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P14598

- NCF1_HUMAN

UniProt

P14598 - NCF1_HUMAN

Protein

Neutrophil cytosol factor 1

Gene

NCF1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 177 (01 Oct 2014)
      Sequence version 3 (08 Mar 2011)
      Previous versions | rss
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    Functioni

    NCF2, NCF1, and a membrane bound cytochrome b558 are required for activation of the latent NADPH oxidase (necessary for superoxide production).3 Publications

    GO - Molecular functioni

    1. electron carrier activity Source: UniProtKB
    2. phosphatidylinositol-3,4-bisphosphate binding Source: UniProtKB
    3. phosphatidylinositol binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. SH3 domain binding Source: BHF-UCL
    6. superoxide-generating NADPH oxidase 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. apoptotic process Source: Ensembl
    5. cell proliferation Source: Ensembl
    6. cellular defense response Source: ProtInc
    7. hydrogen peroxide biosynthetic process Source: Ensembl
    8. inflammatory response Source: Ensembl
    9. innate immune response Source: BHF-UCL
    10. interaction with host Source: Reactome
    11. leukotriene metabolic process Source: Ensembl
    12. negative regulation of smooth muscle contraction Source: Ensembl
    13. neutrophil mediated killing of fungus Source: Ensembl
    14. neutrophil mediated killing of gram-positive bacterium Source: Ensembl
    15. oxidation-reduction process Source: GOC
    16. phagosome maturation Source: Reactome
    17. protein targeting to membrane Source: UniProtKB
    18. respiratory burst Source: BHF-UCL
    19. respiratory burst involved in defense response Source: Ensembl
    20. response to yeast Source: Ensembl
    21. superoxide anion generation Source: UniProtKB
    22. superoxide metabolic process Source: BHF-UCL

    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 1
    Short name:
    NCF-1
    Alternative name(s):
    47 kDa autosomal chronic granulomatous disease protein
    47 kDa neutrophil oxidase factor
    NCF-47K
    Neutrophil NADPH oxidase factor 1
    Nox organizer 2
    Nox-organizing protein 2
    SH3 and PX domain-containing protein 1A
    p47-phox
    Gene namesi
    Name:NCF1
    Synonyms:NOXO2, SH3PXD1A
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:7660. NCF1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. dendrite Source: Ensembl
    3. extrinsic component of membrane Source: UniProtKB
    4. Golgi apparatus Source: Ensembl
    5. NADPH oxidase complex Source: UniProtKB
    6. neuronal cell body Source: Ensembl
    7. phagolysosome Source: Reactome
    8. rough endoplasmic reticulum Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Granulomatous disease, chronic, cytochrome-b-positive 1, autosomal recessive (CGD1) [MIM:233700]: 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 varianti42 – 421R → Q in CGD1. 1 Publication
    VAR_012476

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi43 – 431R → Q: Reduces affinity for membranes enriched in phosphatidylinositol 3,4-bisphosphate. 1 Publication
    Mutagenesisi90 – 901R → A: Reduces affinity for membranes enriched in phosphatidylinositol 3,4-bisphosphate.
    Mutagenesisi263 – 2631W → R: Abolishes autoinhibition and promotes phospholipid binding. 1 Publication
    Mutagenesisi303 – 3031S → E: Abolishes autoinhibition and promotes phospholipid binding; when associated with E-304; E-328; E-359 and E-370. 1 Publication
    Mutagenesisi304 – 3041S → E: Abolishes autoinhibition and promotes phospholipid binding; when associated with E-303; E-328; E-359 and E-370. 1 Publication
    Mutagenesisi328 – 3281S → E: Abolishes autoinhibition and promotes phospholipid binding; when associated with E-303; E-304; E-359 and E-370. 1 Publication
    Mutagenesisi359 – 3591S → E: Abolishes autoinhibition and promotes phospholipid binding; when associated with E-303; E-304; E-328 and E-370. 1 Publication
    Mutagenesisi370 – 3701S → E: Abolishes autoinhibition and promotes phospholipid binding; when associated with E-303; E-304; E-328 and E-359. 1 Publication

    Keywords - Diseasei

    Chronic granulomatous disease, Disease mutation

    Organism-specific databases

    MIMi233700. phenotype.
    Orphaneti379. Chronic granulomatous disease.
    PharmGKBiPA31463.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 390390Neutrophil cytosol factor 1PRO_0000096762Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei303 – 3031Phosphoserine2 Publications
    Modified residuei304 – 3041Phosphoserine2 Publications
    Modified residuei320 – 3201Phosphoserine2 Publications
    Modified residuei328 – 3281Phosphoserine2 Publications
    Modified residuei345 – 3451Phosphoserine2 Publications
    Modified residuei348 – 3481Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylated by PRKCD; phosphorylation induces activation of NCF1 and NADPH oxidase activity.2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP14598.
    PRIDEiP14598.

