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P09104

- ENOG_HUMAN

UniProt

P09104 - ENOG_HUMAN

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Protein

Gamma-enolase

Gene

ENO2

Organism
Homo sapiens (Human)
Status
Reviewed - 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

Magnesium. Required for catalysis and for stabilizing the dimer.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei158 – 1581SubstrateBy similarity
Binding sitei167 – 1671SubstrateBy similarity
Active sitei210 – 2101Proton donorBy similarity
Metal bindingi245 – 2451Magnesium
Metal bindingi293 – 2931Magnesium
Binding sitei293 – 2931SubstrateBy similarity
Metal bindingi318 – 3181Magnesium
Binding sitei318 – 3181SubstrateBy similarity
Active sitei343 – 3431Proton acceptorBy similarity
Binding sitei394 – 3941SubstrateBy similarity

GO - Molecular functioni

  1. magnesium ion binding Source: InterPro
  2. phosphopyruvate hydratase activity Source: ProtInc

GO - Biological processi

  1. carbohydrate metabolic process Source: Reactome
  2. gluconeogenesis Source: Reactome
  3. glucose metabolic process Source: Reactome
  4. glycolytic process Source: Reactome
  5. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS10646-MONOMER.
ReactomeiREACT_1383. Glycolysis.
REACT_1520. 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
ProteomesiUP000005640: 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

  1. cytosol Source: Reactome
  2. extracellular space Source: UniProt
  3. extracellular vesicular exosome Source: UniProtKB
  4. perikaryon Source: Ensembl
  5. phosphopyruvate hydratase complex Source: InterPro
  6. photoreceptor inner segment Source: Ensembl
  7. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27788.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 434434Gamma-enolasePRO_0000134112Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei26 – 261Phosphothreonine1 Publication
Modified residuei44 – 441Phosphotyrosine1 Publication
Modified residuei197 – 1971N6-acetyllysineBy similarity
Modified residuei199 – 1991N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP09104.
PaxDbiP09104.
PRIDEiP09104.

2D gel databases

OGPiP09104.
UCD-2DPAGEP09104.

PTM databases

PhosphoSiteiP09104.

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

BgeeiP09104.
CleanExiHS_ENO2.
ExpressionAtlasiP09104. baseline and differential.
GenevestigatoriP09104.

Organism-specific databases

HPAiCAB000063.

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

Protein-protein interaction databases

BioGridi108340. 44 interactions.
IntActiP09104. 21 interactions.
MINTiMINT-1367862.
STRINGi9606.ENSP00000229277.

Structurei

Secondary structure

1
434
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 128
Beta strandi18 – 269
Beta strandi29 – 346
Helixi57 – 593
Helixi63 – 719
Helixi73 – 808
Helixi87 – 9812
Turni104 – 1063
Helixi108 – 12619
Helixi130 – 1389
Beta strandi147 – 1548
Helixi156 – 1583
Beta strandi159 – 1624
Beta strandi167 – 1715
Helixi178 – 20023
Helixi202 – 2054
Beta strandi211 – 2133
Helixi220 – 23415
Turni237 – 2393
Beta strandi241 – 2455
Helixi248 – 2514
Beta strandi254 – 2574
Turni259 – 2624
Helixi267 – 2693
Helixi273 – 28614
Beta strandi289 – 2935
Helixi301 – 3099
Beta strandi312 – 3187
Turni319 – 3235
Helixi325 – 3339
Beta strandi338 – 3425
Helixi344 – 3474
Helixi350 – 36213
Beta strandi366 – 3705
Helixi380 – 3889
Beta strandi391 – 3944
Helixi401 – 41717
Helixi418 – 4203
Helixi425 – 4273
Helixi431 – 4333

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP09104.
SMRiP09104. Positions 2-434.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09104.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni370 – 3734Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the enolase family.Curated

Phylogenomic databases

eggNOGiCOG0148.
GeneTreeiENSGT00550000074560.
HOGENOMiHOG000072174.
HOVERGENiHBG000067.
InParanoidiP09104.
KOiK01689.
OMAiASTEVYH.
PhylomeDBiP09104.
TreeFamiTF300391.

