P04839 (CY24B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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). Interacts with calprotectin (S100A8/9).
Subcellular location	Cell membrane; Multi-pass membrane protein.
Post-translational modification	Glycosylated.
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.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.32 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.31
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 process	Electron transport Ion transport Transport
Cellular component	Cell membrane Membrane
Coding sequence diversity	Polymorphism
Disease	Chronic granulomatous disease Disease mutation
Domain	Transmembrane Transmembrane helix
Ligand	FAD Heme Iron Metal-binding NADP
Molecular function	Ion channel Oxidoreductase Voltage-gated channel
PTM	Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent Traceable author statement. Source: Reactome electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW hydrogen peroxide biosynthetic process Inferred from electronic annotation. Source: Compara inflammatory response Traceable author statement PubMed 7719350. Source: ProtInc innate immune response Inferred from mutant phenotype PubMed 9774399. Source: BHF-UCL interaction with host Traceable author statement. Source: Reactome phagosome maturation Traceable author statement. Source: Reactome respiratory burst Inferred from mutant phenotype PubMed 9774399. Source: BHF-UCL superoxide anion generation Inferred from direct assay PubMed 12042318. Source: BHF-UCL
Cellular_component	NADPH oxidase complex Inferred from direct assay PubMed 3305576. Source: BHF-UCL mitochondrion Inferred from electronic annotation. Source: Compara phagocytic vesicle membrane Traceable author statement. Source: Reactome
Molecular_function	flavin 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 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.9

Chain

2 – 570

569

Cytochrome b-245 heavy chain

PRO_0000210145

Regions

Topological domain

2 – 8

7

Cytoplasmic Potential

Transmembrane

9 – 29

21

Helical; Potential

Topological domain

30 – 48

19

Extracellular Potential

Transmembrane

49 – 69

21

Helical; Potential

Topological domain

70 – 102

33

Cytoplasmic Potential

Transmembrane

103 – 123

21

Helical; Potential

Topological domain

124 – 169

46

Extracellular Potential

Transmembrane

170 – 190

21

Helical; Potential

Topological domain

191 – 200

10

Cytoplasmic Potential

Transmembrane

201 – 221

21

Helical; Potential

Topological domain

222 – 261

40

Extracellular Potential

Transmembrane

262 – 282

21

Helical; 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

7

FAD Potential

Sites

Metal binding

101

1

Iron (heme axial ligand) Probable

Metal binding

115

1

Iron (heme axial ligand) Probable

Metal binding

209

1

Iron (heme axial ligand) Probable

Metal binding

222

1

Iron (heme axial ligand) Probable

Amino acid modifications

Glycosylation

132

1

N-linked (GlcNAc...) Ref.11

Glycosylation

149

1

N-linked (GlcNAc...) Ref.11

Glycosylation

240

1

N-linked (GlcNAc...) Ref.11

Natural variations

Natural variant

18

1

W → C in CGD.

VAR_047264

Natural variant

20

1

G → R in CGD. Ref.20
Corresponds to variant rs151344455 [ dbSNP | Ensembl ].

VAR_007873

Natural variant

41

1

Y → D in CGD. Ref.2
Corresponds to variant rs151344453 [ dbSNP | Ensembl ].

VAR_025613

Natural variant

54 – 55

2

Missing in CGD.

VAR_047265

Natural variant

54

1

R → M in CGD. Ref.23 Ref.26
Corresponds to variant rs151344479 [ dbSNP | Ensembl ].

VAR_025614

Natural variant

54

1

R → S in CGD. Ref.20
Corresponds to variant rs151344456 [ dbSNP | Ensembl ].

VAR_007874

Natural variant

55

1

A → D in CGD. Ref.23 Ref.26
Corresponds to variant rs151344480 [ dbSNP | Ensembl ].

VAR_025615

Natural variant

57

1

A → E in CGD. Ref.14 Ref.23 Ref.26
Corresponds to variant rs151344481 [ dbSNP | Ensembl ].

VAR_008845

Natural variant

59

1

C → R in CGD. Ref.20
Corresponds to variant rs151344457 [ dbSNP | Ensembl ].

VAR_007875

Natural variant

59

1

C → W in CGD. Ref.27
Corresponds to variant rs151344488 [ dbSNP | Ensembl ].

