Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P13929

- ENOB_HUMAN

UniProt

P13929 - ENOB_HUMAN

Protein

Beta-enolase

Gene

ENO3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 158 (01 Oct 2014)
      Sequence version 5 (28 Nov 2012)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Appears to have a function in striated muscle development and regeneration.

    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 – 2451MagnesiumBy similarity
    Metal bindingi293 – 2931MagnesiumBy similarity
    Binding sitei293 – 2931SubstrateBy similarity
    Metal bindingi318 – 3181MagnesiumBy similarity
    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. aging Source: Ensembl
    2. carbohydrate metabolic process Source: Reactome
    3. gluconeogenesis Source: Reactome
    4. glucose metabolic process Source: Reactome
    5. glycolytic process Source: Reactome
    6. response to drug Source: Ensembl
    7. skeletal muscle tissue regeneration Source: Ensembl
    8. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:ENSG00000108515-MONOMER.
    ReactomeiREACT_1383. Glycolysis.
    REACT_1520. Gluconeogenesis.
    SABIO-RKP13929.
    UniPathwayiUPA00109; UER00187.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-enolase (EC:4.2.1.11)
    Alternative name(s):
    2-phospho-D-glycerate hydro-lyase
    Enolase 3
    Muscle-specific enolase
    Short name:
    MSE
    Skeletal muscle enolase
    Gene namesi
    Name:ENO3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:3354. ENO3.

    Subcellular locationi

    Cytoplasm
    Note: Localized to the Z line. Some colocalization with CKM at M-band By similarity.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. extracellular space Source: UniProt
    4. phosphopyruvate hydratase complex Source: InterPro
    5. plasma membrane Source: HPA

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Glycogen storage disease 13 (GSD13) [MIM:612932]: A metabolic disorder that results in exercise-induced myalgias, generalized muscle weakness and fatigability. It is characterized by increased serum creatine kinase and decreased enolase 3 activity. Dramatically reduced protein levels with focal sarcoplasmic accumulation of glycogen-beta particles are detected on ultrastructural analysis.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti156 – 1561G → D in GSD13; when associated with E-374. 1 Publication
    Corresponds to variant rs121918403 [ dbSNP | Ensembl ].
    VAR_020620
    Natural varianti374 – 3741G → E in GSD13; when associated with D-156. 1 Publication
    VAR_020621

    Keywords - Diseasei

    Disease mutation, Glycogen storage disease

    Organism-specific databases

    MIMi612932. phenotype.
    Orphaneti99849. Glycogen storage disease due to muscle beta-enolase deficiency.
    PharmGKBiPA27789.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 434433Beta-enolasePRO_0000134107Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP13929.
    PaxDbiP13929.
    PRIDEiP13929.

    2D gel databases

    UCD-2DPAGEP13929.

    PTM databases

    PhosphoSiteiP13929.

    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.

    Gene expression databases

    ArrayExpressiP13929.
    BgeeiP13929.
    CleanExiHS_ENO3.
    GenevestigatoriP13929.

    Organism-specific databases

    HPAiHPA000793.

    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. Interacts with PNKD.1 Publication

    Protein-protein interaction databases

    BioGridi108341. 10 interactions.
    IntActiP13929. 17 interactions.
    STRINGi9606.ENSP00000324105.

    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
    Beta strandi43 – 453
    Helixi57 – 593
    Helixi63 – 719
    Helixi73 – 797
    Helixi87 – 9812
    Turni104 – 1063
    Helixi108 – 12518
    Helixi130 – 1389
    Beta strandi150 – 1545
    Helixi156 – 1583
    Beta strandi159 – 1624
    Beta strandi167 – 1715
    Helixi178 – 20023
    Helixi220 – 23415
    Turni237 – 2393
    Beta strandi241 – 2455
    Helixi248 – 2514
    Turni259 – 2624
    Helixi267 – 2693
    Helixi273 – 28614
    Beta strandi289 – 2935
    Helixi301 – 3099
    Beta strandi313 – 3186
    Turni319 – 3235
    Helixi325 – 33410
    Beta strandi338 – 3425
    Helixi344 – 3474
    Helixi350 – 36213
    Beta strandi366 – 3705
    Helixi380 – 3889
    Beta strandi391 – 3944
    Helixi401 – 41717
    Helixi418 – 4203
    Helixi425 – 4273

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2XSXX-ray1.70A/B1-434[»]
    ProteinModelPortaliP13929.
    SMRiP13929. Positions 1-434.
    ModBaseiSearch...
    MobiDBiSearch...

    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.
    InParanoidiP13929.
    KOiK01689.
    OMAiGELYKNF.
    PhylomeDBiP13929.
    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 (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P13929-1) [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

    MAMQKIFARE ILDSRGNPTV EVDLHTAKGR FRAAVPSGAS TGIYEALELR    50
    DGDKGRYLGK GVLKAVENIN NTLGPALLQK KLSVVDQEKV DKFMIELDGT 100
    ENKSKFGANA ILGVSLAVCK AGAAEKGVPL YRHIADLAGN PDLILPVPAF 150
    NVINGGSHAG NKLAMQEFMI LPVGASSFKE AMRIGAEVYH HLKGVIKAKY 200
    GKDATNVGDE GGFAPNILEN NEALELLKTA IQAAGYPDKV VIGMDVAASE 250
    FYRNGKYDLD FKSPDDPARH ITGEKLGELY KSFIKNYPVV SIEDPFDQDD 300
    WATWTSFLSG VNIQIVGDDL TVTNPKRIAQ AVEKKACNCL LLKVNQIGSV 350
    TESIQACKLA QSNGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR 400
    SERLAKYNQL MRIEEALGDK AIFAGRKFRN PKAK 434
    Length:434
    Mass (Da):46,987
    Last modified:November 28, 2012 - v5
    Checksum:i4D9D8DCF32CF153F
    GO
    Isoform 2 (identifier: P13929-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         150-177: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:406
    Mass (Da):44,115
    Checksum:iE0D4621669448D46
    GO
    Isoform 3 (identifier: P13929-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         61-104: GVLKAVENINNTLGPALLQKKLSVVDQEKVDKFMIELDGTENKS → A

    Note: No experimental confirmation available.

    Show »
    Length:391
    Mass (Da):42,248
    Checksum:i0B6DB38924087E00
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti71 – 711N → S.3 Publications
    Corresponds to variant rs238238 [ dbSNP | Ensembl ].
    VAR_020618
    Natural varianti85 – 851V → A.4 Publications
    Corresponds to variant rs238239 [ dbSNP | Ensembl ].
    VAR_020619
    Natural varianti156 – 1561G → D in GSD13; when associated with E-374. 1 Publication
    Corresponds to variant rs121918403 [ dbSNP | Ensembl ].
    VAR_020620
    Natural varianti374 – 3741G → E in GSD13; when associated with D-156. 1 Publication
    VAR_020621

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei61 – 10444GVLKA…TENKS → A in isoform 3. 1 PublicationVSP_037752Add
    BLAST
    Alternative sequencei150 – 17728Missing in isoform 2. 1 PublicationVSP_037753Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X16504 mRNA. Translation: CAA34513.1.
    X51957 mRNA. Translation: CAA36216.1.
    X55976 Genomic DNA. Translation: CAA39446.1.
    X56832 Genomic DNA. Translation: CAA40163.1.
    AK300662 mRNA. Translation: BAG62348.1.
    AK300709 mRNA. Translation: BAG62388.1.
    AC004771 Genomic DNA. No translation available.
    AC109333 Genomic DNA. No translation available.
    CH471108 Genomic DNA. Translation: EAW90375.1.
    CH471108 Genomic DNA. Translation: EAW90379.1.
    CH471108 Genomic DNA. Translation: EAW90380.1.
    BC017249 mRNA. Translation: AAH17249.1.
    CCDSiCCDS11062.1. [P13929-1]
    CCDS54070.1. [P13929-3]
    PIRiS06756.
    RefSeqiNP_001180432.1. NM_001193503.1. [P13929-3]
    NP_001967.3. NM_001976.4. [P13929-1]
    NP_443739.3. NM_053013.3. [P13929-1]
    UniGeneiHs.224171.

    Genome annotation databases

    EnsembliENST00000323997; ENSP00000324105; ENSG00000108515. [P13929-1]
    ENST00000518175; ENSP00000431087; ENSG00000108515. [P13929-1]
    ENST00000519584; ENSP00000430636; ENSG00000108515. [P13929-3]
    GeneIDi2027.
    KEGGihsa:2027.
    UCSCiuc002gab.4. human. [P13929-1]
    uc010vss.2. human. [P13929-3]

    Polymorphism databases

    DMDMi425906077.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X16504 mRNA. Translation: CAA34513.1 .
    X51957 mRNA. Translation: CAA36216.1 .
    X55976 Genomic DNA. Translation: CAA39446.1 .
    X56832 Genomic DNA. Translation: CAA40163.1 .
    AK300662 mRNA. Translation: BAG62348.1 .
    AK300709 mRNA. Translation: BAG62388.1 .
    AC004771 Genomic DNA. No translation available.
    AC109333 Genomic DNA. No translation available.
    CH471108 Genomic DNA. Translation: EAW90375.1 .
    CH471108 Genomic DNA. Translation: EAW90379.1 .
    CH471108 Genomic DNA. Translation: EAW90380.1 .
    BC017249 mRNA. Translation: AAH17249.1 .
    CCDSi CCDS11062.1. [P13929-1 ]
    CCDS54070.1. [P13929-3 ]
    PIRi S06756.
    RefSeqi NP_001180432.1. NM_001193503.1. [P13929-3 ]
    NP_001967.3. NM_001976.4. [P13929-1 ]
    NP_443739.3. NM_053013.3. [P13929-1 ]
    UniGenei Hs.224171.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2XSX X-ray 1.70 A/B 1-434 [» ]
    ProteinModelPortali P13929.
    SMRi P13929. Positions 1-434.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108341. 10 interactions.
    IntActi P13929. 17 interactions.
    STRINGi 9606.ENSP00000324105.

    PTM databases

    PhosphoSitei P13929.

    Polymorphism databases

    DMDMi 425906077.

    2D gel databases

    UCD-2DPAGE P13929.

    Proteomic databases

    MaxQBi P13929.
    PaxDbi P13929.
    PRIDEi P13929.

    Protocols and materials databases

    DNASUi 2027.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000323997 ; ENSP00000324105 ; ENSG00000108515 . [P13929-1 ]
    ENST00000518175 ; ENSP00000431087 ; ENSG00000108515 . [P13929-1 ]
    ENST00000519584 ; ENSP00000430636 ; ENSG00000108515 . [P13929-3 ]
    GeneIDi 2027.
    KEGGi hsa:2027.
    UCSCi uc002gab.4. human. [P13929-1 ]
    uc010vss.2. human. [P13929-3 ]

    Organism-specific databases

    CTDi 2027.
    GeneCardsi GC17P004851.
    H-InvDB HIX0013457.
    HGNCi HGNC:3354. ENO3.
    HPAi HPA000793.
    MIMi 131370. gene.
    612932. phenotype.
    neXtProti NX_P13929.
    Orphaneti 99849. Glycogen storage disease due to muscle beta-enolase deficiency.
    PharmGKBi PA27789.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0148.
    HOGENOMi HOG000072174.
    HOVERGENi HBG000067.
    InParanoidi P13929.
    KOi K01689.
    OMAi GELYKNF.
    PhylomeDBi P13929.
    TreeFami TF300391.

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00187 .
    BioCyci MetaCyc:ENSG00000108515-MONOMER.
    Reactomei REACT_1383. Glycolysis.
    REACT_1520. Gluconeogenesis.
    SABIO-RK P13929.

    Miscellaneous databases

    GeneWikii ENO3.
    GenomeRNAii 2027.
    NextBioi 8207.
    PROi P13929.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P13929.
    Bgeei P13929.
    CleanExi HS_ENO3.
    Genevestigatori P13929.

    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. "Structure of human muscle (beta) enolase mRNA and protein deduced from a genomic clone."
      Peshavaria M., Hinks L.J., Day I.N.M.
      Nucleic Acids Res. 17:8862-8862(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Nucleotide sequence of a cDNA encoding the human muscle-specific enolase (MSE)."
      Cali L., Feo S., Oliva D., Giallongo A.
      Nucleic Acids Res. 18:1893-1893(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ALA-85.
    3. "Molecular structure of the human muscle-specific enolase gene (ENO3)."
      Peshavaria M., Day I.N.M.
      Biochem. J. 275:427-433(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
    4. "Structural features of the human gene for muscle-specific enolase. Differential splicing in the 5'-untranslated sequence generates two forms of mRNA."
      Giallongo A., Venturella S., Oliva D., Barbieri G., Rubino P., Feo S.
      Eur. J. Biochem. 214:367-374(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANTS SER-71 AND ALA-85.
    5. "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] (ISOFORMS 2 AND 3), VARIANTS SER-71 AND ALA-85.
      Tissue: Skeletal muscle.
    6. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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), VARIANTS SER-71 AND ALA-85.
      Tissue: Muscle.
    9. "Characterization of MR-1, a novel myofibrillogenesis regulator in human muscle."
      Li T.-B., Liu X.-H., Feng S., Hu Y., Yang W.-X., Han Y., Wang Y.-G., Gong L.-M.
      Acta Biochim. Biophys. Sin. 36:412-418(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PNKD.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    12. Cited for: VARIANTS GSD13 ASP-156 AND GLU-374.

    Entry informationi

    Entry nameiENOB_HUMAN
    AccessioniPrimary (citable) accession number: P13929
    Secondary accession number(s): B4DUI6
    , B4DUM6, D3DTL2, E7ENK8, Q96AE2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: November 28, 2012
    Last modified: October 1, 2014
    This is version 158 of the entry and version 5 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, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: 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