UniProt Accession

 KPYM_MOUSE; P52480; Q3TBV8; Q3TBW5; Q3TC59; Q3U1X3; Q3U5P6; Q4VC20; Q64484; Q91YI8; Q9CWB1 

Genbank Protein ID

 D38379; X97047; AK002341; AK135397; AK151724; AK153483; AK155110; AK155655; AK170892; AK168943; AK171023; AK171033; AC160637; BC016619; BC094663 

Genbank Nucleotide ID

 BAA07457.1; CAA65761.1; BAB22025.1; BAE22519.1; BAE30642.1; BAE32031.1; BAE33055.1; BAE33370.1; BAE42098.1; BAE40751.1; BAE42192.1; BAE42199.1; AAH16619.1; AAH94663.1 

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	*****MPKPHSEAGT	ubiquitination	[1]
62	SRSVEMLKEMIKSGM	acetylation	[2, 3]
62	SRSVEMLKEMIKSGM	succinylation	[3]
62	SRSVEMLKEMIKSGM	ubiquitination	[1]
66	EMLKEMIKSGMNVAR	acetylation	[2, 3]
66	EMLKEMIKSGMNVAR	succinylation	[3]
66	EMLKEMIKSGMNVAR	ubiquitination	[1]
89	EYHAETIKNVREATE	acetylation	[2]
89	EYHAETIKNVREATE	ubiquitination	[1]
115	VAVALDTKGPEIRTG	ubiquitination	[1]
125	EIRTGLIKGSGTAEV	ubiquitination	[1]
135	GTAEVELKKGATLKI	acetylation	[2, 3]
135	GTAEVELKKGATLKI	ubiquitination	[1]
141	LKKGATLKITLDNAY	ubiquitination	[1]
162	NILWLDYKNICKVVE	ubiquitination	[1]
166	LDYKNICKVVEVGSK	acetylation	[2, 3]
166	LDYKNICKVVEVGSK	succinylation	[3]
166	LDYKNICKVVEVGSK	ubiquitination	[1]
186	GLISLQVKEKGADFL	ubiquitination	[1]
188	ISLQVKEKGADFLVT	acetylation	[4]
188	ISLQVKEKGADFLVT	ubiquitination	[1]
206	NGGSLGSKKGVNLPG	acetylation	[4]
206	NGGSLGSKKGVNLPG	ubiquitination	[1]
207	GGSLGSKKGVNLPGA	acetylation	[3]
207	GGSLGSKKGVNLPGA	succinylation	[3]
207	GGSLGSKKGVNLPGA	ubiquitination	[1]
224	DLPAVSEKDIQDLKF	acetylation	[4]
266	GEKGKNIKIISKIEN	acetylation	[2]
270	KNIKIISKIENHEGV	acetylation	[2, 3]
322	GRCNRAGKPVICATQ	acetylation	[2, 3]
322	GRCNRAGKPVICATQ	succinylation	[3]
475	GIFPVLCKDAVLNAW	acetylation	[3]
498	NLAMDVGKARGFFKK	acetylation	[2, 3]
498	NLAMDVGKARGFFKK	succinylation	[3]

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] 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]
 [4] 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] 

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

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.