CYBA
entrez
1535
canonical
uniprot
P13498
canonical
ensembl
ENSG00000051523
resolver
ensp
ENSP00000261623
resolver
ensp
ENSP00000454951
resolver
enst
ENST00000261623
resolver
enst
ENST00000567174
resolver
genesymbol
CYBA
resolver
hgnc
HGNC:2577
resolver
uniprot
B4DT46
resolver
uniprot
H3BNP7
resolver
uniprot
Q14090
resolver
uniprot
Q9BR72
resolver
uniprot_entry
B4DT46_HUMAN
resolver
uniprot_entry
CY24A_HUMAN
resolver
uniprot_entry
H3BNP7_HUMAN
resolver
uniprot_sec
Q14090
resolver
uniprot_sec
Q9BR72
resolver
amino_acid_sequence
MGQIEWAMWANEQALASGLILITGGIVATAGRFTQWYFGAYSIVAGVFVCLLEYPRGKRKKGSTMERWGQKYMTAVVKLFGPFTRNYYVRAVLHLLLSVPAGFLLATILGTACLAIASGIYLLAAVRGEQWTPIEPKPRERPQIGGTIKQPPSNPPPRPPAEARKKPSEEEAAVAAGGPPGGPQVNPIPVTDEVV
uniprot
proteins
disease_involvement
DISEASE: Granulomatous disease, chronic, autosomal recessive, 4 (CGD4) [MIM:233690]: 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:10759707, ECO:0000269|PubMed:10910929, ECO:0000269|PubMed:10914676, ECO:0000269|PubMed:1415254, ECO:0000269|PubMed:1763037, ECO:0000269|PubMed:18422995, ECO:0000269|PubMed:2243141, ECO:0000269|PubMed:23910690, ECO:0000269|PubMed:7964505, ECO:0000269|PubMed:8168815}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Subunit of NADPH oxidase complexes that is required for the NADPH oxidase activity that generates, in various cell types, superoxide from molecular oxygen utilizing NADPH as an electron donor (PubMed:15824103, PubMed:17140397, PubMed:38355798). 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: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:19948736). Associates with NOX3 to form a functional NADPH oxidase constitutively generating superoxide (PubMed:15824103, PubMed:17140397). {ECO:0000269|PubMed:15824103, ECO:0000269|PubMed:17140397, ECO:0000269|PubMed:19948736, ECO:0000269|PubMed:38355798}.
uniprot
proteins
mass_dalton
21013
uniprot
proteins
mutagenesis
MUTAGEN 157; /note="P->Q: Loss of interaction with NOXO1."; /evidence="ECO:0000269|PubMed:12716910
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Thr-147 enhances NADPH oxidase activity by promoting NCF1/p47-phox binding. {ECO:0000269|PubMed:19948736}.; PTM: Ubiquitinated at Lys-149 likely by RNF145. {ECO:0000250|UniProtKB:Q61462}.
uniprot
proteins
protein_family
P22phox family
uniprot
proteins
pubmed
10759707
uniprot
proteins
pubmed
10910929
uniprot
proteins
pubmed
10914676
uniprot
proteins
pubmed
12716910
uniprot
proteins
pubmed
1415254
uniprot
proteins
pubmed
15322091
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15561711
uniprot
proteins
pubmed
15585859
uniprot
proteins
pubmed
15616553
uniprot
proteins
pubmed
15824103
uniprot
proteins
pubmed
15927447
uniprot
proteins
pubmed
16326715
uniprot
proteins
pubmed
17140397
uniprot
proteins
pubmed
1763037
uniprot
proteins
pubmed
18422995
uniprot
proteins
pubmed
19388116
uniprot
proteins
pubmed
19948736
uniprot
proteins
pubmed
2243141
uniprot
proteins
pubmed
22808130
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23910690
uniprot
proteins
pubmed
2469497
uniprot
proteins
pubmed
3368442
uniprot
proteins
pubmed
36241643
uniprot
proteins
pubmed
36413210
uniprot
proteins
pubmed
38355798
uniprot
proteins
pubmed
7964505
uniprot
proteins
pubmed
8168815
uniprot
proteins
sequence_length
195
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15585859, ECO:0000269|PubMed:17140397, ECO:0000269|PubMed:22808130}; Multi-pass membrane protein {ECO:0000269|PubMed:36241643, ECO:0000269|PubMed:36413210}.
uniprot
proteins
transmembrane_region
TRANSMEM 8..30; /note="Helical"; /evidence="ECO:0000269|PubMed:36241643, ECO:0000269|PubMed:36413210, ECO:0007744|PDB:7U8G, ECO:0007744|PDB:8GZ3"; TRANSMEM 36..53; /note="Helical"; /evidence="ECO:0000269|PubMed:36241643, ECO:0000269|PubMed:36413210, ECO:0007744|PDB:7U8G, ECO:0007744|PDB:8GZ3"; TRANSMEM 87..104; /note="Helical"; /evidence="ECO:0000269|PubMed:36241643, ECO:0000269|PubMed:36413210, ECO:0007744|PDB:7U8G, ECO:0007744|PDB:8GZ3"; TRANSMEM 106..126; /note="Helical"; /evidence="ECO:0000269|PubMed:36241643, ECO:0000269|PubMed:36413210, ECO:0007744|PDB:7U8G, ECO:0007744|PDB:8GZ3
uniprot
proteins