VAR_047266

Natural variant

101

1

H → R in CGD. Ref.13
Corresponds to variant rs137854591 [ dbSNP | Ensembl ].

VAR_002432

Natural variant

101

1

H → Y in CGD. Ref.21 Ref.26
Corresponds to variant rs137854594 [ dbSNP | Ensembl ].

VAR_007876

Natural variant

119

1

H → R in CGD. Ref.20
Corresponds to variant rs151344458 [ dbSNP | Ensembl ].

VAR_007877

Natural variant

156

1

A → T in CGD. Ref.13 Ref.20
Corresponds to variant rs137854590 [ dbSNP | Ensembl ].

VAR_002433

Natural variant

178

1

T → P in AMCBX2. Ref.31
Corresponds to variant rs151344497 [ dbSNP | Ensembl ].

VAR_065365

Natural variant

179

1

G → R in CGD. Ref.22
Corresponds to variant rs151344491 [ dbSNP | Ensembl ].

VAR_047267

Natural variant

193

1

S → F in CGD. Ref.24
Corresponds to variant rs151344493 [ dbSNP | Ensembl ].

VAR_047268

Natural variant

205

1

F → I in CGD. Ref.17
Corresponds to variant rs151344496 [ dbSNP | Ensembl ].

VAR_047269

Natural variant

209

1

H → Q in CGD. Ref.20
Corresponds to variant rs151344459 [ dbSNP | Ensembl ].

VAR_007878

Natural variant

209

1

H → R in CGD. Ref.26
Corresponds to variant rs151344482 [ dbSNP | Ensembl ].

VAR_025616

Natural variant

209

1

H → Y in CGD. Ref.13
Corresponds to variant rs137854587 [ dbSNP | Ensembl ].

VAR_002434

Natural variant

215

1

Missing in CGD. Ref.17 Ref.19

VAR_007879

Natural variant

222

1

H → N in CGD. Ref.20
Corresponds to variant rs151344460 [ dbSNP | Ensembl ].

VAR_007880

Natural variant

222

1

H → R in CGD. Ref.20 Ref.24
Corresponds to variant rs151344462 [ dbSNP | Ensembl ].

VAR_007881

Natural variant

222

1

H → Y in CGD. Ref.20
Corresponds to variant rs151344460 [ dbSNP | Ensembl ].

VAR_007882

Natural variant

223

1

G → L in CGD; requires 2 nucleotide substitutions. Ref.20
Corresponds to variants rs151344463 [ dbSNP | Ensembl ] and rs151344464 [ dbSNP | Ensembl ].

VAR_007883

Natural variant

224

1

A → G in CGD. Ref.26
Corresponds to variant rs151344483 [ dbSNP | Ensembl ].

VAR_025617

Natural variant

225

1

E → V in CGD. Ref.25
Corresponds to variant rs151344494 [ dbSNP | Ensembl ].

VAR_002435

Natural variant

231

1

Q → P in AMCBX2. Ref.31
Corresponds to variant rs151344498 [ dbSNP | Ensembl ].

VAR_065366

Natural variant

244

1

C → R in CGD. Ref.20
Corresponds to variant rs151344465 [ dbSNP | Ensembl ].

VAR_007884

Natural variant

244

1

C → S in CGD. Ref.13
Corresponds to variant rs137854589 [ dbSNP | Ensembl ].

VAR_002436

Natural variant

244

1

C → Y in CGD. Ref.25
Corresponds to variant rs137854589 [ dbSNP | Ensembl ].

VAR_002437

Natural variant

298 – 302

5

Missing in CGD.

VAR_047270

Natural variant

303

1

H → N in CGD; completely inhibits NADPH oxidase activity; NADPH oxidase assembly is abolished. Ref.28 Ref.29
Corresponds to variant rs137854595 [ dbSNP | Ensembl ].

VAR_016880

Natural variant

304

1

P → R in CGD; reduces NADPH oxidase activity to 4% of wild-type; translocation to the membrane of the phagosome is only attenuated. Ref.28 Ref.29
Corresponds to variant rs137854596 [ dbSNP | Ensembl ].

VAR_016881

Natural variant

307

1

T → P in CGD. Ref.27
Corresponds to variant rs151344489 [ dbSNP | Ensembl ].

VAR_047271

Natural variant

309

1

E → K in CGD. Ref.20 Ref.26
Corresponds to variant rs151344466 [ dbSNP | Ensembl ].

VAR_007885

Natural variant

315

1

Missing in CGD. Ref.20

VAR_047272

Natural variant

322

1

G → E in CGD. Ref.20
Corresponds to variant rs151344467 [ dbSNP | Ensembl ].

VAR_007886

Natural variant

325

1

I → F in CGD. Ref.20
Corresponds to variant rs151344468 [ dbSNP | Ensembl ].

VAR_007887

Natural variant

333

1

S → P in CGD. Ref.20
Corresponds to variant rs151344469 [ dbSNP | Ensembl ].

VAR_007888

Natural variant

338

1

H → Y in CGD. Ref.24 Ref.26
Corresponds to variant rs151344484 [ dbSNP | Ensembl ].

VAR_025618

Natural variant

339

1

P → H in CGD. Ref.15 Ref.20 Ref.23 Ref.24 Ref.26
Corresponds to variant rs151344470 [ dbSNP | Ensembl ].

VAR_002438

Natural variant

342

1

L → Q in CGD. Ref.17
Corresponds to variant rs151344495 [ dbSNP | Ensembl ].

VAR_047273

Natural variant

344

1

S → F in CGD. Ref.23 Ref.26
Corresponds to variant rs151344485 [ dbSNP | Ensembl ].

VAR_025619

Natural variant

356

1

R → P in CGD. Ref.20
Corresponds to variant rs151344471 [ dbSNP | Ensembl ].

VAR_007889

Natural variant

364

1

G → R. Ref.2 Ref.24
Corresponds to variant rs141756032 [ dbSNP | Ensembl ].

VAR_025620

Natural variant

389

1

G → A in CGD. Ref.13
Corresponds to variant rs137854586 [ dbSNP | Ensembl ].

VAR_002439

Natural variant

389

1

G → E in CGD. Ref.26
Corresponds to variant rs137854586 [ dbSNP | Ensembl ].

VAR_025621

Natural variant

405

1

M → R in CGD. Ref.20
Corresponds to variant rs151344472 [ dbSNP | Ensembl ].

VAR_007890

Natural variant

408

1

G → E in CGD. Ref.20
Corresponds to variant rs151344474 [ dbSNP | Ensembl ].

VAR_007891

Natural variant

408

1

G → R in CGD. Ref.20 Ref.30
Corresponds to variant rs151344473 [ dbSNP | Ensembl ].

VAR_007892

Natural variant

415

1

P → H in CGD. Ref.12 Ref.20
Corresponds to variant rs137854585 [ dbSNP | Ensembl ].

VAR_002440

Natural variant

415

1

P → L in CGD. Ref.20
Corresponds to variant rs137854585 [ dbSNP | Ensembl ].

VAR_007893

Natural variant

420

1

L → P in CGD. Ref.26
Corresponds to variant rs151344486 [ dbSNP | Ensembl ].

VAR_025622

Natural variant

422

1

S → P in CGD. Ref.20
Corresponds to variant rs151344475 [ dbSNP | Ensembl ].

VAR_007894

Natural variant

453

1

W → R in CGD. Ref.20
Corresponds to variant rs151344476 [ dbSNP | Ensembl ].

VAR_007895

Natural variant

472

1

G → S.
Corresponds to variant rs13306300 [ dbSNP | Ensembl ].

VAR_047274

Natural variant

488

1

A → D in CGD. Ref.32

VAR_068012

Natural variant

500

1

D → E in CGD. Ref.32

VAR_068013

Natural variant

500

1

D → G in CGD. Ref.16
Corresponds to variant rs137854593 [ dbSNP | Ensembl ].

VAR_002441

Natural variant

505

1

L → R in CGD. Ref.27
Corresponds to variant rs151344490 [ dbSNP | Ensembl ].

VAR_047275

Natural variant

516

1

W → C in CGD. Ref.20
Corresponds to variant rs151344477 [ dbSNP | Ensembl ].

VAR_007896

Natural variant

516

1

W → R in CGD. Ref.26
Corresponds to variant rs151344487 [ dbSNP | Ensembl ].

VAR_025623

Natural variant

517

1

D → E. Ref.2
Corresponds to variant rs151344452 [ dbSNP | Ensembl ].

VAR_025624

Natural variant

534

1

V → D in CGD. Ref.20
Corresponds to variant rs151344478 [ dbSNP | Ensembl ].

VAR_007897

Natural variant

537

1

C → R in CGD. Ref.2 Ref.20
Corresponds to variant rs151344454 [ dbSNP | Ensembl ].

VAR_007898

Natural variant

546

1

L → P in CGD. Ref.24
Corresponds to variant rs151344492 [ dbSNP | Ensembl ].

VAR_047276

Experimental info

Sequence conflict

14

1

V → A Ref.1

Sequence conflict

14

1

V → A Ref.5

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

570

Helix Strand Turn

Details...

Helix

393 – 398

6

Beta strand

401 – 409

9

Helix

410 – 412

3

Helix

413 – 429

17

Beta strand

438 – 446

9

Turn

448 – 451

4

Helix

452 – 467

16

Beta strand

473 – 480

8

Beta strand

509 – 512

4

Helix

516 – 526

11

Beta strand

531 – 538

8

Helix

540 – 552

13

Beta strand

562 – 566

5

Sequences

	Sequence		Length	Mass (Da)
	P04839 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 7E84051BD4000CE3	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

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] [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. , 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. , 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.
[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]	"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, MASS SPECTROMETRY. Tissue: Liver.
[12]	"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.
[13]	"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.
[14]	"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.
[15]	"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.
[16]	"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.
[17]	"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.
[18]	Erratum Hui Y.F., Chan S.Y., Lau Y.L. Blood 89:1843-1843(1996)
[19]	"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.
[20]	"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.
[21]	"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.
[22]	"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.
[23]	"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.
[24]	"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.
[25]	"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.
[26]	"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.
[27]	"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.
[28]	"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.
[29]	"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.
[30]	"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.
[31]	"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. , 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.
[32]	"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

GeneReviews

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 , 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.

IPI

IPI00218646.

PIR

S70773.

RefSeq

NP_000388.2. NM_000397.3.

UniGene

Hs.292356.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3A1F	X-ray	2.00	A	385-570	[»]

ProteinModelPortal

P04839.

ModBase

Search...

Protein-protein interaction databases

IntAct

P04839. 1 interaction.

STRING

9606.ENSP00000367851.

Protein family/group databases

PeroxiBase

5962. HsNOx02.

TCDB

5.B.1.1.1. phagocyte (gp91phox) NADPH oxidase family.

PTM databases

PhosphoSite

P04839.

Polymorphism databases

DMDM

115211.

Proteomic databases

PaxDb

P04839.

PeptideAtlas

P04839.

PRIDE

P04839.

Protocols and materials databases

DNASU

1536.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000378588; ENSP00000367851; ENSG00000165168.
ENST00000596392; ENSP00000468868; ENSG00000268765.

GeneID

1536.

KEGG

hsa:1536.

UCSC

uc004ddr.2. human.

Organism-specific databases

CTD

1536.

GeneCards

GC0XP037639.

HGNC

HGNC:2578. CYBB.

HPA

CAB032510.

MIM

300481. gene.
300645. phenotype.
306400. phenotype.

neXtProt

NX_P04839.

Orphanet

379. Chronic granulomatous disease.
748. Mendelian susceptibility to mycobacterial diseases.

PharmGKB

PA27076.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG287712.

HOGENOM

HOG000216669.

HOVERGEN

HBG003760.

InParanoid

P04839.

KO

K08008.

OMA

QCCSRTA.

OrthoDB

EOG4J117S.

PhylomeDB

P04839.

Enzyme and pathway databases

Reactome

REACT_116125. Disease.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P04839.

Bgee

P04839.

CleanEx

HS_CYBB.

Genevestigator

P04839.

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_Rdtase_TM_dom.
IPR013121. Fe_red_NAD-bd_6.
IPR017938. Riboflavin_synthase-like_b-brl.
[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.

SUPFAM

SSF63380. Riboflavin_synthase_like_b-brl. 1 hit.

PROSITE

PS51384. FAD_FR. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P04839.

ChEMBL

CHEMBL1287627.

GenomeRNAi

1536.

NextBio

6353.

SOURCE

Search...

Entry information

Entry name

CY24B_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 149 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.