Cybb
entrez
13058
canonical
uniprot
Q61093
canonical
ensembl
ENSMUSG00000015340
resolver
ensp
ENSMUSP00000015484
resolver
enst
ENSMUST00000015484
resolver
genesymbol
Cybb
resolver
genesymbol_syn
Cgd
resolver
uniprot
Q3U6G0
resolver
uniprot_entry
CY24B_MOUSE
resolver
uniprot_entry
Q3U6G0_MOUSE
resolver
amino_acid_sequence
MGNWAVNEGLSIFVILVWLGLNVFLFINYYKVYDDGPKYNYTRKLLGSALALARAPAACLNFNCMLILLPVCRNLLSFLRGSSACCSTRIRRQLDRNLTFHKMVAWMIALHTAIHTIAHLFNVEWCVNARVGISDRYSIALSDIGDNENEEYLNFAREKIKNPEGGLYVAVTRLAGITGIVITLCLILIITSSTKTIRRSYFEVFWYTHHLFVIFFIGLAIHGAERIVRGQTAESLEEHNLDICADKIEEWGKIKECPVPKFAGNPPMTWKWIVGPMFLYLCERLVRFWRSQQKVVITKVVTHPFKTIELQMKKKGFKMEVGQYIFVKCPKVSKLEWHPFTLTSAPEEDFFSIHIRIVGDWTEGLFNACGCDKQEFQDAWKLPKIAVDGPFGTASEDVFSYEVVMLVGAGIGVTPFASILKSVWYKYCDNATSLKLKKIYFYWLCRDTHAFEWFADLLQLLETQMQERNNANFLSYNIYLTGWDESQANHFAVHHDEEKDVITGLKQKTLYGRPNWDNEFKTIASEHPNTTIGVFLCGPEALAETLSKQSISNSESGPRGVHFIFNKENF
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(-)). 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. 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 (By similarity). 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 (PubMed:24739962). {ECO:0000250|UniProtKB:P04839, ECO:0000250|UniProtKB:P13498, ECO:0000269|PubMed:24739962}.
uniprot
proteins
mass_dalton
65305
uniprot
proteins
post_translational_modification
PTM: Glycosylated. {ECO:0000250|UniProtKB:P04839}.; PTM: Phosphorylated on Ser and Thr residues by PKC during neutrophils activation. Phosphorylation enhances the NADPH oxidase activity and stimulates its interaction with RAC2, NCF2/p67-phox, and NCF1/p47-phox. {ECO:0000250|UniProtKB:P04839}.; PTM: Undergoes 'Lys-48'-linked polyubiquitination, likely by RNF145, triggering endoplasmic reticulum-associated degradation. {ECO:0000269|PubMed:26194095}.
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21551061
uniprot
proteins
pubmed
24739962
uniprot
proteins
pubmed
26194095
uniprot
proteins
pubmed
28351984
uniprot
proteins
pubmed
8634451
uniprot
proteins
sequence_length
570
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P04839}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P04839}. 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:0000250|UniProtKB:P04839"; TRANSMEM 47..72; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P04839"; TRANSMEM 96..130; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P04839"; TRANSMEM 164..194; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P04839"; TRANSMEM 204..222; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P04839"; TRANSMEM 268..285; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P04839
uniprot
proteins