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Q9NPG2

- NGB_HUMAN

UniProt

Q9NPG2 - NGB_HUMAN

Protein

Neuroglobin

Gene

NGB

Organism
Homo sapiens (Human)
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.5 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: UniProtKB

    GO - Biological processi

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

    Keywords - Biological processi

    Apoptosis, Oxygen transport, Transport

    Keywords - Ligandi

    Heme, Iron, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Neuroglobin
    Gene namesi
    Name:NGB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:14077. NGB.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA31612.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 151151NeuroglobinPRO_0000053390Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi46 ↔ 55Redox-active2 Publications

    Post-translational modificationi

    A redox disulfide bond regulates the heme pocket coordination and the rate of nitrite reduction to NO.
    Phosphorylated in vitro by ERK1, ERK2 and PKA, and in vivo during hypoxia. Phosphorylation increases nitrite reductase activity.1 Publication

    Keywords - PTMi

    Disulfide bond, Phosphoprotein

    Proteomic databases

    PaxDbiQ9NPG2.
    PRIDEiQ9NPG2.

    Expressioni

    Tissue specificityi

    Predominantly expressed in brain, the strongest expression is seen in the frontal lobe, the subthalamic nucleus and the thalamus.1 Publication

    Gene expression databases

    ArrayExpressiQ9NPG2.
    BgeeiQ9NPG2.
    CleanExiHS_NGB.
    GenevestigatoriQ9NPG2.

    Organism-specific databases

    HPAiCAB037319.

    Interactioni

    Subunit structurei

    Monomer. Homodimer and homotetramer; disulfide-linked By similarity. Interacts with 14-3-3.By similarity3 Publications

    Protein-protein interaction databases

    BioGridi121798. 3 interactions.
    STRINGi9606.ENSP00000298352.

    Structurei

    Secondary structure

    1
    151
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi6 – 138
    Turni14 – 185
    Helixi20 – 3415
    Helixi38 – 4912
    Helixi55 – 573
    Helixi59 – 7719
    Helixi79 – 857
    Helixi86 – 9813
    Helixi105 – 12117
    Helixi122 – 1243
    Helixi127 – 14418
    Helixi145 – 1484

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1OJ6X-ray1.95A/B/C/D1-151[»]
    4MPMX-ray1.74A/B1-151[»]
    ProteinModelPortaliQ9NPG2.
    SMRiQ9NPG2. Positions 2-149.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NPG2.

    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.
    HOGENOMiHOG000036573.
    HOVERGENiHBG039321.
    InParanoidiQ9NPG2.
    OMAiASIDICA.
    OrthoDBiEOG7JDR08.
    PhylomeDBiQ9NPG2.
    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.

    Q9NPG2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MERPEPELIR QSWRAVSRSP LEHGTVLFAR LFALEPDLLP LFQYNCRQFS    50
    SPEDCLSSPE FLDHIRKVML VIDAAVTNVE DLSSLEEYLA SLGRKHRAVG 100
    VKLSSFSTVG ESLLYMLEKC LGPAFTPATR AAWSQLYGAV VQAMSRGWDG 150
    E 151
    Length:151
    Mass (Da):16,933
    Last modified:October 1, 2000 - v1
    Checksum:i45A292A7D77B9CE3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ245944 Genomic DNA. Translation: CAC12994.1.
    AJ245946 mRNA. Translation: CAC11133.1.
    AF422796 Genomic DNA. Translation: AAL98923.1.
    AF422797 mRNA. Translation: AAL98924.1.
    AC007375 Genomic DNA. Translation: AAF63183.1.
    AC007954 Genomic DNA. Translation: AAF62557.1.
    BC032509 mRNA. Translation: AAH32509.1.
    CCDSiCCDS9856.1.
    RefSeqiNP_067080.1. NM_021257.3.
    UniGeneiHs.274363.

    Genome annotation databases

    EnsembliENST00000298352; ENSP00000298352; ENSG00000165553.
    GeneIDi58157.
    KEGGihsa:58157.
    UCSCiuc001xtg.1. human.

    Polymorphism databases

    DMDMi32171399.

