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Q9ER97

- NGB_MOUSE

UniProt

Q9ER97 - NGB_MOUSE

Protein

Neuroglobin

Gene

Ngb

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Involved in oxygen transport in the brain. Hexacoordinate globin, displaying competitive binding of oxygen or the distal His residue to the iron atom. Not capable of penetrating cell membranes. The deoxygenated form exhibits nitrite reductase activity inhibiting cellular respiration via NO-binding to cytochrome c oxidase. Involved in neuroprotection during oxidative stress. May exert its anti-apoptotic activity by acting to reset the trigger level of mitochondrial cytochrome c release necessary to commit the cells to apoptosis.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi64 – 641Iron (heme distal ligand)
    Metal bindingi96 – 961Iron (heme proximal ligand)

    GO - Molecular functioni

    1. heme binding Source: InterPro
    2. iron ion binding Source: InterPro
    3. oxygen binding Source: InterPro
    4. oxygen transporter activity Source: MGI

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. oxygen transport Source: MGI

    Keywords - Biological processi

    Apoptosis, Oxygen transport, Transport

    Keywords - Ligandi

    Heme, Iron, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Neuroglobin
    Gene namesi
    Name:Ngb
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 12

    Organism-specific databases

    MGIiMGI:2151886. Ngb.

    Subcellular locationi

    Perikaryon By similarity. Cytoplasm 1 Publication. Mitochondrion 1 Publication

    GO - Cellular componenti

    1. mitochondrion Source: UniProtKB-SubCell
    2. perikaryon Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi64 – 641H → L: Improved binding of dioxygen and carbon monoxide to the iron atom. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 151151NeuroglobinPRO_0000053392Add
    BLAST

    Post-translational modificationi

    A redox disulfide bond regulates the heme pocket coordination and the rate of nitrite reduction to NO.By similarity
    Phosphorylated in vitro by ERK1, ERK2 and PKA, and in vivo during hypoxia. Phosphorylation increases nitrite reductase activity By similarity.By similarity

    Keywords - PTMi

    Disulfide bond, Phosphoprotein

    Proteomic databases

    PRIDEiQ9ER97.

    Expressioni

    Tissue specificityi

    Predominantly expressed in brain.

    Gene expression databases

    ArrayExpressiQ9ER97.
    BgeeiQ9ER97.
    CleanExiMM_NGB.
    GenevestigatoriQ9ER97.

    Interactioni

    Subunit structurei

    Monomer. Homodimer and homotetramer; disulfide-linked Probable. Interacts with 14-3-3 By similarity.By similarityCurated

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000105806.

    Structurei

    Secondary structure

    1
    151
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi6 – 1712
    Helixi20 – 3415
    Helixi36 – 416
    Helixi44 – 463
    Helixi52 – 554
    Helixi59 – 7719
    Turni78 – 803
    Beta strandi82 – 854
    Helixi86 – 9914
    Helixi105 – 12117
    Helixi122 – 1243
    Helixi127 – 14519
    Helixi146 – 1483

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1Q1FX-ray1.50A1-151[»]
    1W92X-ray1.70A1-151[»]
    2VRYX-ray1.87A1-151[»]
    3GK9X-ray1.80A1-151[»]
    3GKTX-ray1.86A1-151[»]
    3GLNX-ray2.26A1-151[»]
    4MU5X-ray1.80A1-151[»]
    4NZIX-ray2.10A1-151[»]
    4O1TX-ray1.60A1-151[»]
    4O2GX-ray2.70A1-151[»]
    4O35X-ray1.80A1-151[»]
    ProteinModelPortaliQ9ER97.
    SMRiQ9ER97. Positions 3-150.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9ER97.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 149149GlobinAdd
    BLAST

    Sequence similaritiesi

    Belongs to the globin family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG317570.
    GeneTreeiENSGT00510000048375.
    HOVERGENiHBG039321.
    OrthoDBiEOG7JDR08.
    PhylomeDBiQ9ER97.
    TreeFamiTF333247.

    Family and domain databases

    Gene3Di1.10.490.10. 1 hit.
    InterProiIPR000971. Globin.
    IPR009050. Globin-like.
    IPR012292. Globin_dom.
    [Graphical view]
    PfamiPF00042. Globin. 1 hit.
    [Graphical view]
    SUPFAMiSSF46458. SSF46458. 1 hit.
    PROSITEiPS01033. GLOBIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9ER97-1 [UniParc]FASTAAdd to Basket

    « Hide

    MERPESELIR QSWRVVSRSP LEHGTVLFAR LFALEPSLLP LFQYNGRQFS    50
    SPEDCLSSPE FLDHIRKVML VIDAAVTNVE DLSSLEEYLT SLGRKHRAVG 100
    VRLSSFSTVG ESLLYMLEKC LGPDFTPATR TAWSRLYGAV VQAMSRGWDG 150
    E 151
    Length:151
    Mass (Da):17,037
    Last modified:March 1, 2001 - v1
    Checksum:i377BBE4BF723CCF1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ245945 mRNA. Translation: CAC11135.1.
    BC024263 mRNA. Translation: AAH24263.1.
    CCDSiCCDS36501.1.
    RefSeqiNP_071859.1. NM_022414.2.
    UniGeneiMm.41395.

