NCF1
entrez
653361
canonical
uniprot
P14598
canonical
ensembl
ENSG00000158517
resolver
ensp
ENSP00000289473
resolver
genesymbol
NCF1
resolver
genesymbol_syn
NOXO2
resolver
genesymbol_syn
SH3PXD1A
resolver
hgnc
HGNC:7660
resolver
uniprot
A6NEH2
resolver
uniprot
A8K7S9
resolver
uniprot
O43842
resolver
uniprot
Q2PP07
resolver
uniprot
Q53FR5
resolver
uniprot
Q9BU90
resolver
uniprot
Q9BXI7
resolver
uniprot
Q9BXI8
resolver
uniprot
Q9UDV9
resolver
uniprot
Q9UMU2
resolver
uniprot_entry
NCF1_HUMAN
resolver
uniprot_sec
A6NEH2
resolver
uniprot_sec
A8K7S9
resolver
uniprot_sec
O43842
resolver
uniprot_sec
Q2PP07
resolver
uniprot_sec
Q53FR5
resolver
uniprot_sec
Q9BU90
resolver
uniprot_sec
Q9BXI7
resolver
uniprot_sec
Q9BXI8
resolver
uniprot_sec
Q9UDV9
resolver
uniprot_sec
Q9UMU2
resolver
amino_acid_sequence
MGDTFIRHIALLGFEKRFVPSQHYVYMFLVKWQDLSEKVVYRRFTEIYEFHKTLKEMFPIEAGAINPENRIIPHLPAPKWFDGQRAAENRQGTLTEYCSTLMSLPTKISRCPHLLDFFKVRPDDLKLPTDNQTKKPETYLMPKDGKSTATDITGPIILQTYRAIANYEKTSGSEMALSTGDVVEVVEKSESGWWFCQMKAKRGWIPASFLEPLDSPDETEDPEPNYAGEPYVAIKAYTAVEGDEVSLLEGEAVEVIHKLLDGWWVIRKDDVTGYFPSMYLQKSGQDVSQAQRQIKRGAPPRRSSIRNAHSIHQRSRKRLSQDAYRRNSVRFLQQRRRQARPGPQSPGSPLEEERQTQRSKPQPAVPPRPSADLILNRCSESTKRKLASAV
uniprot
proteins
disease_involvement
DISEASE: Granulomatous disease, chronic, autosomal recessive, 1 (CGD1) [MIM:233700]: A form of chronic granulomatous disease, a primary immunodeficiency characterized by severe recurrent bacterial and fungal infections, along with manifestations of chronic granulomatous inflammation. It results from an impaired ability of phagocytes to mount a burst of reactive oxygen species in response to pathogens. {ECO:0000269|PubMed:11133775, ECO:0000269|PubMed:23910690}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Subunit of the phagocyte NADPH oxidase complex that mediates the transfer of electrons from cytosolic NADPH to O2 to produce the superoxide anion (O2(-)) (PubMed:2547247, PubMed:2550933, PubMed:38355798). In the activated complex, electrons are first transferred from NADPH to flavin adenine dinucleotide (FAD) and subsequently transferred via two heme molecules to molecular oxygen, producing superoxide through an outer-sphere reaction (PubMed:38355798). Activation of the NADPH oxidase complex is initiated by the assembly of cytosolic subunits of the NADPH oxidase complex with the core NADPH oxidase complex to form a complex at the plasma membrane or phagosomal membrane (PubMed:38355798). This activation process is initiated by phosphorylation dependent binding of the cytosolic NCF1/p47-phox subunit to the C-terminus of CYBA/p22-phox (PubMed:12732142, PubMed:19801500). {ECO:0000269|PubMed:12732142, ECO:0000269|PubMed:19801500, ECO:0000269|PubMed:2547247, ECO:0000269|PubMed:2550933, ECO:0000269|PubMed:38355798}.
uniprot
proteins
mass_dalton
44682
uniprot
proteins
mutagenesis
MUTAGEN 43; /note="R->Q: Reduces affinity for membranes enriched in phosphatidylinositol 3,4-bisphosphate."; /evidence="ECO:0000269|PubMed:12356722"; MUTAGEN 90; /note="R->A: Reduces affinity for membranes enriched in phosphatidylinositol 3,4-bisphosphate."; /evidence="ECO:0000269|PubMed:12356722"; MUTAGEN 263; /note="W->R: Abolishes autoinhibition and promotes phospholipid binding."; /evidence="ECO:0000269|PubMed:12356722"; MUTAGEN 303; /note="S->E: Abolishes autoinhibition and promotes phospholipid binding; when associated with E-304; E-328; E-359 and E-370."; /evidence="ECO:0000269|PubMed:12356722"; MUTAGEN 304; /note="S->E: Abolishes autoinhibition and promotes phospholipid binding; when associated with E-303; E-328; E-359 and E-370."; /evidence="ECO:0000269|PubMed:12356722"; MUTAGEN 328; /note="S->E: Abolishes autoinhibition and promotes phospholipid binding; when associated with E-303; E-304; E-359 and E-370."; /evidence="ECO:0000269|PubMed:12356722"; MUTAGEN 359; /note="S->E: Abolishes autoinhibition and promotes phospholipid binding; when associated with E-303; E-304; E-328 and E-370."; /evidence="ECO:0000269|PubMed:12356722"; MUTAGEN 370; /note="S->E: Abolishes autoinhibition and promotes phospholipid binding; when associated with E-303; E-304; E-328 and E-359."; /evidence="ECO:0000269|PubMed:12356722
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by PRKCD; phosphorylation induces activation of NCF1, leading to assembly and activation of the NADPH oxidase complex. {ECO:0000269|PubMed:19801500, ECO:0000269|PubMed:8089108}.
uniprot
proteins
pubmed
10772875
uniprot
proteins
pubmed
11133775
uniprot
proteins
pubmed
11373621
uniprot
proteins
pubmed
11740866
uniprot
proteins
pubmed
12023963
uniprot
proteins
pubmed
12169629
uniprot
proteins
pubmed
12356722
uniprot
proteins
pubmed
12716910
uniprot
proteins
pubmed
12732142
uniprot
proteins
pubmed
12853948
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15147273
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15657040
uniprot
proteins
pubmed
16052631
uniprot
proteins
pubmed
16326715
uniprot
proteins
pubmed
19718658
uniprot
proteins
pubmed
19801500
uniprot
proteins
pubmed
19807924
uniprot
proteins
pubmed
2011585
uniprot
proteins
pubmed
23910690
uniprot
proteins
pubmed
2398896
uniprot
proteins
pubmed
2547247
uniprot
proteins
pubmed
2550933
uniprot
proteins
pubmed
28135245
uniprot
proteins
pubmed
38355798
uniprot
proteins
pubmed
7581362
uniprot
proteins
pubmed
8089108
uniprot
proteins
pubmed
8280052
uniprot
proteins
pubmed
9224653
uniprot
proteins
pubmed
9329953
uniprot
proteins
sequence_length
390
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:2550933}. Membrane {ECO:0000269|PubMed:12356722}; Peripheral membrane protein {ECO:0000269|PubMed:12356722}; Cytoplasmic side {ECO:0000269|PubMed:12356722}.
uniprot
proteins