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Q9NPG2

- NGB_HUMAN

UniProt

Q9NPG2 - NGB_HUMAN

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Protein

Neuroglobin

Gene

NGB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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-KW
Complete GO annotation...

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

BgeeiQ9NPG2.
CleanExiHS_NGB.
ExpressionAtlasiQ9NPG2. baseline.
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.
GeneTreeiENSGT00510000048375.
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

        10         20         30         40         50
MERPEPELIR QSWRAVSRSP LEHGTVLFAR LFALEPDLLP LFQYNCRQFS
60 70 80 90 100
SPEDCLSSPE FLDHIRKVML VIDAAVTNVE DLSSLEEYLA SLGRKHRAVG
110 120 130 140 150
VKLSSFSTVG ESLLYMLEKC LGPAFTPATR AAWSQLYGAV VQAMSRGWDG

E
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.
GeneTreei ENSGT00510000048375.
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

Bgeei Q9NPG2.
CleanExi HS_NGB.
ExpressionAtlasi Q9NPG2. baseline.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 114 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