    Genome annotation databases

    EnsembliENSMUST00000021420; ENSMUSP00000021420; ENSMUSG00000021032.
    GeneIDi64242.
    KEGGimmu:64242.
    UCSCiuc007oii.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ245945 mRNA. Translation: CAC11135.1 .
    BC024263 mRNA. Translation: AAH24263.1 .
    CCDSi CCDS36501.1.
    RefSeqi NP_071859.1. NM_022414.2.
    UniGenei Mm.41395.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1Q1F X-ray 1.50 A 1-151 [» ]
    1W92 X-ray 1.70 A 1-151 [» ]
    2VRY X-ray 1.87 A 1-151 [» ]
    3GK9 X-ray 1.80 A 1-151 [» ]
    3GKT X-ray 1.86 A 1-151 [» ]
    3GLN X-ray 2.26 A 1-151 [» ]
    4MU5 X-ray 1.80 A 1-151 [» ]
    4NZI X-ray 2.10 A 1-151 [» ]
    4O1T X-ray 1.60 A 1-151 [» ]
    4O2G X-ray 2.70 A 1-151 [» ]
    4O35 X-ray 1.80 A 1-151 [» ]
    ProteinModelPortali Q9ER97.
    SMRi Q9ER97. Positions 3-150.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000105806.

    Proteomic databases

    PRIDEi Q9ER97.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000021420 ; ENSMUSP00000021420 ; ENSMUSG00000021032 .
    GeneIDi 64242.
    KEGGi mmu:64242.
    UCSCi uc007oii.1. mouse.

    Organism-specific databases

    CTDi 58157.
    MGIi MGI:2151886. Ngb.

    Phylogenomic databases

    eggNOGi NOG317570.
    GeneTreei ENSGT00510000048375.
    HOVERGENi HBG039321.
    OrthoDBi EOG7JDR08.
    PhylomeDBi Q9ER97.
    TreeFami TF333247.

    Miscellaneous databases

    EvolutionaryTracei Q9ER97.
    NextBioi 319968.
    PROi Q9ER97.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9ER97.
    Bgeei Q9ER97.
    CleanExi MM_NGB.
    Genevestigatori Q9ER97.

    Family and domain databases

    Gene3Di 1.10.490.10. 1 hit.
    InterProi IPR000971. Globin.
    IPR009050. Globin-like.
    IPR012292. Globin_dom.
    [Graphical view ]
    Pfami PF00042. Globin. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46458. SSF46458. 1 hit.
    PROSITEi PS01033. GLOBIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A vertebrate globin expressed in the brain."
      Burmester T., Weich B., Reinhardt S., Hankeln T.
      Nature 407:520-522(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    2. "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].
      Tissue: Liver.
    3. "The heme environment of mouse neuroglobin. Evidence for the presence of two conformations of the heme pocket."
      Couture M., Burmester T., Hankeln T., Rousseau D.L.
      J. Biol. Chem. 276:36377-36382(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    4. "Biochemical characterization and ligand binding properties of neuroglobin, a novel member of the globin family."
      Dewilde S., Kiger L., Burmester T., Hankeln T., Baudin-Creuza V., Aerts T., Marden M.C., Caubergs R., Moens L.
      J. Biol. Chem. 276:38949-38955(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, QUATERNARY STRUCTURE, MUTAGENESIS OF HIS-64.
    5. "Mitochondrial distribution of neuroglobin and its response to oxygen-glucose deprivation in primary-cultured mouse cortical neurons."
      Yu Z., Xu J., Liu N., Wang Y., Li X., Pallast S., van Leyen K., Wang X.
      Neuroscience 218:235-242(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    6. "The structure of carbonmonoxy neuroglobin reveals a heme-sliding mechanism for control of ligand affinity."
      Vallone B., Nienhaus K., Matthes A., Brunori M., Nienhaus G.U.
      Proc. Natl. Acad. Sci. U.S.A. 101:17351-17356(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH CARBON MONOXIDE.
    7. "The structure of murine neuroglobin: Novel pathways for ligand migration and binding."
      Vallone B., Nienhaus K., Brunori M., Nienhaus G.U.
      Proteins 56:85-92(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN A HEXACOORDINATED FE(3+)-BOUND FORM.

    Entry informationi

    Entry nameiNGB_MOUSE
    AccessioniPrimary (citable) accession number: Q9ER97
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 20, 2003
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 91 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3