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Q15080

- NCF4_HUMAN

UniProt

Q15080 - NCF4_HUMAN

Protein

Neutrophil cytosol factor 4

Gene

NCF4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 2 (30 May 2006)
      Previous versions | rss
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    Functioni

    Component of the NADPH-oxidase, a multicomponent enzyme system responsible for the oxidative burst in which electrons are transported from NADPH to molecular oxygen, generating reactive oxidant intermediates. It may be important for the assembly and/or activation of the NADPH-oxidase complex.1 Publication

    GO - Molecular functioni

    1. phosphatidylinositol-3-phosphate binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. protein dimerization activity Source: UniProtKB
    4. superoxide-generating NADPH oxidase activator activity Source: UniProtKB

    GO - Biological processi

    1. antigen processing and presentation of exogenous peptide antigen via MHC class I Source: Reactome
    2. antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent Source: Reactome
    3. antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
    4. immune response Source: UniProtKB
    5. interaction with host Source: Reactome
    6. oxidation-reduction process Source: UniProtKB
    7. phagosome maturation Source: Reactome
    8. positive regulation of catalytic activity Source: GOC

    Keywords - Ligandi

    Lipid-binding

    Enzyme and pathway databases

    ReactomeiREACT_111174. Cross-presentation of particulate exogenous antigens (phagosomes).
    REACT_121256. Phagosomal maturation (early endosomal stage).

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Neutrophil cytosol factor 4
    Short name:
    NCF-4
    Alternative name(s):
    Neutrophil NADPH oxidase factor 4
    SH3 and PX domain-containing protein 4
    p40-phox
    Short name:
    p40phox
    Gene namesi
    Name:NCF4
    Synonyms:SH3PXD4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:7662. NCF4.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. endosome membrane Source: UniProtKB
    3. membrane Source: UniProtKB
    4. NADPH oxidase complex Source: UniProtKB
    5. phagolysosome Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm, Endosome, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Granulomatous disease, chronic, cytochrome-b-positive 3, autosomal recessive (CGD3) [MIM:613960]: 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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti105 – 1051R → Q in CGD3; the protein remains cytosolic, does not localize to phagosomes or endosomes and is unable to bind phosphatidylinositol 3-phosphate (PtdIns(3)P) in a lipid-binding assay; unable to rescue the NADPH-oxidase defect of NCF4 functionally null cells. 1 Publication
    VAR_065949

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi58 – 581R → Q: Abolishes interaction with membranes enriched in phosphatidylinositol 3-phosphate. 1 Publication
    Mutagenesisi60 – 601R → A: Strongly reduces interaction with membranes enriched in phosphatidylinositol 3-phosphate. 1 Publication
    Mutagenesisi92 – 921K → A: Abolishes interaction with membranes enriched in phosphatidylinositol 3-phosphate. 1 Publication
    Mutagenesisi94 – 941Y → A: Slightly reduces interaction with membranes enriched in phosphatidylinositol 3-phosphate. 1 Publication
    Mutagenesisi105 – 1051R → A: Abolishes interaction with membranes enriched in phosphatidylinositol 3-phosphate. 1 Publication
    Mutagenesisi154 – 1541T → A: Reduces phosphorylation. 1 Publication
    Mutagenesisi211 – 2111T → A: No effect on phosphorylation. 1 Publication
    Mutagenesisi251 – 2511T → A: No effect on phosphorylation. 1 Publication
    Mutagenesisi274 – 2741T → A: No effect on phosphorylation. 1 Publication
    Mutagenesisi315 – 3151S → A: Reduces phosphorylation. 1 Publication
    Mutagenesisi327 – 3271T → A: No effect on phosphorylation. 1 Publication

    Keywords - Diseasei

    Chronic granulomatous disease, Disease mutation

    Organism-specific databases

    MIMi613960. phenotype.
    Orphaneti379. Chronic granulomatous disease.
    206. Crohn disease.
    PharmGKBiPA31465.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 339339Neutrophil cytosol factor 4PRO_0000096764Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei154 – 1541Phosphothreonine1 Publication
    Modified residuei315 – 3151Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ15080.
    PaxDbiQ15080.
    PRIDEiQ15080.

    PTM databases

    PhosphoSiteiQ15080.

    Expressioni

    Tissue specificityi

    Expression is restricted to hematopoietic cells.

    Gene expression databases

    ArrayExpressiQ15080.
    BgeeiQ15080.
    CleanExiHS_NCF4.
    GenevestigatoriQ15080.

    Organism-specific databases

    HPAiCAB010146.
    HPA036156.

    Interactioni

    Subunit structurei

    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. NCF4 interacts primarily with NCF2 to form a complex with NCF1.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NCF1P145982EBI-1036870,EBI-395044
    NCF2P198785EBI-1036870,EBI-489611

    Protein-protein interaction databases

    BioGridi110769. 7 interactions.
    DIPiDIP-17019N.
    IntActiQ15080. 5 interactions.
    MINTiMINT-206126.
    STRINGi9606.ENSP00000337605.

    Structurei

    Secondary structure

    1
    339
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 1513
    Beta strandi21 – 3212
    Beta strandi34 – 363
    Beta strandi38 – 4710
    Beta strandi52 – 587
    Helixi59 – 7315
    Helixi80 – 823
    Helixi98 – 11619
    Helixi121 – 1244
    Helixi127 – 1337
    Helixi137 – 1404
    Beta strandi174 – 1796
    Beta strandi184 – 1885
    Beta strandi196 – 2027
    Beta strandi204 – 2129
    Beta strandi215 – 2206
    Helixi221 – 2233
    Beta strandi224 – 2263
    Beta strandi238 – 2469
    Beta strandi249 – 2579
    Helixi267 – 27812
    Beta strandi281 – 2888
    Beta strandi290 – 2923
    Beta strandi294 – 2963
    Helixi300 – 30910
    Beta strandi324 – 3285

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1H6HX-ray1.70A2-144[»]
    1OEYX-ray2.00J/K/L/M237-339[»]
    1W6XX-ray2.00A/B174-228[»]
    1W70X-ray1.46A/B174-228[»]
    1Z9QNMR-A168-233[»]
    2DYBX-ray3.15A/B1-339[»]
    ProteinModelPortaliQ15080.
    SMRiQ15080. Positions 2-339.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ15080.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini19 – 140122PXPROSITE-ProRule annotationAdd
    BLAST
    Domaini170 – 22960SH3PROSITE-ProRule annotationAdd
    BLAST
    Domaini237 – 32993OPRAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni58 – 603Phosphatidylinositol 3-phosphate binding
    Regioni92 – 943Phosphatidylinositol 3-phosphate binding

    Domaini

    The OPR/PB1 domain mediates the association with NCF2/p67-PHOX.
    The PX domain mediates interaction with membranes enriched in phosphatidylnositol 3-phosphate.

    Sequence similaritiesi

    Contains 1 OPR domain.Curated
    Contains 1 PX (phox homology) domain.PROSITE-ProRule annotation
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    SH3 domain

    Phylogenomic databases

    eggNOGiNOG297760.
    HOGENOMiHOG000013076.
    HOVERGENiHBG006452.
    KOiK08012.
    OMAiLFPWKLH.
    PhylomeDBiQ15080.

    Family and domain databases

    Gene3Di3.30.1520.10. 1 hit.
    InterProiIPR000919. NCF_P40.
    IPR000270. OPR_PB1.
    IPR001683. Phox.
    IPR001452. SH3_domain.
    [Graphical view]
    PfamiPF00564. PB1. 1 hit.
    PF00787. PX. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view]
    PRINTSiPR00497. P40PHOX.
    SMARTiSM00666. PB1. 1 hit.
    SM00312. PX. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 1 hit.
    SSF64268. SSF64268. 1 hit.
    PROSITEiPS50195. PX. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q15080-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAVAQQLRAE SDFEQLPDDV AISANIADIE EKRGFTSHFV FVIEVKTKGG    50
    SKYLIYRRYR QFHALQSKLE ERFGPDSKSS ALACTLPTLP AKVYVGVKQE 100
    IAEMRIPALN AYMKSLLSLP VWVLMDEDVR IFFYQSPYDS EQVPQALRRL 150
    RPRTRKVKSV SPQGNSVDRM AAPRAEALFD FTGNSKLELN FKAGDVIFLL 200
    SRINKDWLEG TVRGATGIFP LSFVKILKDF PEEDDPTNWL RCYYYEDTIS 250
    TIKDIAVEED LSSTPLLKDL LELTRREFQR EDIALNYRDA EGDLVRLLSD 300
    EDVALMVRQA RGLPSQKRLF PWKLHITQKD NYRVYNTMP 339
    Length:339
    Mass (Da):39,032
    Last modified:May 30, 2006 - v2
    Checksum:iD82FE9E5BA12890B
    GO
    Isoform 2 (identifier: Q15080-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         254-339: DIAVEEDLSS...DNYRVYNTMP → SVAWEGGACP...WRKISAALPY

    Show »
    Length:348
    Mass (Da):39,001
    Checksum:i49393E82583B7ADD
    GO
    Isoform 3 (identifier: Q15080-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         254-339: DIAVEEDLSS...DNYRVYNTMP → SVAWEGGACP...WRKISAALPY

    Show »
    Length:348
    Mass (Da):39,017
    Checksum:i0C787E82434C16C6
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti105 – 1051R → Q in CGD3; the protein remains cytosolic, does not localize to phagosomes or endosomes and is unable to bind phosphatidylinositol 3-phosphate (PtdIns(3)P) in a lipid-binding assay; unable to rescue the NADPH-oxidase defect of NCF4 functionally null cells. 1 Publication
    VAR_065949
    Natural varianti147 – 1471L → I.2 Publications
    VAR_009314
    Natural varianti153 – 1531R → H.
    Corresponds to variant rs35160112 [ dbSNP | Ensembl ].
    VAR_034136

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei254 – 33986DIAVE…YNTMP → SVAWEGGACPAFLPSLRPPP LTSPSHGSLSHSKAPSGSQM SHNAVTSHQRPGWPGQPHSP FPHPTPHFQPDASLLQPVTP LGTSRWRKISAALPY in isoform 2. 3 PublicationsVSP_004328Add
    BLAST
    Alternative sequencei254 – 33986DIAVE…YNTMP → SVAWEGGACPAFLPSLRPLP LTSPSHGSLSHSKAPSGSQM SHNAVTSHQRPGWPGQPHSP FPHPTPHFQPDASLLQPVTP LGTSRWRKISAALPY in isoform 3. 1 PublicationVSP_042681Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X77094 mRNA. Translation: CAA54372.1.
    U50729
    , U50720, U50721, U50722, U50723, U50724, U50725, U50726, U50727, U50728 Genomic DNA. Translation: AAB39970.1.
    AB025220 mRNA. Translation: BAA89792.1.
    AB025219 mRNA. Translation: BAA89791.1.
    CR456528 mRNA. Translation: CAG30414.1.
    BT007346 mRNA. Translation: AAP36010.1.
    AK290924 mRNA. Translation: BAF83613.1.
    DQ314880 Genomic DNA. Translation: ABC40739.1.
    AL008637 Genomic DNA. Translation: CAQ10741.1.
    AL008637 Genomic DNA. Translation: CAA15486.1.
    BC002798 mRNA. Translation: AAH02798.1.
    CCDSiCCDS13934.1. [Q15080-1]
    CCDS13935.1. [Q15080-3]
    PIRiS39768.
    RefSeqiNP_000622.2. NM_000631.4. [Q15080-1]
    NP_038202.2. NM_013416.3. [Q15080-3]
    UniGeneiHs.474781.

    Genome annotation databases

    EnsembliENST00000248899; ENSP00000248899; ENSG00000100365. [Q15080-1]
    ENST00000397147; ENSP00000380334; ENSG00000100365. [Q15080-3]
    GeneIDi4689.
    KEGGihsa:4689.
    UCSCiuc003apy.4. human. [Q15080-1]
    uc003apz.4. human. [Q15080-3]

