Full text data of ENO2
ENO2
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Gamma-enolase; 4.2.1.11 (2-phospho-D-glycerate hydro-lyase; Enolase 2; Neural enolase; Neuron-specific enolase; NSE)
Gamma-enolase; 4.2.1.11 (2-phospho-D-glycerate hydro-lyase; Enolase 2; Neural enolase; Neuron-specific enolase; NSE)
hRBCD
IPI00216171
IPI00216171 Enolase 2 Glycolysis, 2-phospho-D-glycerate = phosphoenolpyruvate + H2O soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
IPI00216171 Enolase 2 Glycolysis, 2-phospho-D-glycerate = phosphoenolpyruvate + H2O soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
UniProt
P09104
ID ENOG_HUMAN Reviewed; 434 AA.
AC P09104; Q96J33;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 171.
DE RecName: Full=Gamma-enolase;
DE EC=4.2.1.11;
DE AltName: Full=2-phospho-D-glycerate hydro-lyase;
DE AltName: Full=Enolase 2;
DE AltName: Full=Neural enolase;
DE AltName: Full=Neuron-specific enolase;
DE Short=NSE;
GN Name=ENO2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Retina;
RX PubMed=3208766; DOI=10.1111/j.1432-1033.1988.tb14465.x;
RA McAleese S.M., Dunbar B., Fothergill J., Hinks L., Day I.N.M.;
RT "Complete amino acid sequence of the neurone-specific gamma isozyme of
RT enolase (NSE) from human brain and comparison with the non-neuronal
RT alpha form (NNE).";
RL Eur. J. Biochem. 178:413-417(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=3385803; DOI=10.1002/jnr.490190409;
RA van Obberghen E., Kamholz J., Bishop J.G. III, Zomzely-Neurath C.,
RA Lazzarini R.A.;
RT "Human gamma enolase: isolation of a cDNA clone and expression in
RT normal and tumor tissues of human origin.";
RL J. Neurosci. Res. 19:450-456(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2792767; DOI=10.1016/0378-1119(89)90217-5;
RA Oliva D., Barba G., Barbieri G., Giallongo A., Feo S.;
RT "Cloning, expression and sequence homologies of cDNA for human gamma
RT enolase.";
RL Gene 79:355-360(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Hematopoietic;
RX PubMed=2045099; DOI=10.1016/0888-7543(91)90496-2;
RA Oliva D., Cali L., Feo S., Giallongo A.;
RT "Complete structure of the human gene encoding neuron-specific
RT enolase.";
RL Genomics 10:157-165(1991).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Brain;
RX PubMed=9074930;
RA Ansari-Lari M.A., Shen Y., Muzny D.M., Lee W., Gibbs R.A.;
RT "Large-scale sequencing in human chromosome 12p13: experimental and
RT computational gene structure determination.";
RL Genome Res. 7:268-280(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 16-28; 33-50; 90-103; 163-179; 184-193; 240-262;
RP 270-285; 336-372 AND 413-422, AND MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 425-434.
RX PubMed=3653393; DOI=10.1016/0014-5793(87)80207-7;
RA Day I.N.M., Allsopp M.T.E.P., Moore D.C.M., Thompson R.J.;
RT "Sequence conservation in the 3'-untranslated regions of neurone-
RT specific enolase, lymphokine and protooncogene mRNAs.";
RL FEBS Lett. 222:139-143(1987).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-44, AND MASS
RP SPECTROMETRY.
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-26, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS.
RX PubMed=15289101; DOI=10.1016/j.jmb.2004.05.068;
RA Chai G., Brewer J.M., Lovelace L.L., Aoki T., Minor W., Lebioda L.;
RT "Expression, purification and the 1.8 angstroms resolution crystal
RT structure of human neuron specific enolase.";
RL J. Mol. Biol. 341:1015-1021(2004).
CC -!- FUNCTION: Has neurotrophic and neuroprotective properties on a
CC broad spectrum of central nervous system (CNS) neurons. Binds, in
CC a calcium-dependent manner, to cultured neocortical neurons and
CC promotes cell survival (By similarity).
CC -!- CATALYTIC ACTIVITY: 2-phospho-D-glycerate = phosphoenolpyruvate +
CC H(2)O.
CC -!- COFACTOR: Magnesium. Required for catalysis and for stabilizing
CC the dimer.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 4/5.
CC -!- SUBUNIT: Mammalian enolase is composed of 3 isozyme subunits,
CC alpha, beta and gamma, which can form homodimers or heterodimers
CC which are cell-type and development-specific.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cell membrane (By
CC similarity). Note=Can translocate to the plasma membrane in either
CC the homodimeric (alpha/alpha) or heterodimeric (alpha/gamma) form
CC (By similarity).
CC -!- TISSUE SPECIFICITY: The alpha/alpha homodimer is expressed in
CC embryo and in most adult tissues. The alpha/beta heterodimer and
CC the beta/beta homodimer are found in striated muscle, and the
CC alpha/gamma heterodimer and the gamma/gamma homodimer in neurons.