Family and domain databases

Gene3Di3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
HAMAPiMF_00318. Enolase.
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.
SUPFAMiSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
TIGRFAMsiTIGR01060. eno. 1 hit.
PROSITEiPS00164. ENOLASE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41E → Q in CAA31512. (PubMed:3208766)Curated
Sequence conflicti4 – 41E → Q in CAA32505. (PubMed:3208766)Curated
Sequence conflicti27 – 282AK → GC in AAA52388. (PubMed:3385803)Curated
Sequence conflicti127 – 1271E → N in AAA52388. (PubMed:3385803)Curated
Sequence conflicti240 – 2401I → M in CAA31512. (PubMed:3208766)Curated
Sequence conflicti240 – 2401I → M in CAA32505. (PubMed:3208766)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti264 – 2641P → A.
VAR_002354
Natural varianti395 – 3951T → A.
VAR_002355

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei61 – 10444GVLKA…TENKS → A in isoform 2. 1 PublicationVSP_055482Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
UCSCiuc001qru.1. human. [P09104-1]

Polymorphism databases

DMDMi20981682.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS8570.1. [P09104-1 ]
PIRi JU0060. NOHUG.
RefSeqi NP_001966.1. NM_001975.2. [P09104-1 ]
UniGenei Hs.511915.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1TE6 X-ray 1.80 A/B 2-434 [» ]
2AKM X-ray 1.92 A/B 2-434 [» ]
2AKZ X-ray 1.36 A/B 2-434 [» ]
3UCC X-ray 1.50 A/B 2-434 [» ]
3UCD X-ray 1.41 A/B 2-434 [» ]
3UJE X-ray 1.55 A/B 2-434 [» ]
3UJF X-ray 2.10 A/B 2-434 [» ]
3UJR X-ray 1.40 A/B 2-434 [» ]
3UJS X-ray 1.65 A/B 2-434 [» ]
ProteinModelPortali P09104.
SMRi P09104. Positions 2-434.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108340. 44 interactions.
IntActi P09104. 21 interactions.
MINTi MINT-1367862.
STRINGi 9606.ENSP00000229277.

PTM databases

PhosphoSitei P09104.

Polymorphism databases

DMDMi 20981682.

2D gel databases

OGPi P09104.
UCD-2DPAGE P09104.

Proteomic databases

MaxQBi P09104.
PaxDbi P09104.
PRIDEi P09104.

Protocols and materials databases

DNASUi 2026.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000229277 ; ENSP00000229277 ; ENSG00000111674 . [P09104-1 ]
ENST00000535366 ; ENSP00000437402 ; ENSG00000111674 . [P09104-1 ]
ENST00000538763 ; ENSP00000441490 ; ENSG00000111674 . [P09104-2 ]
ENST00000541477 ; ENSP00000438873 ; ENSG00000111674 . [P09104-1 ]
GeneIDi 2026.
KEGGi hsa:2026.
UCSCi uc001qru.1. human. [P09104-1 ]

Organism-specific databases

CTDi 2026.
GeneCardsi GC12P007149.
HGNCi HGNC:3353. ENO2.
HPAi CAB000063.
MIMi 131360. gene.
neXtProti NX_P09104.
PharmGKBi PA27788.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0148.
GeneTreei ENSGT00550000074560.
HOGENOMi HOG000072174.
HOVERGENi HBG000067.
InParanoidi P09104.
KOi K01689.
OMAi ASTEVYH.
PhylomeDBi P09104.
TreeFami TF300391.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00187 .
BioCyci MetaCyc:HS10646-MONOMER.
Reactomei REACT_1383. Glycolysis.
REACT_1520. Gluconeogenesis.
SABIO-RK P09104.

Miscellaneous databases

ChiTaRSi ENO2. human.
EvolutionaryTracei P09104.
GeneWikii Enolase_2.
GenomeRNAii 2026.
NextBioi 35479101.
PMAP-CutDB P09104.
PROi P09104.
SOURCEi Search...

Gene expression databases

Bgeei P09104.
CleanExi HS_ENO2.
ExpressionAtlasi P09104. baseline and differential.
Genevestigatori P09104.

Family and domain databases

Gene3Di 3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
HAMAPi MF_00318. Enolase.
InterProi IPR000941. Enolase.
IPR020810. Enolase_C.
IPR029065. Enolase_C-like.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
IPR029017. Enolase_N_like.
[Graphical view ]
PANTHERi PTHR11902. PTHR11902. 1 hit.
Pfami PF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF001400. Enolase. 1 hit.
PRINTSi PR00148. ENOLASE.
SUPFAMi SSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
TIGRFAMsi TIGR01060. eno. 1 hit.
PROSITEi PS00164. ENOLASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] (ISOFORM 1), 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] (ISOFORM 1).
    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] (ISOFORM 1).
  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. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Caudate nucleus.
  7. "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] (ISOFORM 1).
  8. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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] (ISOFORM 1).
    Tissue: Placenta.
  10. 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, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  11. "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 (ISOFORM 1/2).
  12. "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].
  13. "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.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS.

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: October 29, 2014
This is version 180 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

External Data

Dasty 3