UniProt Accession

 ENOA_HUMAN; P06733; B2RD59; P22712; Q16704; Q4TUS4; Q53FT9; Q53HR3; Q658M5; Q6GMP2; Q71V37; Q7Z3V6; Q8WU71; Q9UCH6; Q9UM55 

Genbank Protein ID

 M14328; X16288; X16289; X16290; M55914; X84907; BT007163; AK315417; AL833741; BX537400; AK222517; AK223192; DQ056744; AL139415; CH471130; BC001810; BC004458; BC009912; BC011130; BC015641; BC021166; BC022545; BC027725; BC050642; U88968; AF035286 

Genbank Nucleotide ID

 AAA52387.1; CAA34360.1; CAA34360.1; CAA34360.1; AAA35698.1; CAA59331.1; AAP35827.1; BAG37806.1; CAH56247.1; CAD97642.1; BAD96237.1; BAD96912.1; AAY43128.1; CAC42425.1; EAW71604.1; AAH01810.1; AAH04458.1; AAH09912.1; AAH11130.1; AAH15641.1; AAH21166.2; AAH22545.1; AAH27725.1; AAH50642.1; AAC39935.1; AAB88178.1 

Protein Name

 Alpha-enolase 

Protein Synonyms/Alias

 2-phospho-D-glycerate hydro-lyase; C-myc promoter-binding protein; Enolase 1; MBP-1; MPB-1; Non-neural enolase; NNE; Phosphopyruvate hydratase; Plasminogen-binding protein 

Gene Name

 ENO1 

Gene Synonyms/Alias

 ENO1L1; MBPB1; MPB1 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
5	***MSILKIHAREIF	acetylation	[1]
5	***MSILKIHAREIF	ubiquitination	[2, 3, 4, 5, 6]
28	EVDLFTSKGLFRAAV	acetylation	[7]
28	EVDLFTSKGLFRAAV	ubiquitination	[2, 3, 4, 5, 6, 8, 9, 10]
54	LELRDNDKTRYMGKG	ubiquitination	[2, 4, 5, 6, 10]
60	DKTRYMGKGVSKAVE	acetylation	[1]
60	DKTRYMGKGVSKAVE	ubiquitination	[3, 5, 8, 10]
64	YMGKGVSKAVEHINK	acetylation	[1, 7]
64	YMGKGVSKAVEHINK	ubiquitination	[2, 3, 4, 5, 6, 8, 9, 10, 11]
71	KAVEHINKTIAPALV	acetylation	[1, 7, 12]
71	KAVEHINKTIAPALV	ubiquitination	[2, 3, 4, 5, 6, 8, 10]
80	IAPALVSKKLNVTEQ	acetylation	[1, 7]
80	IAPALVSKKLNVTEQ	ubiquitination	[2, 3, 5, 6, 8, 10]
81	APALVSKKLNVTEQE	acetylation	[7]
81	APALVSKKLNVTEQE	ubiquitination	[3, 4, 5, 6, 8, 10, 11, 13]
89	LNVTEQEKIDKLMIE	acetylation	[1, 7]
89	LNVTEQEKIDKLMIE	ubiquitination	[3, 4, 5, 8, 10, 13]
92	TEQEKIDKLMIEMDG	acetylation	[7, 14]
92	TEQEKIDKLMIEMDG	ubiquitination	[4, 8, 10]
103	EMDGTENKSKFGANA	acetylation	[7]
103	EMDGTENKSKFGANA	ubiquitination	[5, 8]
105	DGTENKSKFGANAIL	acetylation	[7]
120	GVSLAVCKAGAVEKG	ubiquitination	[3, 5, 8, 10]
126	CKAGAVEKGVPLYRH	acetylation	[1, 7]
126	CKAGAVEKGVPLYRH	ubiquitination	[2, 3, 4, 5, 6, 8, 10]
193	AEVYHNLKNVIKEKY	acetylation	[1, 7, 15, 16, 17]
193	AEVYHNLKNVIKEKY	ubiquitination	[2, 3, 4, 5, 6, 8, 10, 11, 17, 18]
197	HNLKNVIKEKYGKDA	ubiquitination	[5, 6, 11]
199	LKNVIKEKYGKDATN	acetylation	[1]
199	LKNVIKEKYGKDATN	ubiquitination	[3, 5, 8]
202	VIKEKYGKDATNVGD	acetylation	[7, 15, 16, 17]
202	VIKEKYGKDATNVGD	ubiquitination	[3, 4, 5, 8, 9, 10, 13, 17, 18]
221	APNILENKEGLELLK	acetylation	[1, 7, 15]
221	APNILENKEGLELLK	ubiquitination	[2, 3, 5, 6, 8, 10, 18]
228	KEGLELLKTAIGKAG	acetylation	[1, 7, 16, 17]
228	KEGLELLKTAIGKAG	ubiquitination	[3, 4, 5, 8, 9, 10, 17, 18]
233	LLKTAIGKAGYTDKV	acetylation	[1, 7, 15, 16]
233	LLKTAIGKAGYTDKV	malonylation	[19]
233	LLKTAIGKAGYTDKV	ubiquitination	[2, 3, 4, 5, 6, 8, 10, 13, 18]
239	GKAGYTDKVVIGMDV	acetylation	[7]
256	SEFFRSGKYDLDFKS	acetylation	[1, 7, 15, 16, 17]
256	SEFFRSGKYDLDFKS	ubiquitination	[2, 3, 4, 5, 6, 8, 9, 10, 17, 18]
262	GKYDLDFKSPDDPSR	acetylation	[7]
262	GKYDLDFKSPDDPSR	ubiquitination	[2, 5, 6, 8, 9, 10, 18]
281	DQLADLYKSFIKDYP	acetylation	[1, 7, 15, 16]
281	DQLADLYKSFIKDYP	ubiquitination	[2, 5, 6, 8, 10, 18]
285	DLYKSFIKDYPVVSI	acetylation	[1, 7]
285	DLYKSFIKDYPVVSI	ubiquitination	[3, 5, 8, 9, 10, 18]
326	DLTVTNPKRIAKAVN	ubiquitination	[3, 5, 8, 10, 17, 18]
330	TNPKRIAKAVNEKSC	acetylation	[7]
330	TNPKRIAKAVNEKSC	ubiquitination	[5]
335	IAKAVNEKSCNCLLL	acetylation	[7, 16, 17]
335	IAKAVNEKSCNCLLL	phosphoglycerylation	[20]
335	IAKAVNEKSCNCLLL	ubiquitination	[2, 3, 4, 5, 6, 8, 18]
343	SCNCLLLKVNQIGSV	acetylation	[1, 7, 16, 17]
343	SCNCLLLKVNQIGSV	phosphoglycerylation	[20]
343	SCNCLLLKVNQIGSV	ubiquitination	[2, 3, 5, 6, 8, 9, 17, 18]
358	TESLQACKLAQANGW	acetylation	[7]
358	TESLQACKLAQANGW	ubiquitination	[5, 18]
394	GLCTGQIKTGAPCRS	ubiquitination	[9]
406	CRSERLAKYNQLLRI	acetylation	[1, 7, 15, 16]
406	CRSERLAKYNQLLRI	ubiquitination	[2, 3, 4, 5, 6, 8, 9, 10, 17, 18]
420	IEEELGSKAKFAGRN	acetylation	[1, 7, 15]
420	IEEELGSKAKFAGRN	malonylation	[19]
420	IEEELGSKAKFAGRN	ubiquitination	[3, 5, 6, 8, 10, 11, 17]
422	EELGSKAKFAGRNFR	ubiquitination	[17]