CC -!- DEVELOPMENTAL STAGE: During ontogenesis, there is a transition
CC from the alpha/alpha homodimer to the alpha/beta heterodimer in
CC striated muscle cells, and to the alpha/gamma heterodimer in nerve
CC cells.
CC -!- INDUCTION: Levels of ENO2 increase dramatically in cardiovascular
CC accidents, cerebral trauma, brain tumors and Creutzfeldt-Jakob
CC disease.
CC -!- SIMILARITY: Belongs to the enolase family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA52388.1; Type=Erroneous initiation;
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DR EMBL; X13120; CAA31512.1; -; mRNA.
DR EMBL; X14327; CAA32505.1; -; mRNA.
DR EMBL; M36768; AAA52388.1; ALT_INIT; mRNA.
DR EMBL; M22349; AAB59554.1; -; mRNA.
DR EMBL; X51956; CAA36215.1; -; Genomic_DNA.
DR EMBL; U47924; AAB51320.1; -; Genomic_DNA.
DR EMBL; BT007383; AAP36047.1; -; mRNA.
DR EMBL; BC002745; AAH02745.1; -; mRNA.
DR PIR; JU0060; NOHUG.
DR RefSeq; NP_001966.1; NM_001975.2.
DR RefSeq; XP_005253730.1; XM_005253673.1.
DR RefSeq; XP_005253731.1; XM_005253674.1.
DR RefSeq; XP_005277806.1; XM_005277749.1.
DR RefSeq; XP_005277807.1; XM_005277750.1.
DR UniGene; Hs.511915; -.
DR PDB; 1TE6; X-ray; 1.80 A; A/B=2-434.
DR PDB; 2AKM; X-ray; 1.92 A; A/B=2-433.
DR PDB; 2AKZ; X-ray; 1.36 A; A/B=2-433.
DR PDB; 3UCC; X-ray; 1.50 A; A/B=2-434.
DR PDB; 3UCD; X-ray; 1.41 A; A/B=2-434.
DR PDB; 3UJE; X-ray; 1.55 A; A/B=2-434.
DR PDB; 3UJF; X-ray; 2.10 A; A/B=2-434.
DR PDB; 3UJR; X-ray; 1.40 A; A/B=2-434.
DR PDB; 3UJS; X-ray; 1.65 A; A/B=2-434.
DR PDBsum; 1TE6; -.
DR PDBsum; 2AKM; -.
DR PDBsum; 2AKZ; -.
DR PDBsum; 3UCC; -.
DR PDBsum; 3UCD; -.
DR PDBsum; 3UJE; -.
DR PDBsum; 3UJF; -.
DR PDBsum; 3UJR; -.
DR PDBsum; 3UJS; -.
DR ProteinModelPortal; P09104; -.
DR SMR; P09104; 2-434.
DR IntAct; P09104; 21.
DR MINT; MINT-1367862; -.
DR STRING; 9606.ENSP00000229277; -.
DR PhosphoSite; P09104; -.
DR DMDM; 20981682; -.
DR OGP; P09104; -.
DR UCD-2DPAGE; P09104; -.
DR PaxDb; P09104; -.
DR PRIDE; P09104; -.
DR DNASU; 2026; -.
DR Ensembl; ENST00000229277; ENSP00000229277; ENSG00000111674.
DR Ensembl; ENST00000535366; ENSP00000437402; ENSG00000111674.
DR Ensembl; ENST00000541477; ENSP00000438873; ENSG00000111674.
DR Ensembl; ENST00000594987; ENSP00000472373; ENSG00000269528.
DR Ensembl; ENST00000596089; ENSP00000469457; ENSG00000269528.
DR Ensembl; ENST00000601485; ENSP00000471490; ENSG00000269528.
DR GeneID; 2026; -.
DR KEGG; hsa:2026; -.
DR UCSC; uc001qru.1; human.
DR CTD; 2026; -.
DR GeneCards; GC12P007116; -.
DR HGNC; HGNC:3353; ENO2.
DR HPA; CAB000063; -.
DR MIM; 131360; gene.
DR neXtProt; NX_P09104; -.
DR PharmGKB; PA27788; -.
DR eggNOG; COG0148; -.
DR HOGENOM; HOG000072174; -.
DR HOVERGEN; HBG000067; -.
DR InParanoid; P09104; -.
DR KO; K01689; -.
DR OMA; KNEGVER; -.
DR PhylomeDB; P09104; -.
DR BioCyc; MetaCyc:HS10646-MONOMER; -.
DR Reactome; REACT_111217; Metabolism.
DR SABIO-RK; P09104; -.
DR UniPathway; UPA00109; UER00187.
DR ChiTaRS; ENO2; human.
DR EvolutionaryTrace; P09104; -.
DR GeneWiki; Enolase_2; -.
DR GenomeRNAi; 2026; -.
DR NextBio; 8203; -.
DR PMAP-CutDB; P09104; -.
DR PRO; PR:P09104; -.
DR ArrayExpress; P09104; -.
DR Bgee; P09104; -.
DR CleanEx; HS_ENO2; -.
DR Genevestigator; P09104; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043204; C:perikaryon; IEA:Ensembl.
DR GO; GO:0000015; C:phosphopyruvate hydratase complex; IEA:InterPro.
DR GO; GO:0001917; C:photoreceptor inner segment; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004634; F:phosphopyruvate hydratase activity; TAS:ProtInc.
DR GO; GO:0006094; P:gluconeogenesis; TAS:Reactome.
DR GO; GO:0006096; P:glycolysis; TAS:Reactome.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR InterPro; IPR000941; Enolase.
DR InterPro; IPR020810; Enolase_C.
DR InterPro; IPR020809; Enolase_CS.
DR InterPro; IPR020811; Enolase_N.
DR PANTHER; PTHR11902; PTHR11902; 1.
DR Pfam; PF00113; Enolase_C; 1.
DR Pfam; PF03952; Enolase_N; 1.
DR PIRSF; PIRSF001400; Enolase; 1.
DR PRINTS; PR00148; ENOLASE.
DR TIGRFAMs; TIGR01060; eno; 1.
DR PROSITE; PS00164; ENOLASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell membrane; Complete proteome;
KW Cytoplasm; Direct protein sequencing; Glycolysis; Lyase; Magnesium;
KW Membrane; Metal-binding; Phosphoprotein; Polymorphism;
KW Reference proteome.
FT CHAIN 1 434 Gamma-enolase.
FT /FTId=PRO_0000134112.
FT REGION 370 373 Substrate binding (By similarity).
FT ACT_SITE 210 210 Proton donor (By similarity).
FT ACT_SITE 343 343 Proton acceptor (By similarity).
FT METAL 245 245 Magnesium.
FT METAL 293 293 Magnesium.
FT METAL 318 318 Magnesium.
FT BINDING 158 158 Substrate (By similarity).
FT BINDING 167 167 Substrate (By similarity).
FT BINDING 293 293 Substrate (By similarity).
FT BINDING 318 318 Substrate (By similarity).
FT BINDING 394 394 Substrate (By similarity).
FT MOD_RES 26 26 Phosphothreonine.
FT MOD_RES 44 44 Phosphotyrosine.
FT MOD_RES 197 197 N6-acetyllysine (By similarity).
FT MOD_RES 199 199 N6-acetyllysine (By similarity).
FT VARIANT 264 264 P -> A.
FT /FTId=VAR_002354.
FT VARIANT 395 395 T -> A.
FT /FTId=VAR_002355.
FT CONFLICT 4 4 E -> Q (in Ref. 1; CAA31512/CAA32505).
FT CONFLICT 27 28 AK -> GC (in Ref. 2; AAA52388).
FT CONFLICT 127 127 E -> N (in Ref. 2; AAA52388).
FT CONFLICT 240 240 I -> M (in Ref. 1; CAA31512/CAA32505).
FT STRAND 5 12
FT STRAND 18 26
FT STRAND 29 34
FT HELIX 57 59
FT HELIX 63 71
FT HELIX 73 80
FT HELIX 87 98
FT TURN 104 106
FT HELIX 108 126
FT HELIX 130 138
FT STRAND 147 154
FT HELIX 156 158
FT STRAND 159 162
FT STRAND 167 171
FT HELIX 178 200
FT HELIX 202 205
FT STRAND 211 213
FT HELIX 220 234
FT TURN 237 239
FT STRAND 241 245
FT HELIX 248 251
FT STRAND 254 257
FT TURN 259 262
FT HELIX 267 269
FT HELIX 273 286
FT STRAND 289 293
FT HELIX 301 309
FT STRAND 312 318
FT TURN 319 323
FT HELIX 325 333
FT STRAND 338 342
FT HELIX 344 347
FT HELIX 350 362
FT STRAND 366 370
FT HELIX 380 388
FT STRAND 391 394
FT HELIX 401 417
FT HELIX 418 420
FT HELIX 425 427
FT HELIX 431 433
SQ SEQUENCE 434 AA; 47269 MW; 6163DE81F5C67744 CRC64;
MSIEKIWARE ILDSRGNPTV EVDLYTAKGL FRAAVPSGAS TGIYEALELR DGDKQRYLGK
GVLKAVDHIN STIAPALISS GLSVVEQEKL DNLMLELDGT ENKSKFGANA ILGVSLAVCK
AGAAERELPL YRHIAQLAGN SDLILPVPAF NVINGGSHAG NKLAMQEFMI LPVGAESFRD
AMRLGAEVYH TLKGVIKDKY GKDATNVGDE GGFAPNILEN SEALELVKEA IDKAGYTEKI
VIGMDVAASE FYRDGKYDLD FKSPTDPSRY ITGDQLGALY QDFVRDYPVV SIEDPFDQDD
WAAWSKFTAN VGIQIVGDDL TVTNPKRIER AVEEKACNCL LLKVNQIGSV TEAIQACKLA
QENGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQL MRIEEELGDE
ARFAGHNFRN PSVL
//
ID ENOG_HUMAN Reviewed; 434 AA.
AC P09104; Q96J33;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 171.
DE RecName: Full=Gamma-enolase;
DE EC=4.2.1.11;
DE AltName: Full=2-phospho-D-glycerate hydro-lyase;
DE AltName: Full=Enolase 2;
DE AltName: Full=Neural enolase;
DE AltName: Full=Neuron-specific enolase;
DE Short=NSE;
GN Name=ENO2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Retina;
RX PubMed=3208766; DOI=10.1111/j.1432-1033.1988.tb14465.x;
RA McAleese S.M., Dunbar B., Fothergill J., Hinks L., Day I.N.M.;
RT "Complete amino acid sequence of the neurone-specific gamma isozyme of
RT enolase (NSE) from human brain and comparison with the non-neuronal
RT alpha form (NNE).";
RL Eur. J. Biochem. 178:413-417(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=3385803; DOI=10.1002/jnr.490190409;
RA van Obberghen E., Kamholz J., Bishop J.G. III, Zomzely-Neurath C.,
RA Lazzarini R.A.;
RT "Human gamma enolase: isolation of a cDNA clone and expression in
RT normal and tumor tissues of human origin.";
RL J. Neurosci. Res. 19:450-456(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2792767; DOI=10.1016/0378-1119(89)90217-5;
RA Oliva D., Barba G., Barbieri G., Giallongo A., Feo S.;
RT "Cloning, expression and sequence homologies of cDNA for human gamma
RT enolase.";
RL Gene 79:355-360(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Hematopoietic;
RX PubMed=2045099; DOI=10.1016/0888-7543(91)90496-2;
RA Oliva D., Cali L., Feo S., Giallongo A.;
RT "Complete structure of the human gene encoding neuron-specific
RT enolase.";
RL Genomics 10:157-165(1991).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Brain;
RX PubMed=9074930;
RA Ansari-Lari M.A., Shen Y., Muzny D.M., Lee W., Gibbs R.A.;
RT "Large-scale sequencing in human chromosome 12p13: experimental and
RT computational gene structure determination.";
RL Genome Res. 7:268-280(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 16-28; 33-50; 90-103; 163-179; 184-193; 240-262;
RP 270-285; 336-372 AND 413-422, AND MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 425-434.
RX PubMed=3653393; DOI=10.1016/0014-5793(87)80207-7;
RA Day I.N.M., Allsopp M.T.E.P., Moore D.C.M., Thompson R.J.;
RT "Sequence conservation in the 3'-untranslated regions of neurone-
RT specific enolase, lymphokine and protooncogene mRNAs.";
RL FEBS Lett. 222:139-143(1987).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-44, AND MASS
RP SPECTROMETRY.
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-26, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS.
RX PubMed=15289101; DOI=10.1016/j.jmb.2004.05.068;
RA Chai G., Brewer J.M., Lovelace L.L., Aoki T., Minor W., Lebioda L.;
RT "Expression, purification and the 1.8 angstroms resolution crystal
RT structure of human neuron specific enolase.";
RL J. Mol. Biol. 341:1015-1021(2004).
CC -!- FUNCTION: Has neurotrophic and neuroprotective properties on a
CC broad spectrum of central nervous system (CNS) neurons. Binds, in
CC a calcium-dependent manner, to cultured neocortical neurons and
CC promotes cell survival (By similarity).
CC -!- CATALYTIC ACTIVITY: 2-phospho-D-glycerate = phosphoenolpyruvate +
CC H(2)O.
CC -!- COFACTOR: Magnesium. Required for catalysis and for stabilizing
CC the dimer.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 4/5.
CC -!- SUBUNIT: Mammalian enolase is composed of 3 isozyme subunits,
CC alpha, beta and gamma, which can form homodimers or heterodimers
CC which are cell-type and development-specific.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cell membrane (By
CC similarity). Note=Can translocate to the plasma membrane in either
CC the homodimeric (alpha/alpha) or heterodimeric (alpha/gamma) form
CC (By similarity).
CC -!- TISSUE SPECIFICITY: The alpha/alpha homodimer is expressed in
CC embryo and in most adult tissues. The alpha/beta heterodimer and
CC the beta/beta homodimer are found in striated muscle, and the
CC alpha/gamma heterodimer and the gamma/gamma homodimer in neurons.
CC -!- DEVELOPMENTAL STAGE: During ontogenesis, there is a transition
CC from the alpha/alpha homodimer to the alpha/beta heterodimer in
CC striated muscle cells, and to the alpha/gamma heterodimer in nerve
CC cells.
CC -!- INDUCTION: Levels of ENO2 increase dramatically in cardiovascular
CC accidents, cerebral trauma, brain tumors and Creutzfeldt-Jakob
CC disease.
CC -!- SIMILARITY: Belongs to the enolase family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA52388.1; Type=Erroneous initiation;
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DR EMBL; X13120; CAA31512.1; -; mRNA.
DR EMBL; X14327; CAA32505.1; -; mRNA.
DR EMBL; M36768; AAA52388.1; ALT_INIT; mRNA.
DR EMBL; M22349; AAB59554.1; -; mRNA.
DR EMBL; X51956; CAA36215.1; -; Genomic_DNA.
DR EMBL; U47924; AAB51320.1; -; Genomic_DNA.
DR EMBL; BT007383; AAP36047.1; -; mRNA.
DR EMBL; BC002745; AAH02745.1; -; mRNA.
DR PIR; JU0060; NOHUG.
DR RefSeq; NP_001966.1; NM_001975.2.
DR RefSeq; XP_005253730.1; XM_005253673.1.
DR RefSeq; XP_005253731.1; XM_005253674.1.
DR RefSeq; XP_005277806.1; XM_005277749.1.
DR RefSeq; XP_005277807.1; XM_005277750.1.
DR UniGene; Hs.511915; -.
DR PDB; 1TE6; X-ray; 1.80 A; A/B=2-434.
DR PDB; 2AKM; X-ray; 1.92 A; A/B=2-433.
DR PDB; 2AKZ; X-ray; 1.36 A; A/B=2-433.
DR PDB; 3UCC; X-ray; 1.50 A; A/B=2-434.
DR PDB; 3UCD; X-ray; 1.41 A; A/B=2-434.
DR PDB; 3UJE; X-ray; 1.55 A; A/B=2-434.
DR PDB; 3UJF; X-ray; 2.10 A; A/B=2-434.
DR PDB; 3UJR; X-ray; 1.40 A; A/B=2-434.
DR PDB; 3UJS; X-ray; 1.65 A; A/B=2-434.
DR PDBsum; 1TE6; -.
DR PDBsum; 2AKM; -.
DR PDBsum; 2AKZ; -.
DR PDBsum; 3UCC; -.
DR PDBsum; 3UCD; -.
DR PDBsum; 3UJE; -.
DR PDBsum; 3UJF; -.
DR PDBsum; 3UJR; -.
DR PDBsum; 3UJS; -.
DR ProteinModelPortal; P09104; -.
DR SMR; P09104; 2-434.
DR IntAct; P09104; 21.
DR MINT; MINT-1367862; -.
DR STRING; 9606.ENSP00000229277; -.
DR PhosphoSite; P09104; -.
DR DMDM; 20981682; -.
DR OGP; P09104; -.
DR UCD-2DPAGE; P09104; -.
DR PaxDb; P09104; -.
DR PRIDE; P09104; -.
DR DNASU; 2026; -.
DR Ensembl; ENST00000229277; ENSP00000229277; ENSG00000111674.
DR Ensembl; ENST00000535366; ENSP00000437402; ENSG00000111674.
DR Ensembl; ENST00000541477; ENSP00000438873; ENSG00000111674.
DR Ensembl; ENST00000594987; ENSP00000472373; ENSG00000269528.
DR Ensembl; ENST00000596089; ENSP00000469457; ENSG00000269528.
DR Ensembl; ENST00000601485; ENSP00000471490; ENSG00000269528.
DR GeneID; 2026; -.
DR KEGG; hsa:2026; -.
DR UCSC; uc001qru.1; human.
DR CTD; 2026; -.
DR GeneCards; GC12P007116; -.
DR HGNC; HGNC:3353; ENO2.
DR HPA; CAB000063; -.
DR MIM; 131360; gene.
DR neXtProt; NX_P09104; -.
DR PharmGKB; PA27788; -.
DR eggNOG; COG0148; -.
DR HOGENOM; HOG000072174; -.
DR HOVERGEN; HBG000067; -.
DR InParanoid; P09104; -.
DR KO; K01689; -.
DR OMA; KNEGVER; -.
DR PhylomeDB; P09104; -.
DR BioCyc; MetaCyc:HS10646-MONOMER; -.
DR Reactome; REACT_111217; Metabolism.
DR SABIO-RK; P09104; -.
DR UniPathway; UPA00109; UER00187.
DR ChiTaRS; ENO2; human.
DR EvolutionaryTrace; P09104; -.
DR GeneWiki; Enolase_2; -.
DR GenomeRNAi; 2026; -.
DR NextBio; 8203; -.
DR PMAP-CutDB; P09104; -.
DR PRO; PR:P09104; -.
DR ArrayExpress; P09104; -.
DR Bgee; P09104; -.
DR CleanEx; HS_ENO2; -.
DR Genevestigator; P09104; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043204; C:perikaryon; IEA:Ensembl.
DR GO; GO:0000015; C:phosphopyruvate hydratase complex; IEA:InterPro.
DR GO; GO:0001917; C:photoreceptor inner segment; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004634; F:phosphopyruvate hydratase activity; TAS:ProtInc.
DR GO; GO:0006094; P:gluconeogenesis; TAS:Reactome.
DR GO; GO:0006096; P:glycolysis; TAS:Reactome.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR InterPro; IPR000941; Enolase.
DR InterPro; IPR020810; Enolase_C.
DR InterPro; IPR020809; Enolase_CS.
DR InterPro; IPR020811; Enolase_N.
DR PANTHER; PTHR11902; PTHR11902; 1.
DR Pfam; PF00113; Enolase_C; 1.
DR Pfam; PF03952; Enolase_N; 1.
DR PIRSF; PIRSF001400; Enolase; 1.
DR PRINTS; PR00148; ENOLASE.
DR TIGRFAMs; TIGR01060; eno; 1.
DR PROSITE; PS00164; ENOLASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell membrane; Complete proteome;
KW Cytoplasm; Direct protein sequencing; Glycolysis; Lyase; Magnesium;
KW Membrane; Metal-binding; Phosphoprotein; Polymorphism;
KW Reference proteome.
FT CHAIN 1 434 Gamma-enolase.
FT /FTId=PRO_0000134112.
FT REGION 370 373 Substrate binding (By similarity).
FT ACT_SITE 210 210 Proton donor (By similarity).
FT ACT_SITE 343 343 Proton acceptor (By similarity).
FT METAL 245 245 Magnesium.
FT METAL 293 293 Magnesium.
FT METAL 318 318 Magnesium.
FT BINDING 158 158 Substrate (By similarity).
FT BINDING 167 167 Substrate (By similarity).
FT BINDING 293 293 Substrate (By similarity).
FT BINDING 318 318 Substrate (By similarity).
FT BINDING 394 394 Substrate (By similarity).
FT MOD_RES 26 26 Phosphothreonine.
FT MOD_RES 44 44 Phosphotyrosine.
FT MOD_RES 197 197 N6-acetyllysine (By similarity).
FT MOD_RES 199 199 N6-acetyllysine (By similarity).
FT VARIANT 264 264 P -> A.
FT /FTId=VAR_002354.
FT VARIANT 395 395 T -> A.
FT /FTId=VAR_002355.
FT CONFLICT 4 4 E -> Q (in Ref. 1; CAA31512/CAA32505).
FT CONFLICT 27 28 AK -> GC (in Ref. 2; AAA52388).
FT CONFLICT 127 127 E -> N (in Ref. 2; AAA52388).
FT CONFLICT 240 240 I -> M (in Ref. 1; CAA31512/CAA32505).
FT STRAND 5 12
FT STRAND 18 26
FT STRAND 29 34
FT HELIX 57 59
FT HELIX 63 71
FT HELIX 73 80
FT HELIX 87 98
FT TURN 104 106
FT HELIX 108 126
FT HELIX 130 138
FT STRAND 147 154
FT HELIX 156 158
FT STRAND 159 162
FT STRAND 167 171
FT HELIX 178 200
FT HELIX 202 205
FT STRAND 211 213
FT HELIX 220 234
FT TURN 237 239
FT STRAND 241 245
FT HELIX 248 251
FT STRAND 254 257
FT TURN 259 262
FT HELIX 267 269
FT HELIX 273 286
FT STRAND 289 293
FT HELIX 301 309
FT STRAND 312 318
FT TURN 319 323
FT HELIX 325 333
FT STRAND 338 342
FT HELIX 344 347
FT HELIX 350 362
FT STRAND 366 370
FT HELIX 380 388
FT STRAND 391 394
FT HELIX 401 417
FT HELIX 418 420
FT HELIX 425 427
FT HELIX 431 433
SQ SEQUENCE 434 AA; 47269 MW; 6163DE81F5C67744 CRC64;
MSIEKIWARE ILDSRGNPTV EVDLYTAKGL FRAAVPSGAS TGIYEALELR DGDKQRYLGK
GVLKAVDHIN STIAPALISS GLSVVEQEKL DNLMLELDGT ENKSKFGANA ILGVSLAVCK
AGAAERELPL YRHIAQLAGN SDLILPVPAF NVINGGSHAG NKLAMQEFMI LPVGAESFRD
AMRLGAEVYH TLKGVIKDKY GKDATNVGDE GGFAPNILEN SEALELVKEA IDKAGYTEKI
VIGMDVAASE FYRDGKYDLD FKSPTDPSRY ITGDQLGALY QDFVRDYPVV SIEDPFDQDD
WAAWSKFTAN VGIQIVGDDL TVTNPKRIER AVEEKACNCL LLKVNQIGSV TEAIQACKLA
QENGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQL MRIEEELGDE
ARFAGHNFRN PSVL
//
MIM
131360
*RECORD*
*FIELD* NO
131360
*FIELD* TI
*131360 ENOLASE 2; ENO2
;;ENOLASE, GAMMA;;
ENOLASE, NEURON-SPECIFIC; NSE
*FIELD* TX
read more
DESCRIPTION
The enolases (phosphopyruvate hydratase; EC 4.2.1.11) catalyze the
interconversion of 2-phosphoglycerate to phosphoenolpyruvate in the
glycolytic pathway. The functional enzyme is a dimer made up of subunits
referred to as alpha, beta, and gamma. In mammals there are at least 3
isoforms of enolase characterized by different tissue distributions as
well as by distinct biochemical and immunologic properties. The gamma-,
or neuron-specific, enolase (ENO2) is the major form found in mature
neurons and in cells of neuronal origin. The alpha-, or nonneuronal,
enolase (ENO1; 172430) is a nearly ubiquitous form, found in almost all
tissues, and its expression precedes that of the other isoforms in the
early stage of embryonic development. The beta-, or muscle-specific,
enolase (ENO3; 131370) is present in adult skeletal muscle (summary by
Oliva et al., 1991).
GENE FUNCTION
Muller et al. (2012) proposed that homozygous deletions in passenger
genes in cancer deletions can expose cancer-specific therapeutic
vulnerabilities when the collaterally deleted gene is a member of a
functionally redundant family of genes carrying out an essential
function. The glycolytic gene ENO1 in the 1p36 locus is deleted in
glioblastoma, which is tolerated by the expression of ENO2. Muller et
al. (2012) showed that short hairpin RNA-mediated silencing of ENO2
selectively inhibits growth, survival, and the tumorigenic potential of
ENO1-deleted GBM cells, and that the enolase inhibitor
phosphonoacetohydroxamate is selectively toxic to ENO1-deleted GBM cells
relative to ENO1-intact GBM cells or normal astrocytes. Muller et al.
(2012) suggested that the principle of collateral vulnerability should
be applicable to other passenger-deleted genes encoding functionally
redundant essential activities and provide an effective treatment
strategy for cancers containing such genomic events.
MAPPING
Enolase-2 is determined by a gene on chromosome 12 (Grzeschik, 1976).
Herbschleb-Voogt et al. (1978) confirmed assignment to chromosome 12 by
showing synteny with LDHB and PEPB in man-mouse hybrids. Mattei et al.
(1982) assigned ENO2 to 12p11-qter by study of cells trisomic for
12pter-p11. Law and Kao (1982) also assigned the gene to chromosome 12.
By in situ hybridization, Craig et al. (1989, 1990) localized ENO2 to
12p13. Oliva et al. (1991) demonstrated that the ENO2 gene contains 12
exons distributed over 9,213 nucleotides. The putative promoter region
lacks canonical TATA and CAAT boxes, is very G+C-rich, and contains
several potential regulatory sequences.
*FIELD* SA
Hinks and Day (1991)
*FIELD* RF
1. Craig, S. P.; Day, I. N. M.; Thompson, R. J.; Craig, I. W.: Localization
of human neurone-specific enolase to chromosome 12p13. (Abstract) Cytogenet.
Cell Genet. 51: 980 only, 1989.
2. Craig, S. P.; Day, I. N. M.; Thompson, R. J.; Craig, I. W.: Localisation
of neurone-specific enolase (ENO2) to 12p13. Cytogenet. Cell Genet. 54:
71-73, 1990.
3. Grzeschik, K.-H.: Assignment of human genes: beta-glucuronidase
to chromosome 7, adenylate kinase-1 to 9, a second enzyme with enolase
activity to 12, and mitochondrial IDH to 15. Cytogenet. Cell Genet. 16:
142-148, 1976. Note: Alternate: Birth Defects Orig. Art. Ser. 12(7):
142-148, 1976.
4. Herbschleb-Voogt, E.; Monteba-van Heuvel, M.; Wijnen, L. M. M.;
Westerveld, A.; Pearson, P. L.; Meera Khan, P.: Chromosomal assignment
and regional localization of CS, ENO-2, GAPDH, LDH-B, PEP-B and TPI
in man-rodent cell hybrids. Cytogenet. Cell Genet. 22: 482-486,
1978.
5. Hinks, L. J.; Day, I. N. M.: Further studies of enolase loci.
(Abstract) Cytogenet. Cell Genet. 58: 1854 only, 1991.
6. Law, M. L.; Kao, F.: Regional mapping of the gene coding for enolase-2
on human chromosome 12. J. Cell Sci. 53: 245-254, 1982.
7. Mattei, J. F.; Baeteman, M. A.; Mattei, M. G.; Ardissonne, J. P.;
Giraud, F.: Regional assignments of CS and ENO2 on chromosome 12.
(Abstract) Cytogenet. Cell Genet. 32: 297 only, 1982.
8. Muller, F. L.; Colla, S.; Aquilanti, E.; Manzo, V. E.; Genovese,
G.; Lee, J.; Eisenson, D.; Narurkar, R.; Deng, P.; Nezi, L.; Lee,
M. A.; Hu, B.; and 10 others: Passenger deletions generate therapeutic
vulnerabilities in cancer. Nature 488: 337-342, 2012.
9. Oliva, D.; Cali, L.; Feo, S.; Giallongo, A.: Complete structure
of the human gene encoding neuron-specific enolase. Genomics 10:
157-165, 1991.
*FIELD* CN
Ada Hamosh - updated: 09/13/2012
*FIELD* CD
Victor A. McKusick: 6/4/1986
*FIELD* ED
alopez: 09/13/2012
carol: 4/14/1999
dkim: 6/30/1998
warfield: 3/28/1994
supermim: 3/16/1992
carol: 2/21/1992
carol: 8/8/1991
carol: 4/18/1991
carol: 3/21/1991
*RECORD*
*FIELD* NO
131360
*FIELD* TI
*131360 ENOLASE 2; ENO2
;;ENOLASE, GAMMA;;
ENOLASE, NEURON-SPECIFIC; NSE
*FIELD* TX
read more
DESCRIPTION
The enolases (phosphopyruvate hydratase; EC 4.2.1.11) catalyze the
interconversion of 2-phosphoglycerate to phosphoenolpyruvate in the
glycolytic pathway. The functional enzyme is a dimer made up of subunits
referred to as alpha, beta, and gamma. In mammals there are at least 3
isoforms of enolase characterized by different tissue distributions as
well as by distinct biochemical and immunologic properties. The gamma-,
or neuron-specific, enolase (ENO2) is the major form found in mature
neurons and in cells of neuronal origin. The alpha-, or nonneuronal,
enolase (ENO1; 172430) is a nearly ubiquitous form, found in almost all
tissues, and its expression precedes that of the other isoforms in the
early stage of embryonic development. The beta-, or muscle-specific,
enolase (ENO3; 131370) is present in adult skeletal muscle (summary by
Oliva et al., 1991).
GENE FUNCTION
Muller et al. (2012) proposed that homozygous deletions in passenger
genes in cancer deletions can expose cancer-specific therapeutic
vulnerabilities when the collaterally deleted gene is a member of a
functionally redundant family of genes carrying out an essential
function. The glycolytic gene ENO1 in the 1p36 locus is deleted in
glioblastoma, which is tolerated by the expression of ENO2. Muller et
al. (2012) showed that short hairpin RNA-mediated silencing of ENO2
selectively inhibits growth, survival, and the tumorigenic potential of
ENO1-deleted GBM cells, and that the enolase inhibitor
phosphonoacetohydroxamate is selectively toxic to ENO1-deleted GBM cells
relative to ENO1-intact GBM cells or normal astrocytes. Muller et al.
(2012) suggested that the principle of collateral vulnerability should
be applicable to other passenger-deleted genes encoding functionally
redundant essential activities and provide an effective treatment
strategy for cancers containing such genomic events.
MAPPING
Enolase-2 is determined by a gene on chromosome 12 (Grzeschik, 1976).
Herbschleb-Voogt et al. (1978) confirmed assignment to chromosome 12 by
showing synteny with LDHB and PEPB in man-mouse hybrids. Mattei et al.
(1982) assigned ENO2 to 12p11-qter by study of cells trisomic for
12pter-p11. Law and Kao (1982) also assigned the gene to chromosome 12.
By in situ hybridization, Craig et al. (1989, 1990) localized ENO2 to
12p13. Oliva et al. (1991) demonstrated that the ENO2 gene contains 12
exons distributed over 9,213 nucleotides. The putative promoter region
lacks canonical TATA and CAAT boxes, is very G+C-rich, and contains
several potential regulatory sequences.
*FIELD* SA
Hinks and Day (1991)
*FIELD* RF
1. Craig, S. P.; Day, I. N. M.; Thompson, R. J.; Craig, I. W.: Localization
of human neurone-specific enolase to chromosome 12p13. (Abstract) Cytogenet.
Cell Genet. 51: 980 only, 1989.
2. Craig, S. P.; Day, I. N. M.; Thompson, R. J.; Craig, I. W.: Localisation
of neurone-specific enolase (ENO2) to 12p13. Cytogenet. Cell Genet. 54:
71-73, 1990.
3. Grzeschik, K.-H.: Assignment of human genes: beta-glucuronidase
to chromosome 7, adenylate kinase-1 to 9, a second enzyme with enolase
activity to 12, and mitochondrial IDH to 15. Cytogenet. Cell Genet. 16:
142-148, 1976. Note: Alternate: Birth Defects Orig. Art. Ser. 12(7):
142-148, 1976.
4. Herbschleb-Voogt, E.; Monteba-van Heuvel, M.; Wijnen, L. M. M.;
Westerveld, A.; Pearson, P. L.; Meera Khan, P.: Chromosomal assignment
and regional localization of CS, ENO-2, GAPDH, LDH-B, PEP-B and TPI
in man-rodent cell hybrids. Cytogenet. Cell Genet. 22: 482-486,
1978.
5. Hinks, L. J.; Day, I. N. M.: Further studies of enolase loci.
(Abstract) Cytogenet. Cell Genet. 58: 1854 only, 1991.
6. Law, M. L.; Kao, F.: Regional mapping of the gene coding for enolase-2
on human chromosome 12. J. Cell Sci. 53: 245-254, 1982.
7. Mattei, J. F.; Baeteman, M. A.; Mattei, M. G.; Ardissonne, J. P.;
Giraud, F.: Regional assignments of CS and ENO2 on chromosome 12.
(Abstract) Cytogenet. Cell Genet. 32: 297 only, 1982.
8. Muller, F. L.; Colla, S.; Aquilanti, E.; Manzo, V. E.; Genovese,
G.; Lee, J.; Eisenson, D.; Narurkar, R.; Deng, P.; Nezi, L.; Lee,
M. A.; Hu, B.; and 10 others: Passenger deletions generate therapeutic
vulnerabilities in cancer. Nature 488: 337-342, 2012.
9. Oliva, D.; Cali, L.; Feo, S.; Giallongo, A.: Complete structure
of the human gene encoding neuron-specific enolase. Genomics 10:
157-165, 1991.
*FIELD* CN
Ada Hamosh - updated: 09/13/2012
*FIELD* CD
Victor A. McKusick: 6/4/1986
*FIELD* ED
alopez: 09/13/2012
carol: 4/14/1999
dkim: 6/30/1998
warfield: 3/28/1994
supermim: 3/16/1992
carol: 2/21/1992
carol: 8/8/1991
carol: 4/18/1991
carol: 3/21/1991