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Neuroglobin entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ245944 Genomic DNA. Translation: CAC12994.1 .
    AJ245946 mRNA. Translation: CAC11133.1 .
    AF422796 Genomic DNA. Translation: AAL98923.1 .
    AF422797 mRNA. Translation: AAL98924.1 .
    AC007375 Genomic DNA. Translation: AAF63183.1 .
    AC007954 Genomic DNA. Translation: AAF62557.1 .
    BC032509 mRNA. Translation: AAH32509.1 .
    CCDSi CCDS9856.1.
    RefSeqi NP_067080.1. NM_021257.3.
    UniGenei Hs.274363.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1OJ6 X-ray 1.95 A/B/C/D 1-151 [» ]
    4MPM X-ray 1.74 A/B 1-151 [» ]
    ProteinModelPortali Q9NPG2.
    SMRi Q9NPG2. Positions 2-149.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121798. 3 interactions.
    STRINGi 9606.ENSP00000298352.

    Polymorphism databases

    DMDMi 32171399.

    Proteomic databases

    PaxDbi Q9NPG2.
    PRIDEi Q9NPG2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000298352 ; ENSP00000298352 ; ENSG00000165553 .
    GeneIDi 58157.
    KEGGi hsa:58157.
    UCSCi uc001xtg.1. human.

    Organism-specific databases

    CTDi 58157.
    GeneCardsi GC14M077731.
    HGNCi HGNC:14077. NGB.
    HPAi CAB037319.
    MIMi 605304. gene.
    neXtProti NX_Q9NPG2.
    PharmGKBi PA31612.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG317570.
    HOGENOMi HOG000036573.
    HOVERGENi HBG039321.
    InParanoidi Q9NPG2.
    OMAi ASIDICA.
    OrthoDBi EOG7JDR08.
    PhylomeDBi Q9NPG2.
    TreeFami TF333247.

    Miscellaneous databases

    EvolutionaryTracei Q9NPG2.
    GenomeRNAii 58157.
    NextBioi 64865.
    PROi Q9NPG2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NPG2.
    Bgeei Q9NPG2.
    CleanExi HS_NGB.
    Genevestigatori Q9NPG2.

    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 [GENOMIC DNA / MRNA], FUNCTION, TISSUE SPECIFICITY.
      Tissue: Brain.
    2. "Full-length cDNA cloning of human neuroglobin and tissue expression of rat neuroglobin."
      Zhang C.G., Wang C.L., Deng M.Y., Li L., Wang H.Y., Fan M., Xu W.L., Meng F.W., Qian L., He F.C.
      Biochem. Biophys. Res. Commun. 290:1411-1419(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "The DNA sequence and analysis of human chromosome 14."
      Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
      , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
      Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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: Brain.
    5. "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.
    6. "Coupling of the heme and an internal disulfide bond in human neuroglobin."
      Hamdane D., Kiger L., Dewilde S., Green B.N., Pesce A., Uzan J., Burmester T., Hankeln T., Bolognesi M., Moens L., Marden M.C.
      Micron 35:59-62(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISULFIDE BOND.
    7. "Zebrafish neuroglobin is a cell-membrane-penetrating globin."
      Watanabe S., Wakasugi K.
      Biochemistry 47:5266-5270(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. Cited for: FUNCTION IN APOPTOSIS.
    9. Cited for: FUNCTION, DISULFIDE BOND.
    10. "14-3-3 binding and phosphorylation of neuroglobin during hypoxia modulate six-to-five heme pocket coordination and rate of nitrite reduction to nitric oxide."
      Jayaraman T., Tejero J., Chen B.B., Blood A.B., Frizzell S., Shapiro C., Tiso M., Hood B.L., Wang X., Zhao X., Conrads T.P., Mallampalli R.K., Gladwin M.T.
      J. Biol. Chem. 286:42679-42689(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION DURING HYPOXIA, INTERACTION WITH 14-3-3.
    11. "Human brain neuroglobin structure reveals a distinct mode of controlling oxygen affinity."
      Pesce A., Dewilde S., Nardini M., Moens L., Ascenzi P., Hankeln T., Burmester T., Bolognesi M.
      Structure 11:1087-1095(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN A HEXACOORDINATED FE(3+)-BOUND FORM.

    Entry informationi

    Entry nameiNGB_HUMAN
    AccessioniPrimary (citable) accession number: Q9NPG2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 20, 2003
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 113 of the entry and version 1 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 14
      Human chromosome 14: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3