Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Cytochrome b-245 heavy chain (EC 1.-.-.-) (CGD91-phox) (Cytochrome b(558) subunit beta) (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)

 CY24B_HUMAN             Reviewed;         570 AA.
P04839; A8K138; Q2PP16;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
25-OCT-2017, entry version 196.
RecName: Full=Cytochrome b-245 heavy chain;
EC=1.-.-.-;
AltName: Full=CGD91-phox;
AltName: Full=Cytochrome b(558) subunit beta;
Short=Cytochrome b558 subunit beta;
AltName: Full=Heme-binding membrane glycoprotein gp91phox;
AltName: Full=NADPH oxidase 2;
AltName: Full=Neutrophil cytochrome b 91 kDa polypeptide;
AltName: Full=Superoxide-generating NADPH oxidase heavy chain subunit;
AltName: Full=gp91-1;
AltName: Full=gp91-phox;
AltName: Full=p22 phagocyte B-cytochrome;
Name=CYBB; Synonyms=NOX2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2425263; DOI=10.1038/322032a0;
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.;
"Cloning the gene for an inherited human disorder -- chronic
granulomatous disease -- on the basis of its chromosomal location.";
Nature 322:32-38(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS CGD ASP-41 AND ARG-537,
AND VARIANTS ARG-364 AND GLU-517.
PubMed=12139950; DOI=10.1006/clim.2002.5230;
Jirapongsananuruk O., Niemela J.E., Malech H.L., Fleisher T.A.;
"CYBB mutation analysis in X-linked chronic granulomatous disease.";
Clin. Immunol. 104:73-76(2002).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lymph;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-135.
PubMed=3600768; DOI=10.1038/327717a0;
Dinauer M.C., Orkin S.H., Brown R., Jesaitis A.J., Parkos C.A.;
"The glycoprotein encoded by the X-linked chronic granulomatous
disease locus is a component of the neutrophil cytochrome b complex.";
Nature 327:717-720(1987).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 233-267.
TISSUE=Peripheral blood;
PubMed=9790760; DOI=10.1006/geno.1998.5510;
Kumatori A., Faizunnessa N.N., Suzuki S., Moriuchi T., Kurozumi H.,
Nakamura M.;
"Nonhomologous recombination between the cytochrome b558 heavy chain
gene (CYBB) and LINE-1 causes an X-linked chronic granulomatous
disease.";
Genomics 53:123-128(1998).
[9]
PROTEIN SEQUENCE OF 2-44, AND SUBUNIT.
PubMed=3600769; DOI=10.1038/327720a0;
Teahan C., Rowe P., Parker P., Totty N., Segal A.W.;
"The X-linked chronic granulomatous disease gene codes for the beta-
chain of cytochrome b-245.";
Nature 327:720-721(1987).
[10]
CHARACTERIZATION AS A PROTON CHANNEL.
PubMed=10578014; DOI=10.1085/jgp.114.6.771;
Henderson L.M., Meech R.W.;
"Evidence that the product of the human X-linked CGD gene, gp91-phox,
is a voltage-gated H(+) pathway.";
J. Gen. Physiol. 114:771-786(1999).
[11]
SUBUNIT, PHOSPHORYLATION, AND TISSUE SPECIFICITY.
PubMed=19028840; DOI=10.1096/fj.08-114553;
Raad H., Paclet M.H., Boussetta T., Kroviarski Y., Morel F.,
Quinn M.T., Gougerot-Pocidalo M.A., Dang P.M., El-Benna J.;
"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.";
FASEB J. 23:1011-1022(2009).
[12]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-132; ASN-149 AND ASN-240.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[14]
STRUCTURE BY NMR OF 556-570 IN COMPLEX WITH NCF1, AND INTERACTION WITH
NCF1.
PubMed=9224653; DOI=10.1042/bj3250249;
Adams E.R., Dratz E.A., Gizachew D., Deleo F.R., Yu L., Volpp B.D.,
Vlases M., Jesaitis A.J., Quinn M.T.;
"Interaction of human neutrophil flavocytochrome b with cytosolic
proteins: transferred-NOESY NMR studies of a gp91phox C-terminal
peptide bound to p47phox.";
Biochem. J. 325:249-257(1997).
[15]
INVOLVEMENT IN CGD, AND VARIANT CGD HIS-415.
PubMed=2556453; DOI=10.1172/JCI114393;
Dinauer M.C., Curnutte J.T., Rosen H.R., Orkin S.H.;
"A missense mutation in the neutrophil cytochrome b heavy chain in
cytochrome-positive X-linked chronic granulomatous disease.";
J. Clin. Invest. 84:2012-2016(1989).
[16]
VARIANTS CGD ARG-101; THR-156; TYR-209; SER-244 AND ALA-389.
PubMed=1710153;
Bolscher B.G.J.M., de Boer M., de Klein A., Weening R.S., Roos D.;
"Point mutations in the beta-subunit of cytochrome b558 leading to X-
linked chronic granulomatous disease.";
Blood 77:2482-2487(1991).
[17]
VARIANT CGD GLU-57.
PubMed=8101486; DOI=10.1007/BF01955051;
Ariga T., Sakiyama Y., Tomizawa K., Imajoh-Ohmi S., Kanegasaki S.,
Matsumoto S.;
"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.";
Eur. J. Pediatr. 152:469-472(1993).
[18]
VARIANT CGD HIS-339.
PubMed=7927345; DOI=10.1007/BF00201609;
Ariga T., Sakiyama Y., Matsumoto S.;
"Two novel point mutations in the cytochrome b 558 heavy chain gene,
detected in two Japanese patients with X-linked chronic granulomatous
disease.";
Hum. Genet. 94:441-441(1994).
[19]
VARIANT CGD GLY-500.
PubMed=8182143; DOI=10.1172/JCI117207;
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.;
"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.";
J. Clin. Invest. 93:2120-2126(1994).
[20]
VARIANTS CGD ILE-205; PHE-215 DEL AND GLN-342.
