CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-031970
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Enolase 
Protein Synonyms/Alias
  
Gene Name
 ENO2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
5***MSIEKIWAREILubiquitination[1, 2]
28EVDLYTAKGLFRAAVubiquitination[1]
150AEVYHTLKGVIKDKYubiquitination[2]
156LKGVIKDKYGKDATNubiquitination[2]
159VIKDKYGKDATNVGDacetylation[3]
213SEFYRDGKYDLDFKSubiquitination[2]
219GKYDLDFKSPTDPSRubiquitination[2]
292IERAVEEKACNCLLLubiquitination[2]
315TEAIQACKLAQENGWubiquitination[2]
351GLCTGQIKTGAPCRSphosphoglycerylation[4]
351GLCTGQIKTGAPCRSubiquitination[5]
363CRSERLAKYNQLMRIubiquitination[2]
Reference
 [1] 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]
 [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] 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] Functional lysine modification by an intrinsically reactive primary glycolytic metabolite.
 Moellering RE, Cravatt BF.
 Science. 2013 Aug 2;341(6145):549-53. [PMID: 23908237]
 [5] 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] 
Functional Description
  
Sequence Annotation
 REGION 327 330 Substrate binding (By similarity).
 ACT_SITE 167 167 Proton donor (By similarity).
 ACT_SITE 300 300 Proton acceptor (By similarity).
 BINDING 115 115 Substrate (By similarity).
 BINDING 124 124 Substrate (By similarity).
 BINDING 250 250 Substrate (By similarity).
 BINDING 275 275 Substrate (By similarity).
 BINDING 351 351 Substrate (By similarity).  
Keyword
 Complete proteome; Glycolysis; Lyase; Magnesium; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 391 AA 
Protein Sequence
MSIEKIWARE ILDSRGNPTV EVDLYTAKGL FRAAVPSGAS TGIYEALELR DGDKQRYLGK 60
AKFGANAILG VSLAVCKAGA AERELPLYRH IAQLAGNSDL ILPVPAFNVI NGGSHAGNKL 120
AMQEFMILPV GAESFRDAMR LGAEVYHTLK GVIKDKYGKD ATNVGDEGGF APNILENSEA 180
LELVKEAIDK AGYTEKIVIG MDVAASEFYR DGKYDLDFKS PTDPSRYITG DQLGALYQDF 240
VRDYPVVSIE DPFDQDDWAA WSKFTANVGI QIVGDDLTVT NPKRIERAVE EKACNCLLLK 300
VNQIGSVTEA IQACKLAQEN GWGVMVSHRS GETEDTFIAD LVVGLCTGQI KTGAPCRSER 360
LAKYNQLMRI EEELGDEARF AGHNFRNPSV L 391 
Gene Ontology
 GO:0000015; C:phosphopyruvate hydratase complex; IEA:InterPro.
 GO:0000287; F:magnesium ion binding; IEA:InterPro.
 GO:0004634; F:phosphopyruvate hydratase activity; IEA:EC.
 GO:0006096; P:glycolysis; IEA:UniProtKB-UniPathway. 
Interpro
 IPR000941; Enolase.
 IPR020810; Enolase_C.
 IPR020809; Enolase_CS.
 IPR020811; Enolase_N. 
Pfam
 PF00113; Enolase_C
 PF03952; Enolase_N 
SMART
  
PROSITE
 PS00164; ENOLASE 
PRINTS
 PR00148; ENOLASE.