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Protein

Gamma-enolase

Gene

ENO2

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

Functioni

Has neurotrophic and neuroprotective properties on a broad spectrum of central nervous system (CNS) neurons. Binds, in a calcium-dependent manner, to cultured neocortical neurons and promotes cell survival (By similarity).By similarity

Catalytic activityi

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

Cofactori

Mg2+Note: Mg2+ is required for catalysis and for stabilizing the dimer.

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
Binding sitei158SubstrateBy similarity1
Binding sitei167SubstrateBy similarity1
Active sitei210Proton donorBy similarity1
Metal bindingi245Magnesium1
Metal bindingi293Magnesium1
Binding sitei293SubstrateBy similarity1
Metal bindingi318Magnesium1
Binding sitei318SubstrateBy similarity1
Active sitei343Proton acceptorBy similarity1
Binding sitei394SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS10646-MONOMER.
ZFISH:HS10646-MONOMER.
BRENDAi4.2.1.11. 2681.
ReactomeiR-HSA-70171. Glycolysis.
R-HSA-70263. Gluconeogenesis.
SABIO-RKP09104.
UniPathwayiUPA00109; UER00187.

Names & Taxonomyi

Protein namesi
Recommended name:
Gamma-enolase (EC:4.2.1.11)
Alternative name(s):
2-phospho-D-glycerate hydro-lyase
Enolase 2
Neural enolase
Neuron-specific enolase
Short name:
NSE
Gene namesi
Name:ENO2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:3353. ENO2.

Subcellular locationi

  • Cytoplasm By similarity
  • Cell membrane By similarity

  • Note: Can translocate to the plasma membrane in either the homodimeric (alpha/alpha) or heterodimeric (alpha/gamma) form.By similarity

GO - Cellular componenti

  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • extracellular space Source: UniProtKB
  • myelin sheath Source: Ensembl
  • perikaryon Source: Ensembl
  • phosphopyruvate hydratase complex Source: InterPro
  • photoreceptor inner segment Source: Ensembl
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Organism-specific databases

DisGeNETi2026.
OpenTargetsiENSG00000111674.
PharmGKBiPA27788.

Polymorphism and mutation databases

BioMutaiENO2.
DMDMi20981682.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001341122 – 434Gamma-enolaseAdd BLAST433

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei26PhosphothreonineCombined sources1
Modified residuei44PhosphotyrosineCombined sources1
Modified residuei72PhosphothreonineBy similarity1
Modified residuei83PhosphoserineBy similarity1
Modified residuei157PhosphoserineBy similarity1
Modified residuei197N6-acetyllysineBy similarity1
Modified residuei199N6-acetyllysineBy similarity1
Modified residuei205PhosphothreonineBy similarity1
Modified residuei236PhosphotyrosineBy similarity1
Modified residuei263PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP09104.
PaxDbiP09104.
PeptideAtlasiP09104.
PRIDEiP09104.

2D gel databases

OGPiP09104.
UCD-2DPAGEP09104.

PTM databases

iPTMnetiP09104.
PhosphoSitePlusiP09104.
SwissPalmiP09104.

Miscellaneous databases

PMAP-CutDBP09104.

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

Levels of ENO2 increase dramatically in cardiovascular accidents, cerebral trauma, brain tumors and Creutzfeldt-Jakob disease.

Gene expression databases

BgeeiENSG00000111674.
CleanExiHS_ENO2.
ExpressionAtlasiP09104. baseline and differential.
GenevisibleiP09104. HS.

Organism-specific databases

HPAiCAB000063.
CAB073539.

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.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
TINF2Q9BSI42EBI-713154,EBI-717399

Protein-protein interaction databases

BioGridi108340. 85 interactors.
IntActiP09104. 29 interactors.
MINTiMINT-1367862.
STRINGi9606.ENSP00000229277.

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 – 80Combined sources8
Helixi87 – 98Combined sources12
Turni104 – 106Combined sources3
Helixi108 – 126Combined sources19
Helixi130 – 138Combined sources9
Beta strandi147 – 154Combined sources8
Helixi156 – 158Combined sources3
Beta strandi159 – 162Combined sources4
Beta strandi167 – 171Combined sources5
Helixi178 – 200Combined sources23
Helixi202 – 205Combined sources4
Beta strandi211 – 213Combined sources3
Helixi220 – 234Combined sources15
Turni237 – 239Combined sources3
Beta strandi241 – 245Combined sources5
Helixi248 – 251Combined sources4
Beta strandi254 – 257Combined sources4
Turni259 – 262Combined sources4
Helixi267 – 269Combined sources3
Helixi273 – 286Combined sources14
Beta strandi289 – 293Combined sources5
Helixi301 – 309Combined sources9
Beta strandi312 – 318Combined sources7
Turni319 – 323Combined sources5
Helixi325 – 333Combined sources9
Beta strandi338 – 342Combined sources5
Helixi344 – 347Combined sources4
Helixi350 – 362Combined sources13
Beta strandi366 – 370Combined sources5
Helixi380 – 388Combined sources9
Beta strandi391 – 394Combined sources4
Helixi401 – 417Combined sources17
Helixi418 – 420Combined sources3
Helixi425 – 427Combined sources3
Helixi431 – 433Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TE6X-ray1.80A/B2-434[»]
2AKMX-ray1.92A/B2-434[»]
2AKZX-ray1.36A/B2-434[»]
3UCCX-ray1.50A/B2-434[»]
3UCDX-ray1.41A/B2-434[»]
3UJEX-ray1.55A/B2-434[»]
3UJFX-ray2.10A/B2-434[»]
3UJRX-ray1.40A/B2-434[»]
3UJSX-ray1.65A/B2-434[»]
4ZA0X-ray2.31A/B1-434[»]
4ZCWX-ray1.99A/B1-434[»]
ProteinModelPortaliP09104.
SMRiP09104.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09104.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni370 – 373Substrate bindingBy similarity4

Sequence similaritiesi

Belongs to the enolase family.Curated

Phylogenomic databases

eggNOGiKOG2670. Eukaryota.
COG0148. LUCA.
GeneTreeiENSGT00840000129817.
HOGENOMiHOG000072174.
HOVERGENiHBG000067.
InParanoidiP09104.
KOiK01689.
OMAiDQTLICG.
OrthoDBiEOG091G07NH.
PhylomeDBiP09104.
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 splicing. AlignAdd to basket

Isoform 1 (identifier: P09104-1) [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
MSIEKIWARE ILDSRGNPTV EVDLYTAKGL FRAAVPSGAS TGIYEALELR
60 70 80 90 100
DGDKQRYLGK GVLKAVDHIN STIAPALISS GLSVVEQEKL DNLMLELDGT
110 120 130 140 150
ENKSKFGANA ILGVSLAVCK AGAAERELPL YRHIAQLAGN SDLILPVPAF
160 170 180 190 200
NVINGGSHAG NKLAMQEFMI LPVGAESFRD AMRLGAEVYH TLKGVIKDKY
210 220 230 240 250
GKDATNVGDE GGFAPNILEN SEALELVKEA IDKAGYTEKI VIGMDVAASE
260 270 280 290 300
FYRDGKYDLD FKSPTDPSRY ITGDQLGALY QDFVRDYPVV SIEDPFDQDD
310 320 330 340 350
WAAWSKFTAN VGIQIVGDDL TVTNPKRIER AVEEKACNCL LLKVNQIGSV
360 370 380 390 400
TEAIQACKLA QENGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR
410 420 430
SERLAKYNQL MRIEEELGDE ARFAGHNFRN PSVL
Length:434
Mass (Da):47,269
Last modified:January 23, 2007 - v3
Checksum:i6163DE81F5C67744
GO
Isoform 2 (identifier: P09104-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     61-104: GVLKAVDHINSTIAPALISSGLSVVEQEKLDNLMLELDGTENKS → A

Note: No experimental confirmation available.
Show »
Length:391
Mass (Da):42,707
Checksum:iB9133CC7C5A3524C
GO

Sequence cautioni

The sequence AAA52388 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti4E → Q in CAA31512 (PubMed:3208766).Curated1
Sequence conflicti4E → Q in CAA32505 (PubMed:3208766).Curated1
Sequence conflicti27 – 28AK → GC in AAA52388 (PubMed:3385803).Curated2
Sequence conflicti127E → N in AAA52388 (PubMed:3385803).Curated1
Sequence conflicti240I → M in CAA31512 (PubMed:3208766).Curated1
Sequence conflicti240I → M in CAA32505 (PubMed:3208766).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_002354264P → A.1
Natural variantiVAR_002355395T → A.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_05548261 – 104GVLKA…TENKS → A in isoform 2. 1 PublicationAdd BLAST44

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13120 mRNA. Translation: CAA31512.1.
X14327 mRNA. Translation: CAA32505.1.
M36768 mRNA. Translation: AAA52388.1. Different initiation.
M22349 mRNA. Translation: AAB59554.1.
X51956 Genomic DNA. Translation: CAA36215.1.
AK295220 mRNA. Translation: BAH12015.1.
BT007383 mRNA. Translation: AAP36047.1.
U47924 Genomic DNA. Translation: AAB51320.1.
BC002745 mRNA. Translation: AAH02745.1.
CCDSiCCDS8570.1. [P09104-1]
PIRiJU0060. NOHUG.
RefSeqiNP_001966.1. NM_001975.2. [P09104-1]
UniGeneiHs.511915.

Genome annotation databases

EnsembliENST00000229277; ENSP00000229277; ENSG00000111674. [P09104-1]
ENST00000535366; ENSP00000437402; ENSG00000111674. [P09104-1]
ENST00000538763; ENSP00000441490; ENSG00000111674. [P09104-2]
ENST00000541477; ENSP00000438873; ENSG00000111674. [P09104-1]
GeneIDi2026.
KEGGihsa:2026.
UCSCiuc058knm.1. human. [P09104-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13120 mRNA. Translation: CAA31512.1.
X14327 mRNA. Translation: CAA32505.1.
M36768 mRNA. Translation: AAA52388.1. Different initiation.
M22349 mRNA. Translation: AAB59554.1.
X51956 Genomic DNA. Translation: CAA36215.1.
AK295220 mRNA. Translation: BAH12015.1.
BT007383 mRNA. Translation: AAP36047.1.
U47924 Genomic DNA. Translation: AAB51320.1.
BC002745 mRNA. Translation: AAH02745.1.
CCDSiCCDS8570.1. [P09104-1]
PIRiJU0060. NOHUG.
RefSeqiNP_001966.1. NM_001975.2. [P09104-1]
UniGeneiHs.511915.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TE6X-ray1.80A/B2-434[»]
2AKMX-ray1.92A/B2-434[»]
2AKZX-ray1.36A/B2-434[»]
3UCCX-ray1.50A/B2-434[»]
3UCDX-ray1.41A/B2-434[»]
3UJEX-ray1.55A/B2-434[»]
3UJFX-ray2.10A/B2-434[»]
3UJRX-ray1.40A/B2-434[»]
3UJSX-ray1.65A/B2-434[»]
4ZA0X-ray2.31A/B1-434[»]
4ZCWX-ray1.99A/B1-434[»]
ProteinModelPortaliP09104.
SMRiP09104.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108340. 85 interactors.
IntActiP09104. 29 interactors.
MINTiMINT-1367862.
STRINGi9606.ENSP00000229277.

PTM databases

iPTMnetiP09104.
PhosphoSitePlusiP09104.
SwissPalmiP09104.

Polymorphism and mutation databases

BioMutaiENO2.
DMDMi20981682.

2D gel databases

OGPiP09104.
UCD-2DPAGEP09104.

Proteomic databases

EPDiP09104.
PaxDbiP09104.
PeptideAtlasiP09104.
PRIDEiP09104.

Protocols and materials databases

DNASUi2026.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000229277; ENSP00000229277; ENSG00000111674. [P09104-1]
ENST00000535366; ENSP00000437402; ENSG00000111674. [P09104-1]
ENST00000538763; ENSP00000441490; ENSG00000111674. [P09104-2]
ENST00000541477; ENSP00000438873; ENSG00000111674. [P09104-1]
GeneIDi2026.
KEGGihsa:2026.
UCSCiuc058knm.1. human. [P09104-1]

Organism-specific databases

CTDi2026.
DisGeNETi2026.
GeneCardsiENO2.
HGNCiHGNC:3353. ENO2.
HPAiCAB000063.
CAB073539.
MIMi131360. gene.
neXtProtiNX_P09104.
OpenTargetsiENSG00000111674.
PharmGKBiPA27788.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2670. Eukaryota.
COG0148. LUCA.
GeneTreeiENSGT00840000129817.
HOGENOMiHOG000072174.
HOVERGENiHBG000067.
InParanoidiP09104.
KOiK01689.
OMAiDQTLICG.
OrthoDBiEOG091G07NH.
PhylomeDBiP09104.
TreeFamiTF300391.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00187.
BioCyciMetaCyc:HS10646-MONOMER.
ZFISH:HS10646-MONOMER.
BRENDAi4.2.1.11. 2681.
ReactomeiR-HSA-70171. Glycolysis.
R-HSA-70263. Gluconeogenesis.
SABIO-RKP09104.

Miscellaneous databases

ChiTaRSiENO2. human.
EvolutionaryTraceiP09104.
GeneWikiiEnolase_2.
GenomeRNAii2026.
PMAP-CutDBP09104.
PROiP09104.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000111674.
CleanExiHS_ENO2.
ExpressionAtlasiP09104. baseline and differential.
GenevisibleiP09104. 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 nameiENOG_HUMAN
AccessioniPrimary (citable) accession number: P09104
Secondary accession number(s): B7Z2X9, Q96J33
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 203 of the entry and version 3 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

Keywords - Technical termi

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

Documents

  1. Human chromosome 12
    Human chromosome 12: 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.