Cytochrome b-245 heavy chain - Homo sapiens (Human)

Names and origin

Protein names

Recommended name:
    Cytochrome b-245 heavy chain
    EC=1.-.-.-
Alternative name(s):
    p22 phagocyte B-cytochrome
    Neutrophil cytochrome b 91 kDa polypeptide
    Heme-binding membrane glycoprotein gp91phox
    CGD91-phox
    gp91-phox
    gp91-1
    Cytochrome b(558) subunit beta
    Cytochrome b558 subunit beta
    Superoxide-generating NADPH oxidase heavy chain subunit
    NADPH oxidase 2

Gene names

Name:	CYBB
Synonyms:	NOX2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	570 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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).
Subcellular location	Membrane; Multi-pass membrane protein.
Post-translational modification	Glycosylated.
Involvement in disease	Defects in CYBB are a cause of chronic granulomatous disease X-linked (XCGD) [MIM:306400]. 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. Ref.2 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27
Sequence similarities	Contains 1 FAD-binding FR-type domain. Contains 1 ferric oxidoreductase domain.
Sequence caution	The sequence CAA29327.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Electron transport Ion transport Transport
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Disease	Chronic granulomatous disease Disease mutation
Domain	Transmembrane
Ligand	FAD Heme Iron Metal-binding NADP
Molecular function	Ionic channel Oxidoreductase Voltage-gated channel
PTM	Glycoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW inflammatory response Traceable author statement. Source: ProtInc innate immune response Inferred from mutant phenotype. Source: UniProtKB ion transport Inferred from electronic annotation. Source: UniProtKB-KW respiratory burst Inferred from mutant phenotype. Source: UniProtKB superoxide release Inferred from direct assay. Source: UniProtKB
Cellular component	NADPH oxidase complex Inferred from direct assay. Source: UniProtKB
Molecular function	FAD binding Inferred from mutant phenotype. Source: UniProtKB electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from mutant phenotype. Source: UniProtKB protein heterodimerization activity Inferred from physical interaction. Source: UniProtKB superoxide-generating NADPH oxidase activity Traceable author statement. Source: UniProtKB voltage-gated ion channel activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.7

Chain

2 – 570

569

Cytochrome b-245 heavy chain

PRO_0000210145

Regions

Topological domain

2 – 8

Cytoplasmic Potential

Transmembrane

9 – 29

Potential

Topological domain

30 – 48

Extracellular Potential

Transmembrane

49 – 69

Potential

Topological domain

70 – 102

Cytoplasmic Potential

Transmembrane

103 – 123

Potential

Topological domain

124 – 169

Extracellular Potential

Transmembrane

170 – 190

Potential

Topological domain

191 – 200

Cytoplasmic Potential

Transmembrane

201 – 221

Potential

Topological domain

222 – 261

Extracellular Potential

Transmembrane

262 – 282

Potential

Topological domain

283 – 570

288

Cytoplasmic Potential

Domain

54 – 286

233

Ferric oxidoreductase

Domain

287 – 397

111

FAD-binding FR-type

Nucleotide binding

338 – 344

FAD Potential

Sites

Metal binding

101

Iron (heme axial ligand) Probable

Metal binding

115

Iron (heme axial ligand) Probable

Metal binding

Iron (heme axial ligand) Probable

Metal binding

Iron (heme axial ligand) Probable

Amino acid modifications

Glycosylation

132

N-linked (GlcNAc...)

Glycosylation

149

N-linked (GlcNAc...)

Glycosylation

240

N-linked (GlcNAc...)

Natural variations

Natural variant

W → C in XCGD.

VAR_047264

Natural variant

G → R in XCGD. Ref.18

VAR_007873

Natural variant

Y → D in XCGD. Ref.2

VAR_025613

Natural variant

54 – 55

Missing in XCGD. Ref.18 Ref.21 Ref.24

VAR_047265

Natural variant

R → M in XCGD. Ref.18 Ref.21 Ref.24

VAR_025614

Natural variant

R → S in XCGD. Ref.18 Ref.21 Ref.24

VAR_007874

Natural variant

A → D in XCGD. Ref.21 Ref.24

VAR_025615

Natural variant

A → E in XCGD. Ref.12 Ref.21 Ref.24

VAR_008845

Natural variant

C → R in XCGD. Ref.18 Ref.25

VAR_007875

Natural variant

C → W in XCGD. Ref.18 Ref.25

VAR_047266

Natural variant

101

H → R in XCGD. Ref.11 Ref.19 Ref.24

VAR_002432

Natural variant

101

H → Y in XCGD. Ref.11 Ref.19 Ref.24

VAR_007876

Natural variant

119

H → R in XCGD. Ref.18

VAR_007877

Natural variant

156

A → T in XCGD. Ref.11 Ref.18

VAR_002433

Natural variant

179

G → R in XCGD. Ref.20

VAR_047267

Natural variant

193

S → F in XCGD. Ref.22

VAR_047268

Natural variant

205

F → I in XCGD. Ref.15

VAR_047269

Natural variant

H → Q in XCGD. Ref.11 Ref.18 Ref.24

VAR_007878

Natural variant

H → R in XCGD. Ref.11 Ref.18 Ref.24

VAR_025616

Natural variant

H → Y in XCGD. Ref.11 Ref.18 Ref.24

VAR_002434

Natural variant

215

Missing in XCGD. Ref.15 Ref.17

VAR_007879

Natural variant

H → N in XCGD. Ref.18 Ref.22

VAR_007880

Natural variant

H → R in XCGD. Ref.18 Ref.22

VAR_007881

Natural variant

H → Y in XCGD. Ref.18 Ref.22

VAR_007882

Natural variant

223

G → L in XCGD; requires 2 nucleotide substitutions. Ref.18

VAR_007883

Natural variant

224

A → G in XCGD. Ref.24

VAR_025617

Natural variant

225

E → V in XCGD. Ref.23

VAR_002435

Natural variant

244

C → R in XCGD. Ref.11 Ref.18 Ref.23

VAR_007884

Natural variant

244

C → S in XCGD. Ref.11 Ref.18 Ref.23

VAR_002436

Natural variant

244

C → Y in XCGD. Ref.11 Ref.18 Ref.23

VAR_002437

Natural variant

298 – 302

Missing in XCGD. Ref.20

VAR_047270

Natural variant

303

H → N in XCGD; completely inhibits NADPH oxidase activity; NADPH oxidase assembly is abolished. Ref.26 Ref.27

VAR_016880

Natural variant

304

P → R in XCGD; reduces NADPH oxidase activity to 4% of wild-type; translocation to the membrane of the phagosome is only attenuated. Ref.26 Ref.27

VAR_016881

Natural variant

307

T → P in XCGD. Ref.25

VAR_047271

Natural variant

309

E → K in XCGD. Ref.18 Ref.24

VAR_007885

Natural variant

315

Missing in XCGD. Ref.18

VAR_047272

Natural variant

322

G → E in XCGD. Ref.18

VAR_007886

Natural variant

325

I → F in XCGD. Ref.18

VAR_007887

Natural variant

333

S → P in XCGD. Ref.18

VAR_007888

Natural variant

338

H → Y in XCGD. Ref.22 Ref.24

VAR_025618

Natural variant

339

P → H in XCGD. Ref.13 Ref.18 Ref.21 Ref.22 Ref.24

VAR_002438

Natural variant

342

L → Q in XCGD. Ref.15

VAR_047273

Natural variant

344

S → F in XCGD. Ref.21 Ref.24

VAR_025619

Natural variant

356

R → P in XCGD. Ref.18

VAR_007889

Natural variant

364

G → R Ref.2 Ref.22

VAR_025620

Natural variant

389

G → A in XCGD. Ref.11 Ref.24

VAR_002439

Natural variant

389

G → E in XCGD. Ref.11 Ref.24

VAR_025621

Natural variant

405

M → R in XCGD. Ref.18

VAR_007890

Natural variant

408

G → E in XCGD. Ref.18

VAR_007891

Natural variant

408

G → R in XCGD. Ref.18

VAR_007892

Natural variant

415

P → H in XCGD. Ref.10 Ref.18

VAR_002440

Natural variant

415

P → L in XCGD. Ref.10 Ref.18

VAR_007893

Natural variant

420

L → P in XCGD. Ref.24

VAR_025622

Natural variant

422

S → P in XCGD. Ref.18

VAR_007894

Natural variant

453

W → R in XCGD. Ref.18

VAR_007895

Natural variant

472

G → S: dbSNP rs13306300.

VAR_047274

Natural variant

500

D → G in XCGD. Ref.14

VAR_002441

Natural variant

505

L → R in XCGD. Ref.25

VAR_047275

Natural variant

516

W → C in XCGD. Ref.18 Ref.24

VAR_007896

Natural variant

516

W → R in XCGD. Ref.18 Ref.24

VAR_025623

Natural variant

517

D → E Ref.2

VAR_025624

Natural variant

534

V → D in XCGD. Ref.18

VAR_007897

Natural variant

537

C → R in XCGD. Ref.2 Ref.18

VAR_007898

Natural variant

546

L → P in XCGD. Ref.22

VAR_047276

Experimental info

Sequence conflict

V → A Ref.1

Sequence conflict

V → A Ref.5

Sequences

Sequence

Length

Mass (Da)

Tools

P04839-1 [UniParc].

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

FASTA

570

65,336

        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' referencesShow '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: 2425263] [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: 12139950] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS XCGD 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]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lymph.
[5]	"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: 3600768] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-135.
[6]	"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: 9790760] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 233-267. Tissue: Peripheral blood.
[7]	"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: 3600769] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-44.
[8]	"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: 10578014] [Abstract] Cited for: CHARACTERIZATION AS A PROTON CHANNEL.
[9]	"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: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-132; ASN-149 AND ASN-240, MASS SPECTROMETRY. Tissue: Liver.
[10]	"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: 2556453] [Abstract] Cited for: VARIANT XCGD HIS-415.
[11]	"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: 1710153] [Abstract] Cited for: VARIANTS XCGD ARG-101; THR-156; TYR-209; SER-244 AND ALA-389.
[12]	"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: 8101486] [Abstract] Cited for: VARIANT XCGD GLU-57.
[13]	"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: 7927345] [Abstract] Cited for: VARIANT XCGD HIS-339.
[14]	"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: 8182143] [Abstract] Cited for: VARIANT XCGD GLY-500.
[15]	"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: 8916969] [Abstract] Cited for: VARIANTS XCGD ILE-205; PHE-215 DEL AND GLN-342.
[16]	Erratum Hui Y.F., Chan S.Y., Lau Y.L. Blood 89:1843-1843(1996)
[17]	"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: 9111587] [Abstract] Cited for: VARIANT XCGD PHE-215 DEL.
[18]	"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: 9585602] [Abstract] Cited for: VARIANTS XCGD 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.
[19]	"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: 9856476] [Abstract] Cited for: VARIANT XCGD TYR-101.
[20]	"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: 9794433] [Abstract] Cited for: VARIANTS XCGD ARG-179 AND 298-THR--THR-302 DEL.
[21]	"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: 9667376] [Abstract] Cited for: VARIANTS XCGD MET-54; ASP-55; GLU-57; HIS-339 AND PHE-344.
[22]	"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: 10089913] [Abstract] Cited for: VARIANTS XCGD PHE-193; ARG-222; TYR-338; HIS-339 AND PRO-546, VARIANT ARG-364.
[23]	"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: 9888386] [Abstract] Cited for: VARIANTS XCGD VAL-225 AND TYR-244.
[24]	"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: 10914676] [Abstract] Cited for: VARIANTS XCGD 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.
[25]	"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: 11462241] [Abstract] Cited for: VARIANTS XCGD 54-ARG-ALA-55 DEL; TRP-59; PRO-307 AND ARG-505.
[26]	"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: 11997083] [Abstract] Cited for: VARIANTS XCGD ASN-303 AND ARG-304.
[27]	"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: 15338276] [Abstract] Cited for: CHARACTERIZATION OF VARIANTS XCGD ASN-303 AND ARG-304.
+	Additional computationally mapped references.

Web resources

CYBBbase

CYBB deficiency database

GeneReviews

Cross-references

Sequence databases
	X04011 mRNA. Translation: CAA27635.1. Different initiation. AF469769 AF469768 Genomic DNA. Translation: AAL76082.1. DQ314869 Genomic DNA. Translation: ABC40728.1. BC032720 mRNA. Translation: AAH32720.1. X05895 Genomic DNA. Translation: CAA29327.1. Sequence problems. AB013904 Genomic DNA. Translation: BAA34183.1.
IPI	IPI00218646.
PIR	S70773.
RefSeq	NP_000388.2.
UniGene	Hs.292356
3D structure databases
ModBase	Search...
Protein family/group databases
PeroxiBase	5962. HsNOx02.
TCDB	5.B.1.1.1. phagocyte (gp91phox) NADPH oxidase family.
Proteomic databases
PeptideAtlas	P04839.
PRIDE	P04839.
Genome annotation databases
Ensembl	ENSG00000165168. Homo sapiens. [Contig view]
GeneID	1536.
KEGG	hsa:1536.
Organism-specific databases
GeneCards	GC0XP037524.
H-InvDB	HIX0016724.
HGNC	HGNC:2578. CYBB.
MIM	300481. gene. 306400. phenotype.
Orphanet	379. Granulomatous disease, chronic.
PharmGKB	PA27076.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	P04839.
HOVERGEN	P04839.
OMA	P04839. QERNNAN.
Gene expression databases
ArrayExpress	P04839.
Bgee	P04839.
CleanEx	HS_CYBB.
GermOnline	ENSG00000165168. Homo sapiens.
Family and domain databases
InterPro	IPR000778. Cyt_b245_heavy_chain. IPR013112. FAD_bd_8. IPR017927. Fd_Rdtase_FAD-bd. IPR013130. Fe3_reduct_TM_N. IPR013121. Fe_red_NAD_bd_6. [Graphical view]
Pfam	PF08022. FAD_binding_8. 1 hit. PF01794. Ferric_reduct. 1 hit. PF08030. NAD_binding_6. 1 hit. [Graphical view]
PRINTS	PR00466. GP91PHOX.
PROSITE	PS51384. FAD_FR. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	6353.
SOURCE	Search...

Entry information

Entry name

CY24B_HUMAN

Accession

Primary (citable) accession number: P04839
Secondary accession number(s): Q2PP16

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 108 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)