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Q9NPG2 (NGB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Neuroglobin
Gene names
Name:NGB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length151 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.5 Ref.7 Ref.8 Ref.9

Subunit structure

Monomer. Homodimer and homotetramer; disulfide-linked By similarity. Interacts with 14-3-3. Ref.6 Ref.9 Ref.10

Subcellular location

Perikaryon By similarity. Cytoplasm. Mitochondrion.

Tissue specificity

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

Post-translational modification

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. Ref.10

Sequence similarities

Belongs to the globin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 151151Neuroglobin
PRO_0000053390

Regions

Region1 – 149149Globin

Sites

Metal binding641Iron (heme distal ligand)
Metal binding961Iron (heme proximal ligand)

Amino acid modifications

Disulfide bond46 ↔ 55Redox-active Ref.6 Ref.9

Secondary structure

..................... 151
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9NPG2 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 45A292A7D77B9CE3

FASTA15116,933
        10         20         30         40         50         60 
MERPEPELIR QSWRAVSRSP LEHGTVLFAR LFALEPDLLP LFQYNCRQFS SPEDCLSSPE 

        70         80         90        100        110        120 
FLDHIRKVML VIDAAVTNVE DLSSLEEYLA SLGRKHRAVG VKLSSFSTVG ESLLYMLEKC 

       130        140        150 
LGPAFTPATR AAWSQLYGAV VQAMSRGWDG E 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"A role for human neuroglobin in apoptosis."
Brittain T., Skommer J., Henty K., Birch N., Raychaudhuri S.
IUBMB Life 62:878-885(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN APOPTOSIS.
[9]"Human neuroglobin functions as a redox-regulated nitrite reductase."
Tiso M., Tejero J., Basu S., Azarov I., Wang X., Simplaceanu V., Frizzell S., Jayaraman T., Geary L., Shapiro C., Ho C., Shiva S., Kim-Shapiro D.B., Gladwin M.T.
J. Biol. Chem. 286:18277-18289(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

Wikipedia

Neuroglobin entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS9856.1.
RefSeqNP_067080.1. NM_021257.3.
UniGeneHs.274363.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1OJ6X-ray1.95A/B/C/D1-151[»]
4MPMX-ray1.74A/B1-151[»]
ProteinModelPortalQ9NPG2.
SMRQ9NPG2. Positions 2-149.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121798. 3 interactions.
STRING9606.ENSP00000298352.

Polymorphism databases

DMDM32171399.

Proteomic databases

PaxDbQ9NPG2.
PRIDEQ9NPG2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000298352; ENSP00000298352; ENSG00000165553.
GeneID58157.
KEGGhsa:58157.
UCSCuc001xtg.1. human.

Organism-specific databases

CTD58157.
GeneCardsGC14M077731.
HGNCHGNC:14077. NGB.
HPACAB037319.
MIM605304. gene.
neXtProtNX_Q9NPG2.
PharmGKBPA31612.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG317570.
HOGENOMHOG000036573.
HOVERGENHBG039321.
InParanoidQ9NPG2.
OMAASIDICA.
OrthoDBEOG7JDR08.
PhylomeDBQ9NPG2.
TreeFamTF333247.

Gene expression databases

ArrayExpressQ9NPG2.
BgeeQ9NPG2.
CleanExHS_NGB.
GenevestigatorQ9NPG2.

Family and domain databases

Gene3D1.10.490.10. 1 hit.
InterProIPR000971. Globin.
IPR009050. Globin-like.
IPR012292. Globin_dom.
[Graphical view]
PfamPF00042. Globin. 1 hit.
[Graphical view]
SUPFAMSSF46458. SSF46458. 1 hit.
PROSITEPS01033. GLOBIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9NPG2.
GenomeRNAi58157.
NextBio64865.
PROQ9NPG2.
SOURCESearch...

Entry information

Entry nameNGB_HUMAN
AccessionPrimary (citable) accession number: Q9NPG2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: October 1, 2000
Last modified: July 9, 2014
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM