Q95L74 · CY24B_BISBI

Function

function

Critical component of the membrane-bound oxidase of phagocytes that generates superoxide. It is the terminal component of a respiratory chain that transfers single electrons from cytoplasmic NADPH across the plasma membrane to molecular oxygen on the exterior. Also functions as a voltage-gated proton channel that mediates the H+ currents of resting phagocytes.

Cofactor

FAD (UniProtKB | Rhea| CHEBI:57692 )

Features

Showing features for binding site.

157050100150200250300350400450500550
TypeIDPosition(s)Description
Binding site101Fe (UniProtKB | ChEBI) of heme (UniProtKB | ChEBI); axial binding residue
Binding site115Fe (UniProtKB | ChEBI) of heme (UniProtKB | ChEBI); axial binding residue
Binding site209Fe (UniProtKB | ChEBI) of heme (UniProtKB | ChEBI); axial binding residue
Binding site222Fe (UniProtKB | ChEBI) of heme (UniProtKB | ChEBI); axial binding residue
Binding site338-344FAD (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentmonoatomic ion channel complex
Cellular ComponentNADPH oxidase complex
Molecular Functionmetal ion binding
Molecular Functionsuperoxide-generating NAD(P)H oxidase activity
Biological Processinflammatory response
Biological Processinnate immune response
Biological Processmonoatomic ion transmembrane transport
Biological Processsuperoxide anion generation
Biological Processsuperoxide metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Cytochrome b-245 heavy chain
  • EC number
  • Alternative names
    • CGD91-phox
    • Cytochrome b(558) subunit beta (Cytochrome b558 subunit beta)
    • Heme-binding membrane glycoprotein gp91phox
    • Neutrophil cytochrome b 91 kDa polypeptide
    • gp91-1

Gene names

    • Name
      CYBB

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bison

Accessions

  • Primary accession
    Q95L74

Subcellular Location

Cell membrane
; Multi-pass membrane protein
Note: As unassembled monomer may localize to the endoplasmic reticulum.

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-8Cytoplasmic
Transmembrane9-29Helical
Topological domain30-48Extracellular
Transmembrane49-69Helical
Topological domain70-102Cytoplasmic
Transmembrane103-123Helical
Topological domain124-169Extracellular
Transmembrane170-190Helical
Topological domain191-200Cytoplasmic
Transmembrane201-221Helical
Topological domain222-261Extracellular
Transmembrane262-282Helical
Topological domain283-570Cytoplasmic

Keywords

PTM/Processing

Features

Showing features for chain, glycosylation, cross-link.

TypeIDPosition(s)Description
ChainPRO_00002101431-570Cytochrome b-245 heavy chain
Glycosylation132N-linked (GlcNAc...) asparagine
Glycosylation149N-linked (GlcNAc...) asparagine
Cross-link161Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Glycosylation247N-linked (GlcNAc...) asparagine
Cross-link255Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link294Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link299Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link306Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link328Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link334Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link381Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link506Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link567Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

Post-translational modification

Phosphorylated on Ser and Thr residues.
Undergoes 'Lys-48'-linked polyubiquitination, likely by RNF145, triggering endoplasmic reticulum-associated degradation.

Keywords

PTM databases

Interaction

Subunit

Composed of a heavy chain (beta) and a light chain (alpha). Component of an NADPH oxidase complex composed of a heterodimer formed by the membrane proteins CYBA and CYBB and the cytosolic subunits NCF1, NCF2 and NCF4. Interacts with NCF1. Interacts with calprotectin (S100A8/9). Interacts with NRROS; the interaction is direct and impairs formation of a stable NADPH oxidase complex. Interacts with CYBC1; CYBC1 may act as a chaperone stabilizing Cytochrome b-245 heterodimer (By similarity).
Interacts with NCF2; the interaction is enhanced in the presence of GBP7 (By similarity).
The CYBA-CYBB complex interacts with GBP7 (By similarity).

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain54-286Ferric oxidoreductase
Domain287-397FAD-binding FR-type

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    570
  • Mass (Da)
    65,600
  • Last updated
    2001-12-01 v1
  • Checksum
    94F9D1E833E19848
MGNWVVNEGISIFVILVWLGMNVFLFVWYYRVYDIPDKFFYTRKLLGSALALARAPAACLNFNCMLILLPVCRNLLSFLRGSSACCSTRIRRQLDRNLTFHKMVAWMIALHTAIHTIAHLFNVEWCVNARVNNSDPYSIALSDIGDKPNETYLNFVRQRIKNPEGGLYVAVTLLAGITGVVITLCLILIITSSTKTIRRSYFEVFWYTHHLFVIFFIGLAIHGAQRIVRGQTAESLLKHQPRNCYQNISQWGKIKDCPIPEFSGNPPMTWKWIVGPMFLYLCERLVRFWRSQQKVVITKVVTHPFKTIELQMKKKGFKMEVGQYIFVKCPVVSKLEWHPFTLTSAPEEDFFSIHIRIVGDWTEGLFKACGCDKQEFQDAWKLPKIAVDGPFGTASEDVFSYEVVMLVGAGIGVTPFASILKSVWYKYCNKAPNLRLKKIYFYWLCRDTHAFEWFADLLQLLETQMQEKNNTDFLSYNICLTGWDESQASHFAMHHDEEKDVITGLKQKTLYGRPNWDNEFKTIGSQHPNTRIGVFLCGPEALADTLNKQCISNSDSGPRGVHFIFNKENF

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF411135
EMBL· GenBank· DDBJ
AAL11885.1
EMBL· GenBank· DDBJ
mRNA

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