CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001046
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Phosphoglycerate mutase 2 
Protein Synonyms/Alias
 BPG-dependent PGAM 2; Muscle-specific phosphoglycerate mutase; Phosphoglycerate mutase isozyme M; PGAM-M 
Gene Name
 Pgam2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
100GGLTGLNKAETAAKHacetylation[1, 2, 3, 4, 5, 6, 7]
100GGLTGLNKAETAAKHphosphoglycerylation[8]
100GGLTGLNKAETAAKHsuccinylation[6]
100GGLTGLNKAETAAKHubiquitination[9]
106NKAETAAKHGEEQVKubiquitination[9]
113KHGEEQVKIWRRSFDubiquitination[9]
129PPPPMDEKHNYYTSIubiquitination[9]
138NYYTSISKDRRYAGLubiquitination[9]
146DRRYAGLKPEELPTCubiquitination[9]
157LPTCESLKDTIARALubiquitination[9]
174WNEEIAPKIKAGQRVubiquitination[9]
241GDEETVRKAMEAVAAacetylation[6]
241GDEETVRKAMEAVAAsuccinylation[6]
241GDEETVRKAMEAVAAubiquitination[9]
251EAVAAQGKAK*****ubiquitination[9]
Reference
 [1] The fasted/fed mouse metabolic acetylome: N6-acetylation differences suggest acetylation coordinates organ-specific fuel switching.
 Yang L, Vaitheesvaran B, Hartil K, Robinson AJ, Hoopmann MR, Eng JK, Kurland IJ, Bruce JE.
 J Proteome Res. 2011 Sep 2;10(9):4134-49. [PMID: 21728379]
 [2] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [3] 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]
 [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]
 [5] Circadian acetylome reveals regulation of mitochondrial metabolic pathways.
 Masri S, Patel VR, Eckel-Mahan KL, Peleg S, Forne I, Ladurner AG, Baldi P, Imhof A, Sassone-Corsi P.
 Proc Natl Acad Sci U S A. 2013 Feb 26;110(9):3339-44. [PMID: 23341599]
 [6] 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]
 [7] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [8] Functional lysine modification by an intrinsically reactive primary glycolytic metabolite.
 Moellering RE, Cravatt BF.
 Science. 2013 Aug 2;341(6145):549-53. [PMID: 23908237]
 [9] 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
 Interconversion of 3- and 2-phosphoglycerate with 2,3- bisphosphoglycerate as the primer of the reaction. Can also catalyze the reaction of EC 5.4.2.4 (synthase) and EC 3.1.3.13 (phosphatase), but with a reduced activity. 
Sequence Annotation
 ACT_SITE 11 11 Tele-phosphohistidine intermediate (By
 ACT_SITE 186 186 By similarity.
 MOD_RES 92 92 Phosphotyrosine.
 CROSSLNK 195 195 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 Complete proteome; Glycolysis; Hydrolase; Isomerase; Isopeptide bond; Phosphoprotein; Reference proteome; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 253 AA 
Protein Sequence
MTTHRLVMVR HGESLWNQEN RFCGWFDAEL SEKGAEEAKR GATAIKDAKI EFDICYTSVL 60
KRAIRTLWTI LDVTDQMWVP VVRTWRLNER HYGGLTGLNK AETAAKHGEE QVKIWRRSFD 120
TPPPPMDEKH NYYTSISKDR RYAGLKPEEL PTCESLKDTI ARALPFWNEE IAPKIKAGQR 180
VLIAAHGNSL RGIVKHLEGM SDQAIMELNL PTGIPIVYEL DQNLKPTKPM RFLGDEETVR 240
KAMEAVAAQG KAK 253 
Gene Ontology
 GO:0005829; C:cytosol; IEA:Compara.
 GO:0005634; C:nucleus; IEA:Compara.
 GO:0046538; F:2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity; IEA:Compara.
 GO:0004083; F:bisphosphoglycerate 2-phosphatase activity; IEA:EC.
 GO:0004082; F:bisphosphoglycerate mutase activity; IEA:EC.
 GO:0048037; F:cofactor binding; IEA:Compara.
 GO:0004619; F:phosphoglycerate mutase activity; IDA:MGI.
 GO:0006094; P:gluconeogenesis; IEA:Compara.
 GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
 GO:0046689; P:response to mercury ion; IEA:Compara.
 GO:0007283; P:spermatogenesis; IEA:Compara.
 GO:0006941; P:striated muscle contraction; IEA:Compara. 
Interpro
 IPR013078; His_Pase_superF_clade-1.
 IPR001345; PG/BPGM_mutase_AS.
 IPR005952; Phosphogly_mut1. 
Pfam
 PF00300; His_Phos_1 
SMART
 SM00855; PGAM 
PROSITE
 PS00175; PG_MUTASE 
PRINTS