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Reviewed, UniProtKB/Swiss-Prot P04839 (CY24B_HUMAN)

Last modified June 16, 2009. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

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

General annotation (Comments)

Function

Critical component of the membrane-bound oxidase of phagocytes that generates superoxide. It is the terminal component of a respiratory chain that transfers single electrons from cytoplasmic NADPH across the plasma membrane to molecular oxygen on the exterior. Also functions as a voltage-gated proton channel that mediates the H+ currents of resting phagocytes. It participates in the regulation of cellular pH and is blocked by zinc.

Cofactor

FAD Probable.

Subunit structure

Composed of a heavy chain (beta) and a light chain (alpha).

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 570569Cytochrome b-245 heavy chain
PRO_0000210145

Regions

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

Sites

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

Amino acid modifications

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

Natural variations

Natural variant181W → C in XCGD.
VAR_047264
Natural variant201G → R in XCGD. Ref.18
VAR_007873
Natural variant411Y → D in XCGD. Ref.2
VAR_025613
Natural variant54 – 552Missing in XCGD. Ref.18 Ref.21 Ref.24
VAR_047265
Natural variant541R → M in XCGD. Ref.18 Ref.21 Ref.24
VAR_025614
Natural variant541R → S in XCGD. Ref.18 Ref.21 Ref.24
VAR_007874
Natural variant551A → D in XCGD. Ref.21 Ref.24
VAR_025615
Natural variant571A → E in XCGD. Ref.12 Ref.21 Ref.24
VAR_008845
Natural variant591C → R in XCGD. Ref.18 Ref.25
VAR_007875
Natural variant591C → W in XCGD. Ref.18 Ref.25
VAR_047266
Natural variant1011H → R in XCGD. Ref.11 Ref.19 Ref.24
VAR_002432
Natural variant1011H → Y in XCGD. Ref.11 Ref.19 Ref.24
VAR_007876
Natural variant1191H → R in XCGD. Ref.18
VAR_007877
Natural variant1561A → T in XCGD. Ref.11 Ref.18
VAR_002433
Natural variant1791G → R in XCGD. Ref.20
VAR_047267
Natural variant1931S → F in XCGD. Ref.22
VAR_047268
Natural variant2051F → I in XCGD. Ref.15
VAR_047269
Natural variant2091H → Q in XCGD. Ref.11 Ref.18 Ref.24
VAR_007878
Natural variant2091H → R in XCGD. Ref.11 Ref.18 Ref.24
VAR_025616
Natural variant2091H → Y in XCGD. Ref.11 Ref.18 Ref.24
VAR_002434
Natural variant2151Missing in XCGD. Ref.15 Ref.17
VAR_007879
Natural variant2221H → N in XCGD. Ref.18 Ref.22
VAR_007880
Natural variant2221H → R in XCGD. Ref.18 Ref.22
VAR_007881
Natural variant2221H → Y in XCGD. Ref.18 Ref.22
VAR_007882
Natural variant2231G → L in XCGD; requires 2 nucleotide substitutions. Ref.18
VAR_007883
Natural variant2241A → G in XCGD. Ref.24
VAR_025617
Natural variant2251E → V in XCGD. Ref.23
VAR_002435
Natural variant2441C → R in XCGD. Ref.11 Ref.18 Ref.23
VAR_007884
Natural variant2441C → S in XCGD. Ref.11 Ref.18 Ref.23
VAR_002436
Natural variant2441C → Y in XCGD. Ref.11 Ref.18 Ref.23
VAR_002437
Natural variant298 – 3025Missing in XCGD. Ref.20
VAR_047270
Natural variant3031H → N in XCGD; completely inhibits NADPH oxidase activity; NADPH oxidase assembly is abolished. Ref.26 Ref.27
VAR_016880
Natural variant3041P → 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 variant3071T → P in XCGD. Ref.25
VAR_047271
Natural variant3091E → K in XCGD. Ref.18 Ref.24
VAR_007885
Natural variant3151Missing in XCGD. Ref.18
VAR_047272
Natural variant3221G → E in XCGD. Ref.18
VAR_007886
Natural variant3251I → F in XCGD. Ref.18
VAR_007887
Natural variant3331S → P in XCGD. Ref.18
VAR_007888
Natural variant3381H → Y in XCGD. Ref.22 Ref.24
VAR_025618
Natural variant3391P → H in XCGD. Ref.13 Ref.18 Ref.21 Ref.22 Ref.24
VAR_002438
Natural variant3421L → Q in XCGD. Ref.15
VAR_047273
Natural variant3441S → F in XCGD. Ref.21 Ref.24
VAR_025619
Natural variant3561R → P in XCGD. Ref.18
VAR_007889
Natural variant3641G → R Ref.2 Ref.22
VAR_025620
Natural variant3891G → A in XCGD. Ref.11 Ref.24
VAR_002439
Natural variant3891G → E in XCGD. Ref.11 Ref.24
VAR_025621
Natural variant4051M → R in XCGD. Ref.18
VAR_007890
Natural variant4081G → E in XCGD. Ref.18
VAR_007891
Natural variant4081G → R in XCGD. Ref.18
VAR_007892
Natural variant4151P → H in XCGD. Ref.10 Ref.18
VAR_002440
Natural variant4151P → L in XCGD. Ref.10 Ref.18
VAR_007893
Natural variant4201L → P in XCGD. Ref.24
VAR_025622
Natural variant4221S → P in XCGD. Ref.18
VAR_007894
Natural variant4531W → R in XCGD. Ref.18
VAR_007895
Natural variant4721G → S: dbSNP rs13306300.
VAR_047274
Natural variant5001D → G in XCGD. Ref.14
VAR_002441
Natural variant5051L → R in XCGD. Ref.25
VAR_047275
Natural variant5161W → C in XCGD. Ref.18 Ref.24
VAR_007896
Natural variant5161W → R in XCGD. Ref.18 Ref.24
VAR_025623
Natural variant5171D → E Ref.2
VAR_025624
Natural variant5341V → D in XCGD. Ref.18
VAR_007897
Natural variant5371C → R in XCGD. Ref.2 Ref.18
VAR_007898
Natural variant5461L → P in XCGD. Ref.22
VAR_047276

Experimental info

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

Sequences

Sequence LengthMass (Da)Tools
P04839-1 [UniParc].

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

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

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

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

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

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

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

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

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

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

       550        560        570 
ALAETLSKQS ISNSESGPRG VHFIFNKENF 

« Hide

References

« Hide 'large scale' references
[1]"Cloning the gene for an inherited human disorder -- chronic granulomatous disease -- on the basis of its chromosomal location."
Royer-Pokora B., Kunkel L.M., Monaco A.P., Goff S.C., Newburger P.E., Baehner R.L., Cole F.S., Curnutte J.T., Orkin S.H.
Nature 322:32-38(1986) [PubMed: 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 expand/collapse EMBL AC list , AF469757, AF469758, AF469759, AF469760, AF469761, AF469762, AF469763, AF469764, AF469765, AF469766, AF469767, AF469768 Genomic DNA. Translation: AAL76082.1.
DQ314869 Genomic DNA. Translation: ABC40728.1.
BC032720 mRNA. Translation: AAH32720.1.
X05895 Genomic DNA. Translation: CAA29327.1. Sequence problems.
AB013904 Genomic DNA. Translation: BAA34183.1.
IPIIPI00218646.
PIRS70773.
RefSeqNP_000388.2.
UniGeneHs.292356

3D structure databases

ModBaseSearch...

Protein family/group databases

PeroxiBase5962. HsNOx02.
TCDB5.B.1.1.1. phagocyte (gp91phox) NADPH oxidase family.

Proteomic databases

PeptideAtlasP04839.
PRIDEP04839.

Genome annotation databases

EnsemblENSG00000165168. Homo sapiens. [Contig view]
GeneID1536.
KEGGhsa:1536.

Organism-specific databases

GeneCardsGC0XP037524.
H-InvDBHIX0016724.
HGNCHGNC:2578. CYBB.
MIM300481. gene.
306400. phenotype.
Orphanet379. Granulomatous disease, chronic.
PharmGKBPA27076.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP04839.
HOVERGENP04839.
OMAP04839. QERNNAN.

Gene expression databases

ArrayExpressP04839.
BgeeP04839.
CleanExHS_CYBB.
GermOnlineENSG00000165168. Homo sapiens.

Family and domain databases

InterProIPR000778. 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]
PfamPF08022. FAD_binding_8. 1 hit.
PF01794. Ferric_reduct. 1 hit.
PF08030. NAD_binding_6. 1 hit.
[Graphical view]
PRINTSPR00466. GP91PHOX.
PROSITEPS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio6353.
SOURCESearch...

Entry information

Entry nameCY24B_HUMAN
AccessionPrimary (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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome X

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents