 BINDING 328 328 Substrate (By similarity).
 BINDING 464 464 Serine (By similarity).
 BINDING 482 482 D-fructose 1,6-bisphosphate; part of
 BINDING 489 489 D-fructose 1,6-bisphosphate; part of
 MOD_RES 37 37 Phosphoserine (By similarity).
 MOD_RES 62 62 N6-acetyllysine (By similarity).
 MOD_RES 89 89 N6-acetyllysine (By similarity).
 MOD_RES 105 105 Phosphotyrosine.
 MOD_RES 148 148 Phosphotyrosine.
 MOD_RES 166 166 N6-acetyllysine (By similarity).
 MOD_RES 175 175 Phosphotyrosine (By similarity).
 MOD_RES 195 195 Phosphothreonine (By similarity).
 MOD_RES 266 266 N6-acetyllysine (By similarity).
 MOD_RES 305 305 N6-acetyllysine (By similarity).
 MOD_RES 403 403 4-hydroxyproline (By similarity).
 MOD_RES 408 408 4-hydroxyproline (By similarity).
 MOD_RES 433 433 N6-acetyllysine (By similarity).  
Keyword
 Acetylation; Allosteric enzyme; Alternative splicing; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Glycolysis; Hydroxylation; Kinase; Magnesium; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein; Potassium; Pyruvate; Reference proteome; Transferase; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 531 AA 
Protein Sequence
MPKPHSEAGT AFIQTQQLHA AMADTFLEHM CRLDIDSAPI TARNTGIICT IGPASRSVEM 60
LKEMIKSGMN VARLNFSHGT HEYHAETIKN VREATESFAS DPILYRPVAV ALDTKGPEIR 120
TGLIKGSGTA EVELKKGATL KITLDNAYME KCDENILWLD YKNICKVVEV GSKIYVDDGL 180
ISLQVKEKGA DFLVTEVENG GSLGSKKGVN LPGAAVDLPA VSEKDIQDLK FGVEQDVDMV 240
FASFIRKAAD VHEVRKVLGE KGKNIKIISK IENHEGVRRF DEILEASDGI MVARGDLGIE 300
IPAEKVFLAQ KMMIGRCNRA GKPVICATQM LESMIKKPRP TRAEGSDVAN AVLDGADCIM 360
LSGETAKGDY PLEAVRMQHL IAREAEAAMF HRLLFEELVR ASSHSTDLME AMAMGSVEAS 420
YKCLAAALIV LTESGRSAHQ VARYRPRAPI IAVTRNPQTA RQAHLYRGIF PVLCKDAVLN 480
AWAEDVDLRV NLAMDVGKAR GFFKKGDVVI VLTGWRPGSG FTNTMRVVPV P 531 
Gene Ontology
 GO:0005929; C:cilium; IDA:MGI.
 GO:0070062; C:extracellular vesicular exosome; IEA:Compara.
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0005886; C:plasma membrane; IEA:Compara.
 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:MGI.
 GO:0006096; P:glycolysis; IDA:MGI.
 GO:0012501; P:programmed cell death; 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.