CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004697
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Phosphoglycerate mutase 1 
Protein Synonyms/Alias
 BPG-dependent PGAM 1; Phosphoglycerate mutase isozyme B; PGAM-B 
Gene Name
 PGAM1 
Gene Synonyms/Alias
 PGAMA; CDABP0006 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
5***MAAYKLVLIRHGacetylation[1, 2, 3, 4]
5***MAAYKLVLIRHGubiquitination[4, 5, 6, 7, 8, 9, 10]
39PAGHEEAKRGGQALRacetylation[3, 4]
39PAGHEEAKRGGQALRubiquitination[4, 8, 10, 11, 12]
61ICFTSVQKRAIRTLWubiquitination[13]
100GGLTGLNKAETAAKHubiquitination[8, 9, 10, 11, 12]
106NKAETAAKHGEAQVKacetylation[14]
106NKAETAAKHGEAQVKubiquitination[5, 7, 8, 9, 10, 11, 12, 15]
113KHGEAQVKIWRRSYDacetylation[1, 2, 3, 4]
113KHGEAQVKIWRRSYDubiquitination[4, 8, 9, 10, 11, 12]
138PFYSNISKDRRYADLacetylation[3]
138PFYSNISKDRRYADLubiquitination[4, 7, 9, 10]
157LPSCESLKDTIARALacetylation[4]
157LPSCESLKDTIARALubiquitination[4, 8, 10, 11, 13]
176EEIVPQIKEGKRVLIacetylation[1, 3]
176EEIVPQIKEGKRVLIubiquitination[4, 10]
179VPQIKEGKRVLIAAHubiquitination[10]
241GDEETVRKAMEAVAAubiquitination[9, 10]
251EAVAAQGKAKK****ubiquitination[10, 11, 12]
253VAAQGKAKK******ubiquitination[10]
254AAQGKAKK*******ubiquitination[10, 12]
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] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [6] Proteomic snapshot of the EGF-induced ubiquitin network.
 Argenzio E, Bange T, Oldrini B, Bianchi F, Peesari R, Mari S, Di Fiore PP, Mann M, Polo S.
 Mol Syst Biol. 2011 Jan 18;7:462. [PMID: 21245847]
 [7] 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]
 [8] 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]
 [9] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [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] 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]
 [12] 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]
 [13] 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]
 [14] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
 Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
 Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647]
 [15] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931
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 14 14 Phosphoserine.
 MOD_RES 26 26 Phosphotyrosine (By similarity).
 MOD_RES 31 31 Phosphoserine.
 MOD_RES 118 118 Phosphoserine (By similarity).
 MOD_RES 251 251 N6-acetyllysine.
 MOD_RES 253 253 N6-acetyllysine.
 MOD_RES 254 254 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Complete proteome; Direct protein sequencing; Glycolysis; Hydrolase; Isomerase; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 254 AA 
Protein Sequence
MAAYKLVLIR HGESAWNLEN RFSGWYDADL SPAGHEEAKR GGQALRDAGY EFDICFTSVQ 60
KRAIRTLWTV LDAIDQMWLP VVRTWRLNER HYGGLTGLNK AETAAKHGEA QVKIWRRSYD 120
VPPPPMEPDH PFYSNISKDR RYADLTEDQL PSCESLKDTI ARALPFWNEE IVPQIKEGKR 180
VLIAAHGNSL RGIVKHLEGL SEEAIMELNL PTGIPIVYEL DKNLKPIKPM QFLGDEETVR 240
KAMEAVAAQG KAKK 254 
Gene Ontology
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0004083; F:bisphosphoglycerate 2-phosphatase activity; IEA:EC.
 GO:0004082; F:bisphosphoglycerate mutase activity; IEA:EC.
 GO:0004619; F:phosphoglycerate mutase activity; IMP:UniProtKB.
 GO:0006094; P:gluconeogenesis; TAS:Reactome.
 GO:0006096; P:glycolysis; TAS:Reactome.
 GO:0006110; P:regulation of glycolysis; IDA:UniProtKB.
 GO:0043456; P:regulation of pentose-phosphate shunt; IDA:UniProtKB.
 GO:0045730; P:respiratory burst; IDA:UniProtKB.
 GO:0044281; P:small molecule metabolic process; TAS:Reactome. 
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