Gamma-enolase - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot P09104 (ENOG_HUMAN)

Last modified November 3, 2009. Version 129. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Gamma-enolase
    EC=4.2.1.11
Alternative name(s):
    2-phospho-D-glycerate hydro-lyase
    Neural enolase
    Neuron-specific enolase
      Short name=NSE
    Enolase 2

Gene names

Name:

ENO2

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	434 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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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.
Catalytic activity	2-phospho-D-glycerate = phosphoenolpyruvate + H₂O.
Cofactor	Magnesium. Required for catalysis and for stabilizing the dimer.
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5.
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.
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.
Induction	Levels of ENO2 increase dramatically in cardiovascular accidents, cerebral trauma, brain tumors and Creutzfeldt-Jacob disease.
Sequence similarities	Belongs to the enolase family.

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Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cell membrane Cytoplasm Membrane
Coding sequence diversity	Polymorphism
Ligand	Magnesium Metal-binding
Molecular function	Lyase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	phosphopyruvate hydratase complex Inferred from electronic annotation. Source: InterPro plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphopyruvate hydratase activity Ref.4 Traceable author statement. Source: ProtInc
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed

Chain

2 – 434

433

Gamma-enolase

PRO_0000134112

Regions

Region

370 – 373

Substrate binding By similarity

Sites

Active site

210

Proton donor By similarity

Active site

343

Proton acceptor By similarity

Metal binding

245

Magnesium

Metal binding

293

Magnesium

Metal binding

318

Magnesium

Binding site

158

Substrate By similarity

Binding site

167

Substrate By similarity

Binding site

293

Substrate By similarity

Binding site

318

Substrate By similarity

Binding site

394

Substrate By similarity

Amino acid modifications

Modified residue

Phosphotyrosine By similarity

Modified residue

Phosphotyrosine Ref.10 Ref.11 Ref.12 Ref.14

Modified residue

Phosphoserine By similarity

Natural variations

Natural variant

264

P → A

VAR_002354

Natural variant

395

T → A

VAR_002355

Experimental info

Sequence conflict

E → Q in CAA31512. Ref.1

Sequence conflict

E → Q in CAA32505. Ref.1

Sequence conflict

27 – 28

AK → GC in AAA52388. Ref.2

Sequence conflict

127

E → N in AAA52388. Ref.2

Sequence conflict

240

I → M in CAA31512. Ref.1

Sequence conflict

240

I → M in CAA32505. Ref.1

Secondary structure

434

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P09104-1 [UniParc].

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

434

47,269

        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

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References

	« Hide 'large scale' referencesShow '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: 3208766] [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: 3385803] [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: 2792767] [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: 2045099] [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: 9074930] [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: 15489334] [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: 3653393] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 425-434.
[10]	"Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules." Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., Lauffenburger D.A., White F.M. Mol. Cell. Proteomics 4:1240-1250(2005) [PubMed: 15951569] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-44, MASS SPECTROMETRY. Tissue: Epithelium.
[11]	"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: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-44, MASS SPECTROMETRY.
[12]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-44, MASS SPECTROMETRY.
[13]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[14]	"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells." Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J. J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-44, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[15]	"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: 15289101] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

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.

IPI

IPI00216171.

PIR

NOHUG. JU0060.

RefSeq

NP_001966.1.

UniGene

Hs.143766
Hs.511915

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1TE6	X-ray	1.80	A/B	2-434	[»]
2AKM	X-ray	1.92	A/B	2-433	[»]
2AKZ	X-ray	1.36	A/B	2-433	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P09104. 16 interactions.

STRING

P09104.

PTM databases

PhosphoSite

P09104.

2-D gel databases

Cornea-2DPAGE

P09104.

OGP

P09104.

Proteomic databases

PRIDE

P09104.

Genome annotation databases

Ensembl

ENST00000229277; ENSP00000229277; ENSG00000111674; Homo sapiens. [Genome view]

GeneID

2026.

KEGG

hsa:2026.

UCSC

uc001qru.1. human.

Organism-specific databases

CTD

2026.

GeneCards

GC12P006898.

H-InvDB

HIX0010392.

HGNC

HGNC:3353. ENO2.

HPA

CAB000063.

MIM

131360. gene.

Orphanet

299. Enolase deficiency.

PharmGKB

PA27788.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P09104.

HOVERGEN

P09104.

OMA

RNAKYNQ.

Enzyme and pathway databases

BRENDA

4.2.1.11. 247.

Reactome

REACT_1505. Integration of energy metabolism.
REACT_15380. Diabetes pathways.
REACT_474. Metabolism of carbohydrates.

Gene expression databases

ArrayExpress

P09104.

Bgee

P09104.

CleanEx

HS_ENO2.

Genevestigator

P09104.

GermOnline

ENSG00000111674. Homo sapiens.

Family and domain databases

InterPro

IPR000941. Enolase.
[Graphical view]

PANTHER

PTHR11902. Enolase. 1 hit.

Pfam

PF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
[Graphical view]

PIRSF

PIRSF001400. Enolase. 1 hit.

PRINTS

PR00148. ENOLASE.

ProDom

PD000902. Enolase. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR01060. eno. 1 hit.

PROSITE

PS00164. ENOLASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

8203.

PMAP-CutDB

P09104.

SOURCE

Search...

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Entry information

Entry name

ENOG_HUMAN

Accession

Primary (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:	November 3, 2009
This is version 129 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.

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