CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004318
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
 PGAMM 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
100GGLTGLNKAETAAKHacetylation[1, 2, 3, 4]
100GGLTGLNKAETAAKHphosphoglycerylation[5]
100GGLTGLNKAETAAKHubiquitination[4, 6, 7, 8, 9, 10, 11]
113KHGEEQVKIWRRSFDubiquitination[10]
179VPQIKAGKRVLIAAHubiquitination[12]
195NSLRGIVKHLEGMSDubiquitination[12]
241GDEETVRKAMEAVAAubiquitination[10]
251EAVAAQGKAK*****ubiquitination[7, 10]
253VAAQGKAK*******ubiquitination[10]
Reference
 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [3] 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]
 [4] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [5] Functional lysine modification by an intrinsically reactive primary glycolytic metabolite.
 Moellering RE, Cravatt BF.
 Science. 2013 Aug 2;341(6145):549-53. [PMID: 23908237]
 [6] 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]
 [7] 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]
 [8] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [9] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [10] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [11] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [12] Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry.
 Denis NJ, Vasilescu J, Lambert JP, Smith JC, Figeys D.
 Proteomics. 2007 Mar;7(6):868-74. [PMID: 17370265] 
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.
 ACT_SITE 186 186
 MOD_RES 92 92 Phosphotyrosine (By similarity).
 CROSSLNK 179 179 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 195 195 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 Complete proteome; Disease mutation; Glycogen storage disease; Glycolysis; Hydrolase; Isomerase; Isopeptide bond; Phosphoprotein; Reference proteome; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 253 AA 
Protein Sequence
MATHRLVMVR HGESTWNQEN RFCGWFDAEL SEKGTEEAKR GAKAIKDAKM EFDICYTSVL 60
KRAIRTLWAI LDGTDQMWLP VVRTWRLNER HYGGLTGLNK AETAAKHGEE QVKIWRRSFD 120
IPPPPMDEKH PYYNSISKER RYAGLKPGEL PTCESLKDTI ARALPFWNEE IVPQIKAGKR 180
VLIAAHGNSL RGIVKHLEGM SDQAIMELNL PTGIPIVYEL NKELKPTKPM QFLGDEETVR 240
KAMEAVAAQG KAK 253 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 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; IMP:UniProtKB.
 GO:0006094; P:gluconeogenesis; TAS:Reactome.
 GO:0006096; P:glycolysis; IMP:UniProtKB.
 GO:0046689; P:response to mercury ion; IEA:Compara.
 GO:0044281; P:small molecule metabolic process; TAS:Reactome.
 GO:0007283; P:spermatogenesis; IEA:Compara.
 GO:0006941; P:striated muscle contraction; IMP:UniProtKB. 
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