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UniProtKB/Swiss-Prot entry P13498


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CY24A_HUMAN
Primary accession number P13498
Secondary accession numbers Q14090 Q9BR72
Integrated into Swiss-Prot on January 1, 1990
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 88)
Name and origin of the protein
Protein name Cytochrome b-245 light chain
Synonyms p22 phagocyte B-cytochrome
Neutrophil cytochrome b 22 kDa polypeptide
p22-phox
p22phox
Cytochrome b(558) alpha chain
Cytochrome b558 subunit alpha
Superoxide-generating NADPH oxidase light chain subunit
Gene name
Name: CYBA
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-26.
PubMed=3368442 [NCBI, ExPASy, EBI, Israel, Japan]
Parkos C.A., Dinauer M.C., Walker L.E., Allen R.A., Jesaitis A.J., Orkin S.H.;
"Primary structure and unique expression of the 22-kilodalton light chain of human neutrophil cytochrome b.";
Proc. Natl. Acad. Sci. U.S.A. 85:3319-3323(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT TYR-72.
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 12-123, AND VARIANT AR-CGD ARG-118.
PubMed=2243141 [NCBI, ExPASy, EBI, Israel, Japan]
Dinauer M.C., Pierce E.A., Bruns G.A.P., Curnutte J.T., Orkin S.H.;
"Human neutrophil cytochrome b light chain (p22-phox). Gene structure, chromosomal location, and mutations in cytochrome-negative autosomal recessive chronic granulomatous disease.";
J. Clin. Invest. 86:1729-1737(1990).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 51-195.
PubMed=2469497 [NCBI, ExPASy, EBI, Israel, Japan]
Verhoeven A.J., Bolscher B.G., Meerhof L.J., van Zwieten R., Keijer J., Weening R.S., Roos D.;
"Characterization of two monoclonal antibodies against cytochrome b558 of human neutrophils.";
Blood 73:1686-1694(1989).
[6]
INTERACTION WITH NOXO1, AND MUTAGENESIS OF PRO-157.
DOI=10.1074/jbc.M212856200; PubMed=12716910 [NCBI, ExPASy, EBI, Israel, Japan]
Takeya R., Ueno N., Kami K., Taura M., Kohjima M., Izaki T., Nunoi H., Sumimoto H.;
"Novel human homologues of p47phox and p67phox participate in activation of superoxide-producing NADPH oxidases.";
J. Biol. Chem. 278:25234-25246(2003).
[7]
INTERACTION WITH DUOX1; DUOX2 AND TPO.
DOI=10.1074/jbc.M407709200; PubMed=15561711 [NCBI, ExPASy, EBI, Israel, Japan]
Wang D., De Deken X., Milenkovic M., Song Y., Pirson I., Dumont J.E., Miot F.;
"Identification of a novel partner of duox: EFP1, a thioredoxin-related protein.";
J. Biol. Chem. 280:3096-3103(2005).
[8]
FUNCTION.
DOI=10.1074/jbc.M414548200; PubMed=15824103 [NCBI, ExPASy, EBI, Israel, Japan]
Ueno N., Takeya R., Miyano K., Kikuchi H., Sumimoto H.;
"The NADPH oxidase Nox3 constitutively produces superoxide in a p22phox-dependent manner: its regulation by oxidase organizers and activators.";
J. Biol. Chem. 280:23328-23339(2005).
[9]
INTERACTION WITH NOX4.
DOI=10.1016/j.cellsig.2005.03.023; PubMed=15927447 [NCBI, ExPASy, EBI, Israel, Japan]
Martyn K.D., Frederick L.M., von Loehneysen K., Dinauer M.C., Knaus U.G.;
"Functional analysis of Nox4 reveals unique characteristics compared to other NADPH oxidases.";
Cell. Signal. 18:69-82(2006).
[10]
VARIANTS AR-CGD GLN-90 AND ARG-94.
PubMed=1415254 [NCBI, ExPASy, EBI, Israel, Japan]
de Boer M., de Klein A., Hossle J.-P., Seger R., Corbeel L., Weening R.S., Roos D.;
"Cytochrome b558-negative, autosomal recessive chronic granulomatous disease: two new mutations in the cytochrome b558 light chain of the NADPH oxidase (p22-phox).";
Am. J. Hum. Genet. 51:1127-1135(1992).
[11]
VARIANT AR-CGD GLN-156.
PubMed=1763037 [NCBI, ExPASy, EBI, Israel, Japan]
Dinauer M.C., Pierce E.A., Erickson R.W., Muhlebach T.J., Messner H., Orkin S.H., Seger R.A., Curnutte J.T.;
"Point mutation in the cytoplasmic domain of the neutrophil p22-phox cytochrome b subunit is associated with a nonfunctional NADPH oxidase and chronic granulomatous disease.";
Proc. Natl. Acad. Sci. U.S.A. 88:11231-11235(1991).
[12]
CHARACTERIZATION OF VARIANT AR-CGD GLN-156.
DOI=10.1084/jem.180.6.2329; PubMed=7964505 [NCBI, ExPASy, EBI, Israel, Japan]
Leusen J.H., Bolscher B.G., Hilarius P.M., Weening R.S., Kaulfersch W., Seger R.A., Roos D., Verhoeven A.J.;
"156Pro-->Gln substitution in the light chain of cytochrome b558 of the human NADPH oxidase (p22-phox) leads to defective translocation of the cytosolic proteins p47-phox and p67-phox.";
J. Exp. Med. 180:2329-2334(1994).
[13]
VARIANT AR-CGD ARG-24.
DOI=10.1046/j.1365-2141.2000.01857.x; PubMed=10759707 [NCBI, ExPASy, EBI, Israel, Japan]
Yamada M., Ariga T., Kawamura N., Ohtsu M., Imajoh-Ohmi S., Ohshika E., Tatsuzawa O., Kobayashi K., Sakiyama Y.;
"Genetic studies of three Japanese patients with p22-phox-deficient chronic granulomatous disease: detection of a possible common mutant CYBA allele in Japan and a genotype-phenotype correlation in these patients.";
Br. J. Haematol. 108:511-517(2000).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M21186; AAA90925.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT006861; AAP35507.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC006465; AAH06465.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M62818; AAA52134.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M61106; AAA52134.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M62817; AAA52134.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M61107; AAA52134.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A28201; A28201.
RefSeq NP_000092.2; -.
UniGene Hs.513803
3D structure databases
PDB
1WLP; NMR; -; A=144-168.[ExPASy / RCSB / EBI]
PDBsum 1WLP; -.
ModBase P13498.
Protein-protein interaction databases
IntAct P13498; -.
Organism-specific databases
H-InvDB HIX0013335; -.
HGNC HGNC:2577; CYBA.
GenAtlas CYBA.
HPA CAB009492; -.
MIM 233690; phenotype. [NCBI / EBI]
608508; gene. [NCBI / EBI]
PharmGKB PA27075; -.
GeneCards P13498.
Gene expression databases
ArrayExpress P13498; -.
CleanEx HS_CYBA; -.
GermOnline ENSG00000051523; Homo sapiens.
Ontologies
GO
GO:0009055; Molecular function: electron carrier activity (traceable author statement from UniProtKB).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.
Family and domain databases
InterPro IPR007732; Cytochr_b558a.
Graphical view of domain structure.
PANTHER PTHR15168; Cytochr_b558a; 1.
Pfam PF05038; Cytochrom_B558a; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF019635; Cytochr_b558a; 1.
BLOCKS P13498.
Proteomic databases
PeptideAtlas P13498; -.
Genome annotation databases
Ensembl ENSG00000051523; Homo sapiens. [Contig view]
GeneID 1535; -.
KEGG hsa:1535; -.
Phylogenomic databases
HOGENOM P13498; -.
HOVERGEN P13498; -.
Other
SOURCE CYBA; Homo sapiens.
ProtoNet P13498.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Chronic granulomatous disease; Direct protein sequencing; Disease mutation; Electron transport; Heme; Iron; Membrane; Metal-binding; NADP; Oxidoreductase; Polymorphism; Transport.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   195  194     Cytochrome b-245 light chain. PRO_0000144907
METAL   94    94        Iron (heme axial ligand) (Potential). 
VARIANT   24    24  1     G -> R (in AR-CGD). VAR_012755 
VARIANT   72    72  1     H -> Y (in dbSNP:rs4673 [NCBI]). VAR_005122 
VARIANT   90    90  1     R -> Q (in AR-CGD). VAR_005123 
VARIANT   94    94  1     H -> R (in AR-CGD). VAR_005124 
VARIANT   118   118  1     S -> R (in AR-CGD). VAR_005125 
VARIANT   156   156  1     P -> Q (in AR-CGD). VAR_005126 
MUTAGEN   157   157        P->Q: Loss of interaction with NOXO1. 
HELIX   161   165  5      
Sequence information
Length: 195 AA [This is the length of the unprocessed precursor] Molecular weight: 20958 Da [This is the MW of the unprocessed precursor] CRC64: 429E97A6A9303510 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGQIEWAMWA NEQALASGLI LITGGIVATA GRFTQWYFGA YSIVAGVFVC LLEYPRGKRK 

        70         80         90        100        110        120 
KGSTMERWGQ KHMTAVVKLF GPFTRNYYVR AVLHLLLSVP AGFLLATILG TACLAIASGI 

       130        140        150        160        170        180 
YLLAAVRGEQ WTPIEPKPRE RPQIGGTIKQ PPSNPPPRPP AEARKKPSEE EAAAAAGGPP 

       190 
GGPQVNPIPV TDEVV 

P13498 in FASTA format

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