    PTM databases

    PhosphoSiteiP14598.

    Expressioni

    Tissue specificityi

    Detected in peripheral blood monocytes and neutrophils (at protein level).2 Publications

    Gene expression databases

    BgeeiP14598.
    GenevestigatoriP14598.

    Organism-specific databases

    HPAiCAB004524.
    HPA047836.
    HPA052095.

    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. Interacts (via C-terminus) with NCF2 (via the C-terminal SH3 domain). Interacts with NCF4. Interacts with CYBB. Interacts (via the second SH3 domain) with CYBA. Interacts with NOXA1. Interacts with ADAM15. Interacts with TRAF4. Interacts with FASLG.11 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ABI1Q8IZP05EBI-395044,EBI-375446
    ACTBP607093EBI-395044,EBI-353944
    CYBAP134987EBI-395044,EBI-986058
    GNAI2P048992EBI-395044,EBI-353997
    NCF2P1987811EBI-395044,EBI-489611
    NCF4Q150802EBI-395044,EBI-1036870

    Protein-protein interaction databases

    BioGridi575724. 36 interactions.
    DIPiDIP-126N.
    IntActiP14598. 14 interactions.
    MINTiMINT-139338.

    Structurei

    Secondary structure

    1
    390
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 1712
    Beta strandi19 – 213
    Beta strandi23 – 3210
    Beta strandi37 – 426
    Helixi44 – 5714
    Turni59 – 635
    Helixi67 – 693
    Helixi78 – 803
    Helixi84 – 10118
    Helixi106 – 1094
    Helixi112 – 1187
    Helixi122 – 1254
    Beta strandi137 – 1404
    Beta strandi153 – 1553
    Beta strandi159 – 1624
    Beta strandi171 – 1744
    Beta strandi182 – 1876
    Beta strandi195 – 1984
    Beta strandi202 – 2065
    Helixi207 – 2093
    Beta strandi210 – 2145
    Beta strandi229 – 2357
    Beta strandi241 – 2444
    Beta strandi252 – 2576
    Beta strandi262 – 2687
    Beta strandi271 – 2766
    Helixi277 – 2793
    Beta strandi280 – 2823
    Helixi287 – 2926
    Helixi302 – 3043
    Helixi321 – 3288
    Helixi371 – 3766
    Helixi380 – 3856

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GD5NMR-A1-128[»]
    1K4UNMR-P359-390[»]
    1KQ6X-ray1.18A1-141[»]
    1NG2X-ray1.70A156-340[»]
    1O7KX-ray2.00A/B/C1-123[»]
    1OV3X-ray1.80A/B156-285[»]
    1UECX-ray1.82A151-340[»]
    1W70X-ray1.46C/D360-372[»]
    1WLPNMR-B151-286[»]
    ProteinModelPortaliP14598.
    SMRiP14598. Positions 2-141, 157-332, 359-390.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP14598.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini4 – 125122PXPROSITE-ProRule annotationAdd
    BLAST
    Domaini156 – 21560SH3 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini226 – 28560SH3 2PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi211 – 25444Asp/Glu-rich (highly acidic)Add
    BLAST
    Compositional biasi292 – 39099Arg/Lys-rich (highly basic)Add
    BLAST

    Domaini

    The PX domain mediates interaction with phosphatidylinositol 3,4-bisphosphate and other anionic phospholipids. In the autoinhibited, unphosphorylated state an intramolecular interaction with the C-terminal SH3 domain precludes phospholipid binding and interaction with CYBA. Phosphorylation disrupts the autoinhibited state.2 Publications

    Sequence similaritiesi

    Contains 1 PX (phox homology) domain.PROSITE-ProRule annotation
    Contains 2 SH3 domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, SH3 domain

    Phylogenomic databases

    eggNOGiNOG326975.
    HOVERGENiHBG002055.
    InParanoidiP14598.
    KOiK08011.
    OMAiSAYITTH.
    PhylomeDBiP14598.
    TreeFamiTF329347.

    Family and domain databases

    Gene3Di3.30.1520.10. 1 hit.
    InterProiIPR015039. NADPH_oxidase_p47Phox_C.
    IPR001655. P47PHOX.
    IPR001683. Phox.
    IPR001452. SH3_domain.
    [Graphical view]
    PfamiPF08944. p47_phox_C. 1 hit.
    PF00787. PX. 1 hit.
    PF00018. SH3_1. 2 hits.
    [Graphical view]
    PRINTSiPR00498. P47PHOX.
    SMARTiSM00312. PX. 1 hit.
    SM00326. SH3. 2 hits.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 2 hits.
    SSF64268. SSF64268. 1 hit.
    PROSITEiPS50195. PX. 1 hit.
    PS50002. SH3. 2 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P14598-1) [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

    MGDTFIRHIA LLGFEKRFVP SQHYVYMFLV KWQDLSEKVV YRRFTEIYEF    50
    HKTLKEMFPI EAGAINPENR IIPHLPAPKW FDGQRAAENR QGTLTEYCGT 100
    LMSLPTKISR CPHLLDFFKV RPDDLKLPTD NQTKKPETYL MPKDGKSTAT 150
    DITGPIILQT YRAIANYEKT SGSEMALSTG DVVEVVEKSE SGWWFCQMKA 200
    KRGWIPASFL EPLDSPDETE DPEPNYAGEP YVAIKAYTAV EGDEVSLLEG 250
    EAVEVIHKLL DGWWVIRKDD VTGYFPSMYL QKSGQDVSQA QRQIKRGAPP 300
    RRSSIRNAHS IHQRSRKRLS QDAYRRNSVR FLQQRRRQAR PGPQSPGSPL 350
    EEERQTQRSK PQPAVPPRPS ADLILNRCSE STKRKLASAV 390
    Length:390
    Mass (Da):44,652
    Last modified:March 8, 2011 - v3
    Checksum:i5A0F9F0EF101D2DB
    GO
    Isoform 2 (identifier: P14598-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         193-193: W → QTSHLTGLLP...LDGYGTVCSL
         194-390: Missing.

    Note: Due to intron retention.

    Show »
    Length:278
    Mass (Da):30,781
    Checksum:iAB0F8221EE55FCAF
    GO

    Sequence cautioni

    The sequence BAF84783.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAG54596.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti200 – 2001A → T in AAK19516. (PubMed:11740866)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti42 – 421R → Q in CGD1. 1 Publication
    VAR_012476
    Natural varianti90 – 901R → H.
    Corresponds to variant rs13447 [ dbSNP | Ensembl ].
    VAR_014735
    Natural varianti99 – 991G → S.8 Publications
    Corresponds to variant rs17856077 [ dbSNP | Ensembl ].
    VAR_018479
    Natural varianti160 – 1601T → S.
    VAR_012477
    Natural varianti166 – 1661N → D.4 Publications
    Corresponds to variant rs4868 [ dbSNP | Ensembl ].
    VAR_012478
    Natural varianti258 – 2581K → E.1 Publication
    VAR_018476
    Natural varianti262 – 2621G → S.1 Publication
    VAR_012479
    Natural varianti308 – 3081A → V.
    Corresponds to variant rs13739 [ dbSNP | Ensembl ].
    VAR_012480

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei193 – 1931W → QTSHLTGLLPLVLRNPQPQA PCQGSGSLAPGRTPALLGAL NVLPTLWVAFCLSVHPVVAV GICAWQAGAGHVCVFCLDGY GTVCSL in isoform 2. 1 PublicationVSP_035032
    Alternative sequencei194 – 390197Missing in isoform 2. 1 PublicationVSP_035033Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M25665 mRNA. Translation: AAA57209.1.
    M55067 mRNA. Translation: AAA59901.1.
    U57835, U57833, U57834 Genomic DNA. Translation: AAB95193.1.
    AF184614 Genomic DNA. Translation: AAF34737.1.
    AF330625 mRNA. Translation: AAK19516.1.
    AF330626 mRNA. Translation: AAK19517.1.
    AF330627 mRNA. Translation: AAK19518.1.
    AK127905 mRNA. Translation: BAG54596.1. Different initiation.
    AK292094 mRNA. Translation: BAF84783.1. Different initiation.
    AK223217 mRNA. Translation: BAD96937.1.
    AC004883 Genomic DNA. No translation available.
    AC083884 Genomic DNA. Translation: AAS07465.1.
    AC124781 Genomic DNA. No translation available.
    BC002816 mRNA. Translation: AAH02816.1.
    BC065731 mRNA. Translation: AAH65731.1.
    U25793 mRNA. Translation: AAA93232.1.
    DQ314878 Genomic DNA. Translation: ABC40737.1.
    CCDSiCCDS34657.1. [P14598-1]
    PIRiA35926. A39249.
    RefSeqiNP_000256.4. NM_000265.5.
    UniGeneiHs.647047.
    Hs.648940.
    Hs.655201.

    Genome annotation databases

    EnsembliENST00000289473; ENSP00000289473; ENSG00000158517. [P14598-1]
    GeneIDi653361.
    KEGGihsa:653361.
    UCSCiuc003ubb.3. human. [P14598-1]
    uc010lbs.1. human. [P14598-2]

    Polymorphism databases

    DMDMi325511390.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NCF1base

    NCF1 deficiency database

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M25665 mRNA. Translation: AAA57209.1 .
    M55067 mRNA. Translation: AAA59901.1 .
    U57835 , U57833 , U57834 Genomic DNA. Translation: AAB95193.1 .
    AF184614 Genomic DNA. Translation: AAF34737.1 .
    AF330625 mRNA. Translation: AAK19516.1 .
    AF330626 mRNA. Translation: AAK19517.1 .
    AF330627 mRNA. Translation: AAK19518.1 .
    AK127905 mRNA. Translation: BAG54596.1 . Different initiation.
    AK292094 mRNA. Translation: BAF84783.1 . Different initiation.
    AK223217 mRNA. Translation: BAD96937.1 .
    AC004883 Genomic DNA. No translation available.
    AC083884 Genomic DNA. Translation: AAS07465.1 .
    AC124781 Genomic DNA. No translation available.
    BC002816 mRNA. Translation: AAH02816.1 .
    BC065731 mRNA. Translation: AAH65731.1 .
    U25793 mRNA. Translation: AAA93232.1 .
    DQ314878 Genomic DNA. Translation: ABC40737.1 .
    CCDSi CCDS34657.1. [P14598-1 ]
    PIRi A35926. A39249.
    RefSeqi NP_000256.4. NM_000265.5.
    UniGenei Hs.647047.
    Hs.648940.
    Hs.655201.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GD5 NMR - A 1-128 [» ]
    1K4U NMR - P 359-390 [» ]
    1KQ6 X-ray 1.18 A 1-141 [» ]
    1NG2 X-ray 1.70 A 156-340 [» ]
    1O7K X-ray 2.00 A/B/C 1-123 [» ]
    1OV3 X-ray 1.80 A/B 156-285 [» ]
    1UEC X-ray 1.82 A 151-340 [» ]
    1W70 X-ray 1.46 C/D 360-372 [» ]
    1WLP NMR - B 151-286 [» ]
    ProteinModelPortali P14598.
    SMRi P14598. Positions 2-141, 157-332, 359-390.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 575724. 36 interactions.
    DIPi DIP-126N.
    IntActi P14598. 14 interactions.
    MINTi MINT-139338.

    Chemistry

    BindingDBi P14598.

    PTM databases

    PhosphoSitei P14598.

    Polymorphism databases

    DMDMi 325511390.

    Proteomic databases

    PaxDbi P14598.
    PRIDEi P14598.

    Protocols and materials databases

    DNASUi 653361.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000289473 ; ENSP00000289473 ; ENSG00000158517 . [P14598-1 ]
    GeneIDi 653361.
    KEGGi hsa:653361.
    UCSCi uc003ubb.3. human. [P14598-1 ]
    uc010lbs.1. human. [P14598-2 ]

    Organism-specific databases

    CTDi 653361.
    GeneCardsi GC07P074188.
    GeneReviewsi NCF1.
    H-InvDB HIX0033553.
    HGNCi HGNC:7660. NCF1.
    HPAi CAB004524.
    HPA047836.
    HPA052095.
    MIMi 233700. phenotype.
    608512. gene.
    neXtProti NX_P14598.
    Orphaneti 379. Chronic granulomatous disease.
    PharmGKBi PA31463.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG326975.
    HOVERGENi HBG002055.
    InParanoidi P14598.
    KOi K08011.
    OMAi SAYITTH.
    PhylomeDBi P14598.
    TreeFami TF329347.

    Enzyme and pathway databases

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

    Miscellaneous databases

    EvolutionaryTracei P14598.
    GeneWikii Neutrophil_cytosolic_factor_1.
    GenomeRNAii 653361.
    NextBioi 123127.
    PROi P14598.
    SOURCEi Search...

    Gene expression databases

    Bgeei P14598.
    Genevestigatori P14598.

    Family and domain databases

    Gene3Di 3.30.1520.10. 1 hit.
    InterProi IPR015039. NADPH_oxidase_p47Phox_C.
    IPR001655. P47PHOX.
    IPR001683. Phox.
    IPR001452. SH3_domain.
    [Graphical view ]
    Pfami PF08944. p47_phox_C. 1 hit.
    PF00787. PX. 1 hit.
    PF00018. SH3_1. 2 hits.
    [Graphical view ]
    PRINTSi PR00498. P47PHOX.
    SMARTi SM00312. PX. 1 hit.
    SM00326. SH3. 2 hits.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 2 hits.
    SSF64268. SSF64268. 1 hit.
    PROSITEi PS50195. PX. 1 hit.
    PS50002. SH3. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of the cDNA and functional expression of the 47-kilodalton cytosolic component of human neutrophil respiratory burst oxidase."
      Volpp B.D., Nauseef W.M., Clark R.A.
      Proc. Natl. Acad. Sci. U.S.A. 86:7195-7199(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    2. Erratum
      Volpp B.D., Nauseef W.M., Clark R.A.
      Proc. Natl. Acad. Sci. U.S.A. 86:9563-9563(1989)
      Cited for: SEQUENCE REVISION.
    3. "Recombinant 47-kilodalton cytosol factor restores NADPH oxidase in chronic granulomatous disease."
      Lomax K.J., Leto T.L., Nunoi H., Gallin J.I., Malech H.L.
      Science 245:409-412(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, VARIANTS SER-99 AND ASP-166.
    4. "Characterization of the 47-kilodalton autosomal chronic granulomatous disease protein: tissue-specific expression and transcriptional control by retinoic acid."
      Rodaway A.R.F., Teahan C.G., Casimir C.M., Segal A.W., Bentley D.L.
      Mol. Cell. Biol. 10:5388-5396(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS SER-99 AND ASP-166.
    5. "A p47-phox pseudogene carries the most common mutation causing p47-phox-deficient chronic granulomatous disease."
      Gorlach A., Lee P.L., Roesler J., Hopkins P.J., Christensen B., Green E.D., Chanock S.J., Curnutte J.T.
      J. Clin. Invest. 100:1907-1918(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT SER-99.
    6. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT SER-99.
    7. "TNFalpha activates c-jun amino terminal kinase through p47(phox)."
      Gu Y., Xu Y.C., Wu R.F., Souza R.F., Nwariaku F.E., Terada L.S.
      Exp. Cell Res. 272:62-74(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS SER-99; ASP-166 AND GLU-258.
      Tissue: Umbilical vein.
    8. "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 2), VARIANT SER-99.
      Tissue: Spleen and Synovium.
    9. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT SER-99.
      Tissue: Spleen.
    10. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    11. "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 1), VARIANT SER-99.
      Tissue: Lymph.
    12. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8-31 (ISOFORM 1).
      Tissue: Ovary.
    13. "Autosomal recessive chronic granulomatous disease caused by deletion at a dinucleotide repeat."
      Casimir C.M., Bu-Ghanim H.N., Rodaway A.R., Bentley D.L., Rowe P., Segal A.W.
      Proc. Natl. Acad. Sci. U.S.A. 88:2753-2757(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 14-24, INVOLVEMENT IN CHRONIC GRANULOMATOUS DISEASE.
    14. NHLBI resequencing and genotyping service (RS&G)
      Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 133-390, VARIANT ASP-166.
    15. "The phosphorylation of the respiratory burst oxidase component p47phox during neutrophil activation. Phosphorylation of sites recognized by protein kinase C and by proline-directed kinases."
      el Benna J., Faust L.P., Babior B.M.
      J. Biol. Chem. 269:23431-23436(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-303; SER-304; SER-320; SER-328; SER-345 AND SER-348.
    16. "Interaction of human neutrophil flavocytochrome b with cytosolic proteins: transferred-NOESY NMR studies of a gp91phox C-terminal peptide bound to p47phox."
      Adams E.R., Dratz E.A., Gizachew D., Deleo F.R., Yu L., Volpp B.D., Vlases M., Jesaitis A.J., Quinn M.T.
      Biochem. J. 325:249-257(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CYBB.
    17. "Involvement of TRAF4 in oxidative activation of c-Jun N-terminal kinase."
      Xu Y.C., Wu R.F., Gu Y., Yang Y.S., Yang M.C., Nwariaku F.E., Terada L.S.
      J. Biol. Chem. 277:28051-28057(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRAF4, SUBCELLULAR LOCATION.
    18. "Novel human homologues of p47phox and p67phox participate in activation of superoxide-producing NADPH oxidases."
      Takeya R., Ueno N., Kami K., Taura M., Kohjima M., Izaki T., