Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Alpha-enolase

Gene

ENO1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

Catalytic activityi

2-phospho-D-glycerate = phosphoenolpyruvate + H2O.1 Publication

Cofactori

Mg2+1 PublicationNote: Binds two Mg2+ per subunit. Required for catalysis and for stabilizing the dimer.1 Publication

pH dependencei

Enolase activity is lost above pH 9.0. Immunoglobulin production stimulating activity is retained at pH 13.0.1 Publication

Pathwayi: glycolysis

This protein is involved in step 4 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase (HEL-S-162eP), Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), Glyceraldehyde-3-phosphate dehydrogenase (HEL-S-278), Glyceraldehyde-3-phosphate dehydrogenase, testis-specific (GAPDHS)
  2. Phosphoglycerate kinase 2 (PGK2), Phosphoglycerate kinase 1 (PGK1)
  3. no protein annotated in this organism
  4. Alpha-enolase (ENO1), Beta-enolase (ENO3), Enolase 4 (ENO4), Gamma-enolase (ENO2)
  5. Pyruvate kinase, Pyruvate kinase PKM (PKM), Pyruvate kinase (PKM2), Pyruvate kinase (PKM), Pyruvate kinase (PKM2), Pyruvate kinase (PKM), Pyruvate kinase, Pyruvate kinase (PKM), Pyruvate kinase, Pyruvate kinase PKLR (PKLR), Pyruvate kinase, Pyruvate kinase (PKM2), Pyruvate kinase (PKM), Pyruvate kinase (HEL-S-30), Pyruvate kinase (PKM2)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi40Magnesium 11
Binding sitei158SubstrateBy similarity1
Binding sitei167SubstrateBy similarity1
Active sitei210Proton donorBy similarity1
Metal bindingi245Magnesium 21
Metal bindingi293Magnesium 21
Binding sitei293SubstrateBy similarity1
Metal bindingi318Magnesium 21
Binding sitei318SubstrateBy similarity1
Active sitei343Proton acceptorBy similarity1
Binding sitei394SubstrateBy similarity1

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • DNA binding Source: UniProtKB-KW
  • GTPase binding Source: UniProtKB
  • magnesium ion binding Source: InterPro
  • phosphopyruvate hydratase activity Source: Reactome
  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  • canonical glycolysis Source: Reactome
  • gluconeogenesis Source: Reactome
  • negative regulation of cell growth Source: UniProtKB
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • response to virus Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Lyase, Repressor

Keywords - Biological processi

Glycolysis, Plasminogen activation, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000074800-MONOMER.
ZFISH:ENSG00000074800-MONOMER.
BRENDAi4.2.1.11. 2681.
ReactomeiR-HSA-70171. Glycolysis.
R-HSA-70263. Gluconeogenesis.
SABIO-RKP06733.
SIGNORiP06733.
UniPathwayiUPA00109; UER00187.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-enolase (EC:4.2.1.11)
Alternative name(s):
2-phospho-D-glycerate hydro-lyase
C-myc promoter-binding protein
Enolase 1
MBP-1
MPB-1
Non-neural enolase
Short name:
NNE
Phosphopyruvate hydratase
Plasminogen-binding protein
Gene namesi
Name:ENO1
Synonyms:ENO1L1, MBPB1, MPB1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:3350. ENO1.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Cell membrane 1 Publication
  • CytoplasmmyofibrilsarcomereM line 1 Publication

  • Note: Can translocate to the plasma membrane in either the homodimeric (alpha/alpha) or heterodimeric (alpha/gamma) form. ENO1 is localized to the M line.

GO - Cellular componenti

  • cell-cell adherens junction Source: BHF-UCL
  • cytoplasm Source: LIFEdb
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • extracellular space Source: UniProtKB
  • M band Source: UniProtKB-SubCell
  • membrane Source: UniProtKB
  • nucleus Source: UniProtKB
  • phosphopyruvate hydratase complex Source: InterPro
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi94M → I: MBP1 protein production. No MBP1 protein production; when associated with I-97. 1 Publication1
Mutagenesisi97M → I: MBP1 protein production. No MBP1 protein production; when associated with I-94. 1 Publication1
Mutagenesisi384L → A: Loss of transcriptional repression and cell growth inhibition; when associated with A-388. 1 Publication1
Mutagenesisi388L → A: Loss of transcriptional repression and cell growth inhibition; when associated with A-384. 1 Publication1

Organism-specific databases

DisGeNETi2023.
OpenTargetsiENSG00000074800.
PharmGKBiPA27786.

Chemistry databases

ChEMBLiCHEMBL3298.

Polymorphism and mutation databases

BioMutaiENO1.
DMDMi119339.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00001340972 – 434Alpha-enolaseAdd BLAST433

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1 Publication1
Modified residuei5N6-acetyllysineCombined sources1
Modified residuei27PhosphoserineCombined sources1
Modified residuei44PhosphotyrosineCombined sources1
Modified residuei60N6-acetyllysine; alternateBy similarity1
Modified residuei60N6-succinyllysine; alternateBy similarity1
Modified residuei64N6-acetyllysineCombined sources1
Modified residuei71N6-acetyllysineCombined sources1
Modified residuei89N6-acetyllysine; alternateCombined sources1
Modified residuei89N6-succinyllysine; alternateBy similarity1
Modified residuei92N6-acetyllysineBy similarity1
Modified residuei126N6-acetyllysineCombined sources1
Modified residuei193N6-acetyllysineCombined sources1
Modified residuei199N6-acetyllysineCombined sources1
Modified residuei202N6-acetyllysineBy similarity1
Modified residuei228N6-acetyllysine; alternateCombined sources1
Modified residuei228N6-succinyllysine; alternateBy similarity1
Modified residuei233N6-acetyllysine; alternateCombined sources1
Modified residuei233N6-malonyllysine; alternate1 Publication1
Modified residuei254PhosphoserineCombined sources1
Modified residuei256N6-acetyllysineCombined sources1
Modified residuei263PhosphoserineCombined sources1
Modified residuei272PhosphoserineCombined sources1
Modified residuei281N6-acetyllysineCombined sources1
Modified residuei285N6-acetyllysineCombined sources1
Modified residuei287PhosphotyrosineCombined sources1
Modified residuei291PhosphoserineCombined sources1
Modified residuei335N6-acetyllysineBy similarity1
Modified residuei343N6-acetyllysineBy similarity1
Modified residuei406N6-acetyllysineBy similarity1
Modified residuei420N6-acetyllysine; alternateCombined sources1
Modified residuei420N6-malonyllysine; alternate1 Publication1
Modified residuei420N6-succinyllysine; alternateBy similarity1

Post-translational modificationi

ISGylated.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP06733.
MaxQBiP06733.
PaxDbiP06733.
PeptideAtlasiP06733.
PRIDEiP06733.
TopDownProteomicsiP06733-1. [P06733-1]
P06733-2. [P06733-2]

2D gel databases

DOSAC-COBS-2DPAGEP06733.
OGPiP06733.
REPRODUCTION-2DPAGEIPI00465248.
P06733.
SWISS-2DPAGEP06733.
UCD-2DPAGEP06733.

PTM databases

iPTMnetiP06733.
PhosphoSitePlusiP06733.
SwissPalmiP06733.

Miscellaneous databases

PMAP-CutDBP06733.

Expressioni

Tissue specificityi

The alpha/alpha homodimer is expressed in embryo and in most adult tissues. The alpha/beta heterodimer and the beta/beta homodimer are found in striated muscle, and the alpha/gamma heterodimer and the gamma/gamma homodimer in neurons.

Developmental stagei

During ontogenesis, there is a transition from the alpha/alpha homodimer to the alpha/beta heterodimer in striated muscle cells, and to the alpha/gamma heterodimer in nerve cells.

