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P09104

- ENOG_HUMAN

UniProt

P09104 - ENOG_HUMAN

Protein

Gamma-enolase

Gene

ENO2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 179 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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

    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: UniProt
    4. perikaryon Source: Ensembl
    5. phosphopyruvate hydratase complex Source: InterPro
    6. photoreceptor inner segment Source: Ensembl
    7. plasma membrane Source: UniProtKB-SubCell

    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

    ArrayExpressiP09104.
    BgeeiP09104.
    CleanExiHS_ENO2.
    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. 42 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.
    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

    MSIEKIWARE ILDSRGNPTV EVDLYTAKGL FRAAVPSGAS TGIYEALELR    50
    DGDKQRYLGK GVLKAVDHIN STIAPALISS GLSVVEQEKL DNLMLELDGT 100
    ENKSKFGANA ILGVSLAVCK AGAAERELPL YRHIAQLAGN SDLILPVPAF 150
    NVINGGSHAG NKLAMQEFMI LPVGAESFRD AMRLGAEVYH TLKGVIKDKY 200
    GKDATNVGDE GGFAPNILEN SEALELVKEA IDKAGYTEKI VIGMDVAASE 250
    FYRDGKYDLD FKSPTDPSRY ITGDQLGALY QDFVRDYPVV SIEDPFDQDD 300
    WAAWSKFTAN VGIQIVGDDL TVTNPKRIER AVEEKACNCL LLKVNQIGSV 350
    TEAIQACKLA QENGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR 400
    SERLAKYNQL MRIEEELGDE ARFAGHNFRN PSVL 434
    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.
    PIRiJU0060. NOHUG.
    RefSeqiNP_001966.1. NM_001975.2.
    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.

    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.
    PIRi JU0060. NOHUG.
    RefSeqi NP_001966.1. NM_001975.2.
    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. 42 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.

    Organism-specific databases

    CTDi 2026.
    GeneCardsi GC12P007116.
    HGNCi HGNC:3353. ENO2.
    HPAi CAB000063.
    MIMi 131360. gene.
    neXtProti NX_P09104.
    PharmGKBi PA27788.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0148.
    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 8203.
    PMAP-CutDB P09104.
    PROi P09104.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P09104.
    Bgeei P09104.
    CleanExi HS_ENO2.
    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

    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 1, 2014
    This is version 179 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