PubMed=8916969;
Hui Y.F., Chan S.Y., Lau Y.L.;
"Identification of mutations in seven Chinese patients with X-linked
chronic granulomatous disease.";
Blood 88:4021-4028(1996).
[21]
ERRATUM.
Hui Y.F., Chan S.Y., Lau Y.L.;
Blood 89:1843-1843(1996).
[22]
VARIANT CGD PHE-215 DEL.
PubMed=9111587;
Jendrossek V., Ritzel A., Neubauer B., Heyden S., Gahr M.;
"An in-frame triplet deletion within the gp91-phox gene in an adult X-
linked chronic granulomatous disease patient with residual NADPH-
oxidase activity.";
Eur. J. Haematol. 58:78-85(1997).
[23]
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.
PubMed=9585602; DOI=10.1086/301874;
Rae J., Newburger P.E., Dinauer M.C., Noack D., Hopkins P.J.,
Kuruto R., Curnutte J.T.;
"X-linked chronic granulomatous disease: mutations in the CYBB gene
encoding the gp91-phox component of respiratory-burst oxidase.";
Am. J. Hum. Genet. 62:1320-1331(1998).
[24]
VARIANT CGD TYR-101.
PubMed=9856476; DOI=10.1007/s004390050836;
Tsuda M., Kaneda M., Sakiyama T., Inana I., Owada M., Kiryu C.,
Shiraishi T., Kakinuma K.;
"A novel mutation at a probable heme-binding ligand in neutrophil
cytochrome b558 in atypical X-linked chronic granulomatous disease.";
Hum. Genet. 103:377-381(1998).
[25]
VARIANTS CGD ARG-179 AND 298-THR--THR-302 DEL.
PubMed=9794433;
Dusi S., Nadalini K.A., Donini M., Zentilin L., Wientjes F.B.,
Roos D., Giacca M., Rossi F.;
"Nicotinamide-adenine dinucleotide phosphate oxidase assembly and
activation in EBV-transformed B lymphoblastoid cell lines of normal
and chronic granulomatous disease patients.";
J. Immunol. 161:4968-4974(1998).
[26]
VARIANTS CGD MET-54; ASP-55; GLU-57; HIS-339 AND PHE-344.
PubMed=9667376; DOI=10.1203/00006450-199807000-00014;
Ariga T., Furuta H., Cho K., Sakiyama Y.;
"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.";
Pediatr. Res. 44:85-92(1998).
[27]
VARIANTS CGD PHE-193; ARG-222; TYR-338; HIS-339 AND PRO-546, AND
VARIANT ARG-364.
PubMed=10089913; DOI=10.1016/S0301-472X(98)00024-1;
Roesler J., Heyden S., Burdelski M., Schaefer H., Kreth H.-W.,
Lehmann R., Paul D., Marzahn J., Gahr M., Roesen-Wolff A.;
"Uncommon missense and splice mutations and resulting biochemical
phenotypes in German patients with X-linked chronic granulomatous
disease.";
Exp. Hematol. 27:505-511(1999).
[28]
VARIANTS CGD VAL-225 AND TYR-244.
PubMed=9888386;
DOI=10.1002/(SICI)1098-1004(1999)13:1<29::AID-HUMU3>3.0.CO;2-X;
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.;
"Molecular analysis of chronic granulomatous disease caused by defects
in gp91-phox.";
Hum. Mutat. 13:29-37(1999).
[29]
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.
PubMed=10914676; DOI=10.1007/s004390000288;
Ishibashi F., Nunoi H., Endo F., Matsuda I., Kanegasaki S.;
"Statistical and mutational analysis of chronic granulomatous disease
in Japan with special reference to gp91-phox and p22-phox
deficiency.";
Hum. Genet. 106:473-481(2000).
[30]
VARIANTS CGD 54-ARG-ALA-55 DEL; TRP-59; PRO-307 AND ARG-505.
PubMed=11462241; DOI=10.1002/humu.1166;
Gerard B., El Benna J., Alcain F., Gougerot-Pocidalo M.-A.,
Grandchamp B., Chollet-Martin S.;
"Characterization of 11 novel mutations in the X-linked chronic
granulomatous disease (CYBB gene).";
Hum. Mutat. 18:163-163(2001).
[31]
VARIANTS CGD ASN-303 AND ARG-304.
PubMed=11997083; DOI=10.1016/S0925-4439(01)00110-7;
Stasia M.J., Lardy B., Maturana A., Rousseau P., Martel C.,
Bordigoni P., Demaurex N., Morel F.;
"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.";
Biochim. Biophys. Acta 1586:316-330(2002).
[32]
CHARACTERIZATION OF VARIANTS CGD ASN-303 AND ARG-304.
PubMed=15338276; DOI=10.1007/s00439-004-1173-z;
Bionda C., Li X.J., van Bruggen R., Eppink M., Roos D., Morel F.,
Stasia M.-J.;
"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.";
Hum. Genet. 115:418-427(2004).
[33]
VARIANT CGD ARG-408.
PubMed=18773283; DOI=10.1007/s10875-008-9243-y;
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.;
"First report of clinical, functional, and molecular investigation of
chronic granulomatous disease in nine Jordanian families.";
J. Clin. Immunol. 29:215-230(2009).
[34]
VARIANTS IMD34 PRO-178 AND PRO-231.
PubMed=21278736; DOI=10.1038/ni.1992;
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.;
"Germline CYBB mutations that selectively affect macrophages in
kindreds with X-linked predisposition to tuberculous mycobacterial
disease.";
Nat. Immunol. 12:213-221(2011).
[35]
VARIANTS CGD ASP-488 AND GLU-500.
PubMed=22125116; DOI=10.1002/humu.22003;
Boog B., Quach A., Costabile M., Smart J., Quinn P., Singh H.,
Gold M., Booker G., Choo S., Hii C.S., Ferrante A.;
"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.";
Hum. Mutat. 33:471-475(2012).
[36]
VARIANTS CGD ASN-299; ASP-338; HIS-339; PHE-344 AND GLU-412.
PubMed=23910690; DOI=10.1016/j.jaci.2013.05.039;
Koeker M.Y., Camcioglu Y., van Leeuwen K., Kilic S.S., Barlan I.,
Yilmaz M., Metin A., de Boer M., Avcilar H., Patiroglu T.,
Yildiran A., Yegin O., Tezcan I., Sanal O., Roos D.;
"Clinical, functional, and genetic characterization of chronic
granulomatous disease in 89 Turkish patients.";
J. Allergy Clin. Immunol. 132:1156-1163(2013).
[37]
VARIANT CGD GLY-409.
PubMed=27666509; DOI=10.1016/j.micpath.2016.09.020;
Khan T.A., Kalsoom K., Iqbal A., Asif H., Rahman H., Farooq S.O.,
Naveed H., Nasir U., Amin M.U., Hussain M., Tipu H.N., Florea A.;
"A novel missense mutation in the NADPH binding domain of CYBB
abolishes the NADPH oxidase activity in a male patient with increased
susceptibility to infections.";
Microb. Pathog. 100:163-169(2016).
-!- 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:
Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
-!- SUBUNIT: 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. {ECO:0000269|PubMed:19028840,
ECO:0000269|PubMed:3600769, ECO:0000269|PubMed:9224653}.
-!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
-!- TISSUE SPECIFICITY: Detected in neutrophils (at protein level).
{ECO:0000269|PubMed:19028840}.
-!- PTM: Glycosylated. {ECO:0000269|PubMed:19159218}.
-!- PTM: Phosphorylated on Ser and Thr residues.
{ECO:0000269|PubMed:19028840}.
-!- 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. {ECO:0000269|PubMed:10089913,
ECO:0000269|PubMed:10914676, ECO:0000269|PubMed:11462241,
ECO:0000269|PubMed:11997083, ECO:0000269|PubMed:12139950,
ECO:0000269|PubMed:15338276, ECO:0000269|PubMed:1710153,
ECO:0000269|PubMed:18773283, ECO:0000269|PubMed:22125116,
ECO:0000269|PubMed:23910690, ECO:0000269|PubMed:2556453,
ECO:0000269|PubMed:27666509, ECO:0000269|PubMed:7927345,
ECO:0000269|PubMed:8101486, ECO:0000269|PubMed:8182143,
ECO:0000269|PubMed:8916969, ECO:0000269|PubMed:9111587,
ECO:0000269|PubMed:9585602, ECO:0000269|PubMed:9667376,
ECO:0000269|PubMed:9794433, ECO:0000269|PubMed:9856476,
ECO:0000269|PubMed:9888386}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Immunodeficiency 34 (IMD34) [MIM:300645]: A form of
Mendelian susceptibility to mycobacterial disease, a rare
condition characterized by predisposition to illness caused by
moderately virulent mycobacterial species, such as Bacillus
Calmette-Guerin (BCG) vaccine, 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, with
the exception of Salmonella which infects less than 50% of these
individuals. {ECO:0000269|PubMed:21278736}. Note=Disease
susceptibility is associated with variations affecting the gene
represented in this entry.
-!- SEQUENCE CAUTION:
Sequence=CAA27635.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=CAA29327.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=CYBBbase; Note=CYBB deficiency database;
URL="http://structure.bmc.lu.se/idbase/CYBBbase/";
-!- WEB RESOURCE: Name=Mendelian genes cytochrome b-245, beta
polypeptide (CYBB); Note=Leiden Open Variation Database (LOVD);
URL="http://www.lovd.nl/CYBB";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X04011; CAA27635.1; ALT_INIT; mRNA.
EMBL; AF469769; AAL76082.1; -; Genomic_DNA.
EMBL; AF469757; AAL76082.1; JOINED; Genomic_DNA.
EMBL; AF469758; AAL76082.1; JOINED; Genomic_DNA.
EMBL; AF469759; AAL76082.1; JOINED; Genomic_DNA.
EMBL; AF469760; AAL76082.1; JOINED; Genomic_DNA.
EMBL; AF469761; AAL76082.1; JOINED; Genomic_DNA.
EMBL; AF469762; AAL76082.1; JOINED; Genomic_DNA.
EMBL; AF469763; AAL76082.1; JOINED; Genomic_DNA.
EMBL; AF469764; AAL76082.1; JOINED; Genomic_DNA.
EMBL; AF469765; AAL76082.1; JOINED; Genomic_DNA.
EMBL; AF469766; AAL76082.1; JOINED; Genomic_DNA.
EMBL; AF469767; AAL76082.1; JOINED; Genomic_DNA.
EMBL; AF469768; AAL76082.1; JOINED; Genomic_DNA.
EMBL; DQ314869; ABC40728.1; -; Genomic_DNA.
EMBL; AK289753; BAF82442.1; -; mRNA.
EMBL; CH471141; EAW59453.1; -; Genomic_DNA.
EMBL; BC032720; AAH32720.1; -; mRNA.
EMBL; X05895; CAA29327.1; ALT_SEQ; Genomic_DNA.
EMBL; AB013904; BAA34183.1; -; Genomic_DNA.
CCDS; CCDS14242.1; -.
PIR; S70773; S70773.
RefSeq; NP_000388.2; NM_000397.3.
UniGene; Hs.292356; -.
PDB; 3A1F; X-ray; 2.00 A; A=385-570.
PDBsum; 3A1F; -.
ProteinModelPortal; P04839; -.
SMR; P04839; -.
BioGrid; 107916; 9.
DIP; DIP-42005N; -.
IntAct; P04839; 2.
MINT; MINT-191276; -.
STRING; 9606.ENSP00000367851; -.
BindingDB; P04839; -.
ChEMBL; CHEMBL1287627; -.
DrugBank; DB00514; Dextromethorphan.
PeroxiBase; 5962; HsNOx02.
TCDB; 5.B.1.1.1; the phagocyte (gp91(phox)) nadph oxidase family.
iPTMnet; P04839; -.
PhosphoSitePlus; P04839; -.
SwissPalm; P04839; -.
BioMuta; CYBB; -.
DMDM; 115211; -.
EPD; P04839; -.
MaxQB; P04839; -.
PaxDb; P04839; -.
PeptideAtlas; P04839; -.
PRIDE; P04839; -.
DNASU; 1536; -.
Ensembl; ENST00000378588; ENSP00000367851; ENSG00000165168.
GeneID; 1536; -.
KEGG; hsa:1536; -.
UCSC; uc004ddr.3; human.
CTD; 1536; -.
DisGeNET; 1536; -.
EuPathDB; HostDB:ENSG00000165168.7; -.
GeneCards; CYBB; -.
GeneReviews; CYBB; -.
HGNC; HGNC:2578; CYBB.
HPA; HPA051227; -.
MalaCards; CYBB; -.
MIM; 300481; gene.
MIM; 300645; phenotype.
MIM; 306400; phenotype.
neXtProt; NX_P04839; -.
OpenTargets; ENSG00000165168; -.
Orphanet; 379; Chronic granulomatous disease.
Orphanet; 319623; X-linked mendelian susceptibility to mycobacterial diseases due to CYBB deficiency.
PharmGKB; PA27076; -.
eggNOG; KOG0039; Eukaryota.
eggNOG; ENOG410XNZY; LUCA.
GeneTree; ENSGT00550000074350; -.
HOGENOM; HOG000216669; -.
HOVERGEN; HBG003760; -.
InParanoid; P04839; -.
KO; K21421; -.
OMA; KAGQWLF; -.
OrthoDB; EOG091G09RV; -.
PhylomeDB; P04839; -.
TreeFam; TF105354; -.
Reactome; R-HSA-1222556; ROS, RNS production in phagocytes.
Reactome; R-HSA-1236973; Cross-presentation of particulate exogenous antigens (phagosomes).
Reactome; R-HSA-3299685; Detoxification of Reactive Oxygen Species.
Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-HSA-5668599; RHO GTPases Activate NADPH Oxidases.
Reactome; R-HSA-6798695; Neutrophil degranulation.
SIGNOR; P04839; -.
ChiTaRS; CYBB; human.
GeneWiki; CYBB; -.
GenomeRNAi; 1536; -.
PRO; PR:P04839; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000165168; -.
CleanEx; HS_CYBB; -.
ExpressionAtlas; P04839; baseline and differential.
Genevisible; P04839; HS.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0043020; C:NADPH oxidase complex; IDA:BHF-UCL.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005635; C:nuclear envelope; IEA:Ensembl.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005791; C:rough endoplasmic reticulum; IEA:Ensembl.
GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IMP:BHF-UCL.
GO; GO:0020037; F:heme binding; IMP:BHF-UCL.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0046982; F:protein heterodimerization activity; IPI:BHF-UCL.
GO; GO:0016175; F:superoxide-generating NADPH oxidase activity; TAS:BHF-UCL.
GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
GO; GO:0045454; P:cell redox homeostasis; TAS:Reactome.
GO; GO:0071276; P:cellular response to cadmium ion; IEA:Ensembl.
GO; GO:0071361; P:cellular response to ethanol; IEA:Ensembl.
GO; GO:1904845; P:cellular response to L-glutamine; IEA:Ensembl.
GO; GO:0034599; P:cellular response to oxidative stress; TAS:Reactome.
GO; GO:0050665; P:hydrogen peroxide biosynthetic process; IEA:Ensembl.
GO; GO:0097411; P:hypoxia-inducible factor-1alpha signaling pathway; IEA:Ensembl.
GO; GO:0006954; P:inflammatory response; ISS:UniProtKB.
GO; GO:0045087; P:innate immune response; IMP:BHF-UCL.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0055114; P:oxidation-reduction process; IDA:BHF-UCL.
GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
GO; GO:0042535; P:positive regulation of tumor necrosis factor biosynthetic process; IEA:Ensembl.
GO; GO:0045730; P:respiratory burst; IMP:BHF-UCL.
GO; GO:1904044; P:response to aldosterone; IEA:Ensembl.
GO; GO:1990776; P:response to angiotensin; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
GO; GO:0042554; P:superoxide anion generation; IDA:BHF-UCL.
GO; GO:0006801; P:superoxide metabolic process; IDA:BHF-UCL.
GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; TAS:Reactome.
InterPro; IPR000778; Cyt_b245_heavy_chain.
InterPro; IPR013112; FAD-bd_8.
InterPro; IPR017927; Fd_Rdtase_FAD-bd.
InterPro; IPR013130; Fe3_Rdtase_TM_dom.
InterPro; IPR013121; Fe_red_NAD-bd_6.
InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
Pfam; PF08022; FAD_binding_8; 1.
Pfam; PF01794; Ferric_reduct; 1.
Pfam; PF08030; NAD_binding_6; 1.
PRINTS; PR00466; GP91PHOX.
SUPFAM; SSF63380; SSF63380; 1.
PROSITE; PS51384; FAD_FR; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Chronic granulomatous disease;
Complete proteome; Direct protein sequencing; Disease mutation;
Electron transport; FAD; Flavoprotein; Glycoprotein; Heme;
Ion channel; Ion transport; Iron; Membrane; Metal-binding; NADP;
Oxidoreductase; Phosphoprotein; Polymorphism; Reference proteome;
Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:3600769}.
CHAIN 2 570 Cytochrome b-245 heavy chain.
/FTId=PRO_0000210145.
TOPO_DOM 2 8 Cytoplasmic. {ECO:0000255}.
TRANSMEM 9 29 Helical. {ECO:0000255}.
TOPO_DOM 30 48 Extracellular. {ECO:0000255}.
TRANSMEM 49 69 Helical. {ECO:0000255}.
TOPO_DOM 70 102 Cytoplasmic. {ECO:0000255}.
TRANSMEM 103 123 Helical. {ECO:0000255}.
TOPO_DOM 124 169 Extracellular. {ECO:0000255}.
TRANSMEM 170 190 Helical. {ECO:0000255}.
TOPO_DOM 191 200 Cytoplasmic. {ECO:0000255}.
TRANSMEM 201 221 Helical. {ECO:0000255}.
TOPO_DOM 222 261 Extracellular. {ECO:0000255}.
TRANSMEM 262 282 Helical. {ECO:0000255}.
TOPO_DOM 283 570 Cytoplasmic. {ECO:0000255}.
DOMAIN 54 286 Ferric oxidoreductase.
DOMAIN 287 397 FAD-binding FR-type.
{ECO:0000255|PROSITE-ProRule:PRU00716}.
NP_BIND 338 344 FAD. {ECO:0000255}.
METAL 101 101 Iron (heme axial ligand). {ECO:0000305}.
METAL 115 115 Iron (heme axial ligand). {ECO:0000305}.
METAL 209 209 Iron (heme axial ligand). {ECO:0000305}.
METAL 222 222 Iron (heme axial ligand). {ECO:0000305}.
CARBOHYD 132 132 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 149 149 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 240 240 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
VARIANT 18 18 W -> C (in CGD).
/FTId=VAR_047264.
VARIANT 20 20 G -> R (in CGD; dbSNP:rs151344455).
{ECO:0000269|PubMed:9585602}.
/FTId=VAR_007873.
VARIANT 41 41 Y -> D (in CGD; dbSNP:rs151344453).
{ECO:0000269|PubMed:12139950}.
/FTId=VAR_025613.
VARIANT 54 55 Missing (in CGD).
{ECO:0000269|PubMed:11462241}.
/FTId=VAR_047265.
VARIANT 54 54 R -> M (in CGD; dbSNP:rs151344479).
{ECO:0000269|PubMed:10914676,
ECO:0000269|PubMed:23910690,
ECO:0000269|PubMed:9667376}.
/FTId=VAR_025614.
VARIANT 54 54 R -> S (in CGD; dbSNP:rs151344456).
{ECO:0000269|PubMed:9585602}.
/FTId=VAR_007874.
VARIANT 55 55 A -> D (in CGD; dbSNP:rs151344480).
{ECO:0000269|PubMed:10914676,
ECO:0000269|PubMed:9667376}.
/FTId=VAR_025615.
VARIANT 57 57 A -> E (in CGD; dbSNP:rs151344481).
{ECO:0000269|PubMed:10914676,
ECO:0000269|PubMed:8101486,
ECO:0000269|PubMed:9667376}.
/FTId=VAR_008845.
VARIANT 59 59 C -> R (in CGD; dbSNP:rs151344457).
{ECO:0000269|PubMed:9585602}.
/FTId=VAR_007875.
VARIANT 59 59 C -> W (in CGD; dbSNP:rs151344488).
{ECO:0000269|PubMed:11462241}.
/FTId=VAR_047266.
VARIANT 101 101 H -> R (in CGD; dbSNP:rs137854591).
{ECO:0000269|PubMed:1710153}.
/FTId=VAR_002432.
VARIANT 101 101 H -> Y (in CGD; dbSNP:rs137854594).
{ECO:0000269|PubMed:10914676,
ECO:0000269|PubMed:9856476}.
/FTId=VAR_007876.
VARIANT 119 119 H -> R (in CGD; dbSNP:rs151344458).
{ECO:0000269|PubMed:9585602}.
/FTId=VAR_007877.
VARIANT 156 156 A -> T (in CGD; dbSNP:rs137854590).
{ECO:0000269|PubMed:1710153,
ECO:0000269|PubMed:9585602}.
/FTId=VAR_002433.
VARIANT 178 178 T -> P (in IMD34; dbSNP:rs151344497).
{ECO:0000269|PubMed:21278736}.
/FTId=VAR_065365.
VARIANT 179 179 G -> R (in CGD; dbSNP:rs151344491).
{ECO:0000269|PubMed:9794433}.
/FTId=VAR_047267.
VARIANT 193 193 S -> F (in CGD; dbSNP:rs151344493).
{ECO:0000269|PubMed:10089913}.
/FTId=VAR_047268.
VARIANT 205 205 F -> I (in CGD; dbSNP:rs151344496).
{ECO:0000269|PubMed:8916969}.
/FTId=VAR_047269.
VARIANT 209 209 H -> Q (in CGD; dbSNP:rs151344459).
{ECO:0000269|PubMed:9585602}.
/FTId=VAR_007878.
VARIANT 209 209 H -> R (in CGD; dbSNP:rs151344482).
{ECO:0000269|PubMed:10914676}.
/FTId=VAR_025616.
VARIANT 209 209 H -> Y (in CGD; dbSNP:rs137854587).
{ECO:0000269|PubMed:1710153}.
/FTId=VAR_002434.
VARIANT 215 215 Missing (in CGD).
{ECO:0000269|PubMed:8916969,
ECO:0000269|PubMed:9111587}.
/FTId=VAR_007879.
VARIANT 222 222 H -> N (in CGD; dbSNP:rs151344460).
{ECO:0000269|PubMed:9585602}.
/FTId=VAR_007880.
VARIANT 222 222 H -> R (in CGD; dbSNP:rs151344462).
{ECO:0000269|PubMed:10089913,
ECO:0000269|PubMed:9585602}.
/FTId=VAR_007881.
VARIANT 222 222 H -> Y (in CGD; dbSNP:rs151344460).
{ECO:0000269|PubMed:9585602}.
/FTId=VAR_007882.
VARIANT 223 223 G -> L (in CGD; requires 2 nucleotide
substitutions; dbSNP:rs151344463 and
dbSNP:rs151344464).
{ECO:0000269|PubMed:9585602}.
/FTId=VAR_007883.
VARIANT 224 224 A -> G (in CGD; dbSNP:rs151344483).
{ECO:0000269|PubMed:10914676}.
/FTId=VAR_025617.
VARIANT 225 225 E -> V (in CGD; dbSNP:rs151344494).
{ECO:0000269|PubMed:9888386}.
/FTId=VAR_002435.
VARIANT 231 231 Q -> P (in IMD34; dbSNP:rs151344498).
{ECO:0000269|PubMed:21278736}.
/FTId=VAR_065366.
VARIANT 244 244 C -> R (in CGD; dbSNP:rs151344465).
{ECO:0000269|PubMed:9585602}.
/FTId=VAR_007884.
VARIANT 244 244 C -> S (in CGD; dbSNP:rs137854589).
{ECO:0000269|PubMed:1710153}.
/FTId=VAR_002436.
VARIANT 244 244 C -> Y (in CGD; dbSNP:rs137854589).
{ECO:0000269|PubMed:9888386}.
/FTId=VAR_002437.
VARIANT 298 302 Missing (in CGD).
{ECO:0000269|PubMed:9794433}.
/FTId=VAR_047270.
VARIANT 299 299 K -> N (in CGD).
{ECO:0000269|PubMed:23910690}.
/FTId=VAR_071861.
VARIANT 303 303 H -> N (in CGD; completely inhibits NADPH
oxidase activity; NADPH oxidase assembly
is abolished; dbSNP:rs137854595).
{ECO:0000269|PubMed:11997083,
ECO:0000269|PubMed:15338276}.
/FTId=VAR_016880.
VARIANT 304 304 P -> R (in CGD; reduces NADPH oxidase
activity to 4% of wild-type;
translocation to the membrane of the
phagosome is only attenuated;
dbSNP:rs137854596).
{ECO:0000269|PubMed:11997083,
ECO:0000269|PubMed:15338276}.
/FTId=VAR_016881.
VARIANT 307 307 T -> P (in CGD; dbSNP:rs151344489).
{ECO:0000269|PubMed:11462241}.
/FTId=VAR_047271.
VARIANT 309 309 E -> K (in CGD; dbSNP:rs151344466).
{ECO:0000269|PubMed:10914676,
ECO:0000269|PubMed:9585602}.
/FTId=VAR_007885.
VARIANT 315 315 Missing (in CGD).
{ECO:0000269|PubMed:9585602}.
/FTId=VAR_047272.
VARIANT 322 322 G -> E (in CGD; dbSNP:rs151344467).
{ECO:0000269|PubMed:9585602}.
/FTId=VAR_007886.
VARIANT 325 325 I -> F (in CGD; dbSNP:rs151344468).
{ECO:0000269|PubMed:9585602}.
/FTId=VAR_007887.
VARIANT 333 333 S -> P (in CGD; dbSNP:rs151344469).
{ECO:0000269|PubMed:9585602}.
/FTId=VAR_007888.
VARIANT 338 338 H -> D (in CGD).
{ECO:0000269|PubMed:23910690}.
/FTId=VAR_071862.
VARIANT 338 338 H -> Y (in CGD; dbSNP:rs151344484).
{ECO:0000269|PubMed:10089913,
ECO:0000269|PubMed:10914676}.
/FTId=VAR_025618.
VARIANT 339 339 P -> H (in CGD; dbSNP:rs151344470).
{ECO:0000269|PubMed:10089913,
ECO:0000269|PubMed:10914676,
ECO:0000269|PubMed:23910690,
ECO:0000269|PubMed:7927345,
ECO:0000269|PubMed:9585602,
ECO:0000269|PubMed:9667376}.
/FTId=VAR_002438.
VARIANT 342 342 L -> Q (in CGD; dbSNP:rs151344495).
{ECO:0000269|PubMed:8916969}.
/FTId=VAR_047273.
VARIANT 344 344 S -> F (in CGD; dbSNP:rs151344485).
{ECO:0000269|PubMed:10914676,
ECO:0000269|PubMed:23910690,
ECO:0000269|PubMed:9667376}.
/FTId=VAR_025619.
VARIANT 356 356 R -> P (in CGD; dbSNP:rs151344471).
{ECO:0000269|PubMed:9585602}.
/FTId=VAR_007889.
VARIANT 364 364 G -> R (in dbSNP:rs141756032).
{ECO:0000269|PubMed:10089913,
ECO:0000269|PubMed:12139950}.
/FTId=VAR_025620.
VARIANT 389 389 G -> A (in CGD; dbSNP:rs137854586).
{ECO:0000269|PubMed:1710153}.
/FTId=VAR_002439.
VARIANT 389 389 G -> E (in CGD; dbSNP:rs137854586).
{ECO:0000269|PubMed:10914676}.
/FTId=VAR_025621.
VARIANT 405 405 M -> R (in CGD; dbSNP:rs151344472).
{ECO:0000269|PubMed:9585602}.
/FTId=VAR_007890.
VARIANT 408 408 G -> E (in CGD; dbSNP:rs151344474).
{ECO:0000269|PubMed:9585602}.
/FTId=VAR_007891.
VARIANT 408 408 G -> R (in CGD; dbSNP:rs151344473).
{ECO:0000269|PubMed:18773283,
ECO:0000269|PubMed:9585602}.
/FTId=VAR_007892.
VARIANT 409 409 A -> G (in CGD).
{ECO:0000269|PubMed:27666509}.
/FTId=VAR_078386.
VARIANT 412 412 G -> E (in CGD).
{ECO:0000269|PubMed:23910690}.
/FTId=VAR_071863.
VARIANT 415 415 P -> H (in CGD; dbSNP:rs137854585).
{ECO:0000269|PubMed:2556453,
ECO:0000269|PubMed:9585602}.
/FTId=VAR_002440.
VARIANT 415 415 P -> L (in CGD; dbSNP:rs137854585).
{ECO:0000269|PubMed:9585602}.
/FTId=VAR_007893.
VARIANT 420 420 L -> P (in CGD; dbSNP:rs151344486).
{ECO:0000269|PubMed:10914676}.
/FTId=VAR_025622.
VARIANT 422 422 S -> P (in CGD; dbSNP:rs151344475).
{ECO:0000269|PubMed:9585602}.
/FTId=VAR_007894.
VARIANT 453 453 W -> R (in CGD; dbSNP:rs151344476).
{ECO:0000269|PubMed:9585602}.
/FTId=VAR_007895.
VARIANT 472 472 G -> S (in dbSNP:rs13306300).
/FTId=VAR_047274.
VARIANT 488 488 A -> D (in CGD).
{ECO:0000269|PubMed:22125116}.
/FTId=VAR_068012.
VARIANT 500 500 D -> E (in CGD).
{ECO:0000269|PubMed:22125116}.
/FTId=VAR_068013.
VARIANT 500 500 D -> G (in CGD; dbSNP:rs137854593).
{ECO:0000269|PubMed:8182143}.
/FTId=VAR_002441.
VARIANT 505 505 L -> R (in CGD; dbSNP:rs151344490).
{ECO:0000269|PubMed:11462241}.
/FTId=VAR_047275.
VARIANT 516 516 W -> C (in CGD; dbSNP:rs151344477).
{ECO:0000269|PubMed:9585602}.
/FTId=VAR_007896.
VARIANT 516 516 W -> R (in CGD; dbSNP:rs151344487).
{ECO:0000269|PubMed:10914676}.
/FTId=VAR_025623.
VARIANT 517 517 D -> E (in dbSNP:rs151344452).
{ECO:0000269|PubMed:12139950}.
/FTId=VAR_025624.
VARIANT 534 534 V -> D (in CGD; dbSNP:rs151344478).
{ECO:0000269|PubMed:9585602}.
/FTId=VAR_007897.
VARIANT 537 537 C -> R (in CGD; dbSNP:rs151344454).
{ECO:0000269|PubMed:12139950,
ECO:0000269|PubMed:9585602}.
/FTId=VAR_007898.
VARIANT 546 546 L -> P (in CGD; dbSNP:rs151344492).
{ECO:0000269|PubMed:10089913}.
/FTId=VAR_047276.
CONFLICT 14 14 V -> A (in Ref. 1 and 5). {ECO:0000305}.
HELIX 393 398 {ECO:0000244|PDB:3A1F}.
STRAND 401 409 {ECO:0000244|PDB:3A1F}.
HELIX 410 412 {ECO:0000244|PDB:3A1F}.
HELIX 413 429 {ECO:0000244|PDB:3A1F}.
STRAND 438 446 {ECO:0000244|PDB:3A1F}.
TURN 448 451 {ECO:0000244|PDB:3A1F}.
HELIX 452 467 {ECO:0000244|PDB:3A1F}.
STRAND 473 480 {ECO:0000244|PDB:3A1F}.
STRAND 509 512 {ECO:0000244|PDB:3A1F}.
HELIX 516 526 {ECO:0000244|PDB:3A1F}.
STRAND 531 538 {ECO:0000244|PDB:3A1F}.
HELIX 540 552 {ECO:0000244|PDB:3A1F}.
STRAND 562 566 {ECO:0000244|PDB:3A1F}.
SEQUENCE 570 AA; 65336 MW; 7E84051BD4000CE3 CRC64;
MGNWAVNEGL SIFVILVWLG LNVFLFVWYY RVYDIPPKFF YTRKLLGSAL ALARAPAACL
NFNCMLILLP VCRNLLSFLR GSSACCSTRV RRQLDRNLTF HKMVAWMIAL HSAIHTIAHL
FNVEWCVNAR VNNSDPYSVA LSELGDRQNE SYLNFARKRI KNPEGGLYLA VTLLAGITGV
VITLCLILII TSSTKTIRRS YFEVFWYTHH LFVIFFIGLA IHGAERIVRG QTAESLAVHN
ITVCEQKISE WGKIKECPIP QFAGNPPMTW KWIVGPMFLY LCERLVRFWR SQQKVVITKV
VTHPFKTIEL QMKKKGFKME VGQYIFVKCP KVSKLEWHPF TLTSAPEEDF FSIHIRIVGD
WTEGLFNACG CDKQEFQDAW KLPKIAVDGP FGTASEDVFS YEVVMLVGAG IGVTPFASIL
KSVWYKYCNN ATNLKLKKIY FYWLCRDTHA FEWFADLLQL LESQMQERNN AGFLSYNIYL
TGWDESQANH FAVHHDEEKD VITGLKQKTL YGRPNWDNEF KTIASQHPNT RIGVFLCGPE
ALAETLSKQS ISNSESGPRG VHFIFNKENF


Related products :

Catalog number Product name Quantity
EIAAB10225 CGD91-phox,CYBB,Cytochrome b(558) subunit beta,Cytochrome b-245 heavy chain,Cytochrome b558 subunit beta,gp91-1,gp91-phox,Heme-binding membrane glycoprotein gp91phox,Homo sapiens,Human,NADPH oxidase 2
EIAAB10228 CGD91-phox,CYBB,Cytochrome b(558) subunit beta,Cytochrome b-245 heavy chain,Cytochrome b558 subunit beta,gp91-1,gp91-phox,Heme-binding membrane glycoprotein gp91phox,Neutrophil cytochrome b 91 kDa pol
EIAAB10227 Cgd,CGD91-phox,Cybb,Cytochrome b(558) subunit beta,Cytochrome b-245 heavy chain,Cytochrome b558 subunit beta,gp91-1,gp91-phox,Heme-binding membrane glycoprotein gp91phox,Mouse,Mus musculus,Neutrophil
EIAAB10226 Bos taurus,Bovine,CGD91-phox,CYBB,Cytochrome b(558) subunit beta,Cytochrome b-245 heavy chain,Cytochrome b558 subunit beta,gp91-1,gp91-phox,Heme-binding membrane glycoprotein gp91phox,Neutrophil cytoc
EIAAB10222 CYBA,Cytochrome b(558) alpha chain,Cytochrome b-245 light chain,Cytochrome b558 subunit alpha,Neutrophil cytochrome b 22 kDa polypeptide,p22 phagocyte B-cytochrome,p22phox,p22-phox,Pig,Superoxide-gene
EIAAB10220 CYBA,Cytochrome b(558) alpha chain,Cytochrome b-245 light chain,Cytochrome b558 subunit alpha,Homo sapiens,Human,Neutrophil cytochrome b 22 kDa polypeptide,p22 phagocyte B-cytochrome,p22phox,p22-phox,
EIAAB10224 Cyba,Cytochrome b(558) alpha chain,Cytochrome b-245 light chain,Cytochrome b558 subunit alpha,Neutrophil cytochrome b 22 kDa polypeptide,p22 phagocyte B-cytochrome,p22phox,p22-phox,Rat,Rattus norvegic
EIAAB10219 Cyba,Cytochrome b(558) alpha chain,Cytochrome b-245 light chain,Cytochrome b558 subunit alpha,Mouse,Mus musculus,Neutrophil cytochrome b 22 kDa polypeptide,p22 phagocyte B-cytochrome,p22phox,p22-phox,
EIAAB10221 Bos taurus,Bovine,CYBA,Cytochrome b(558) alpha chain,Cytochrome b-245 light chain,Cytochrome b558 subunit alpha,Neutrophil cytochrome b 22 kDa polypeptide,p22 phagocyte B-cytochrome,p22phox,p22-phox,S
EIAAB10223 CYBA,Cytochrome b(558) alpha chain,Cytochrome b-245 light chain,Cytochrome b558 subunit alpha,Neutrophil cytochrome b 22 kDa polypeptide,Oryctolagus cuniculus,p22 phagocyte B-cytochrome,p22phox,p22-ph
EIAAB08789 COX8B,COX8H,Cytochrome c oxidase polypeptide VIII-liver_heart,Cytochrome c oxidase subunit 8-1,Cytochrome c oxidase subunit 8B, mitochondrial,Cytochrome c oxidase subunit 8H,Oryctolagus cuniculus,Rabb
EIAAB08785 Bos taurus,Bovine,COX8B,COX8H,Cytochrome c oxidase polypeptide VIII-heart,Cytochrome c oxidase subunit 8-1,Cytochrome c oxidase subunit 8B, mitochondrial,Cytochrome c oxidase subunit 8H,IX,VIIIb
EIAAB08788 Cox8b,Cox8h,Cytochrome c oxidase polypeptide VIII-heart,Cytochrome c oxidase subunit 8-1,Cytochrome c oxidase subunit 8B, mitochondrial,Cytochrome c oxidase subunit 8H,Rat,Rattus norvegicus
EIAAB08787 Cox8b,Cox8h,Cytochrome c oxidase polypeptide VIII-heart,Cytochrome c oxidase subunit 8-1,Cytochrome c oxidase subunit 8B, mitochondrial,Cytochrome c oxidase subunit 8H,Mouse,Mus musculus
EIAAB10091 Bos taurus,Bovine,COX VIb-1,COX6B,COX6B1,Cytochrome c oxidase polypeptide VII,Cytochrome c oxidase subunit 6B1,Cytochrome c oxidase subunit AED,Cytochrome c oxidase subunit VIb isoform 1
EIAAB10105 COX7A2,COX7AL,Cytochrome c oxidase subunit 7A2, mitochondrial,Cytochrome c oxidase subunit VIIaL,Cytochrome c oxidase subunit VIIa-L,Cytochrome c oxidase subunit VIIa-liver_heart,Homo sapiens,Human
EIAAB10086 COX VIa-M,COX6A,COX6A2,COX6AH,COXVIAH,Cytochrome c oxidase polypeptide VIa-heart,Cytochrome c oxidase subunit 6A2, mitochondrial,Cytochrome c oxidase subunit VIA-muscle,Homo sapiens,Human
EIAAB08781 COX8,COX8A,COX8L,Cytochrome c oxidase polypeptide VIII-liver_heart,Cytochrome c oxidase subunit 8-2,Cytochrome c oxidase subunit 8A, mitochondrial,Homo sapiens,Human
EIAAB08783 Cox8,Cox8a,Cox8l,Cytochrome c oxidase polypeptide VIII-liver,Cytochrome c oxidase subunit 8-2,Cytochrome c oxidase subunit 8A, mitochondrial,Rat,Rattus norvegicus
EIAAB08784 Cox8,Cox8a,Cox8l,Cytochrome c oxidase polypeptide VIII-liver,Cytochrome c oxidase subunit 8-2,Cytochrome c oxidase subunit 8A, mitochondrial,Mouse,Mus musculus
EIAAB08782 Bos taurus,Bovine,COX8,COX8A,COX8L,Cytochrome c oxidase polypeptide VIII-liver,Cytochrome c oxidase subunit 8-2,Cytochrome c oxidase subunit 8A, mitochondrial,IX
EIAAB08786 Canis familiaris,Canis lupus familiaris,COX8B,COX8H,Cytochrome c oxidase polypeptide VIII-heart,Cytochrome c oxidase subunit 8-1,Cytochrome c oxidase subunit 8B, mitochondrial,Cytochrome c oxidase sub
EIAAB10080 Bos taurus,Bovine,COX6A1,Cytochrome c oxidase polypeptide VIa-liver,Cytochrome c oxidase subunit 6A1, mitochondrial,Cytochrome c oxidase subunit SSG
EIAAB10102 Cox7a,Cox7a1,Cox7ah,Cytochrome c oxidase subunit 7A1, mitochondrial,Cytochrome c oxidase subunit VIIa-H,Cytochrome c oxidase subunit VIIa-heart,Cytochrome c oxidase subunit VIIa-M,Cytochrome c oxidase
EIAAB10101 COX7A1,COX7AH,Cytochrome c oxidase subunit 7A1, mitochondrial,Cytochrome c oxidase subunit VIIa-H,Cytochrome c oxidase subunit VIIa-heart,Cytochrome c oxidase subunit VIIa-M,Cytochrome c oxidase subun


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur