CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006966
UniProt Accession
Genbank Protein ID
 L11694 
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
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
16TQAYPDQKPGTSGLRacetylation[1]
146APEAITDKIFQISKTacetylation[1]
209IFDFNALKELLSGPNacetylation[1]
234GVVGPYVKKILCEELacetylation[1]
440VEAEGANKMMKDLEAacetylation[1]
443EGANKMMKDLEALMLacetylation[1]
457LDRSFVGKQFSANDKacetylation[1]
464KQFSANDKVYTVEKAacetylation[1]
470DKVYTVEKADNFEYSacetylation[1]
486PVDGSISKNQGLRLIacetylation[1]
523LYIDSYEKDAAKINQacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405] 
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 (By similarity).
 MOD_RES 115 115 Phosphothreonine (By similarity).
 MOD_RES 117 117 Phosphoserine (By similarity).
 MOD_RES 353 353 Phosphotyrosine (By similarity).
 MOD_RES 467 467 Phosphothreonine; by PAK1 (By  
Keyword
 Acetylation; Carbohydrate metabolism; Complete proteome; Cytoplasm; Glucose metabolism; Isomerase; Magnesium; Metal-binding; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 562 AA 
Protein Sequence
MVKIVTVKTQ AYPDQKPGTS GLRKRVKVFQ GNANYAENFI QSIVSTVEPA LRQEATLVVG 60
GDGRFYMTEA IQLIVRIAAA NGIGRLVIGQ NGILSTPAVS CIIRKIKAIG GIILTASHNP 120
GGPNGDFGIK FNISNGGPAP EAITDKIFQI SKTIEEYAIC PDLKVDLGVL GKQQFDLENK 180
FKPFTVEIVD SVEAYATMLR NIFDFNALKE LLSGPNRLKI RIDAMHGVVG PYVKKILCEE 240
LGAPANSAVN CVPLEDFGGH HPDPNLTYAA DLVETMKSGE HDFGAAFDGD GDRNMILGKH 300
GFFVNPSDSV AVIAANIFSI PYFQQTGVRG FARSMPTSGA LDRVANATKI ASYETPTGWK 360
FFGNLMDASK LSLCGEESFG TGSDHIREKD GLWAVLAWLS ILATRKQRVE DILKDHWQKF 420
GRNFFTRYDY EEVEAEGANK MMKDLEALML DRSFVGKQFS ANDKVYTVEK ADNFEYSDPV 480
DGSISKNQGL RLIFADGSRI IFRLSGTGSA GATIRLYIDS YEKDAAKINQ DPQVMLAPLI 540
SIALKVSQLQ ERTGRTAPTV IT 562 
Gene Ontology
 GO:0005829; C:cytosol; IBA:RefGenome.
 GO:0000287; F:magnesium ion binding; IEA:InterPro.
 GO:0004614; F:phosphoglucomutase activity; IBA:RefGenome.
 GO:0006874; P:cellular calcium ion homeostasis; TAS:RGD.
 GO:0019388; P:galactose catabolic process; IBA:RefGenome.
 GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
 GO:0005978; P:glycogen biosynthetic process; IBA:RefGenome.
 GO:0009314; P:response to radiation; IEP:RGD. 
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.