    Polymorphism databases

    DMDMi108884815.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X77094 mRNA. Translation: CAA54372.1 .
    U50729
    , U50720 , U50721 , U50722 , U50723 , U50724 , U50725 , U50726 , U50727 , U50728 Genomic DNA. Translation: AAB39970.1 .
    AB025220 mRNA. Translation: BAA89792.1 .
    AB025219 mRNA. Translation: BAA89791.1 .
    CR456528 mRNA. Translation: CAG30414.1 .
    BT007346 mRNA. Translation: AAP36010.1 .
    AK290924 mRNA. Translation: BAF83613.1 .
    DQ314880 Genomic DNA. Translation: ABC40739.1 .
    AL008637 Genomic DNA. Translation: CAQ10741.1 .
    AL008637 Genomic DNA. Translation: CAA15486.1 .
    BC002798 mRNA. Translation: AAH02798.1 .
    CCDSi CCDS13934.1. [Q15080-1 ]
    CCDS13935.1. [Q15080-3 ]
    PIRi S39768.
    RefSeqi NP_000622.2. NM_000631.4. [Q15080-1 ]
    NP_038202.2. NM_013416.3. [Q15080-3 ]
    UniGenei Hs.474781.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1H6H X-ray 1.70 A 2-144 [» ]
    1OEY X-ray 2.00 J/K/L/M 237-339 [» ]
    1W6X X-ray 2.00 A/B 174-228 [» ]
    1W70 X-ray 1.46 A/B 174-228 [» ]
    1Z9Q NMR - A 168-233 [» ]
    2DYB X-ray 3.15 A/B 1-339 [» ]
    ProteinModelPortali Q15080.
    SMRi Q15080. Positions 2-339.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110769. 7 interactions.
    DIPi DIP-17019N.
    IntActi Q15080. 5 interactions.
    MINTi MINT-206126.
    STRINGi 9606.ENSP00000337605.

    PTM databases

    PhosphoSitei Q15080.

    Polymorphism databases

    DMDMi 108884815.

    Proteomic databases

    MaxQBi Q15080.
    PaxDbi Q15080.
    PRIDEi Q15080.

    Protocols and materials databases

    DNASUi 4689.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000248899 ; ENSP00000248899 ; ENSG00000100365 . [Q15080-1 ]
    ENST00000397147 ; ENSP00000380334 ; ENSG00000100365 . [Q15080-3 ]
    GeneIDi 4689.
    KEGGi hsa:4689.
    UCSCi uc003apy.4. human. [Q15080-1 ]
    uc003apz.4. human. [Q15080-3 ]

    Organism-specific databases

    CTDi 4689.
    GeneCardsi GC22P037257.
    GeneReviewsi NCF4.
    HGNCi HGNC:7662. NCF4.
    HPAi CAB010146.
    HPA036156.
    MIMi 601488. gene.
    613960. phenotype.
    neXtProti NX_Q15080.
    Orphaneti 379. Chronic granulomatous disease.
    206. Crohn disease.
    PharmGKBi PA31465.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG297760.
    HOGENOMi HOG000013076.
    HOVERGENi HBG006452.
    KOi K08012.
    OMAi LFPWKLH.
    PhylomeDBi Q15080.

    Enzyme and pathway databases

    Reactomei REACT_111174. Cross-presentation of particulate exogenous antigens (phagosomes).
    REACT_121256. Phagosomal maturation (early endosomal stage).

    Miscellaneous databases

    EvolutionaryTracei Q15080.
    GenomeRNAii 4689.
    NextBioi 18080.
    PROi Q15080.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15080.
    Bgeei Q15080.
    CleanExi HS_NCF4.
    Genevestigatori Q15080.

    Family and domain databases

    Gene3Di 3.30.1520.10. 1 hit.
    InterProi IPR000919. NCF_P40.
    IPR000270. OPR_PB1.
    IPR001683. Phox.
    IPR001452. SH3_domain.
    [Graphical view ]
    Pfami PF00564. PB1. 1 hit.
    PF00787. PX. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00497. P40PHOX.
    SMARTi SM00666. PB1. 1 hit.
    SM00312. PX. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 1 hit.
    SSF64268. SSF64268. 1 hit.
    PROSITEi PS50195. PX. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "p40phox, a third cytosolic component of the activation complex of the NADPH oxidase to contain src homology 3 domains."
      Wientjes F.B., Hsuan J.J., Totty N.F., Segal A.W.
      Biochem. J. 296:557-561(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, VARIANT ILE-147, PARTIAL PROTEIN SEQUENCE.
    2. "Genomic structure, chromosomal localization, start of transcription, and tissue expression of the human p40-phox, a new component of the nicotinamide adenine dinucleotide phosphate-oxidase complex."
      Zhan S., Vazquez N., Zhan S., Wientjes F.B., Budarf M.L., Schrock E., Ried T., Green E.D., Chanock S.J.
      Blood 88:2714-2721(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ILE-147.
    3. "Identification of a splice variant mRNA of p40phox, an NADPH oxidase component of phagocytes."
      Hasebe T., Someya A., Nagaoka I.
      FEBS Lett. 455:257-261(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    5. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      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.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    6. "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] (ISOFORM 3).
    7. NHLBI resequencing and genotyping service (RS&G)
      Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    8. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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] (ISOFORM 2).
      Tissue: Lymph.
    10. "p40(phox) is phosphorylated on threonine 154 and serine 315 during activation of the phagocyte NADPH oxidase. Implication of a protein kinase c-type kinase in the phosphorylation process."
      Bouin A.-P., Grandvaux N., Vignais P.V., Fuchs A.
      J. Biol. Chem. 273:30097-30103(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-154 AND SER-315, MUTAGENESIS OF THR-154; THR-211; THR-251; THR-274; SER-315 AND THR-327.
    11. "The crystal structure of the PX domain from p40(phox) bound to phosphatidylinositol 3-phosphate."
      Bravo J., Karathanassis D., Pacold C.M., Pacold M.E., Ellson C.D., Anderson K.E., Butler P.J.G., Lavenir I., Perisic O., Hawkins P.T., Stephens L., Williams R.L.
      Mol. Cell 8:829-839(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 2-144 IN COMPLEX WITH PHOSPHATIDYLINOSITOL 3-PHOSPHATE, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF ARG-58; ARG-60; LYS-92; TYR-94 AND ARG-105, LIPID-BINDING.
    12. "PB1 domain-mediated heterodimerization in NADPH oxidase and signaling complexes of atypical protein kinase C with Par6 and p62."
      Wilson M.I., Gill D.J., Perisic O., Quinn M.T., Williams R.L.
      Mol. Cell 12:39-50(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 237-339 IN COMPLEX WITH NCF2, INTERACTION WITH NCF2.
    13. "Effects of p47phox C terminus phosphorylations on binding interactions with p40phox and p67phox. Structural and functional comparison of p40phox and p67phox SH3 domains."
      Massenet C., Chenavas S., Cohen-Addad C., Dagher M.-C., Brandolin G., Pebay-Peyroula E., Fieschi F.
      J. Biol. Chem. 280:13752-13761(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.46 ANGSTROMS) OF 174-228 IN COMPLEX WITH NCF1, INTERACTION WITH NCF1.
    14. "Full-length p40phox structure suggests a basis for regulation mechanism of its membrane binding."
      Honbou K., Minakami R., Yuzawa S., Takeya R., Suzuki N.N., Kamakura S., Sumimoto H., Inagaki F.
      EMBO J. 26:1176-1186(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS), DOMAIN OPR/PB1.
    15. "A new genetic subgroup of chronic granulomatous disease with autosomal recessive mutations in p40 phox and selective defects in neutrophil NADPH oxidase activity."
      Matute J.D., Arias A.A., Wright N.A., Wrobel I., Waterhouse C.C., Li X.J., Marchal C.C., Stull N.D., Lewis D.B., Steele M., Kellner J.D., Yu W., Meroueh S.O., Nauseef W.M., Dinauer M.C.
      Blood 114:3309-3315(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CGD3 GLN-105, CHARACTERIZATION OF VARIANT CGD3 GLN-105.

    Entry informationi

    Entry nameiNCF4_HUMAN
    AccessioniPrimary (citable) accession number: Q15080
    Secondary accession number(s): A8K4F9
    , O60808, Q86U56, Q9BU98, Q9NP45
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: May 30, 2006
    Last modified: October 1, 2014
    This is version 156 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny 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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 22
      Human chromosome 22: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3