CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006670
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Phosphoglucomutase-1 
Protein Synonyms/Alias
 PGM 1; Glucose phosphomutase 1 
Gene Name
 PGM1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
16TQAYQDQKPGTSGLRacetylation[1]
16TQAYQDQKPGTSGLRubiquitination[2, 3]
146APEAITDKIFQISKTubiquitination[4]
164YAVCPDLKVDLGVLGubiquitination[4]
219LSGPNRLKIRIDAMHacetylation[5]
234GVVGPYVKKILCEELacetylation[1]
349DRVASATKIALYETPubiquitination[4, 6, 7, 8, 9]
419ILKDHWQKYGRNFFTacetylation[1]
419ILKDHWQKYGRNFFTubiquitination[4]
470DKVYTVEKADNFEYSubiquitination[6, 8]
523LYIDSYEKDVAKINQacetylation[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] 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]
 [3] 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]
 [4] 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]
 [5] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [6] 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]
 [7] 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]
 [8] 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]
 [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] 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
 This enzyme participates in both the breakdown and synthesis of glucose. 
Sequence Annotation
 ACT_SITE 117 117 Phosphoserine intermediate (By
 METAL 117 117 Magnesium; via phosphate group (By
 METAL 288 288 Magnesium (By similarity).
 METAL 290 290 Magnesium (By similarity).
 METAL 292 292 Magnesium (By similarity).
 MOD_RES 16 16 N6-acetyllysine.
 MOD_RES 115 115 Phosphothreonine (By similarity).
 MOD_RES 117 117 Phosphoserine.
 MOD_RES 353 353 Phosphotyrosine (By similarity).
 MOD_RES 467 467 Phosphothreonine; by PAK1.  
Keyword
 Acetylation; Alternative splicing; Carbohydrate metabolism; Complete proteome; Congenital disorder of glycosylation; Cytoplasm; Disease mutation; Glucose metabolism; Glycogen storage disease; Isomerase; Magnesium; Metal-binding; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 562 AA 
Protein Sequence
MVKIVTVKTQ AYQDQKPGTS GLRKRVKVFQ SSANYAENFI QSIISTVEPA QRQEATLVVG 60
GDGRFYMKEA IQLIARIAAA NGIGRLVIGQ NGILSTPAVS CIIRKIKAIG GIILTASHNP 120
GGPNGDFGIK FNISNGGPAP EAITDKIFQI SKTIEEYAVC PDLKVDLGVL GKQQFDLENK 180
FKPFTVEIVD SVEAYATMLR SIFDFSALKE LLSGPNRLKI RIDAMHGVVG PYVKKILCEE 240
LGAPANSAVN CVPLEDFGGH HPDPNLTYAA DLVETMKSGE HDFGAAFDGD GDRNMILGKH 300
GFFVNPSDSV AVIAANIFSI PYFQQTGVRG FARSMPTSGA LDRVASATKI ALYETPTGWK 360
FFGNLMDASK LSLCGEESFG TGSDHIREKD GLWAVLAWLS ILATRKQSVE DILKDHWQKY 420
GRNFFTRYDY EEVEAEGANK MMKDLEALMF DRSFVGKQFS ANDKVYTVEK ADNFEYSDPV 480
DGSISRNQGL RLIFTDGSRI VFRLSGTGSA GATIRLYIDS YEKDVAKINQ DPQVMLAPLI 540
SIALKVSQLQ ERTGRTAPTV IT 562 
Gene Ontology
 GO:0015629; C:actin cytoskeleton; IDA:HPA.
 GO:0005829; C:cytosol; IBA:RefGenome.
 GO:0000287; F:magnesium ion binding; IEA:InterPro.
 GO:0004614; F:phosphoglucomutase activity; IDA:UniProtKB.
 GO:0019388; P:galactose catabolic process; IBA:RefGenome.
 GO:0006094; P:gluconeogenesis; TAS:UniProtKB.
 GO:0005978; P:glycogen biosynthetic process; IBA:RefGenome.
 GO:0005980; P:glycogen catabolic process; TAS:Reactome.
 GO:0006096; P:glycolysis; TAS:UniProtKB.
 GO:0044281; P:small molecule metabolic process; TAS:Reactome. 
Interpro
 IPR005844; A-D-PHexomutase_a/b/a-I.
 IPR016055; A-D-PHexomutase_a/b/a-I/II/III.
 IPR005845; A-D-PHexomutase_a/b/a-II.
 IPR005846; A-D-PHexomutase_a/b/a-III.
 IPR005843; A-D-PHexomutase_C.
 IPR016066; A-D-PHexomutase_CS.
 IPR005841; Alpha-D-phosphohexomutase_SF. 
Pfam
 PF02878; PGM_PMM_I
 PF02879; PGM_PMM_II
 PF02880; PGM_PMM_III
 PF00408; PGM_PMM_IV 
SMART
  
PROSITE
 PS00710; PGM_PMM 
PRINTS
 PR00509; PGMPMM.