Inductioni

Induced in diffuse large cell lymphoma (DLCL) after treatment with the natural biological agent, Bryo1. Up-regulated in response to enterovirus 71 (EV71) infection (at protein level).2 Publications

Gene expression databases

BgeeiENSG00000074800.
ExpressionAtlasiP06733. baseline and differential.
GenevisibleiP06733. HS.

Organism-specific databases

HPAiCAB018614.
CAB069394.

Interactioni

Subunit structurei

Mammalian enolase is composed of 3 isozyme subunits, alpha, beta and gamma, which can form homodimers or heterodimers which are cell-type and development-specific (PubMed:18560153). ENO1 interacts with PLG in the neuronal plasma membrane and promotes its activation. The C-terminal lysine is required for this binding (PubMed:9308760). Isoform MBP-1 interacts with TRAPPC2B (PubMed:11134351). Interacts with ENO4 and PGAM2 (By similarity).By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ACHEP223032EBI-353877,EBI-1637793
Akt2Q608232EBI-353877,EBI-400263From a different organism.
PCNAP120043EBI-353877,EBI-358311
TTNQ8WZ423EBI-353877,EBI-681210
YWHAZP631042EBI-353877,EBI-347088

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • GTPase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi108338. 284 interactors.
IntActiP06733. 83 interactors.
MINTiMINT-155303.
STRINGi9606.ENSP00000234590.

Structurei

Secondary structure

1434
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 12Combined sources8
Beta strandi18 – 26Combined sources9
Beta strandi29 – 34Combined sources6
Helixi57 – 59Combined sources3
Helixi63 – 71Combined sources9
Helixi73 – 79Combined sources7
Helixi87 – 98Combined sources12
Turni104 – 106Combined sources3
Helixi108 – 125Combined sources18
Helixi130 – 138Combined sources9
Beta strandi147 – 154Combined sources8
Helixi156 – 158Combined sources3
Beta strandi159 – 162Combined sources4
Beta strandi167 – 171Combined sources5
Helixi178 – 200Combined sources23
Helixi202 – 204Combined sources3
Helixi220 – 233Combined sources14
Turni237 – 239Combined sources3
Beta strandi241 – 245Combined sources5
Helixi248 – 250Combined sources3
Turni259 – 262Combined sources4
Helixi267 – 269Combined sources3
Helixi273 – 286Combined sources14
Beta strandi289 – 293Combined sources5
Helixi301 – 311Combined sources11
Beta strandi313 – 318Combined sources6
Turni319 – 323Combined sources5
Helixi325 – 334Combined sources10
Beta strandi338 – 342Combined sources5
Helixi344 – 347Combined sources4
Helixi350 – 362Combined sources13
Beta strandi366 – 370Combined sources5
Helixi380 – 387Combined sources8
Beta strandi391 – 394Combined sources4
Helixi401 – 417Combined sources17
Helixi418 – 420Combined sources3
Helixi425 – 427Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2PSNX-ray2.20A/B/C/D1-434[»]
3B97X-ray2.20A/B/C/D2-434[»]
ProteinModelPortaliP06733.
SMRiP06733.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06733.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni31 – 38Epitope recognized by CAR and healthy patient antibodies8
Regioni56 – 63Epitope recognized by CAR antibodies8
Regioni97 – 237Required for repression of c-myc promoter activityAdd BLAST141
Regioni370 – 373Substrate bindingBy similarity4
Regioni405 – 434Required for interaction with PLGBy similarityAdd BLAST30

Sequence similaritiesi

Belongs to the enolase family.Curated

Phylogenomic databases

eggNOGiKOG2670. Eukaryota.
COG0148. LUCA.
GeneTreeiENSGT00840000129817.
HOVERGENiHBG000067.
InParanoidiP06733.
KOiK01689.
OMAiNFRNPRI.
OrthoDBiEOG091G07NH.
PhylomeDBiP06733.
TreeFamiTF300391.

