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P09104 (ENOG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 173. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:ENO2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length434 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. HAMAP-Rule MF_00318

Catalytic activity

2-phospho-D-glycerate = phosphoenolpyruvate + H2O. HAMAP-Rule MF_00318

Cofactor

Magnesium. Required for catalysis and for stabilizing the dimer.

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. HAMAP-Rule MF_00318

Subunit structure

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.

Subcellular location

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. HAMAP-Rule MF_00318

Tissue specificity

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 stage

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. HAMAP-Rule MF_00318

Induction

Levels of ENO2 increase dramatically in cardiovascular accidents, cerebral trauma, brain tumors and Creutzfeldt-Jakob disease. HAMAP-Rule MF_00318

Sequence similarities

Belongs to the enolase family.

Sequence caution

The sequence AAA52388.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 434434Gamma-enolase HAMAP-Rule MF_00318
PRO_0000134112

Regions

Region370 – 3734Substrate binding By similarity

Sites

Active site2101Proton donor By similarity
Active site3431Proton acceptor By similarity
Metal binding2451Magnesium
Metal binding2931Magnesium
Metal binding3181Magnesium
Binding site1581Substrate By similarity
Binding site1671Substrate By similarity
Binding site2931Substrate By similarity
Binding site3181Substrate By similarity
Binding site3941Substrate By similarity

Amino acid modifications

Modified residue261Phosphothreonine Ref.11
Modified residue441Phosphotyrosine Ref.10
Modified residue1971N6-acetyllysine By similarity
Modified residue1991N6-acetyllysine By similarity

Natural variations

Natural variant2641P → A.
VAR_002354
Natural variant3951T → A.
VAR_002355

Experimental info

Sequence conflict41E → Q in CAA31512. Ref.1
Sequence conflict41E → Q in CAA32505. Ref.1
Sequence conflict27 – 282AK → GC in AAA52388. Ref.2
Sequence conflict1271E → N in AAA52388. Ref.2
Sequence conflict2401I → M in CAA31512. Ref.1
Sequence conflict2401I → M in CAA32505. Ref.1

Secondary structure

.............................................................................. 434
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P09104 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 6163DE81F5C67744

FASTA43447,269
        10         20         30         40         50         60 
MSIEKIWARE ILDSRGNPTV EVDLYTAKGL FRAAVPSGAS TGIYEALELR DGDKQRYLGK 

        70         80         90        100        110        120 
GVLKAVDHIN STIAPALISS GLSVVEQEKL DNLMLELDGT ENKSKFGANA ILGVSLAVCK 

       130        140        150        160        170        180 
AGAAERELPL YRHIAQLAGN SDLILPVPAF NVINGGSHAG NKLAMQEFMI LPVGAESFRD 

       190        200        210        220        230        240 
AMRLGAEVYH TLKGVIKDKY GKDATNVGDE GGFAPNILEN SEALELVKEA IDKAGYTEKI 

       250        260        270        280        290        300 
VIGMDVAASE FYRDGKYDLD FKSPTDPSRY ITGDQLGALY QDFVRDYPVV SIEDPFDQDD 

       310        320        330        340        350        360 
WAAWSKFTAN VGIQIVGDDL TVTNPKRIER AVEEKACNCL LLKVNQIGSV TEAIQACKLA 

       370        380        390        400        410        420 
QENGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQL MRIEEELGDE 

       430 
ARFAGHNFRN PSVL 

« Hide

References

« Hide 'large scale' references
[1]"Complete amino acid sequence of the neurone-specific gamma isozyme of enolase (NSE) from human brain and comparison with the non-neuronal alpha form (NNE)."
McAleese S.M., Dunbar B., Fothergill J., Hinks L., Day I.N.M.
Eur. J. Biochem. 178:413-417(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Retina.
[2]"Human gamma enolase: isolation of a cDNA clone and expression in normal and tumor tissues of human origin."
van Obberghen E., Kamholz J., Bishop J.G. III, Zomzely-Neurath C., Lazzarini R.A.
J. Neurosci. Res. 19:450-456(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[3]"Cloning, expression and sequence homologies of cDNA for human gamma enolase."
Oliva D., Barba G., Barbieri G., Giallongo A., Feo S.
Gene 79:355-360(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"Complete structure of the human gene encoding neuron-specific enolase."
Oliva D., Cali L., Feo S., Giallongo A.
Genomics 10:157-165(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Hematopoietic.
[5]"Large-scale sequencing in human chromosome 12p13: experimental and computational gene structure determination."
Ansari-Lari M.A., Shen Y., Muzny D.M., Lee W., Gibbs R.A.
Genome Res. 7:268-280(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Brain.
[6]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Placenta.
[8]Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 16-28; 33-50; 90-103; 163-179; 184-193; 240-262; 270-285; 336-372 AND 413-422, MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[9]"Sequence conservation in the 3'-untranslated regions of neurone-specific enolase, lymphokine and protooncogene mRNAs."
Day I.N.M., Allsopp M.T.E.P., Moore D.C.M., Thompson R.J.
FEBS Lett. 222:139-143(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 425-434.
[10]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-44, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-26, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Expression, purification and the 1.8 angstroms resolution crystal structure of human neuron specific enolase."
Chai G., Brewer J.M., Lovelace L.L., Aoki T., Minor W., Lebioda L.
J. Mol. Biol. 341:1015-1021(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
U47924 Genomic DNA. Translation: AAB51320.1.
BT007383 mRNA. Translation: AAP36047.1.
BC002745 mRNA. Translation: AAH02745.1.
PIRNOHUG. JU0060.
RefSeqNP_001966.1. NM_001975.2.
XP_005253730.1. XM_005253673.1.
XP_005253731.1. XM_005253674.1.
XP_005277806.1. XM_005277749.1.
XP_005277807.1. XM_005277750.1.
UniGeneHs.511915.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1TE6X-ray1.80A/B2-434[»]
2AKMX-ray1.92A/B2-433[»]
2AKZX-ray1.36A/B2-433[»]
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[»]
ProteinModelPortalP09104.
SMRP09104. Positions 2-434.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108340. 40 interactions.
IntActP09104. 21 interactions.
MINTMINT-1367862.
STRING9606.ENSP00000229277.

PTM databases

PhosphoSiteP09104.

Polymorphism databases

DMDM20981682.

2D gel databases

OGPP09104.
UCD-2DPAGEP09104.

Proteomic databases

PaxDbP09104.
PRIDEP09104.

Protocols and materials databases

DNASU2026.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000229277; ENSP00000229277; ENSG00000111674.
ENST00000535366; ENSP00000437402; ENSG00000111674.
ENST00000541477; ENSP00000438873; ENSG00000111674.
ENST00000594987; ENSP00000472373; ENSG00000269528.
ENST00000596089; ENSP00000469457; ENSG00000269528.
ENST00000601485; ENSP00000471490; ENSG00000269528.
GeneID2026.
KEGGhsa:2026.
UCSCuc001qru.1. human.

Organism-specific databases

CTD2026.
GeneCardsGC12P007116.
HGNCHGNC:3353. ENO2.
HPACAB000063.
MIM131360. gene.
neXtProtNX_P09104.
PharmGKBPA27788.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0148.
HOGENOMHOG000072174.
HOVERGENHBG000067.
InParanoidP09104.
KOK01689.
OMAKNEGVER.
PhylomeDBP09104.
TreeFamTF300391.

Enzyme and pathway databases

BioCycMetaCyc:HS10646-MONOMER.
ReactomeREACT_111217. Metabolism.
SABIO-RKP09104.
UniPathwayUPA00109; UER00187.

Gene expression databases

ArrayExpressP09104.
BgeeP09104.
CleanExHS_ENO2.
GenevestigatorP09104.

Family and domain databases

HAMAPMF_00318. Enolase.
InterProIPR000941. Enolase.
IPR020810. Enolase_C.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
[Graphical view]
PANTHERPTHR11902. PTHR11902. 1 hit.
PfamPF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
[Graphical view]
PIRSFPIRSF001400. Enolase. 1 hit.
PRINTSPR00148. ENOLASE.
TIGRFAMsTIGR01060. eno. 1 hit.
PROSITEPS00164. ENOLASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSENO2. human.
EvolutionaryTraceP09104.
GeneWikiEnolase_2.
GenomeRNAi2026.
NextBio8203.
PMAP-CutDBP09104.
PROP09104.
SOURCESearch...

Entry information

Entry nameENOG_HUMAN
AccessionPrimary (citable) accession number: P09104
Secondary accession number(s): Q96J33
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: March 19, 2014
This is version 173 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM