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P04839 (CY24B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 163. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytochrome b-245 heavy chain

EC=1.-.-.-
Alternative name(s):
CGD91-phox
Cytochrome b(558) subunit beta
Short name=Cytochrome b558 subunit beta
Heme-binding membrane glycoprotein gp91phox
NADPH oxidase 2
Neutrophil cytochrome b 91 kDa polypeptide
Superoxide-generating NADPH oxidase heavy chain subunit
gp91-1
gp91-phox
p22 phagocyte B-cytochrome
Gene names
Name:CYBB
Synonyms:NOX2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length570 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. It participates in the regulation of cellular pH and is blocked by zinc.

Cofactor

FAD Probable.

Subunit structure

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. Ref.9 Ref.11 Ref.13

Subcellular location

Cell membrane; Multi-pass membrane protein.

Tissue specificity

Detected in neutrophils (at protein level). Ref.11

Post-translational modification

Glycosylated.

Phosphorylated on Ser and Thr residues. Ref.11

Involvement in disease

Granulomatous disease, chronic, X-linked (CGD) [MIM:306400]: 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.2 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.34

Mycobacteriosis atypical X-linked 2 (AMCBX2) [MIM:300645]: 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: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.33

Sequence similarities

Contains 1 FAD-binding FR-type domain.

Contains 1 ferric oxidoreductase domain.

Sequence caution

The sequence CAA27635.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAA29327.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processElectron transport
Ion transport
Transport
   Cellular componentCell membrane
Membrane
   Coding sequence diversityPolymorphism
   DiseaseChronic granulomatous disease
Disease mutation
   DomainTransmembrane
Transmembrane helix
   LigandFAD
Flavoprotein
Heme
Iron
Metal-binding
NADP
   Molecular functionIon channel
Oxidoreductase
Voltage-gated channel
   PTMGlycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processantigen processing and presentation of exogenous peptide antigen via MHC class I

Traceable author statement. Source: Reactome

antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent

Traceable author statement. Source: Reactome

antigen processing and presentation of peptide antigen via MHC class I

Traceable author statement. Source: Reactome

hydrogen peroxide biosynthetic process

Inferred from electronic annotation. Source: Ensembl

inflammatory response

Inferred from sequence or structural similarity. Source: UniProtKB

innate immune response

Inferred from mutant phenotype PubMed 9774399. Source: BHF-UCL

interaction with host

Traceable author statement. Source: Reactome

oxidation-reduction process

Inferred from direct assay PubMed 12042318. Source: BHF-UCL

phagosome maturation

Traceable author statement. Source: Reactome

respiratory burst

Inferred from mutant phenotype PubMed 9774399. Source: BHF-UCL

response to drug

Inferred from electronic annotation. Source: Ensembl

response to nutrient

Inferred from electronic annotation. Source: Ensembl

superoxide anion generation

Inferred from direct assay PubMed 12042318. Source: BHF-UCL

superoxide metabolic process

Inferred from direct assay PubMed 12042318. Source: BHF-UCL

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Ensembl

NADPH oxidase complex

Inferred from direct assay PubMed 3305576. Source: BHF-UCL

dendrite

Inferred from electronic annotation. Source: Ensembl

integral component of plasma membrane

Inferred from direct assay PubMed 15233623. Source: UniProtKB

mitochondrion

Inferred from electronic annotation. Source: Ensembl

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

phagocytic vesicle membrane

Traceable author statement. Source: Reactome

rough endoplasmic reticulum

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionflavin adenine dinucleotide binding

Inferred from mutant phenotype PubMed 9774399. Source: BHF-UCL

heme binding

Inferred from mutant phenotype PubMed 9774399. Source: BHF-UCL

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 3305576. Source: BHF-UCL

protein heterodimerization activity

Inferred from physical interaction PubMed 12042318. Source: BHF-UCL

superoxide-generating NADPH oxidase activity

Traceable author statement PubMed 12716910. Source: BHF-UCL

voltage-gated ion channel activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9
Chain2 – 570569Cytochrome b-245 heavy chain
PRO_0000210145

Regions

Topological domain2 – 87Cytoplasmic Potential
Transmembrane9 – 2921Helical; Potential
Topological domain30 – 4819Extracellular Potential
Transmembrane49 – 6921Helical; Potential
Topological domain70 – 10233Cytoplasmic Potential
Transmembrane103 – 12321Helical; Potential
Topological domain124 – 16946Extracellular Potential
Transmembrane170 – 19021Helical; Potential
Topological domain191 – 20010Cytoplasmic Potential
Transmembrane201 – 22121Helical; Potential
Topological domain222 – 26140Extracellular Potential
Transmembrane262 – 28221Helical; Potential
Topological domain283 – 570288Cytoplasmic Potential
Domain54 – 286233Ferric oxidoreductase
Domain287 – 397111FAD-binding FR-type
Nucleotide binding338 – 3447FAD Potential

Sites

Metal binding1011Iron (heme axial ligand) Probable
Metal binding1151Iron (heme axial ligand) Probable
Metal binding2091Iron (heme axial ligand) Probable
Metal binding2221Iron (heme axial ligand) Probable

Amino acid modifications

Glycosylation1321N-linked (GlcNAc...) Ref.12
Glycosylation1491N-linked (GlcNAc...) Ref.12
Glycosylation2401N-linked (GlcNAc...) Ref.12

Natural variations

Natural variant181W → C in CGD.
VAR_047264
Natural variant201G → R in CGD. Ref.22
Corresponds to variant rs151344455 [ dbSNP | Ensembl ].
VAR_007873
Natural variant411Y → D in CGD. Ref.2
Corresponds to variant rs151344453 [ dbSNP | Ensembl ].
VAR_025613
Natural variant54 – 552Missing in CGD.
VAR_047265
Natural variant541R → M in CGD. Ref.25 Ref.28
Corresponds to variant rs151344479 [ dbSNP | Ensembl ].
VAR_025614
Natural variant541R → S in CGD. Ref.22
Corresponds to variant rs151344456 [ dbSNP | Ensembl ].
VAR_007874
Natural variant551A → D in CGD. Ref.25 Ref.28
Corresponds to variant rs151344480 [ dbSNP | Ensembl ].
VAR_025615
Natural variant571A → E in CGD. Ref.16 Ref.25 Ref.28
Corresponds to variant rs151344481 [ dbSNP | Ensembl ].
VAR_008845
Natural variant591C → R in CGD. Ref.22
Corresponds to variant rs151344457 [ dbSNP | Ensembl ].
VAR_007875
Natural variant591C → W in CGD. Ref.29
Corresponds to variant rs151344488 [ dbSNP | Ensembl ].
VAR_047266
Natural variant1011H → R in CGD. Ref.15
Corresponds to variant rs137854591 [ dbSNP | Ensembl ].
VAR_002432
Natural variant1011H → Y in CGD. Ref.23 Ref.28
Corresponds to variant rs137854594 [ dbSNP | Ensembl ].
VAR_007876
Natural variant1191H → R in CGD. Ref.22
Corresponds to variant rs151344458 [ dbSNP | Ensembl ].
VAR_007877
Natural variant1561A → T in CGD. Ref.15 Ref.22
Corresponds to variant rs137854590 [ dbSNP | Ensembl ].
VAR_002433
Natural variant1781T → P in AMCBX2. Ref.33
Corresponds to variant rs151344497 [ dbSNP | Ensembl ].
VAR_065365
Natural variant1791G → R in CGD. Ref.24
Corresponds to variant rs151344491 [ dbSNP | Ensembl ].
VAR_047267
Natural variant1931S → F in CGD. Ref.26
Corresponds to variant rs151344493 [ dbSNP | Ensembl ].
VAR_047268
Natural variant2051F → I in CGD. Ref.19
Corresponds to variant rs151344496 [ dbSNP | Ensembl ].
VAR_047269
Natural variant2091H → Q in CGD. Ref.22
Corresponds to variant rs151344459 [ dbSNP | Ensembl ].
VAR_007878
Natural variant2091H → R in CGD. Ref.28
Corresponds to variant rs151344482 [ dbSNP | Ensembl ].
VAR_025616
Natural variant2091H → Y in CGD. Ref.15
Corresponds to variant rs137854587 [ dbSNP | Ensembl ].
VAR_002434
Natural variant2151Missing in CGD. Ref.19 Ref.21
VAR_007879
Natural variant2221H → N in CGD. Ref.22
Corresponds to variant rs151344460 [ dbSNP | Ensembl ].
VAR_007880
Natural variant2221H → R in CGD. Ref.22 Ref.26
Corresponds to variant rs151344462 [ dbSNP | Ensembl ].
VAR_007881
Natural variant2221H → Y in CGD. Ref.22
Corresponds to variant rs151344460 [ dbSNP | Ensembl ].
VAR_007882
Natural variant2231G → L in CGD; requires 2 nucleotide substitutions. Ref.22
Corresponds to variants rs151344463 [ dbSNP | Ensembl ] and rs151344464 [ dbSNP | Ensembl ].
VAR_007883
Natural variant2241A → G in CGD. Ref.28
Corresponds to variant rs151344483 [ dbSNP | Ensembl ].
VAR_025617
Natural variant2251E → V in CGD. Ref.27
Corresponds to variant rs151344494 [ dbSNP | Ensembl ].
VAR_002435
Natural variant2311Q → P in AMCBX2. Ref.33
Corresponds to variant rs151344498 [ dbSNP | Ensembl ].
VAR_065366
Natural variant2441C → R in CGD. Ref.22
Corresponds to variant rs151344465 [ dbSNP | Ensembl ].
VAR_007884
Natural variant2441C → S in CGD. Ref.15
Corresponds to variant rs137854589 [ dbSNP | Ensembl ].
VAR_002436
Natural variant2441C → Y in CGD. Ref.27
Corresponds to variant rs137854589 [ dbSNP | Ensembl ].
VAR_002437
Natural variant298 – 3025Missing in CGD.
VAR_047270
Natural variant3031H → N in CGD; completely inhibits NADPH oxidase activity; NADPH oxidase assembly is abolished. Ref.30 Ref.31
Corresponds to variant rs137854595 [ dbSNP | Ensembl ].
VAR_016880
Natural variant3041P → R in CGD; reduces NADPH oxidase activity to 4% of wild-type; translocation to the membrane of the phagosome is only attenuated. Ref.30 Ref.31
Corresponds to variant rs137854596 [ dbSNP | Ensembl ].
VAR_016881
Natural variant3071T → P in CGD. Ref.29
Corresponds to variant rs151344489 [ dbSNP | Ensembl ].
VAR_047271
Natural variant3091E → K in CGD. Ref.22 Ref.28
Corresponds to variant rs151344466 [ dbSNP | Ensembl ].
VAR_007885
Natural variant3151Missing in CGD. Ref.22
VAR_047272
Natural variant3221G → E in CGD. Ref.22
Corresponds to variant rs151344467 [ dbSNP | Ensembl ].
VAR_007886
Natural variant3251I → F in CGD. Ref.22
Corresponds to variant rs151344468 [ dbSNP | Ensembl ].
VAR_007887
Natural variant3331S → P in CGD. Ref.22
Corresponds to variant rs151344469 [ dbSNP | Ensembl ].
VAR_007888
Natural variant3381H → Y in CGD. Ref.26 Ref.28
Corresponds to variant rs151344484 [ dbSNP | Ensembl ].
VAR_025618
Natural variant3391P → H in CGD. Ref.17 Ref.22 Ref.25 Ref.26 Ref.28
Corresponds to variant rs151344470 [ dbSNP | Ensembl ].
VAR_002438
Natural variant3421L → Q in CGD. Ref.19
Corresponds to variant rs151344495 [ dbSNP | Ensembl ].
VAR_047273
Natural variant3441S → F in CGD. Ref.25 Ref.28
Corresponds to variant rs151344485 [ dbSNP | Ensembl ].
VAR_025619
Natural variant3561R → P in CGD. Ref.22
Corresponds to variant rs151344471 [ dbSNP | Ensembl ].
VAR_007889
Natural variant3641G → R. Ref.2 Ref.26
Corresponds to variant rs141756032 [ dbSNP | Ensembl ].
VAR_025620
Natural variant3891G → A in CGD. Ref.15
Corresponds to variant rs137854586 [ dbSNP | Ensembl ].
VAR_002439
Natural variant3891G → E in CGD. Ref.28
Corresponds to variant rs137854586 [ dbSNP | Ensembl ].
VAR_025621
Natural variant4051M → R in CGD. Ref.22
Corresponds to variant rs151344472 [ dbSNP | Ensembl ].
VAR_007890
Natural variant4081G → E in CGD. Ref.22
Corresponds to variant rs151344474 [ dbSNP | Ensembl ].
VAR_007891
Natural variant4081G → R in CGD. Ref.22 Ref.32
Corresponds to variant rs151344473 [ dbSNP | Ensembl ].
VAR_007892
Natural variant4151P → H in CGD. Ref.14 Ref.22
Corresponds to variant rs137854585 [ dbSNP | Ensembl ].
VAR_002440
Natural variant4151P → L in CGD. Ref.22
Corresponds to variant rs137854585 [ dbSNP | Ensembl ].
VAR_007893
Natural variant4201L → P in CGD. Ref.28
Corresponds to variant rs151344486 [ dbSNP | Ensembl ].
VAR_025622
Natural variant4221S → P in CGD. Ref.22
Corresponds to variant rs151344475 [ dbSNP | Ensembl ].
VAR_007894
Natural variant4531W → R in CGD. Ref.22
Corresponds to variant rs151344476 [ dbSNP | Ensembl ].
VAR_007895
Natural variant4721G → S.
Corresponds to variant rs13306300 [ dbSNP | Ensembl ].
VAR_047274
Natural variant4881A → D in CGD. Ref.34
VAR_068012
Natural variant5001D → E in CGD. Ref.34
VAR_068013
Natural variant5001D → G in CGD. Ref.18
Corresponds to variant rs137854593 [ dbSNP | Ensembl ].
VAR_002441
Natural variant5051L → R in CGD. Ref.29
Corresponds to variant rs151344490 [ dbSNP | Ensembl ].
VAR_047275
Natural variant5161W → C in CGD. Ref.22
Corresponds to variant rs151344477 [ dbSNP | Ensembl ].
VAR_007896
Natural variant5161W → R in CGD. Ref.28
Corresponds to variant rs151344487 [ dbSNP | Ensembl ].
VAR_025623
Natural variant5171D → E. Ref.2
Corresponds to variant rs151344452 [ dbSNP | Ensembl ].
VAR_025624
Natural variant5341V → D in CGD. Ref.22
Corresponds to variant rs151344478 [ dbSNP | Ensembl ].
VAR_007897
Natural variant5371C → R in CGD. Ref.2 Ref.22
Corresponds to variant rs151344454 [ dbSNP | Ensembl ].
VAR_007898
Natural variant5461L → P in CGD. Ref.26
Corresponds to variant rs151344492 [ dbSNP | Ensembl ].
VAR_047276

Experimental info

Sequence conflict141V → A Ref.1
Sequence conflict141V → A Ref.5

Secondary structure

........................ 570
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P04839 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 7E84051BD4000CE3

FASTA57065,336
        10         20         30         40         50         60 
MGNWAVNEGL SIFVILVWLG LNVFLFVWYY RVYDIPPKFF YTRKLLGSAL ALARAPAACL 

        70         80         90        100        110        120 
NFNCMLILLP VCRNLLSFLR GSSACCSTRV RRQLDRNLTF HKMVAWMIAL HSAIHTIAHL 

       130        140        150        160        170        180 
FNVEWCVNAR VNNSDPYSVA LSELGDRQNE SYLNFARKRI KNPEGGLYLA VTLLAGITGV 

       190        200        210        220        230        240 
VITLCLILII TSSTKTIRRS YFEVFWYTHH LFVIFFIGLA IHGAERIVRG QTAESLAVHN 

       250        260        270        280        290        300 
ITVCEQKISE WGKIKECPIP QFAGNPPMTW KWIVGPMFLY LCERLVRFWR SQQKVVITKV 

       310        320        330        340        350        360 
VTHPFKTIEL QMKKKGFKME VGQYIFVKCP KVSKLEWHPF TLTSAPEEDF FSIHIRIVGD 

       370        380        390        400        410        420 
WTEGLFNACG CDKQEFQDAW KLPKIAVDGP FGTASEDVFS YEVVMLVGAG IGVTPFASIL 

       430        440        450        460        470        480 
KSVWYKYCNN ATNLKLKKIY FYWLCRDTHA FEWFADLLQL LESQMQERNN AGFLSYNIYL 

       490        500        510        520        530        540 
TGWDESQANH FAVHHDEEKD VITGLKQKTL YGRPNWDNEF KTIASQHPNT RIGVFLCGPE 

       550        560        570 
ALAETLSKQS ISNSESGPRG VHFIFNKENF 

« Hide

References

« Hide 'large scale' references
[1]"Cloning the gene for an inherited human disorder -- chronic granulomatous disease -- on the basis of its chromosomal location."
Royer-Pokora B., Kunkel L.M., Monaco A.P., Goff S.C., Newburger P.E., Baehner R.L., Cole F.S., Curnutte J.T., Orkin S.H.
Nature 322:32-38(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"CYBB mutation analysis in X-linked chronic granulomatous disease."
Jirapongsananuruk O., Niemela J.E., Malech H.L., Fleisher T.A.
Clin. Immunol. 104:73-76(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS CGD ASP-41 AND ARG-537, VARIANTS ARG-364 AND GLU-517.
[3]NHLBI resequencing and genotyping service (RS&G)
Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lymph.
[7]"The glycoprotein encoded by the X-linked chronic granulomatous disease locus is a component of the neutrophil cytochrome b complex."
Dinauer M.C., Orkin S.H., Brown R., Jesaitis A.J., Parkos C.A.
Nature 327:717-720(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-135.
[8]"Nonhomologous recombination between the cytochrome b558 heavy chain gene (CYBB) and LINE-1 causes an X-linked chronic granulomatous disease."
Kumatori A., Faizunnessa N.N., Suzuki S., Moriuchi T., Kurozumi H., Nakamura M.
Genomics 53:123-128(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 233-267.
Tissue: Peripheral blood.
[9]"The X-linked chronic granulomatous disease gene codes for the beta-chain of cytochrome b-245."
Teahan C., Rowe P., Parker P., Totty N., Segal A.W.
Nature 327:720-721(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-44, SUBUNIT.
[10]"Evidence that the product of the human X-linked CGD gene, gp91-phox, is a voltage-gated H(+) pathway."
Henderson L.M., Meech R.W.
J. Gen. Physiol. 114:771-786(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION AS A PROTON CHANNEL.
[11]"Regulation of the phagocyte NADPH oxidase activity: phosphorylation of gp91phox/NOX2 by protein kinase C enhances its diaphorase activity and binding to Rac2, p67phox, and p47phox."
Raad H., Paclet M.H., Boussetta T., Kroviarski Y., Morel F., Quinn M.T., Gougerot-Pocidalo M.A., Dang P.M., El-Benna J.
FASEB J. 23:1011-1022(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, PHOSPHORYLATION, TISSUE SPECIFICITY.
[12]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-132; ASN-149 AND ASN-240.
Tissue: Liver.
[13]"Interaction of human neutrophil flavocytochrome b with cytosolic proteins: transferred-NOESY NMR studies of a gp91phox C-terminal peptide bound to p47phox."
Adams E.R., Dratz E.A., Gizachew D., Deleo F.R., Yu L., Volpp B.D., Vlases M., Jesaitis A.J., Quinn M.T.
Biochem. J. 325:249-257(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 556-570 IN COMPLEX WITH NCF1, INTERACTION WITH NCF1.
[14]"A missense mutation in the neutrophil cytochrome b heavy chain in cytochrome-positive X-linked chronic granulomatous disease."
Dinauer M.C., Curnutte J.T., Rosen H.R., Orkin S.H.
J. Clin. Invest. 84:2012-2016(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CGD HIS-415.
[15]"Point mutations in the beta-subunit of cytochrome b558 leading to X-linked chronic granulomatous disease."
Bolscher B.G.J.M., de Boer M., de Klein A., Weening R.S., Roos D.
Blood 77:2482-2487(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CGD ARG-101; THR-156; TYR-209; SER-244 AND ALA-389.
[16]"A newly recognized point mutation in the cytochrome b558 heavy chain gene replacing alanine57 by glutamic acid, in a patient with cytochrome b positive X-linked chronic granulomatous disease."
Ariga T., Sakiyama Y., Tomizawa K., Imajoh-Ohmi S., Kanegasaki S., Matsumoto S.
Eur. J. Pediatr. 152:469-472(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CGD GLU-57.
[17]"Two novel point mutations in the cytochrome b 558 heavy chain gene, detected in two Japanese patients with X-linked chronic granulomatous disease."
Ariga T., Sakiyama Y., Matsumoto S.
Hum. Genet. 94:441-441(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CGD HIS-339.
[18]"A point mutation in gp91-phox of cytochrome b558 of the human NADPH oxidase leading to defective translocation of the cytosolic proteins p47-phox and p67-phox."
Leusen J.H.W., de Boer M., Bolscher B.G.J.M., Hilarius P.M., Weening R.S., Ochs H.D., Roos D., Verhoeven A.J.
J. Clin. Invest. 93:2120-2126(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CGD GLY-500.
[19]"Identification of mutations in seven Chinese patients with X-linked chronic granulomatous disease."
Hui Y.F., Chan S.Y., Lau Y.L.
Blood 88:4021-4028(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CGD ILE-205; PHE-215 DEL AND GLN-342.
[20]Erratum
Hui Y.F., Chan S.Y., Lau Y.L.
Blood 89:1843-1843(1996)
[21]"An in-frame triplet deletion within the gp91-phox gene in an adult X-linked chronic granulomatous disease patient with residual NADPH-oxidase activity."
Jendrossek V., Ritzel A., Neubauer B., Heyden S., Gahr M.
Eur. J. Haematol. 58:78-85(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CGD PHE-215 DEL.
[22]"X-linked chronic granulomatous disease: mutations in the CYBB gene encoding the gp91-phox component of respiratory-burst oxidase."
Rae J., Newburger P.E., Dinauer M.C., Noack D., Hopkins P.J., Kuruto R., Curnutte J.T.
Am. J. Hum. Genet. 62:1320-1331(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CGD ARG-20; SER-54; ARG-59; ARG-119; THR-156; GLN-209; ASN-222; ARG-222; TYR-222; LEU-223; ARG-244; LYS-309; LYS-315 DEL; GLU-322; PHE-325; PRO-333; HIS-339; PRO-356; ARG-405; GLU-408; ARG-408; HIS-415; LEU-415; PRO-422; ARG-453; CYS-516; ASP-534 AND ARG-537.
[23]"A novel mutation at a probable heme-binding ligand in neutrophil cytochrome b558 in atypical X-linked chronic granulomatous disease."
Tsuda M., Kaneda M., Sakiyama T., Inana I., Owada M., Kiryu C., Shiraishi T., Kakinuma K.
Hum. Genet. 103:377-381(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CGD TYR-101.
[24]"Nicotinamide-adenine dinucleotide phosphate oxidase assembly and activation in EBV-transformed B lymphoblastoid cell lines of normal and chronic granulomatous disease patients."
Dusi S., Nadalini K.A., Donini M., Zentilin L., Wientjes F.B., Roos D., Giacca M., Rossi F.
J. Immunol. 161:4968-4974(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CGD ARG-179 AND 298-THR--THR-302 DEL.
[25]"Genetic analysis of 13 families with X-linked chronic granulomatous disease reveals a low proportion of sporadic patients and a high proportion of sporadic carriers."
Ariga T., Furuta H., Cho K., Sakiyama Y.
Pediatr. Res. 44:85-92(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CGD MET-54; ASP-55; GLU-57; HIS-339 AND PHE-344.
[26]"Uncommon missense and splice mutations and resulting biochemical phenotypes in German patients with X-linked chronic granulomatous disease."
Roesler J., Heyden S., Burdelski M., Schaefer H., Kreth H.-W., Lehmann R., Paul D., Marzahn J., Gahr M., Roesen-Wolff A.
Exp. Hematol. 27:505-511(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CGD PHE-193; ARG-222; TYR-338; HIS-339 AND PRO-546, VARIANT ARG-364.
[27]"Molecular analysis of chronic granulomatous disease caused by defects in gp91-phox."
Patino P.J., Perez J.E., Lopez J.A., Condino-Neto A., Grumach A.S., Botero J.H., Curnutte J.T., Garcia de Olarte D.
Hum. Mutat. 13:29-37(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CGD VAL-225 AND TYR-244.
[28]"Statistical and mutational analysis of chronic granulomatous disease in Japan with special reference to gp91-phox and p22-phox deficiency."
Ishibashi F., Nunoi H., Endo F., Matsuda I., Kanegasaki S.
Hum. Genet. 106:473-481(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CGD MET-54; ASP-55; GLU-57; TYR-101; ARG-209; GLY-224; LYS-309; TYR-338; HIS-339; PHE-344; GLU-389; PRO-420 AND ARG-516.
[29]"Characterization of 11 novel mutations in the X-linked chronic granulomatous disease (CYBB gene)."
Gerard B., El Benna J., Alcain F., Gougerot-Pocidalo M.-A., Grandchamp B., Chollet-Martin S.
Hum. Mutat. 18:163-163(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CGD 54-ARG-ALA-55 DEL; TRP-59; PRO-307 AND ARG-505.
[30]"Molecular and functional characterization of a new X-linked chronic granulomatous disease variant (X91+) case with a double missense mutation in the cytosolic gp91phox C-terminal tail."
Stasia M.J., Lardy B., Maturana A., Rousseau P., Martel C., Bordigoni P., Demaurex N., Morel F.
Biochim. Biophys. Acta 1586:316-330(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CGD ASN-303 AND ARG-304.
[31]"Functional analysis of two-amino acid substitutions in gp91 phox in a patient with X-linked flavocytochrome b558-positive chronic granulomatous disease by means of transgenic PLB-985 cells."
Bionda C., Li X.J., van Bruggen R., Eppink M., Roos D., Morel F., Stasia M.-J.
Hum. Genet. 115:418-427(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANTS CGD ASN-303 AND ARG-304.
[32]"First report of clinical, functional, and molecular investigation of chronic granulomatous disease in nine Jordanian families."
Bakri F.G., Martel C., Khuri-Bulos N., Mahafzah A., El-Khateeb M.S., Al-Wahadneh A.M., Hayajneh W.A., Hamamy H.A., Maquet E., Molin M., Stasia M.J.
J. Clin. Immunol. 29:215-230(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CGD ARG-408.
[33]"Germline CYBB mutations that selectively affect macrophages in kindreds with X-linked predisposition to tuberculous mycobacterial disease."
Bustamante J., Arias A.A., Vogt G., Picard C., Galicia L.B., Prando C., Grant A.V., Marchal C.C., Hubeau M., Chapgier A., de Beaucoudrey L., Puel A., Feinberg J., Valinetz E., Janniere L., Besse C., Boland A., Brisseau J.M. expand/collapse author list , Blanche S., Lortholary O., Fieschi C., Emile J.F., Boisson-Dupuis S., Al-Muhsen S., Woda B., Newburger P.E., Condino-Neto A., Dinauer M.C., Abel L., Casanova J.L.
Nat. Immunol. 12:213-221(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AMCBX2 PRO-178 AND PRO-231.
[34]"Identification and functional characterization of two novel mutations in the alpha-helical loop (residues 484-503) of CYBB/gp91(phox) resulting in the rare X91(+) variant of chronic granulomatous disease."
Boog B., Quach A., Costabile M., Smart J., Quinn P., Singh H., Gold M., Booker G., Choo S., Hii C.S., Ferrante A.
Hum. Mutat. 33:471-475(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CGD ASP-488 AND GLU-500.
+Additional computationally mapped references.

