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Protein Page:
CYBB (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
CYBB 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. It participates in the regulation of cellular pH and is blocked by zinc. Defects in CYBB are a cause of granulomatous disease,chronic, X-linked (CGD). A disorder characterized by the inability of neutrophils and phagocytes to kill microbes that they have ingested. Patients suffer from life- threatening bacterial/fungal infections. Defects in CYBB are a cause of mycobacteriosis atypical X-linked type 2 (AMCBX2). A rare condition characterized by predisposition to illness caused by moderately virulent mycobacterial species, such as Bacillus Calmette-Guerin (BCG) vaccine and 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. Note: This description may include information from UniProtKB.
Protein type: Membrane protein, multi-pass; EC 1.-.-.-; Membrane protein, integral; Oxidoreductase; Mitochondrial
Cellular Component: Golgi apparatus; phagocytic vesicle membrane; rough endoplasmic reticulum; mitochondrion; cell soma; integral to plasma membrane; dendrite; NADPH oxidase complex
Molecular Function: protein binding; electron carrier activity; FAD binding; protein heterodimerization activity; superoxide-generating NADPH oxidase activity; metal ion binding; heme binding; voltage-gated ion channel activity
Biological Process: response to drug; respiratory burst; interaction with host; antigen processing and presentation of peptide antigen via MHC class I; superoxide metabolic process; antigen processing and presentation of exogenous peptide antigen via MHC class I; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; innate immune response; inflammatory response; superoxide release; hydrogen peroxide biosynthetic process; response to nutrient
Reference #:  P04839 (UniProtKB)
Alt. Names/Synonyms: CGD; CGD91-phox; CY24B; CYBB; Cytochrome b(558) subunit beta; Cytochrome b-245 heavy chain; cytochrome b-245, beta polypeptide; Cytochrome b558 subunit beta; gp91-1; gp91-phox; GP91PHOX; Heme-binding membrane glycoprotein gp91phox; NADPH oxidase 2; Neutrophil cytochrome b 91 kDa polypeptide; NOX2; p22 phagocyte B-cytochrome; p91-PHOX; Superoxide-generating NADPH oxidase heavy chain subunit
Gene Symbols: CYBB
Molecular weight: 65,336 Da
Basal Isoelectric point: 8.9  Predict pI for various phosphorylation states
Select Structure to View Below

CYBB

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 4 T42-p IPPKFFytRkLLGSA
0 4 Y41-p DIPPKFFytRkLLGS
0 9 K44-u PKFFytRkLLGSALA
0 2 K294-u RFWRSQQkVVITKVV
0 2 K506 KDVITGLKQKTLYGR
  mouse

 
T42 DGPKYNYTRKLLGSA
Y41 DDGPKYNYTRKLLGS
K44 PKYNYTRKLLGSALA
K294 RFWRSQQKVVITKVV
K506-u KDVITGLkQKTLYGR
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