CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002532
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Bisphosphoglycerate mutase 
Protein Synonyms/Alias
 BPGM; 2,3-bisphosphoglycerate mutase, erythrocyte; 2,3-bisphosphoglycerate synthase; 2,3-diphosphoglycerate mutase; DPGM; BPG-dependent PGAM 
Gene Name
 BPGM 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
3*****MSKYKLIMLRglycation[1]
5***MSKYKLIMLRHGglycation[1]
5***MSKYKLIMLRHGubiquitination[2, 3, 4]
18HGEGAWNKENRFCSWglycation[1]
43EEARNCGKQLKALNFglycation[1]
159LPRSESLKDVLERLLglycation[1]
197NSSRALLKHLEGISDglycation[1]
Reference
 [1] Human erythrocyte bisphosphoglycerate mutase: inactivation by glycation in vivo and in vitro.
 Fujita T, Suzuki K, Tada T, Yoshihara Y, Hamaoka R, Uchida K, Matuo Y, Sasaki T, Hanafusa T, Taniguchi N.
 J Biochem. 1998 Dec 1;124(6):1237-44. [PMID: 9832630]
 [2] 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]
 [3] 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]
 [4] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789] 
Functional Description
 Plays a major role in regulating hemoglobin oxygen affinity by controlling the levels of its allosteric effector 2,3- bisphosphoglycerate (2,3-BPG). Also exhibits mutase (EC 5.4.2.1) and phosphatase (EC 3.1.3.13) activities. 
Sequence Annotation
 REGION 23 24 2,3-bisphospho-D-glycerate binding.
 REGION 89 92 2,3-bisphospho-D-glycerate binding.
 REGION 116 117 2,3-diphosphoglyceric acid binding.
 REGION 188 190 2,3-bisphospho-D-glycerate binding.
 ACT_SITE 11 11 Tele-phosphohistidine intermediate.
 ACT_SITE 188 188
 BINDING 17 17 2,3-bisphospho-D-glycerate.
 BINDING 62 62 2,3-bisphospho-D-glycerate.
 BINDING 100 100 2,3-bisphospho-D-glycerate.
 CARBOHYD 3 3 N-linked (Glc) (glycation); in vitro.
 CARBOHYD 5 5 N-linked (Glc) (glycation); in vitro.
 CARBOHYD 18 18 N-linked (Glc) (glycation); in vitro.
 CARBOHYD 43 43 N-linked (Glc) (glycation); in vitro.
 CARBOHYD 159 159 N-linked (Glc) (glycation).
 CARBOHYD 197 197 N-linked (Glc) (glycation); in vitro.  
Keyword
 3D-structure; Complete proteome; Direct protein sequencing; Disease mutation; Glycation; Glycolysis; Glycoprotein; Hereditary hemolytic anemia; Hydrolase; Isomerase; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 259 AA 
Protein Sequence
MSKYKLIMLR HGEGAWNKEN RFCSWVDQKL NSEGMEEARN CGKQLKALNF EFDLVFTSVL 60
NRSIHTAWLI LEELGQEWVP VESSWRLNER HYGALIGLNR EQMALNHGEE QVRLWRRSYN 120
VTPPPIEESH PYYQEIYNDR RYKVCDVPLD QLPRSESLKD VLERLLPYWN ERIAPEVLRG 180
KTILISAHGN SSRALLKHLE GISDEDIINI TLPTGVPILL ELDENLRAVG PHQFLGDQEA 240
IQAAIKKVED QGKVKQAKK 259 
Gene Ontology
 GO:0004083; F:bisphosphoglycerate 2-phosphatase activity; IEA:EC.
 GO:0004082; F:bisphosphoglycerate mutase activity; TAS:ProtInc.
 GO:0004619; F:phosphoglycerate mutase activity; IEA:EC.
 GO:0005975; P:carbohydrate metabolic process; NAS:ProtInc.
 GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
 GO:0007585; P:respiratory gaseous exchange; TAS:ProtInc. 
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