UniProt Accession

 ENOA_MOUSE; P17182; Q99KT7; Q9DCY7 

Genbank Protein ID

 X52379; AK002336; BC003891; BC004017; BC010685; BC024644; BC085098 

Genbank Nucleotide ID

 CAA36605.1; BAB22021.1; AAH03891.1; AAH04017.1; AAH10685.1; AAH24644.1; AAH85098.1 

Protein Name

 Alpha-enolase 

Protein Synonyms/Alias

 2-phospho-D-glycerate hydro-lyase; Enolase 1; Non-neural enolase; NNE 

Gene Name

 Eno1 

Gene Synonyms/Alias

 Eno-1 

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
28	EVDLYTAKGLFRAAV	ubiquitination	[1]
54	LELRDNDKTRFMGKG	ubiquitination	[1]
60	DKTRFMGKGVSQAVE	ubiquitination	[1]
71	QAVEHINKTIAPALV	ubiquitination	[1]
80	IAPALVSKKVNVVEQ	acetylation	[2]
80	IAPALVSKKVNVVEQ	ubiquitination	[1]
81	APALVSKKVNVVEQE	ubiquitination	[1]
89	VNVVEQEKIDKLMIE	acetylation	[2]
89	VNVVEQEKIDKLMIE	ubiquitination	[1]
92	VEQEKIDKLMIEMDG	ubiquitination	[1]
103	EMDGTENKSKFGANA	ubiquitination	[1]
193	AEVYHNLKNVIKEKY	acetylation	[2]
193	AEVYHNLKNVIKEKY	ubiquitination	[1]
199	LKNVIKEKYGKDATN	acetylation	[2]
202	VIKEKYGKDATNVGD	acetylation	[2]
202	VIKEKYGKDATNVGD	ubiquitination	[1]
221	APNILENKEALELLK	acetylation	[3, 4]
221	APNILENKEALELLK	ubiquitination	[1]
228	KEALELLKTAIAKAG	acetylation	[2, 3, 4, 5, 6]
228	KEALELLKTAIAKAG	succinylation	[6]
228	KEALELLKTAIAKAG	ubiquitination	[1]
256	SEFYRSGKYDLDFKS	acetylation	[2, 3, 4, 5, 6, 7]
256	SEFYRSGKYDLDFKS	succinylation	[6]
256	SEFYRSGKYDLDFKS	ubiquitination	[1]
262	GKYDLDFKSPDDPSR	acetylation	[4, 6]
326	DLTVTNPKRIAKAAS	ubiquitination	[1]
335	IAKAASEKSCNCLLL	acetylation	[2, 4, 6]
335	IAKAASEKSCNCLLL	succinylation	[6]
335	IAKAASEKSCNCLLL	ubiquitination	[1]
343	SCNCLLLKVNQIGSV	acetylation	[3, 4, 5, 6]
343	SCNCLLLKVNQIGSV	phosphoglycerylation	[8]
358	TESLQACKLAQSNGW	acetylation	[4]
406	CRSERLAKYNQILRI	acetylation	[4, 5, 6]
406	CRSERLAKYNQILRI	ubiquitination	[1]
420	IEEELGSKAKFAGRS	acetylation	[6]
420	IEEELGSKAKFAGRS	succinylation	[6]
420	IEEELGSKAKFAGRS	ubiquitination	[1]

Reference

 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [3] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [4] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [5] 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]
 [6] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [7] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [8] Functional lysine modification by an intrinsically reactive primary glycolytic metabolite.
 Moellering RE, Cravatt BF.
 Science. 2013 Aug 2;341(6145):549-53. [PMID: 23908237] 

Functional Description

 Multifunctional enzyme that, as well as its role in glycolysis, plays a part in various processes such as growth control, hypoxia tolerance and allergic responses (By similarity). May also function in the intravascular and pericellular fibrinolytic system due to its ability to serve as a receptor and activator of plasminogen on the cell surface of several cell-types such as leukocytes and neurons. Stimulates immunoglobulin production (By similarity). 

Sequence Annotation

 REGION 370 373 Substrate binding (By similarity).
 REGION 405 434 Required for interaction with PLG (By
 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).
 MOD_RES 2 2 N-acetylserine (By similarity).
 MOD_RES 44 44 Phosphotyrosine.
 MOD_RES 71 71 N6-acetyllysine (By similarity).
 MOD_RES 89 89 N6-acetyllysine (By similarity).
 MOD_RES 126 126 N6-acetyllysine (By similarity).
 MOD_RES 193 193 N6-acetyllysine (By similarity).
 MOD_RES 199 199 N6-acetyllysine (By similarity).
 MOD_RES 228 228 N6-acetyllysine (By similarity).
 MOD_RES 233 233 N6-acetyllysine; alternate (By
 MOD_RES 233 233 N6-malonyllysine; alternate (By
 MOD_RES 254 254 Phosphoserine (By similarity).
 MOD_RES 256 256 N6-acetyllysine (By similarity).
 MOD_RES 263 263 Phosphoserine.
 MOD_RES 281 281 N6-acetyllysine (By similarity).
 MOD_RES 287 287 Phosphotyrosine (By similarity).
 MOD_RES 420 420 N6-acetyllysine; alternate (By
 MOD_RES 420 420 N6-malonyllysine; alternate (By  

Keyword

 Acetylation; Cell membrane; Complete proteome; Cytoplasm; Direct protein sequencing; Glycolysis; Lyase; Magnesium; Membrane; Metal-binding; Phosphoprotein; Reference proteome; Ubl conjugation. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 434 AA 

Protein Sequence

Gene Ontology

 GO:0000015; C:phosphopyruvate hydratase complex; IEA:InterPro.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 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.