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Protein Page:
CYBA (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
CYBA Critical component of the membrane-bound oxidase of phagocytes that generates superoxide. Associates with NOX3 to form a functional NADPH oxidase constitutively generating superoxide. Defects in CYBA are a cause of chronic granulomatous disease autosomal recessive cytochrome-b-negative (ARCGD). Chronic granulomatous disease is a genetically heterogeneous disorder characterized by the inability of neutrophils and phagocytes to kill microbes that they have ingested. Patients suffer from life-threatening bacterial/fungal infections. Belongs to the p22phox family. Note: This description may include information from UniProtKB.
Protein type: Oxidoreductase; EC 1.-.-.-; Membrane protein, integral
Chromosomal Location of Human Ortholog: 16q24
Cellular Component: endoplasmic reticulum membrane; membrane; NADPH oxidase complex; phagocytic vesicle membrane; plasma membrane; secretory granule
Molecular Function: electron carrier activity; protein binding; protein heterodimerization activity; SH3 domain binding; superoxide-generating NADPH oxidase activity
Biological Process: antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; cell redox homeostasis; cytochrome complex assembly; hydrogen peroxide biosynthetic process; inflammatory response; innate immune response; positive regulation of interleukin-6 production; positive regulation of phagocytosis; positive regulation of toll-like receptor 2 signaling pathway; positive regulation of tumor necrosis factor production; respiratory burst; response to reactive oxygen species; smooth muscle hypertrophy; superoxide metabolic process; superoxide release; vascular endothelial growth factor receptor signaling pathway
Disease: Granulomatous Disease, Chronic, Autosomal Recessive, Cytochrome B-negative
Reference #:  P13498 (UniProtKB)
Alt. Names/Synonyms: CY24A; CYBA; cytochrome b light chain; Cytochrome b(558) alpha chain; cytochrome b(558) alpha-subunit; cytochrome b, alpha polypeptide; Cytochrome b-245 light chain; cytochrome b-245, alpha polypeptide; Cytochrome b558 subunit alpha; flavocytochrome b-558 alpha polypeptide; Neutrophil cytochrome b 22 kDa polypeptide; p22 phagocyte B-cytochrome; p22-phox; p22phox; Superoxide-generating NADPH oxidase light chain subunit
Gene Symbols: CYBA
Molecular weight: 21,013 Da
Basal Isoelectric point: 9.58  Predict pI for various phosphorylation states
Select Structure to View Below

CYBA

Protein Structure Not Found.
Download PyMol Script
Download ChimeraX Script


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Sites Implicated In
enzymatic activity, induced: T147‑p
molecular association, regulation: T147‑p

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



 LTP 

LTP: 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.


 HTP 

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


       human

 
0 2 K60‑ub EYPRGKRkkGSTMER
0 5 K61‑ub YPRGKRkkGSTMERW
0 5 K71‑ub TMERWGQkyMTAVVk
0 1 Y72‑p MERWGQkyMTAVVkL
0 1 K78‑ub kyMTAVVkLFGPFTR
0 1 Y87‑p FGPFTRNyyVRAVLH
0 1 Y88‑p GPFTRNyyVRAVLHL
0 7 K137‑ub QWTPIEPkPRERPQI
0 1 R139 TPIEPkPRERPQIGG
1 12 T147‑p ERPQIGGtIkQPPsN
0 11 K149‑ub PQIGGtIkQPPsNPP
0 1 S153‑p GtIkQPPsNPPPRPP
0 8 S168‑p AEARKKPsEEEAAVA
0 6 A176 EEEAAVAAGGPPGGP
  mouse

 
K60 EYPRGKRKKGSTMER
K61 YPRGKRKKGSTMERC
K71 TMERCGQKYLTSVVK
Y72 MERCGQKYLTSVVKL
K78 KYLTSVVKLFGPLTR
Y87 FGPLTRNYYVRAALH
Y88 GPLTRNYYVRAALHF
K137 QWTPIEPKPkERPQV
K139‑ub TPIEPKPkERPQVGG
T147‑p ERPQVGGtIkQPPTN
K149‑ub PQVGGtIkQPPTNPP
T153 GtIkQPPTNPPPRPP
S168‑p AEVRKKPsEGEEEAA
S176‑p EGEEEAAsAGGPQVN
  rat

 
K60 EYPRGKRKKGSTMER
K61 YPRGKRKKGSTMERC
K71 TMERCGQKYLTAVVK
Y72 MERCGQKYLTAVVKL
K78 KYLTAVVKLFGPLTR
Y87 FGPLTRNYYVRAVLH
Y88 GPLTRNYYVRAVLHL
K137 QWTPIEPKPKERPQV
K139 TPIEPKPKERPQVGG
T147‑p ERPQVGGtIKQPPTN
K149 PQVGGtIKQPPTNPP
T153 GtIKQPPTNPPPRPP
S168‑p AEVRKKPsEAEEEAA
S176‑p EAEEEAAsAGGPQVN
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