NGB
entrez
58157
canonical
uniprot
Q9NPG2
canonical
ensembl
ENSG00000165553
resolver
ensp
ENSP00000298352
resolver
enst
ENST00000298352
resolver
genesymbol
NGB
resolver
hgnc
HGNC:14077
resolver
uniprot
A0M8W9
resolver
uniprot_entry
A0M8W9_HUMAN
resolver
uniprot_entry
NGB_HUMAN
resolver
amino_acid_sequence
MERPEPELIRQSWRAVSRSPLEHGTVLFARLFALEPDLLPLFQYNCRQFSSPEDCLSSPEFLDHIRKVMLVIDAAVTNVEDLSSLEEYLASLGRKHRAVGVKLSSFSTVGESLLYMLEKCLGPAFTPATRAAWSQLYGAVVQAMSRGWDGE
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:11473128, PubMed:12962627, PubMed:24699645). 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:11473128, PubMed:12860983, PubMed:12962627, PubMed:24699645). 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 (PubMed:21296891). 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 (PubMed:12860983, PubMed:18302932). {ECO:0000269|PubMed:11473128, ECO:0000269|PubMed:12860983, ECO:0000269|PubMed:12962627, ECO:0000269|PubMed:18302932, ECO:0000269|PubMed:21296891, ECO:0000269|PubMed:24699645}.
uniprot
proteins
mass_dalton
16933
uniprot
proteins
mutagenesis
MUTAGEN 17; /note="S->A: No effect on interaction with 14-3-3 proteins."; /evidence="ECO:0000269|PubMed:21965683"; MUTAGEN 46; /note="C->A: Decreased nitrite reductase activity."; /evidence="ECO:0000269|PubMed:21296891"; MUTAGEN 46; /note="C->S: Loss of intramolecular disulfide bond."; /evidence="ECO:0000269|PubMed:12860983"; MUTAGEN 50; /note="S->A: Decreased interaction with 14-3-3 proteins."; /evidence="ECO:0000269|PubMed:21965683"; MUTAGEN 55; /note="C->A: Decreased affinity for nitrite. Decreased nitrite reductase activity."; /evidence="ECO:0000269|PubMed:21296891"; MUTAGEN 55; /note="C->S: Loss of intramolecular disulfide bond."; /evidence="ECO:0000269|PubMed:12860983"; MUTAGEN 64; /note="H->L,Q: Increased nitrite reductase activity."; /evidence="ECO:0000269|PubMed:21296891"; MUTAGEN 120; /note="C->S: No effect on disulfide bond."; /evidence="ECO:0000269|PubMed:12860983
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:0000269|PubMed:21965683}.; PTM: An intramolecular Cys-46/Cys-55 disulfide bond, not necessarily present in orthologs, 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. {ECO:0000269|PubMed:15036292, ECO:0000269|PubMed:21296891}.
uniprot
proteins
protein_family
Globin family
uniprot
proteins
pubmed
11029004
uniprot
proteins
pubmed
11473128
uniprot
proteins
pubmed
11820779
uniprot
proteins
pubmed
12508121
uniprot
proteins
pubmed
12860983
uniprot
proteins
pubmed
12962627
uniprot
proteins
pubmed
15036292
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
18302932
uniprot
proteins
pubmed
21296891
uniprot
proteins
pubmed
21965683
uniprot
proteins
pubmed
24699645
uniprot
proteins
sequence_length
151
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9ER97}. Mitochondrion matrix {ECO:0000250|UniProtKB:Q9ER97}. Note=Enriched in mitochondrial matrix upon oxygen-glucose deprivation. {ECO:0000250|UniProtKB:Q9ER97}.
uniprot
proteins