Family and domain databases

CDDicd03313. enolase. 1 hit.
Gene3Di3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
HAMAPiMF_00318. Enolase. 1 hit.
InterProiIPR000941. Enolase.
IPR020810. Enolase_C.
IPR029065. Enolase_C-like.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
IPR029017. Enolase_N-like.
[Graphical view]
PANTHERiPTHR11902. PTHR11902. 1 hit.
PfamiPF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF001400. Enolase. 1 hit.
PRINTSiPR00148. ENOLASE.
SMARTiSM01192. Enolase_C. 1 hit.
SM01193. Enolase_N. 1 hit.
[Graphical view]
SUPFAMiSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
TIGRFAMsiTIGR01060. eno. 1 hit.
PROSITEiPS00164. ENOLASE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative initiation. AlignAdd to basket

Isoform alpha-enolase (identifier: P06733-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSILKIHARE IFDSRGNPTV EVDLFTSKGL FRAAVPSGAS TGIYEALELR
60 70 80 90 100
DNDKTRYMGK GVSKAVEHIN KTIAPALVSK KLNVTEQEKI DKLMIEMDGT
110 120 130 140 150
ENKSKFGANA ILGVSLAVCK AGAVEKGVPL YRHIADLAGN SEVILPVPAF
160 170 180 190 200
NVINGGSHAG NKLAMQEFMI LPVGAANFRE AMRIGAEVYH NLKNVIKEKY
210 220 230 240 250
GKDATNVGDE GGFAPNILEN KEGLELLKTA IGKAGYTDKV VIGMDVAASE
260 270 280 290 300
FFRSGKYDLD FKSPDDPSRY ISPDQLADLY KSFIKDYPVV SIEDPFDQDD
310 320 330 340 350
WGAWQKFTAS AGIQVVGDDL TVTNPKRIAK AVNEKSCNCL LLKVNQIGSV
360 370 380 390 400
TESLQACKLA QANGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR
410 420 430
SERLAKYNQL LRIEEELGSK AKFAGRNFRN PLAK
Length:434
Mass (Da):47,169
Last modified:January 23, 2007 - v2
Checksum:iA0ED663FCC15ADA5
GO
Isoform MBP-1 (identifier: P06733-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-93: Missing.

Note: It is uncertain whether the alternative initiation site is at Met-94 or at Met-97.
Show »
Length:341
Mass (Da):36,928
Checksum:i96D437CF21772928
GO

Sequence cautioni

The sequence AAA35698 differs from that shown. Sequencing errors.Curated
The sequence AAA35698 differs from that shown. Reason: Frameshift at several positions.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti55T → A in CAD97642 (PubMed:17974005).Curated1
Sequence conflicti78V → A in BAD96237 (Ref. 7) Curated1
Sequence conflicti187E → G in CAD97642 (PubMed:17974005).Curated1
Sequence conflicti199K → R in BAD96912 (Ref. 7) Curated1
Sequence conflicti252F → S in CAA59331 (PubMed:8824716).Curated1
Sequence conflicti310S → I in CAD97642 (PubMed:17974005).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_025172177N → K.1 PublicationCorresponds to variant rs11544513dbSNPEnsembl.1
Natural variantiVAR_048936325P → Q.Corresponds to variant rs11544514dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0187251 – 93Missing in isoform MBP-1. 1 PublicationAdd BLAST93

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14328 mRNA. Translation: AAA52387.1.
X16288, X16289, X16290 Genomic DNA. Translation: CAA34360.1.
M55914 mRNA. Translation: AAA35698.1. Frameshift.
X84907 mRNA. Translation: CAA59331.1.
BT007163 mRNA. Translation: AAP35827.1.
AK315417 mRNA. Translation: BAG37806.1.
AL833741 mRNA. Translation: CAH56247.1.
BX537400 mRNA. Translation: CAD97642.1.
AK222517 mRNA. Translation: BAD96237.1.
AK223192 mRNA. Translation: BAD96912.1.
DQ056744 Genomic DNA. Translation: AAY43128.1.
AL139415 Genomic DNA. Translation: CAC42425.1.
CH471130 Genomic DNA. Translation: EAW71604.1.
BC001810 mRNA. Translation: AAH01810.1.
BC004325 mRNA. Translation: AAH04325.1.
BC004458 mRNA. Translation: AAH04458.1.
BC009218 mRNA. Translation: AAH09218.2.
BC009912 mRNA. Translation: AAH09912.1.
BC011130 mRNA. Translation: AAH11130.1.
BC015641 mRNA. Translation: AAH15641.1.
BC021166 mRNA. Translation: AAH21166.2.
BC022545 mRNA. Translation: AAH22545.1.
BC027725 mRNA. Translation: AAH27725.1.
BC050642 mRNA. Translation: AAH50642.1.
U88968 mRNA. Translation: AAC39935.1.
AF035286 mRNA. Translation: AAB88178.1.
CCDSiCCDS97.1. [P06733-1]
PIRiA39579.
S11696. A29170.
RefSeqiNP_001188412.1. NM_001201483.1. [P06733-2]
NP_001419.1. NM_001428.3. [P06733-1]
UniGeneiHs.517145.

Genome annotation databases

EnsembliENST00000234590; ENSP00000234590; ENSG00000074800. [P06733-1]
GeneIDi2023.
KEGGihsa:2023.
UCSCiuc001apj.3. human. [P06733-1]

Keywords - Coding sequence diversityi

Alternative initiation, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14328 mRNA. Translation: AAA52387.1.
X16288, X16289, X16290 Genomic DNA. Translation: CAA34360.1.
M55914 mRNA. Translation: AAA35698.1. Frameshift.
X84907 mRNA. Translation: CAA59331.1.
BT007163 mRNA. Translation: AAP35827.1.
AK315417 mRNA. Translation: BAG37806.1.
AL833741 mRNA. Translation: CAH56247.1.
BX537400 mRNA. Translation: CAD97642.1.
AK222517 mRNA. Translation: BAD96237.1.
AK223192 mRNA. Translation: BAD96912.1.
DQ056744 Genomic DNA. Translation: AAY43128.1.
AL139415 Genomic DNA. Translation: CAC42425.1.
CH471130 Genomic DNA. Translation: EAW71604.1.
BC001810 mRNA. Translation: AAH01810.1.
BC004325 mRNA. Translation: AAH04325.1.
BC004458 mRNA. Translation: AAH04458.1.
BC009218 mRNA. Translation: AAH09218.2.
BC009912 mRNA. Translation: AAH09912.1.
BC011130 mRNA. Translation: AAH11130.1.
BC015641 mRNA. Translation: AAH15641.1.
BC021166 mRNA. Translation: AAH21166.2.
BC022545 mRNA. Translation: AAH22545.1.
BC027725 mRNA. Translation: AAH27725.1.
BC050642 mRNA. Translation: AAH50642.1.
U88968 mRNA. Translation: AAC39935.1.
AF035286 mRNA. Translation: AAB88178.1.
CCDSiCCDS97.1. [P06733-1]
PIRiA39579.
S11696. A29170.
RefSeqiNP_001188412.1. NM_001201483.1. [P06733-2]
NP_001419.1. NM_001428.3. [P06733-1]
UniGeneiHs.517145.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2PSNX-ray2.20A/B/C/D1-434[»]
3B97X-ray2.20A/B/C/D2-434[»]
ProteinModelPortaliP06733.
SMRiP06733.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108338. 284 interactors.
IntActiP06733. 83 interactors.
MINTiMINT-155303.
STRINGi9606.ENSP00000234590.

Chemistry databases

ChEMBLiCHEMBL3298.

PTM databases

iPTMnetiP06733.
PhosphoSitePlusiP06733.
SwissPalmiP06733.

Polymorphism and mutation databases

BioMutaiENO1.
DMDMi119339.

2D gel databases

DOSAC-COBS-2DPAGEP06733.
OGPiP06733.
REPRODUCTION-2DPAGEIPI00465248.
P06733.
SWISS-2DPAGEP06733.
UCD-2DPAGEP06733.

Proteomic databases

EPDiP06733.
MaxQBiP06733.
PaxDbiP06733.
PeptideAtlasiP06733.
PRIDEiP06733.
TopDownProteomicsiP06733-1. [P06733-1]
P06733-2. [P06733-2]

Protocols and materials databases

DNASUi2023.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000234590; ENSP00000234590; ENSG00000074800. [P06733-1]
GeneIDi2023.
KEGGihsa:2023.
UCSCiuc001apj.3. human. [P06733-1]

Organism-specific databases

CTDi2023.
DisGeNETi2023.
GeneCardsiENO1.
HGNCiHGNC:3350. ENO1.
HPAiCAB018614.
CAB069394.
MIMi172430. gene.
neXtProtiNX_P06733.
OpenTargetsiENSG00000074800.
PharmGKBiPA27786.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2670. Eukaryota.
COG0148. LUCA.
GeneTreeiENSGT00840000129817.
HOVERGENiHBG000067.
InParanoidiP06733.
KOiK01689.
OMAiNFRNPRI.
OrthoDBiEOG091G07NH.
PhylomeDBiP06733.
TreeFamiTF300391.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00187.
BioCyciMetaCyc:ENSG00000074800-MONOMER.
ZFISH:ENSG00000074800-MONOMER.
BRENDAi4.2.1.11. 2681.
ReactomeiR-HSA-70171. Glycolysis.
R-HSA-70263. Gluconeogenesis.
SABIO-RKP06733.
SIGNORiP06733.

Miscellaneous databases

ChiTaRSiENO1. human.
EvolutionaryTraceiP06733.
GeneWikiiAlpha-enolase.
GenomeRNAii2023.
PMAP-CutDBP06733.
PROiP06733.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000074800.
ExpressionAtlasiP06733. baseline and differential.
GenevisibleiP06733. HS.

Family and domain databases

CDDicd03313. enolase. 1 hit.
Gene3Di3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
HAMAPiMF_00318. Enolase. 1 hit.
InterProiIPR000941. Enolase.
IPR020810. Enolase_C.
IPR029065. Enolase_C-like.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
IPR029017. Enolase_N-like.
[Graphical view]
PANTHERiPTHR11902. PTHR11902. 1 hit.
PfamiPF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF001400. Enolase. 1 hit.
PRINTSiPR00148. ENOLASE.
SMARTiSM01192. Enolase_C. 1 hit.
SM01193. Enolase_N. 1 hit.
[Graphical view]
SUPFAMiSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
TIGRFAMsiTIGR01060. eno. 1 hit.
PROSITEiPS00164. ENOLASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiENOA_HUMAN
AccessioniPrimary (citable) accession number: P06733
Secondary accession number(s): B2RD59
, P22712, Q16704, Q4TUS4, Q53FT9, Q53HR3, Q658M5, Q6GMP2, Q71V37, Q7Z3V6, Q8WU71, Q96GV1, Q9BT62, Q9UCH6, Q9UM55
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 208 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

Used as a diagnostic marker for many tumors and, in the heterodimeric form, alpha/gamma, as a marker for hypoxic brain injury after cardiac arrest. Also marker for endometriosis. Antibodies against alpha-enolase are present in sera from patients with cancer-associated retinopathy syndrome (CAR), a progressive blinding disease which occurs in the presence of systemic tumor growth, primarily small-cell carcinoma of the lung and other malignancies. Is identified as an autoantigen in Hashimoto encephalopathy (HE) a rare autoimmune disease associated with Hashimoto thyroiditis (HT). HT is a disorder in which destructive processes overcome the potential capacity of thyroid replacement leading to hypothyroidism.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.