P06733

※ Protein Information

Tag	Content
UniProt Accession	ENOA_HUMAN; P06733;
Entrez ID	2023
GenBank Protein ID	NM_001201483.1; NM_001428.3;
GenBank Nucleotide ID	NP_001188412.1; NP_001419.1;
Protein Name	Alpha-enolase (EC 4.2.1.11) (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; ENO1L1; MBPB1; MPB1
Organism	Homo sapiens
NCBI Taxa ID	9606
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.;MBP1 binds to the myc promoter and acts as a transcriptional repressor. May be a tumor suppressor. 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.;MBP1 binds to the myc promoter and acts as a transcriptional repressor. May be a tumor suppressor.
Sequence (Fasta)	MSILKIHARE IFDSRGNPTV EVDLFTSKGL FRAAVPSGAS TGIYEALELR DNDKTRYMGK 60 GVSKAVEHIN KTIAPALVSK KLNVTEQEKI DKLMIEMDGT ENKSKFGANA ILGVSLAVCK 120 AGAVEKGVPL YRHIADLAGN SEVILPVPAF NVINGGSHAG NKLAMQEFMI LPVGAANFRE 180 AMRIGAEVYH NLKNVIKEKY GKDATNVGDE GGFAPNILEN KEGLELLKTA IGKAGYTDKV 240 VIGMDVAASE FFRSGKYDLD FKSPDDPSRY ISPDQLADLY KSFIKDYPVV SIEDPFDQDD 300 WGAWQKFTAS AGIQVVGDDL TVTNPKRIAK AVNEKSCNCL LLKVNQIGSV TESLQACKLA 360 QANGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQL LRIEEELGSK 420 AKFAGRNFRN PLAK 435 Fasta Sequence >P06733\|ENO1; ENO1L1; MBPB1; MPB1\|Homo sapiens (Human) MSILKIHAREIFDSRGNPTVEVDLFTSKGLFRAAVPSGASTGIYEALELRDNDKTRYMGKGVSKAVEHINKTIAPALVSKKLNVTEQEKIDKLMIEMDGTENKSKFGANAILGVSLAVCKAGAVEKGVPLYRHIADLAGNSEVILPVPAFNVINGGSHAGNKLAMQEFMILPVGAANFREAMRIGAEVYHNLKNVIKEKYGKDATNVGDEGGFAPNILENKEGLELLKTAIGKAGYTDKVVIGMDVAASEFFRSGKYDLDFKSPDDPSRYISPDQLADLYKSFIKDYPVVSIEDPFDQDDWGAWQKFTASAGIQVVGDDLTVTNPKRIAKAVNEKSCNCLLLKVNQIGSVTESLQACKLAQANGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRSERLAKYNQLLRIEEELGSKAKFAGRNFRNPLAK

※ PTM-Disease Association

Num	PTM	Disease	Cell Type	Type	PTM Site	PMID
1	Acetylation	Pancreatic cancer/carcinoma/adenocarcinoma		U	K28	20433201
1	[Reference]: Mass spectrometry analysis of the post-translational modifications of alpha-enolase from pancreatic ductal adenocarcinoma cells.
2	Acetylation	Pancreatic cancer/carcinoma/adenocarcinoma		U	K103	20433201
2	[Reference]: Mass spectrometry analysis of the post-translational modifications of alpha-enolase from pancreatic ductal adenocarcinoma cells.
3	Acetylation	Pancreatic cancer/carcinoma/adenocarcinoma		U	K105	20433201
3	[Reference]: Mass spectrometry analysis of the post-translational modifications of alpha-enolase from pancreatic ductal adenocarcinoma cells.
4	Acetylation	Pancreatic cancer/carcinoma/adenocarcinoma		U	K221	20433201
4	[Reference]: sites phosphorylated in pancreatic ductal adenocarcinoma (PDAC) cells and not in normal pancreatic duct cells
5	Acetylation	Pancreatic cancer/carcinoma/adenocarcinoma		U	K239	20433201
5	[Reference]: Mass spectrometry analysis of the post-translational modifications of alpha-enolase from pancreatic ductal adenocarcinoma cells.
6	Acetylation	Pancreatic cancer/carcinoma/adenocarcinoma		U	K256	20433201
6	[Reference]: sites phosphorylated in pancreatic ductal adenocarcinoma (PDAC) cells and not in normal pancreatic duct cells
7	Acetylation	Pancreatic cancer/carcinoma/adenocarcinoma		U	K262	20433201
7	[Reference]: Mass spectrometry analysis of the post-translational modifications of alpha-enolase from pancreatic ductal adenocarcinoma cells.
8	Acetylation	Pancreatic cancer/carcinoma/adenocarcinoma		U	K285	20433201
8	[Reference]: Mass spectrometry analysis of the post-translational modifications of alpha-enolase from pancreatic ductal adenocarcinoma cells.
9	Acetylation	Pancreatic cancer/carcinoma/adenocarcinoma		U	K330	20433201
9	[Reference]: Mass spectrometry analysis of the post-translational modifications of alpha-enolase from pancreatic ductal adenocarcinoma cells.
10	Serine Phosphorylation	Pancreatic cancer/carcinoma/adenocarcinoma	tumor tissue	U	S419	20455595
10	[Reference]: Mass spectrometry showed that ENOA1,2 isoforms were phosphorylated on serine 419. ROC analysis demonstrated that autoantibodies to ENOA1,2 usefully complement the diagnostic performance of serum CA19.9 levels, achieving approximately 95% diagnostic accuracy in both advanced and resectable PDAC.

※ Disease Cross-ref Annotation

Database	Annotation
CTD (Curated) (count: 21) (view all)	MESH:D054058 ; Acute Coronary Syndrome MESH:D000230 ; Adenocarcinoma MESH:C538231 ; Adenocarcinoma of lung MESH:D000544 ; Alzheimer Disease MESH:D001172 ; Arthritis, Rheumatoid MESH:D001943 ; Breast Neoplasms MESH:D002277 ; Carcinoma MESH:D006528 ; Carcinoma, Hepatocellular MESH:D002294 ; Carcinoma, Squamous Cell MESH:D056486 ; Chemical and Drug Induced Liver Injury MESH:D020345 ; Enterocolitis, Necrotizing MESH:D004938 ; Esophageal Neoplasms MESH:D007248 ; Infertility, Male MESH:D015674 ; Mammary Neoplasms, Animal MESH:D008325 ; Mammary Neoplasms, Experimental MESH:D009062 ; Mouth Neoplasms MESH:D009361 ; Neoplasm Invasiveness MESH:D002289 ; Carcinoma, Non-Small-Cell Lung MESH:D010003 ; Osteoarthritis MESH:D010024 ; Osteoporosis MESH:D013274 ; Stomach Neoplasms
DisGeNet (Curated) (count: 21) (view all)	C0001418; Adenocarcinoma C0002395; Alzheimer's Disease C0003873; Rheumatoid Arthritis C0007131; Non-Small Cell Lung Carcinoma C0007137; Squamous cell carcinoma C0014859; Esophageal Neoplasms C0021364; Male infertility C0024667; Animal Mammary Neoplasms C0024668; Mammary Neoplasms, Experimental C0026640; Mouth Neoplasms C0027626; Neoplasm Invasiveness C0029408; Degenerative polyarthritis C0029456; Osteoporosis C0036341; Schizophrenia C0038356; Stomach Neoplasms C0152013; Adenocarcinoma of lung (disorder) C0520459; Necrotizing Enterocolitis C0948089; Acute Coronary Syndrome C1458155; Mammary Neoplasms C2239176; Liver carcinoma C4277682; Chemical and Drug Induced Liver Injury

Database

Annotation

CTD (Curated)
(count: 21)
(view all)

MESH:D054058 ; Acute Coronary Syndrome
MESH:D000230 ; Adenocarcinoma
MESH:C538231 ; Adenocarcinoma of lung
MESH:D000544 ; Alzheimer Disease
MESH:D001172 ; Arthritis, Rheumatoid
MESH:D001943 ; Breast Neoplasms

DisGeNet (Curated)
(count: 21)
(view all)

C0001418; Adenocarcinoma
C0002395; Alzheimer's Disease
C0003873; Rheumatoid Arthritis
C0007131; Non-Small Cell Lung Carcinoma
C0007137; Squamous cell carcinoma
C0014859; Esophageal Neoplasms

※ PTM Sites

PTM	Modification Sites
Phosphorylation (count: 40) (view all)	100 LMIEMDGTENKSKFG dbPAF 131 VEKGVPLYRHIADLA dbPAF 14 HAREIFDSRGNPTVE dbPAF 141 IADLAGNSEVILPVP dbPAF 157 FNVINGGSHAGNKLA dbPAF 189 MRIGAEVYHNLKNVI dbPAF 19 FDSRGNPTVEVDLFT dbPAF 205 EKYGKDATNVGDEGG dbPAF 236 TAIGKAGYTDKVVIG dbPAF 237 AIGKAGYTDKVVIGM dbPAF 254 AASEFFRSGKYDLDF dbPAF 257 EFFRSGKYDLDFKSP dbPAF 26 TVEVDLFTSKGLFRA dbPAF 263 KYDLDFKSPDDPSRY dbPAF 268 FKSPDDPSRYISPDQ dbPAF 27 VEVDLFTSKGLFRAA dbPAF 270 SPDDPSRYISPDQLA dbPAF 272 DDPSRYISPDQLADL dbPAF 280 PDQLADLYKSFIKDY dbPAF 282 QLADLYKSFIKDYPV dbPAF 287 YKSFIKDYPVVSIED dbPAF 291 IKDYPVVSIEDPFDQ dbPAF 308 WGAWQKFTASAGIQV dbPAF 310 AWQKFTASAGIQVVG dbPAF 336 AKAVNEKSCNCLLLK dbPAF 349 LKVNQIGSVTESLQA dbPAF 351 VNQIGSVTESLQACK dbPAF 353 QIGSVTESLQACKLA dbPAF 37 LFRAAVPSGASTGIY dbPAF 370 NGWGVMVSHRSGETE dbPAF 390 DLVVGLCTGQIKTGA dbPAF 40 AAVPSGASTGIYEAL dbPAF 41 AVPSGASTGIYEALE dbPAF 419 RIEEELGSKAKFAGR dbPAF 44 SGASTGIYEALELRD dbPAF 55 ELRDNDKTRYMGKGV dbPAF 57 RDNDKTRYMGKGVSK dbPAF 63 RYMGKGVSKAVEHIN dbPAF 72 AVEHINKTIAPALVS dbPAF 79 TIAPALVSKKLNVTE dbPAF
Acetylation (count: 32) (view all)	103 EMDGTENKSKFGANA PLMD 105 DGTENKSKFGANAIL PLMD 126 CKAGAVEKGVPLYRH PLMD 193 AEVYHNLKNVIKEKY PLMD 197 HNLKNVIKEKYGKDA PLMD 199 LKNVIKEKYGKDATN PLMD 202 VIKEKYGKDATNVGD PLMD 221 APNILENKEGLELLK PLMD 228 KEGLELLKTAIGKAG PLMD 233 LLKTAIGKAGYTDKV PLMD 239 GKAGYTDKVVIGMDV PLMD 256 SEFFRSGKYDLDFKS PLMD 262 GKYDLDFKSPDDPSR PLMD 28 EVDLFTSKGLFRAAV PLMD 281 DQLADLYKSFIKDYP PLMD 285 DLYKSFIKDYPVVSI PLMD 326 DLTVTNPKRIAKAVN PLMD 330 TNPKRIAKAVNEKSC PLMD 335 IAKAVNEKSCNCLLL PLMD 343 SCNCLLLKVNQIGSV PLMD 358 TESLQACKLAQANGW PLMD 406 CRSERLAKYNQLLRI PLMD 420 IEEELGSKAKFAGRN PLMD 5 ***MSILKIHAREIF PLMD 54 LELRDNDKTRYMGKG PLMD 60 DKTRYMGKGVSKAVE PLMD 64 YMGKGVSKAVEHINK PLMD 71 KAVEHINKTIAPALV PLMD 80 IAPALVSKKLNVTEQ PLMD 81 APALVSKKLNVTEQE PLMD 89 LNVTEQEKIDKLMIE PLMD 92 TEQEKIDKLMIEMDG PLMD
Ubiquitination (count: 35) (view all)	103 EMDGTENKSKFGANA PLMD 105 DGTENKSKFGANAIL PLMD 120 GVSLAVCKAGAVEKG PLMD 126 CKAGAVEKGVPLYRH PLMD 193 AEVYHNLKNVIKEKY PLMD 197 HNLKNVIKEKYGKDA PLMD 199 LKNVIKEKYGKDATN PLMD 202 VIKEKYGKDATNVGD PLMD 221 APNILENKEGLELLK PLMD 228 KEGLELLKTAIGKAG PLMD 233 LLKTAIGKAGYTDKV PLMD 239 GKAGYTDKVVIGMDV PLMD 256 SEFFRSGKYDLDFKS PLMD 262 GKYDLDFKSPDDPSR PLMD 28 EVDLFTSKGLFRAAV PLMD 281 DQLADLYKSFIKDYP PLMD 285 DLYKSFIKDYPVVSI PLMD 326 DLTVTNPKRIAKAVN PLMD 330 TNPKRIAKAVNEKSC PLMD 335 IAKAVNEKSCNCLLL PLMD 343 SCNCLLLKVNQIGSV PLMD 358 TESLQACKLAQANGW PLMD 394 GLCTGQIKTGAPCRS PLMD 406 CRSERLAKYNQLLRI PLMD 420 IEEELGSKAKFAGRN PLMD 422 EELGSKAKFAGRNFR PLMD 5 ***MSILKIHAREIF PLMD 54 LELRDNDKTRYMGKG PLMD 60 DKTRYMGKGVSKAVE PLMD 64 YMGKGVSKAVEHINK PLMD 71 KAVEHINKTIAPALV PLMD 80 IAPALVSKKLNVTEQ PLMD 81 APALVSKKLNVTEQE PLMD 89 LNVTEQEKIDKLMIE PLMD 92 TEQEKIDKLMIEMDG PLMD
Sumoylation (count: 3)	221 APNILENKEGLELLK PLMD 326 DLTVTNPKRIAKAVN PLMD 80 IAPALVSKKLNVTEQ PLMD
Glycation (count: 1)	89 LNVTEQEKIDKLMIE PLMD
Malonylation (count: 10) (view all)	126 CKAGAVEKGVPLYRH PLMD 193 AEVYHNLKNVIKEKY PLMD 202 VIKEKYGKDATNVGD PLMD 233 LLKTAIGKAGYTDKV PLMD 256 SEFFRSGKYDLDFKS PLMD 420 IEEELGSKAKFAGRN PLMD 5 ***MSILKIHAREIF PLMD 71 KAVEHINKTIAPALV PLMD 80 IAPALVSKKLNVTEQ PLMD 81 APALVSKKLNVTEQE PLMD
Phosphoglycerylation (count: 4)	335 IAKAVNEKSCNCLLL PLMD 343 SCNCLLLKVNQIGSV PLMD 394 GLCTGQIKTGAPCRS PLMD 92 TEQEKIDKLMIEMDG PLMD
Succinylation (count: 22) (view all)	126 CKAGAVEKGVPLYRH PLMD 193 AEVYHNLKNVIKEKY PLMD 202 VIKEKYGKDATNVGD PLMD 221 APNILENKEGLELLK PLMD 228 KEGLELLKTAIGKAG PLMD 233 LLKTAIGKAGYTDKV PLMD 256 SEFFRSGKYDLDFKS PLMD 262 GKYDLDFKSPDDPSR PLMD 28 EVDLFTSKGLFRAAV PLMD 281 DQLADLYKSFIKDYP PLMD 285 DLYKSFIKDYPVVSI PLMD 330 TNPKRIAKAVNEKSC PLMD 335 IAKAVNEKSCNCLLL PLMD 358 TESLQACKLAQANGW PLMD 406 CRSERLAKYNQLLRI PLMD 5 ***MSILKIHAREIF PLMD 60 DKTRYMGKGVSKAVE PLMD 64 YMGKGVSKAVEHINK PLMD 71 KAVEHINKTIAPALV PLMD 80 IAPALVSKKLNVTEQ PLMD 81 APALVSKKLNVTEQE PLMD 89 LNVTEQEKIDKLMIE PLMD

※ Protein-Protein Interaction

Network

Interaction

Source

O15264	P06733	IntAct
P06733	P12004	MINT
P06733	P16104	IntAct

PTMD Annotation Information

※ Protein Information

Functional Description

Fasta Sequence

※ PTM-Disease Association

※ Disease Cross-ref Annotation

※ PTM Sites

※ Protein-Protein Interaction