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ENO1 (Enolase 1, (alpha))

Written2009-08Bogusz Trojanowicz, Cuong Hoang-Vu, Carsten Sekulla
AG Experimentelle, Chirurgische Onkologie, Universitatsklinik und Poliklinik fur Allgemein-, Viszeral- und Gefasschirurgie, Martin-Luther Universitat, Magdeburger Strasse 18, 06097 Halle/S, Germany (BT, CHV, CS); AG Experimentelle, Chirurgische Onkologie, Universitatsklinik und Poliklinik fur Kinderchirurgie, Martin-Luther Universitat, Magdeburger Strasse 18, 06097 Halle/S, Germany (BT)

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Alias (NCBI)EC
HGNC (Hugo) ENO1
HGNC Alias symbPPH
HGNC Alias namealpha-enolase
HGNC Previous nameENO1L1
HGNC Previous name"enolase 1, (alpha)"
LocusID (NCBI) 2023
Atlas_Id 40453
Location 1p36.23  [Link to chromosome band 1p36]
Location_base_pair Starts at 8861000 and ends at 8878686 bp from pter ( according to GRCh38/hg38-Dec_2013)  [Mapping ENO1.png]
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
AKNA (9q32) / ENO1 (1p36.23)ARHGDIB (12p12.3) / ENO1 (1p36.23)CCDC58 (3q21.1) / ENO1 (1p36.23)
ENO1 (1p36.23) / APP (21q21.3)ENO1 (1p36.23) / CCT7 (2p13.2)ENO1 (1p36.23) / COL4A2 (13q34)
ENO1 (1p36.23) / ENO1 (1p36.23)ENO1 (1p36.23) / MAPRE1 (20q11.21)ENO1 (1p36.23) / MCUR1 (6p23)
ENO1 (1p36.23) / RPA1 (17p13.3)ENO1 (1p36.23) / UBE4A (11q23.3)ESYT2 (7q36.3) / ENO1 (1p36.23)
EXOSC6 (16q22.1) / ENO1 (1p36.23)ICAM2 (17q23.3) / ENO1 (1p36.23)IFI16 (1q23.1) / ENO1 (1p36.23)
IQCG (3q29) / ENO1 (1p36.23)LGMN (14q32.12) / ENO1 (1p36.23)LOC100507412 (-) / ENO1 (1p36.23)
SAAL1 (11p15.1) / ENO1 (1p36.23)SPTBN1 (2p16.2) / ENO1 (1p36.23)


Note Alpha-Enolase (ENO1, alpha enolase, non-neuronal enolase) is one of the three enolase enzymes, expressed in a wide variety of tissues. The other two enolase genes, ENO2 and ENO3, encode gamma (neuron-specific) and beta (muscle-specific) enolase, respectively. The active enolase enzymes exist as homodimers of non-covalently bound subunits. Each alpha, beta or gamma subunit is encoded by separate genes. The genomic organisation of ENO1 gene is identical with that of human gamma-enolase gene. All the coding exons have exactly the same length and introns occur at analogous positions.
  Structure of ENO1 mRNA ; note that nucleotides number (nt), exon positions (1-12) and two translation initiation sites (ATG) are labelled.
Description The ENO1 gene consists of 12 exons distributed over 17718 bp of genomic DNA. Single alpha-enolase transcript contains two translation initiation positions and encodes two structurally and functionally distinct proteins, alpha-enolase enzyme and MYC promotor-binding protein (MBP-1).
Transcription Transcription start sites of ENO1 gene are heterogeneous and spread over 38-bp region located at 116 bp upstream from the initiation codon ATG. These multiple start sites of transcription in ENO1 gene are consistent with lack of a canonical TATA box, usually found at the position 19-27 bp upstream of the cap sites. It is worth to notice that promoter of ENO1 gene contains two perfect Myc-Max binding motifs CACGTC. Other regulatory sites found in the 5'-flanking region of ENO1 gene include AP1 (T[T/G]AGTCA), AP2 (CCCCAGGC), AP3 (GGGTGTGGAAAG), AP4 (CAGCTGTGG), AP5 (CTGTGGAATG), ATF/CREB ([T/G][A/T]CGTCA), C2 (CATGTG), CTF/NF1 (TGGCTNNNAGCCAA), E2AE-C beta (TGGGAATT), E2F (TTTCGCGC), E4TF1 (GGAAGTG), EF-C (GTTGCNNGGCAAC), MLTF/USF (GGTCACGTGGCC), Ig octamer (ATTTGCAT), PEA2 (GACCGCA), SP1 (GGGCGG), CACCC (may function as CAAT boxes) and viral core (GTGG[A/T][A/T][A/T]G).
Pseudogene A pseudogene has been identified that is located on the other arm of the same chromosome (provided by RefSeq).


  Structure of ENO1/MBP-1 protein; N and C termini, and amino acid (aa) positions are labelled.
Description Alpha-Enolase (ENO1), like two other isoenzymes (gamma-ENO2 and beta-ENO3), is made up of two identical (homodimer), non-covalently bound alpha alpha subunits; alpha-Enolase is resolved during 1D-PAGE as a protein with molecular weight of about 48kDa (434 amino acids). It was demonstrated that in brain and neurons, specific enolases may exist as heterodimers, such as alpha alpha, alpha beta, beta beta, alpha gamma and gamma gamma. The proportions of isoenzymes alpha alpha, alpha beta and beta beta change in heart and muscle during embryonic development. In both mentioned tissues, isoform alpha was found predominantly in fetus. In adult heart this subunit is replaced by types alpha beta and beta beta, and in muscle by type beta beta. In human adult brain tissues, apha-type and gamma-type enolase subunits are present at similar concentrations.
Two identical subunits of alpha-Enolase facilitate each other in an antiparallel fashion. Each subunit is made up of two distinct domains: N-terminal domain, consisting of three beta-sheets and four alpha-helices (beta3 alpha4 topology), and larger C-terminal domain with eightfold alpha beta barrel structure with beta beta alpha alpha(beta alpha)6 topology. This domain contains two beta-sheets at the beginning, followed by two alpha-helices and ends with a barrel made up of alternating beta-sheets and alpha-helices (beta - sheets are surrounded by the alpha - helices). The N-terminal of one subunit contacts the C-terminal of the second in such way, that glutamic acid at position 20 (Glu20) forms an ionic pair with arginine at position 414 (Arg414).
Alternatively translated product of ENO1 gene, called MBP-1 (MYC promotor-binding protein), is expressed as a 37kDa (338 amino acids) protein and does not posses the enolase enzyme activity.
Expression Apha-Enolase is widely expressed in variety of tissues including liver, brain, kidney, spleen, adipose as well as thyroid. In comparison with gamma-type subunit found only in neurons, type alpha subunit was also detected in astrocytes, ependymal cells, capillary endothelial cells, Schwann cells and arachnoidal endothelial cells.
Localisation Alpha-Enolase is most abundantly found in cytoplasm and also on the cell surface. MBP-1 is localised in the nucleus.
Function Enolase enzymes (2-phospho-D-glycerate hydrolases) catalyse the dehydration of 2-phospho-D-glycerate (PGA) to phosphoenolopyruvate (PEP) in Emden Mayerhoff-Parnas glycolytic pathway (catabolic direction). In anabolic pathway (reverse reaction) during gluconeogenesis, the same enzyme catalyses hydration of PEP to PGA (hence it is called phosphopyruvate hydratase). Metal ions are cofactors impairing the increase of enolase activity; hence it is also called metal-activated metalloenzyme. Magnesium is a natural cofactor causing the highest activity. The relative activation strength profile of metal ions involved in the enzyme activity appears in the following rank of order Mg2+ > Zn2+ > Mn2+ > Fe(II)2+ > Cd2+ > Co2+, Ni2+, Sm3+, Tb3+ and most other divalent metal ions. In reaction catalyzed by enolases, the alpha-proton from a carbon adjacent to a carboxylate group of PGA, is abstracted, and PGA is conversed to enolate anion intermediate. This intermediate is further processed in a variety of chemical reactions, including racemization, cycloisomerization and beta-elimination of either water or ammonia.