Reference

 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [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] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] Mass spectrometry analysis of the post-translational modifications of alpha-enolase from pancreatic ductal adenocarcinoma cells.
 Zhou W, Capello M, Fredolini C, Piemonti L, Liotta LA, Novelli F, Petricoin EF.
 J Proteome Res. 2010 Jun 4;9(6):2929-36. [PMID: 20433201]
 [8] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [9] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [10] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [11] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [12] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
 Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
 Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647]
 [13] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [14] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [15] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [16] 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]
 [17] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [18] 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]
 [19] The first identification of lysine malonylation substrates and its regulatory enzyme.
 Peng C, Lu Z, Xie Z, Cheng Z, Chen Y, Tan M, Luo H, Zhang Y, He W, Yang K, Zwaans BM, Tishkoff D, Ho L, Lombard D, He TC, Dai J, Verdin E, Ye Y, Zhao Y.
 Mol Cell Proteomics. 2011 Dec;10(12):M111.012658. [PMID: 21908771]
 [20] 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. 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. 

Sequence Annotation

 REGION 31 38 Epitope recognized by CAR and healthy
 REGION 56 63 Epitope recognized by CAR antibodies.
 REGION 97 237 Required for repression of c-myc promoter
 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.
 MOD_RES 5 5 N6-acetyllysine.
 MOD_RES 44 44 Phosphotyrosine.
 MOD_RES 64 64 N6-acetyllysine.
 MOD_RES 71 71 N6-acetyllysine.
 MOD_RES 89 89 N6-acetyllysine.
 MOD_RES 126 126 N6-acetyllysine.
 MOD_RES 193 193 N6-acetyllysine.
 MOD_RES 199 199 N6-acetyllysine.
 MOD_RES 228 228 N6-acetyllysine.
 MOD_RES 233 233 N6-acetyllysine; alternate.
 MOD_RES 233 233 N6-malonyllysine; alternate.
 MOD_RES 254 254 Phosphoserine.
 MOD_RES 256 256 N6-acetyllysine.
 MOD_RES 263 263 Phosphoserine.
 MOD_RES 272 272 Phosphoserine.
 MOD_RES 281 281 N6-acetyllysine.
 MOD_RES 285 285 N6-acetyllysine.
 MOD_RES 287 287 Phosphotyrosine.
 MOD_RES 420 420 N6-acetyllysine; alternate.
 MOD_RES 420 420 N6-malonyllysine; alternate.  

Keyword

 3D-structure; Acetylation; Alternative initiation; Cell membrane; Complete proteome; Cytoplasm; Direct protein sequencing; DNA-binding; Glycolysis; Lyase; Magnesium; Membrane; Metal-binding; Nucleus; Phosphoprotein; Plasminogen activation; Polymorphism; Reference proteome; Repressor; Transcription; Transcription regulation; Ubl conjugation. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 434 AA 

Protein Sequence

Gene Ontology

 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB.
 GO:0031430; C:M band; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IC:UniProtKB.
 GO:0000015; C:phosphopyruvate hydratase complex; IEA:InterPro.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0000287; F:magnesium ion binding; IEA:InterPro.
 GO:0004634; F:phosphopyruvate hydratase activity; TAS:ProtInc.
 GO:0003700; F:sequence-specific DNA binding transcription factor activity; TAS:ProtInc.
 GO:0003714; F:transcription corepressor activity; TAS:ProtInc.
 GO:0006094; P:gluconeogenesis; TAS:Reactome.
 GO:0006096; P:glycolysis; TAS:Reactome.
 GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
 GO:0009615; P:response to virus; IEP:UniProtKB.
 GO:0044281; P:small molecule metabolic process; TAS:Reactome.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 

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.