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Protein

Neuroglobin

Gene

Ngb

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi64Iron (heme distal ligand)Combined sources1 Publication1
Metal bindingi96Iron (heme proximal ligand)Combined sources2 Publications1

GO - Molecular functioni

  • heme binding Source: InterPro
  • metal ion binding Source: UniProtKB-KW
  • oxygen binding Source: InterPro
  • oxygen transporter activity Source: MGI

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • oxygen transport Source: MGI
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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:2151886. Ngb.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi64H → L: Improved binding of dioxygen and carbon monoxide to the iron atom. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000533921 – 151NeuroglobinAdd BLAST151

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

PaxDbiQ9ER97.
PRIDEiQ9ER97.

Expressioni

Tissue specificityi

Predominantly expressed in brain.

Gene expression databases

BgeeiENSMUSG00000021032.
CleanExiMM_NGB.
ExpressionAtlasiQ9ER97. baseline and differential.
GenevisibleiQ9ER97. MM.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000021420.

Structurei

Secondary structure

1151
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 17Combined sources12
Helixi20 – 34Combined sources15
Helixi36 – 41Combined sources6
Helixi44 – 46Combined sources3
Helixi52 – 55Combined sources4
Helixi59 – 77Combined sources19
Turni78 – 80Combined sources3
Beta strandi82 – 85Combined sources4
Helixi86 – 99Combined sources14
Helixi105 – 121Combined sources17
Helixi122 – 124Combined sources3
Helixi127 – 145Combined sources19
Helixi146 – 148Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4O4TX-ray1.90A1-151[»]
4O4ZX-ray1.70A1-151[»]
5EETX-ray2.00A3-150[»]
5EOHX-ray1.90A3-150[»]
5EQMX-ray2.05A3-150[»]
5EU2X-ray2.00A3-150[»]
5EV5X-ray2.00A3-150[»]
5EYJX-ray2.40A3-150[»]
5EYSX-ray1.75A3-150[»]
5F0BX-ray2.15A3-151[»]
5F2AX-ray2.10A1-151[»]
ProteinModelPortaliQ9ER97.
SMRiQ9ER97.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9ER97.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 149GlobinAdd BLAST149

Sequence similaritiesi

Belongs to the globin family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3378. Eukaryota.
COG1018. LUCA.
GeneTreeiENSGT00510000048375.
HOVERGENiHBG039321.
InParanoidiQ9ER97.
PhylomeDBiQ9ER97.
TreeFamiTF333247.

Family and domain databases

Gene3Di1.10.490.10. 1 hit.
InterProiIPR000971. Globin.
IPR009050. Globin-like.
IPR012292. Globin/Proto.
[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

        10         20         30         40         50
MERPESELIR QSWRVVSRSP LEHGTVLFAR LFALEPSLLP LFQYNGRQFS
60 70 80 90 100
SPEDCLSSPE FLDHIRKVML VIDAAVTNVE DLSSLEEYLT SLGRKHRAVG
110 120 130 140 150
VRLSSFSTVG ESLLYMLEKC LGPDFTPATR TAWSRLYGAV VQAMSRGWDG

E
Length:151
Mass (Da):17,037
Last modified:March 1, 2001 - v1
Checksum:i377BBE4BF723CCF1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
AJ245945 mRNA. Translation: CAC11135.1.
BC024263 mRNA. Translation: AAH24263.1.
CCDSiCCDS36501.1.
RefSeqiNP_071859.1. NM_022414.2.
UniGeneiMm.41395.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4O4TX-ray1.90A1-151[»]
4O4ZX-ray1.70A1-151[»]
5EETX-ray2.00A3-150[»]
5EOHX-ray1.90A3-150[»]
5EQMX-ray2.05A3-150[»]
5EU2X-ray2.00A3-150[»]
5EV5X-ray2.00A3-150[»]
5EYJX-ray2.40A3-150[»]
5EYSX-ray1.75A3-150[»]
5F0BX-ray2.15A3-151[»]
5F2AX-ray2.10A1-151[»]
ProteinModelPortaliQ9ER97.
SMRiQ9ER97.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000021420.

Proteomic databases

PaxDbiQ9ER97.
PRIDEiQ9ER97.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi58157.
MGIiMGI:2151886. Ngb.

Phylogenomic databases

eggNOGiKOG3378. Eukaryota.
COG1018. LUCA.
GeneTreeiENSGT00510000048375.
HOVERGENiHBG039321.
InParanoidiQ9ER97.
PhylomeDBiQ9ER97.
TreeFamiTF333247.

Miscellaneous databases

EvolutionaryTraceiQ9ER97.
PROiQ9ER97.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000021032.
CleanExiMM_NGB.
ExpressionAtlasiQ9ER97. baseline and differential.
GenevisibleiQ9ER97. MM.

Family and domain databases

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

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: November 30, 2016
This is version 108 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.