Web resources

CYBBbase

CYBB deficiency database

Mendelian genes cytochrome b-245, beta polypeptide (CYBB)

Leiden Open Variation Database (LOVD)

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X04011 mRNA. Translation: CAA27635.1. Different initiation.
AF469769 expand/collapse EMBL AC list , AF469757, AF469758, AF469759, AF469760, AF469761, AF469762, AF469763, AF469764, AF469765, AF469766, AF469767, AF469768 Genomic DNA. Translation: AAL76082.1.
DQ314869 Genomic DNA. Translation: ABC40728.1.
AK289753 mRNA. Translation: BAF82442.1.
CH471141 Genomic DNA. Translation: EAW59453.1.
BC032720 mRNA. Translation: AAH32720.1.
X05895 Genomic DNA. Translation: CAA29327.1. Sequence problems.
AB013904 Genomic DNA. Translation: BAA34183.1.
CCDSCCDS14242.1.
PIRS70773.
RefSeqNP_000388.2. NM_000397.3.
UniGeneHs.292356.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3A1FX-ray2.00A385-570[»]
ProteinModelPortalP04839.
SMRP04839. Positions 385-570.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107916. 4 interactions.
DIPDIP-42005N.
IntActP04839. 1 interaction.
MINTMINT-191276.
STRING9606.ENSP00000367851.

Chemistry

BindingDBP04839.
ChEMBLCHEMBL1287627.

Protein family/group databases

PeroxiBase5962. HsNOx02.
TCDB5.B.1.1.1. the phagocyte (gp91(phox)) nadph oxidase family.

PTM databases

PhosphoSiteP04839.

Polymorphism databases

DMDM115211.

Proteomic databases

MaxQBP04839.
PaxDbP04839.
PeptideAtlasP04839.
PRIDEP04839.

Protocols and materials databases

DNASU1536.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000378588; ENSP00000367851; ENSG00000165168.
ENST00000596392; ENSP00000468868; ENSG00000268765.
GeneID1536.
KEGGhsa:1536.
UCSCuc004ddr.2. human.

Organism-specific databases

CTD1536.
GeneCardsGC0XP037639.
GeneReviewsCYBB.
HGNCHGNC:2578. CYBB.
HPACAB032510.
MIM300481. gene.
300645. phenotype.
306400. phenotype.
neXtProtNX_P04839.
Orphanet379. Chronic granulomatous disease.
319623. X-linked mendelian susceptibility to mycobacterial diseases due to CYBB deficiency.
PharmGKBPA27076.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG287712.
HOGENOMHOG000216669.
HOVERGENHBG003760.
InParanoidP04839.
KOK08008.
OMAACPIPQF.
PhylomeDBP04839.
TreeFamTF105354.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressP04839.
BgeeP04839.
CleanExHS_CYBB.
GenevestigatorP04839.

Family and domain databases

InterProIPR000778. Cyt_b245_heavy_chain.
IPR013112. FAD-bd_8.
IPR017927. Fd_Rdtase_FAD-bd.
IPR013130. Fe3_Rdtase_TM_dom.
IPR013121. Fe_red_NAD-bd_6.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamPF08022. FAD_binding_8. 1 hit.
PF01794. Ferric_reduct. 1 hit.
PF08030. NAD_binding_6. 1 hit.
[Graphical view]
PRINTSPR00466. GP91PHOX.
SUPFAMSSF63380. SSF63380. 1 hit.
PROSITEPS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiCYBB.
GenomeRNAi1536.
NextBio6353.
PROP04839.
SOURCESearch...

Entry information

Entry nameCY24B_HUMAN
AccessionPrimary (citable) accession number: P04839
Secondary accession number(s): A8K138, Q2PP16
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 163 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM