CYBB
entrez
1536
canonical
uniprot
P04839
canonical
ensembl
ENSG00000165168
resolver
ensp
ENSP00000367851
resolver
ensp
ENSP00000638617
resolver
enst
ENST00000378588
resolver
enst
ENST00000968558
resolver
genesymbol
CYBB
resolver
genesymbol_syn
NOX2
resolver
hgnc
HGNC:2578
resolver
uniprot
A0A0S2Z3S6
resolver
uniprot
A8K138
resolver
uniprot
Q2PP16
resolver
uniprot_entry
A0A0S2Z3S6_HUMAN
resolver
uniprot_entry
CY24B_HUMAN
resolver
uniprot_sec
A8K138
resolver
uniprot_sec
Q2PP16
resolver
amino_acid_sequence
MGNWAVNEGLSIFVILVWLGLNVFLFVWYYRVYDIPPKFFYTRKLLGSALALARAPAACLNFNCMLILLPVCRNLLSFLRGSSACCSTRVRRQLDRNLTFHKMVAWMIALHSAIHTIAHLFNVEWCVNARVNNSDPYSVALSELGDRQNESYLNFARKRIKNPEGGLYLAVTLLAGITGVVITLCLILIITSSTKTIRRSYFEVFWYTHHLFVIFFIGLAIHGAERIVRGQTAESLAVHNITVCEQKISEWGKIKECPIPQFAGNPPMTWKWIVGPMFLYLCERLVRFWRSQQKVVITKVVTHPFKTIELQMKKKGFKMEVGQYIFVKCPKVSKLEWHPFTLTSAPEEDFFSIHIRIVGDWTEGLFNACGCDKQEFQDAWKLPKIAVDGPFGTASEDVFSYEVVMLVGAGIGVTPFASILKSVWYKYCNNATNLKLKKIYFYWLCRDTHAFEWFADLLQLLESQMQERNNAGFLSYNIYLTGWDESQANHFAVHHDEEKDVITGLKQKTLYGRPNWDNEFKTIASQHPNTRIGVFLCGPEALAETLSKQSISNSESGPRGVHFIFNKENF
uniprot
proteins
disease_involvement
DISEASE: Granulomatous disease, chronic, X-linked (CGDX) [MIM:306400]: 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:10089913, ECO:0000269|PubMed:10914676, ECO:0000269|PubMed:11162142, ECO:0000269|PubMed:11462241, ECO:0000269|PubMed:11997083, ECO:0000269|PubMed:12139950, ECO:0000269|PubMed:15338276, ECO:0000269|PubMed:1710153, ECO:0000269|PubMed:18773283, ECO:0000269|PubMed:22125116, ECO:0000269|PubMed:23910690, ECO:0000269|PubMed:2556453, ECO:0000269|PubMed:27666509, ECO:0000269|PubMed:7927345, ECO:0000269|PubMed:8101486, ECO:0000269|PubMed:8182143, ECO:0000269|PubMed:8916969, ECO:0000269|PubMed:9111587, ECO:0000269|PubMed:9585602, ECO:0000269|PubMed:9667376, ECO:0000269|PubMed:9794433, ECO:0000269|PubMed:9856476, ECO:0000269|PubMed:9888386}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Immunodeficiency 34 (IMD34) [MIM:300645]: A form of Mendelian susceptibility to mycobacterial disease, a rare condition characterized by predisposition to illness caused by moderately virulent mycobacterial species, such as Bacillus Calmette-Guerin (BCG) vaccine, environmental non-tuberculous mycobacteria, and by the more virulent Mycobacterium tuberculosis. Other microorganisms rarely cause severe clinical disease in individuals with susceptibility to mycobacterial infections, with the exception of Salmonella which infects less than 50% of these individuals. {ECO:0000269|PubMed:21278736}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
1.6.3.-
uniprot
proteins
function
FUNCTION: Catalytic 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:15338276, PubMed:36241643, PubMed:36413210, 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 (Probable) (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:19028840, 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 (By similarity). NADPH oxidase complex assembly is impaired through interaction with NRROS (By similarity). {ECO:0000250|UniProtKB:P13498, ECO:0000250|UniProtKB:Q61093, ECO:0000269|PubMed:15338276, ECO:0000269|PubMed:19028840, ECO:0000269|PubMed:36241643, ECO:0000269|PubMed:36413210, ECO:0000269|PubMed:38355798, ECO:0000305|PubMed:36241643}.
uniprot
proteins
mass_dalton
65336
uniprot
proteins
mutagenesis
MUTAGEN 570; /note="F->A: Moderately decreases superoxide-generating NADPH oxidase activity."; /evidence="ECO:0000269|PubMed:38355798"; MUTAGEN 570; /note="F->G: Moderately decreases superoxide-generating NADPH oxidase activity."; /evidence="ECO:0000269|PubMed:38355798
uniprot
proteins
post_translational_modification
PTM: Glycosylated. {ECO:0000269|PubMed:19159218}.; PTM: Phosphorylated on Ser and Thr residues by PKC during neutrophils activation (PubMed:19028840). Phosphorylation enhances the NADPH oxidase activity and stimulates its interaction with RAC2, NCF2/p67-phox, and NCF1/p47-phox (PubMed:19028840). {ECO:0000269|PubMed:19028840}.; PTM: Undergoes 'Lys-48'-linked polyubiquitination, likely by RNF145, triggering endoplasmic reticulum-associated degradation. {ECO:0000250|UniProtKB:Q61093}.
uniprot
proteins
pubmed
10089913
uniprot
proteins
pubmed
10578014
uniprot
proteins
pubmed
10914676
uniprot
proteins
pubmed
11162142
uniprot
proteins
pubmed
11462241
uniprot
proteins
pubmed
11477065
uniprot
proteins
pubmed
11997083
uniprot
proteins
pubmed
12034764
uniprot
proteins
pubmed
12139950
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15338276
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15772651
uniprot
proteins
pubmed
1710153
uniprot
proteins
pubmed
18773283
uniprot
proteins
pubmed
19028840
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
21278736
uniprot
proteins
pubmed
22125116
uniprot
proteins
pubmed
22808130
uniprot
proteins
pubmed
23910690
uniprot
proteins
pubmed
2425263
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
2556453
uniprot
proteins
pubmed
27666509
uniprot
proteins
pubmed
28351984
uniprot
proteins
pubmed
3600768
uniprot
proteins
pubmed
3600769
uniprot
proteins
pubmed
36241643
uniprot
proteins
pubmed
36413210
uniprot
proteins
pubmed
38355798
uniprot
proteins
pubmed
7927345
uniprot
proteins
pubmed
8101486
uniprot
proteins
pubmed
8182143
uniprot
proteins
pubmed
8916969
uniprot
proteins
pubmed
9111587
uniprot
proteins
pubmed
9224653
uniprot
proteins
pubmed
9585602
uniprot
proteins
pubmed
9667376
uniprot
proteins
pubmed
9790760
uniprot
proteins
pubmed
9794433
uniprot
proteins
pubmed
9856476
uniprot
proteins
pubmed
9888386
uniprot
proteins
sequence_length
570
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15338276, ECO:0000269|PubMed:22808130}; Multi-pass membrane protein. Note=As unassembled monomer may localize to the endoplasmic reticulum. {ECO:0000305|PubMed:28351984}.
uniprot
proteins
transmembrane_region
TRANSMEM 10..36; /note="Helical"; /evidence="ECO:0000269|PubMed:36241643, ECO:0000269|PubMed:36413210, ECO:0007744|PDB:7U8G, ECO:0007744|PDB:8GZ3"; TRANSMEM 47..72; /note="Helical"; /evidence="ECO:0000269|PubMed:36241643, ECO:0000269|PubMed:36413210, ECO:0007744|PDB:7U8G, ECO:0007744|PDB:8GZ3"; TRANSMEM 96..130; /note="Helical"; /evidence="ECO:0000269|PubMed:36241643, ECO:0000269|PubMed:36413210, ECO:0007744|PDB:7U8G, ECO:0007744|PDB:8GZ3"; TRANSMEM 164..194; /note="Helical"; /evidence="ECO:0000269|PubMed:36241643, ECO:0000269|PubMed:36413210, ECO:0007744|PDB:7U8G, ECO:0007744|PDB:8GZ3"; TRANSMEM 204..222; /note="Helical"; /evidence="ECO:0000269|PubMed:36241643, ECO:0000269|PubMed:36413210, ECO:0007744|PDB:7U8G, ECO:0007744|PDB:8GZ3"; TRANSMEM 268..285; /note="Helical"; /evidence="ECO:0000269|PubMed:36241643, ECO:0000269|PubMed:36413210, ECO:0007744|PDB:7U8G, ECO:0007744|PDB:8GZ3
uniprot
proteins