The smaller product of ENO1 gene, MBP-1, is known as c-myc binding protein and negative regulator of its expression. C-myc is a DNA-binding phosphoprotein and a key regulator of cell behaviour. Many of c-myc targeting pathways are deregulated in cancer cells and contribute to its enhanced expression. There are four c-myc promoters, designated as P0, P1, P2 and P3, although in normal and cancer cells most mRNAs initiate at the P2 promoter. MBP-1 binds in a region +123 to +153 relative to the c-myc P2 promoter and probably by preventing the formation of a transcription initiation complex, decrease c-myc promoter activity. Hence MBP-1 is considered as tumor suppressor.
ENO1 protein was also found as a structural component of the eye lenses and was designated as tau-crystalin. ENO1 enzyme and tau-crystalin are the products of the same gene. Tau-crystalins are the major components of vertebrate lens. These proteins are mainly found in monomeric form with a low enzymatic activity, while the active ENO1 enzyme exists as a dimer. Irrespective of ENO1 enzyme activity, its significant presence in eye lens (23% of the total protein of the lens) clearly indicate ENO1 structural role in lens and cataracts.
In hypoxic conditions elevated ENO1 levels may provide protection to the cells by increasing anaerobic metabolism.
  Reaction catalyzed by Enolase.
Homology Currently, amino acid sequences of more than 50 enolase enzymes are known. The five residues that participate in catalytic activity of this enzyme are highly conserved throughout evolution. Studies in vitro revealed that mutant enolase enzymes that differs at either positions Glu168, Glu211, Lys345, Lys396 or His159, demonstrated dramatically decreased activity level. An integral and conserved part of enolases are two Mg2+ ions that participate in conformational changes of the active site of enolase and enable binding of a substrate or its analogues.


Note The ENO1 gene maps to a region of chromosome 1 (1p35-p36) reported to be often deleted in several human malignancies, including neuroblastoma, melanoma, pheochromocytoma, breast, liver and colon cancer. However screening of neuroblastomas at different stages, failed to detect any mutations in ENO1 gene.
Amplification of ENO1 gene, as well as PAX7 (region 1pter-p33) was found to be a common phenomenon in squamous cell lung carcinoma.

Implicated in

Entity Non-Small Cell Lung Cancer (NSCLC)
Note Higher expression of ENO1 was demonstrated in NSCLC tissues as compared with normal lung tissues. Detection and expression level of ENO1 in primary tumors were the key factors contributing to overall patient's survival rates. Relatively higher ENO1 levels in tumors correlated with poorer survival outcomes and tumor recurrence.
Other report suggests that ENO1 down-regulation in patients with NSCLC, predicts more aggressive biological behaviour. The patients whose tumors showed decreased ENO1 production had significantly poorer overall survival when compared with those without ENO1 reduction.
Also in proteomic studies, ENO1 was one of the secreted proteins demonstrated to be overexpressed by NSCLC cell line A549 as compared to controls.
Studies in vitro performed on NSCLC cell line H1299, revealed that MBP-1 overexpression correlated with decreased cell proliferation as compared with corresponding controls. Investigations in vivo demonstrated tumor suppressive properties of MBP-1. In mice with induced tumors (injection of H1299) administration of adenovirus MBP-1 construct significantly reduced tumor growth and prolonged animal survival rates.
Entity Small Cell Lung Cancer
Note There is some evidence concerning the role of anti-alpha-enolase antibodies in cancer associated retinopathy with SCLC. In serum obtained from patient with a sudden loss of vision, the only detectable antibodies were those against a 35-kDa anti-retinal protein. Surgical treatment performed after 1 week and 1 month, led to changes in the antibody response from antibodies against p35kDa to alpha-enolase after tumor resection. SCLC may express high levels of alpha-enolase and anti-alpha-enolase antibodies are typically detected after diagnosis of cancer.
Entity Thyroid carcinoma
Note In thyroid oncocytomas, which represent a subgroup of follicular thyroid carcinoma (FTC), the up-regulation of ENO1, GPI (glucose phosphate isomerase) and GAPDH (glyceraldehydes-3-phosphate dehydrogenase) was identified as metabolic signature of thyroid carcinoma.
Important role of ENO1 in progression of thyroid carcinoma was also demonstrated for cell lines established from FTC. Pre-treatment of these cell lines with retinoic acid (RA) used in therapy and chemoprevention of solid cancers, led to decrease in ENO1 and MBP-1 expression, accompanied by reduced invasiveness of the thyroid carcinoma cells. Similar effects were also observed after silencing of common the MYC promoter-binding domain found in ENO1 and MBP-1. Both, RA-mediated and siRNA induced reduction of ENO1/MBP-1 resulted in down-regulation of c-Myc oncoprotein. It seems that in FTC the bi-functional role of ENO1 gene products is diminished and ENO1 posses the enzymatic activity only. It is worth to notice that ENO1 promoter contains two MYC binding sites (CACGTG). C-Myc over-expression and interaction with these sites may result in increased ENO1 expression and/or energy production.
In well differentiated medullary thyroid carcinomas MTC the relatively high amount of alpha beta and gamma gamma enolase isoenzymes was observed, indicating presumed neuroectodermal origin of these tumors. In highly undifferentiated and anaplastic MTCs, the majority of enzyme was represented as alpha alpha-enolase while alpha gamma-enolase was only weakly detectable.
Entity Hepatocellular carcinoma (HCC)
Note In proteomic studies performed on HCC cell lines and tissues, ENO1 was identified as a protein that showed stronger expression in tumor tissues when comparing to nontumorous samples. Additionally, expression of ENO1 increased with tumor dedifferentiation status. Significantly higher ENO1 expression was found in poorly differentiated HCC than in well differentiated HCC. Moreover, expression of ENO1 positively correlated with tumor size and venous invasion. Also reduction of ENO1 by specific siRNAs decreased the proliferation rates of HCC cell lines and prolonged the G2/M phase of the cell cycle.
Investigations of MBP-1 revealed its significant reduction in cirrhosis and even more diminished expression in HCC. This reduction was surprisingly accompanied by decrease in c-myc expression.
Entity Breast carcinoma
Note Increased expression of ENO1 was found in HER-2/neu positive breast tumors and cell lines when compared with corresponding controls. HER-2/neu is the receptor tyrosine kinase found to be overexpressed in up to 30% of breast cancers and is associated with increased metastasis rate and poor prognosis.
Introduction of MBP-1 gene into human breast carcinoma cells MDA-MB-231 and MCF-7 reduced their ability to penetrate basement membrane matrix and suppressed tumor formation in athymic nude mice. It is worth to notice that MCF-7 cell line is estrogen receptor positive and estrogen dependent for tumorigenicity.
It was demonstrated that translation of ENO1 mRNA in MCF-7 cell line is glucose concentration-dependent. Low glucose concentrations increased the level of MBP-1 protein accompanied by reduced proliferation rates. The levels of ENO1 mRNA remained unaffected. This suggests that effects induced by low glucose concentrations are mediated by preferential translation of MBP-1 (using the down-stream ATG codon). In contrast, physiologic or high glucose concentrations correlated with reduced levels of MBP-1 protein and markedly induced growth of the cells. Interestingly the low glucose group exhibited a dramatic increase in c-Myc expression, not observed in physiologic or high glucose conditions. As demonstrated for follicular thyroid carcinoma cells, also in this case c-Myc might directly transactivate ENO1 promoter, resulting in an increase in glucose uptake and elevated proliferation rates.
Entity Prostate cancer
Note Investigations performed on human prostate cancer cells PC3, revealed that tumor suppressive function of MBP-1 is diminished. Reduction of endogenous MBP-1 by employing specific siRNAs resulted in decreased proliferation rates accompanied by inhibition of cyclin A1 and cyclin B1 expression. Additionally, the cell size increased after depletion of MBP-1. Introduction of exogenous MBP-1 restored cyclins expression, leading to dose-dependent increase in cyclin A1 and B1 levels.
Entity Brain tumors
Note Generally, the increased levels and activity of alpha alpha-enolase correlate with brain tumorigenicity. In astrocytomas with different degrees of malignancy, oligodendrogliomas, meningiomas and ependymomas, alpha alpha-enolase was more abundant than in normal brain tissues. Among astrocytic tumors, glioblastomas revealed the highest proportion of alpha alpha-enolase as compared with control tissues.
Introduction of full length, exogenous ENO1 sequence into 1p-deleted or other neuroblastoma cell lines, led to reduction of cell growth. This suggests that in this cell lines ENO1 is preferentially translated as MBP-1 and probably does not posses the enolase enzyme activity.
Entity Multiple myeloma (plasma cell myeloma, Kahler's disease)
Note It was demonstrated, that interleukin 6 (IL-6) is implicated in the in vivo proliferation of malignant plasma cells in multiple myeloma. Studies in vitro revealed that myeloma cell line U266 treated with IL-6, responded with increased levels of MBP-1 and XBP-1 (X-box binding protein).
Entity Acute lung inflammation (pneumonia)
Note Increased ENO1 cell-surface expression on peripheral blood monocytes (PBMs) and strong ENO1 production in mononuclear cells in the alveolar space were demonstrated for pneumonia patients when compared with healthy volunteers. Elevated cell-surface expression of ENO1 on PBMs and on human leukemic monocyte lymphoma cell line U937, led to increased plasmin generation, enhanced monocyte migration through epithelial monolayers and promoted matrix degradation.
Entity Vasculitis
Note In sera from patients with clinically proven vaculitis, anti-neutrophil cytoplasmic antibodies (ANCA) reacted with proteins present in the granules of human neutrophils. 37.3 % of these sera contained the antibodies raised against 48kDa protein, identified further as cytoplasmic alpha-enolase. Antibodies directed against enolase protein, recognised only alpha isoform and were detected in sera giving ANCA staining pattern.
Disease Vasculitis (inflammatory destruction of blood vessels).
Entity Nephritis
Note In two independent studies antibodies raised against alpha-enolase were detected in 10/41 and 9/33 sera of patients with clinically proved SLE, respectively. 80% of patients from the first report and 66.7% from the second one, suffered from active nephritis.
Disease Nephritis (renal disease) caused by systemic lupus erythematosus (SLE, chronic autoimmune connective tissue disease that can affect any part of the body).
Entity Ulcerative colitis
Note Alpha-enolase antibodies were found in about 10% of ulcerative colitis patients.
Entity Crohn's disease
Note Alpha-enolase antibodies were found in about 18% of patients with Crohn's disease.
Disease Crohn's disease (autoimmune, inflammatory disease of the intestines that may affect any part of the gastrointestinal tract).
Entity Primary biliary cirrhosis and autoimmune hepatitis
Note Alpha-enolase antibodies were present in 28.6% of patients with primary biliary cirrhosis and in 31.6% with autoimmune hepatitis. Normal subjects revealed significantly lower levels of alpha-enolase antibodies when compared with both diseases. Note that antibodies against beta and gamma enolases were not found in any serum sample analysed.


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PMID 17020980
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Introduction of in vitro transcribed ENO1 mRNA into neuroblastoma cells induces cell death.
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PMID 10802057
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This paper should be referenced as such :
Trojanowicz, B ; Hoang-Vu, C ; Sekulla, C
ENO1 (Enolase 1, (alpha))
Atlas Genet Cytogenet Oncol Haematol. 2010;14(7):635-640.
Free journal version : [ pdf ]   [ DOI ]

External links

HGNC (Hugo)ENO1   3350
LRG (Locus Reference Genomic)LRG_1165
Entrez_Gene (NCBI)ENO1    enolase 1
AliasesENO1L1; HEL-S-17; MPB1; NNE; 
GeneCards (Weizmann)ENO1
Ensembl hg19 (Hinxton)ENSG00000074800 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000074800 [Gene_View]  ENSG00000074800 [Sequence]  chr1:8861000-8878686 [Contig_View]  ENO1 [Vega]
ICGC DataPortalENSG00000074800
TCGA cBioPortalENO1
AceView (NCBI)ENO1
Genatlas (Paris)ENO1
SOURCE (Princeton)ENO1
Genetics Home Reference (NIH)ENO1
Genomic and cartography
GoldenPath hg38 (UCSC)ENO1  -     chr1:8861000-8878686 -  1p36.23   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)ENO1  -     1p36.23   [Description]    (hg19-Feb_2009)
GoldenPathENO1 - 1p36.23 [CytoView hg19]  ENO1 - 1p36.23 [CytoView hg38]
genome Data Viewer NCBIENO1 [Mapview hg19]  
Gene and transcription
Genbank (Entrez)AF035286 AK098420 AK222517 AK223192 AK298600
RefSeq transcript (Entrez)NM_001201483 NM_001353346 NM_001428
RefSeq genomic (Entrez)
Consensus coding sequences : CCDS (NCBI)ENO1
Alternative Splicing GalleryENSG00000074800
Gene ExpressionENO1 [ NCBI-GEO ]   ENO1 [ EBI - ARRAY_EXPRESS ]   ENO1 [ SEEK ]   ENO1 [ MEM ]
Gene Expression Viewer (FireBrowse)ENO1 [ Firebrowse - Broad ]
GenevisibleExpression of ENO1 in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)2023
GTEX Portal (Tissue expression)ENO1
Human Protein AtlasENSG00000074800-ENO1 [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtP06733   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtP06733  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProP06733
Splice isoforms : SwissVarP06733
Domaine pattern : Prosite (Expaxy)ENOLASE (PS00164)   
Domains : Interpro (EBI)Enolase    Enolase-like_C_sf    Enolase-like_N    Enolase_C    Enolase_CS    Enolase_N   
Domain families : Pfam (Sanger)Enolase_C (PF00113)    Enolase_N (PF03952)   
Domain families : Pfam (NCBI)pfam00113    pfam03952   
Domain families : Smart (EMBL)Enolase_C (SM01192)  Enolase_N (SM01193)  
Conserved Domain (NCBI)ENO1
Blocks (Seattle)ENO1
PDB (RSDB)2PSN    3B97    5JLZ    5LAX    5NI9    5NIG    5OCK   
PDB Europe2PSN    3B97    5JLZ    5LAX    5NI9    5NIG    5OCK   
PDB (PDBSum)2PSN    3B97    5JLZ    5LAX    5NI9    5NIG    5OCK   
PDB (IMB)2PSN    3B97    5JLZ    5LAX    5NI9    5NIG    5OCK   
Structural Biology KnowledgeBase2PSN    3B97    5JLZ    5LAX    5NI9    5NIG    5OCK   
SCOP (Structural Classification of Proteins)2PSN    3B97    5JLZ    5LAX    5NI9    5NIG    5OCK   
CATH (Classification of proteins structures)2PSN    3B97    5JLZ    5LAX    5NI9    5NIG    5OCK   
Human Protein Atlas [tissue]ENSG00000074800-ENO1 [tissue]
Peptide AtlasP06733
IPIIPI00465248   IPI00759806   
Protein Interaction databases
IntAct (EBI)P06733
Ontologies - Pathways
Ontology : AmiGO"phosphopyruvate hydratase complex  phosphopyruvate hydratase complex  negative regulation of transcription by RNA polymerase II  magnesium ion binding  RNA polymerase II regulatory region sequence-specific DNA binding  DNA-binding transcription repressor activity, RNA polymerase II-specific  RNA binding  phosphopyruvate hydratase activity  phosphopyruvate hydratase activity  phosphopyruvate hydratase activity  protein binding  extracellular space  nucleus  nucleus  cytoplasm  cytosol  cytosol  plasma membrane  gluconeogenesis  glycolytic process  response to virus  cell surface  positive regulation of plasminogen activation  membrane  membrane  negative regulation of cell growth  M band  regulation of vacuole fusion, non-autophagic  protein homodimerization activity  cadherin binding  negative regulation of transcription, DNA-templated  negative regulation of transcription, DNA-templated  positive regulation of muscle contraction  GTPase binding  canonical glycolysis  canonical glycolysis  canonical glycolysis  extracellular exosome  cell cortex region  negative regulation of hypoxia-induced intrinsic apoptotic signaling pathway  negative regulation of hypoxia-induced intrinsic apoptotic signaling pathway  positive regulation of ATP biosynthetic process  positive regulation of ATP biosynthetic process"  
Ontology : EGO-EBI"phosphopyruvate hydratase complex  phosphopyruvate hydratase complex  negative regulation of transcription by RNA polymerase II  magnesium ion binding  RNA polymerase II regulatory region sequence-specific DNA binding  DNA-binding transcription repressor activity, RNA polymerase II-specific  RNA binding  phosphopyruvate hydratase activity  phosphopyruvate hydratase activity  phosphopyruvate hydratase activity  protein binding  extracellular space  nucleus  nucleus  cytoplasm  cytosol  cytosol  plasma membrane  gluconeogenesis  glycolytic process  response to virus  cell surface  positive regulation of plasminogen activation  membrane  membrane  negative regulation of cell growth  M band  regulation of vacuole fusion, non-autophagic  protein homodimerization activity  cadherin binding  negative regulation of transcription, DNA-templated  negative regulation of transcription, DNA-templated  positive regulation of muscle contraction  GTPase binding  canonical glycolysis  canonical glycolysis  canonical glycolysis  extracellular exosome  cell cortex region  negative regulation of hypoxia-induced intrinsic apoptotic signaling pathway  negative regulation of hypoxia-induced intrinsic apoptotic signaling pathway  positive regulation of ATP biosynthetic process  positive regulation of ATP biosynthetic process"  
Pathways : KEGGGlycolysis / Gluconeogenesis    RNA degradation    HIF-1 signaling pathway   
REACTOMEP06733 [protein]
REACTOME PathwaysR-HSA-70263 [pathway]   
NDEx NetworkENO1
Atlas of Cancer Signalling NetworkENO1
Wikipedia pathwaysENO1
Orthology - Evolution
GeneTree (enSembl)ENSG00000074800
Phylogenetic Trees/Animal Genes : TreeFamENO1
Homologs : HomoloGeneENO1
Homology/Alignments : Family Browser (UCSC)ENO1
Gene fusions - Rearrangements
Fusion Cancer (Beijing)ENO1 [1p36.23]  -  UBE4A [11q23.3]  [FUSC001354]
Fusion : FusionGDB4.2.1.11   
Fusion : Fusion_HubABCB7--ENO1    ACTB--ENO1    ACTR1A--ENO1    AGPS--ENO1    AKNA--ENO1    ANKRD11--ENO1    ANXA1--ENO1    ARHGDIB--ENO1    C4ORF3--ENO1    CASC5--ENO1    CCDC58--ENO1    CEBPZ--ENO1    COL12A1--ENO1    CREG1--ENO1    CRTAP--ENO1   
CXORF57--ENO1    DCAF17--ENO1    EDARADD--ENO1    EEF1A1--ENO1    EEF1G--ENO1    ENO1--ACOT7    ENO1--ADAM28    ENO1--ADAM33    ENO1--APP    ENO1--ARHGAP30    ENO1--CCDC90A    ENO1--CCT7    ENO1--CDV3    ENO1--CNBP    ENO1--COL4A2   
ENO1--DDX27    ENO1--DHCR24    ENO1--DLC1    ENO1--EDARADD    ENO1--ENO1    ENO1--ERBB2    ENO1--GOLGA1    ENO1--GOLGA2B    ENO1--GOLGA8B    ENO1--GUK1    ENO1--HBB    ENO1--IGFBP5    ENO1--ITPRIPL2    ENO1--JAK1    ENO1--LOC729668   
ENO1--LYZ    ENO1--MAGT1    ENO1--MAP3K3    ENO1--MAPRE1    ENO1--MCM5    ENO1--MRPL53    ENO1--MSH2    ENO1--MTR    ENO1--MTRR    ENO1--MYH11    ENO1--NOC2L    ENO1--PAN2    ENO1--PARK7    ENO1--PDK4    ENO1--PEX26   
ENO1--PRMT7    ENO1--PSMD7    ENO1--REXO4    ENO1--RFWD2    ENO1--RP3-477M7.5    ENO1--RPA1    ENO1--RPL30    ENO1--SCAND1    ENO1--SHMT1    ENO1--SIAE    ENO1--SLC11A1    ENO1--SLC2A5    ENO1--SLC6A2    ENO1--SNW1    ENO1--SRF   
ENO1--SUN2    ENO1--TAPBP    ENO1--TAS1R1    ENO1--UBE4A    ENO1--UTRN    ENO1--UVRAG    ENO1--VEGFA    ENO1--WDR54    ENO1--XIRP1    ERCC1--ENO1    ESYT2--ENO1    EXOSC10--ENO1    EXOSC6--ENO1    FCER1G--ENO1    FN1--ENO1   
GNAS--ENO1    GNB2L1--ENO1    HBA1--ENO1    HBA2--ENO1    HSA-MIR-6723--ENO1    ICAM2--ENO1    IER5--ENO1    IFI16--ENO1    IQCG--ENO1    JA040725--ENO1    KLHL21--ENO1    LGMN--ENO1    LOC100507412--ENO1    MAP3K2--ENO1    MPZL1--ENO1   
MRFAP1--ENO1    MTATP6P1--ENO1    MXD4--ENO1    NAPSA--ENO1    P4HB--ENO1    PRDX5--ENO1    PRRG3--ENO1    PSMB1--ENO1    PSME1--ENO1    RBMX--ENO1    RCC1--ENO1    RERE--ENO1    RHCG--ENO1    RNF11--ENO1    RP5-857K21.11--ENO1   
RPL14P1--ENO1    RPL37--ENO1    RPL8--ENO1    RPS5--ENO1    RPS6KA1--ENO1    RPS8--ENO1    SAAL1--ENO1    SCAP--ENO1    SIPA1--ENO1    SLC37A4--ENO1    SPTBN1--ENO1    SREK1IP1--ENO1    SRP72--ENO1    SYNJ2BP--ENO1    TENM3--ENO1   
TNFRSF1A--ENO1    TNFSF12--ENO1    TNS1--ENO1    WDR92--ENO1    WIPF3--ENO1    YTHDF2--ENO1   
Fusion : QuiverENO1
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerENO1 [hg38]
Exome Variant ServerENO1
GNOMAD BrowserENSG00000074800
Varsome BrowserENO1
Genomic Variants (DGV)ENO1 [DGVbeta]
DECIPHERENO1 [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisENO1 
ICGC Data PortalENO1 
TCGA Data PortalENO1 
Broad Tumor PortalENO1
OASIS PortalENO1 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICENO1  [overview]  [genome browser]  [tissue]  [distribution]  
Somatic Mutations in Cancer : COSMIC3DENO1
Mutations and Diseases : HGMDENO1
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD - Leiden Open Variation Database
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
BioMutasearch ENO1
DgiDB (Drug Gene Interaction Database)ENO1
DoCM (Curated mutations)ENO1 (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)ENO1 (select a term)
NCG6 (London) select ENO1
Cancer3DENO1(select the gene name)
Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Genetic Testing Registry ENO1
NextProtP06733 [Medical]
Target ValidationENO1
Huge Navigator ENO1 [HugePedia]
Clinical trials, drugs, therapy
Protein Interactions : CTD
Pharm GKB GenePA27786
Clinical trialENO1
canSAR (ICR)ENO1 (select the gene name)
DataMed IndexENO1
PubMed298 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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indexed on : Fri Feb 19 17:49:58 CET 2021

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