CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004339
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Beta-enolase 
Protein Synonyms/Alias
 2-phospho-D-glycerate hydro-lyase; Enolase 3; Muscle-specific enolase; MSE; Skeletal muscle enolase 
Gene Name
 Eno3 
Gene Synonyms/Alias
 Eno-3 
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
5***MAMQKIFAREILacetylation[1]
28EVDLHTAKGRFRAAVacetylation[1]
54LELRDGDKSRYLGKGacetylation[1]
64YLGKGVLKAVEHINKacetylation[1]
71KAVEHINKTLGPALLacetylation[1]
80LGPALLEKKLSVVDQacetylation[1]
89LSVVDQEKVDKFMIEacetylation[1]
126CKAGAAEKGVPLYRHacetylation[1]
179PVGASSFKEAMRIGAacetylation[1]
193AEVYHHLKGVIKAKYacetylation[1]
199LKGVIKAKYGKDATNacetylation[1]
202VIKAKYGKDATNVGDacetylation[1]
256SEFYRNGKYDLDFKSacetylation[1]
262GKYDLDFKSPDDPARacetylation[1]
275ARHISGEKLGELYKSacetylation[1]
281EKLGELYKSFIKNYPacetylation[1]
334RIAQAVEKKACNCLLacetylation[1]
420IEEALGDKAVFAGRKacetylation[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
 Appears to have a function in striated muscle development and regeneration. 
Sequence Annotation
 REGION 370 373 Substrate binding (By similarity).
 ACT_SITE 210 210 Proton donor (By similarity).
 ACT_SITE 343 343 Proton acceptor (By similarity).
 METAL 245 245 Magnesium (By similarity).
 METAL 293 293 Magnesium (By similarity).
 METAL 318 318 Magnesium (By similarity).
 BINDING 158 158 Substrate (By similarity).
 BINDING 167 167 Substrate (By similarity).
 BINDING 293 293 Substrate (By similarity).
 BINDING 318 318 Substrate (By similarity).
 BINDING 394 394 Substrate (By similarity).  
Keyword
 Complete proteome; Cytoplasm; Direct protein sequencing; Glycolysis; Lyase; Magnesium; Metal-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 434 AA 
Protein Sequence
MAMQKIFARE ILDSRGNPTV EVDLHTAKGR FRAAVPSGAS TGIYEALELR DGDKSRYLGK 60
GVLKAVEHIN KTLGPALLEK KLSVVDQEKV DKFMIELDGT ENKSKFGANA ILGVSLAVCK 120
AGAAEKGVPL YRHIADLAGN PDLVLPVPAF NVINGGSHAG NKLAMQEFMI LPVGASSFKE 180
AMRIGAEVYH HLKGVIKAKY GKDATNVGDE GGFAPNILEN NEALELLKTA IQAAGYPDKV 240
VIGMDVAASE FYRNGKYDLD FKSPDDPARH ISGEKLGELY KSFIKNYPVV SIEDPFDQDD 300
WATWTSFLSG VDIQIVGDDL TVTNPKRIAQ AVEKKACNCL LLKVNQIGSV TESIQACKLA 360
QSNGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQL MRIEEALGDK 420
AVFAGRKFRN PKAK 434 
Gene Ontology
 GO:0016020; C:membrane; IDA:RGD.
 GO:0000015; C:phosphopyruvate hydratase complex; IEA:InterPro.
 GO:0000287; F:magnesium ion binding; IEA:InterPro.
 GO:0004634; F:phosphopyruvate hydratase activity; IDA:RGD.
 GO:0046982; F:protein heterodimerization activity; IDA:RGD.
 GO:0042803; F:protein homodimerization activity; IDA:RGD.
 GO:0007568; P:aging; IEP:RGD.
 GO:0006096; P:glycolysis; IEA:UniProtKB-UniPathway.
 GO:0042493; P:response to drug; IEP:RGD.
 GO:0043403; P:skeletal muscle tissue regeneration; IEP:RGD. 
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.