Ngb
entrez
64242
canonical
uniprot
Q9ER97
canonical
ensembl
ENSMUSG00000021032
resolver
ensp
ENSMUSP00000021420
resolver
ensp
ENSMUSP00000105806
resolver
enst
ENSMUST00000021420
resolver
enst
ENSMUST00000110177
resolver
genesymbol
Ngb
resolver
uniprot
F8WJ84
resolver
uniprot
Q3USR6
resolver
uniprot
Q5ZPR7
resolver
uniprot_entry
F8WJ84_MOUSE
resolver
uniprot_entry
NGB_MOUSE
resolver
uniprot_entry
Q3USR6_MOUSE
resolver
uniprot_entry
Q5ZPR7_MOUSE
resolver
amino_acid_sequence
MERPESELIRQSWRVVSRSPLEHGTVLFARLFALEPSLLPLFQYNGRQFSSPEDCLSSPEFLDHIRKVMLVIDAAVTNVEDLSSLEEYLTSLGRKHRAVGVRLSSFSTVGESLLYMLEKCLGPDFTPATRTAWSRLYGAVVQAMSRGWDGE
uniprot
proteins
ec_number
1.7.-.-
uniprot
proteins
function
FUNCTION: Monomeric globin with a bis-histidyl six-coordinate heme-iron atom through which it can bind dioxygen, carbon monoxide and nitric oxide (PubMed:11029004, PubMed:11473111, PubMed:11473128). Could help transport oxygen and increase its availability to the metabolically active neuronal tissues, though its low quantity in tissues as well as its high affinity for dioxygen, which may limit its oxygen-releasing ability, argue against it (PubMed:11029004, PubMed:11473128). The ferrous/deoxygenated form exhibits a nitrite reductase activity and it could produce nitric oxide which in turn inhibits cellular respiration in response to hypoxia. In its ferrous/deoxygenated state, it may also exhibit GDI (Guanine nucleotide Dissociation Inhibitor) activity toward heterotrimeric G-alpha proteins, thereby regulating signal transduction to facilitate neuroprotective responses in the wake of hypoxia and associated oxidative stress (By similarity). {ECO:0000250|UniProtKB:Q9NPG2, ECO:0000269|PubMed:11029004, ECO:0000269|PubMed:11473111, ECO:0000269|PubMed:11473128}.
uniprot
proteins
mass_dalton
17037
uniprot
proteins
mutagenesis
MUTAGEN 64; /note="H->L: Improved binding of dioxygen and carbon monoxide to the iron atom."; /evidence="ECO:0000269|PubMed:11473128
uniprot
proteins
post_translational_modification
PTM: Phosphorylated during hypoxia by ERK1/ERK2. Phosphorylation regulates the heme pocket hexacoordination preventing the association of His-64 with the heme metal center. Thereby, promotes the access of dioxygen and nitrite to the heme and stimulates the nitrite reductase activity. Phosphorylation during hypoxia is stabilized by 14-3-3 proteins. {ECO:0000250|UniProtKB:Q9NPG2}.
uniprot
proteins
protein_family
Globin family
uniprot
proteins
pubmed
11029004
uniprot
proteins
pubmed
11473111
uniprot
proteins
pubmed
11473128
uniprot
proteins
pubmed
15162488
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15548613
uniprot
proteins
pubmed
22659017
uniprot
proteins
sequence_length
151
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:22659017}. Mitochondrion matrix {ECO:0000269|PubMed:22659017}. Note=Enriched in mitochondrial matrix upon oxygen-glucose deprivation. {ECO:0000269|PubMed:22659017}.
uniprot
proteins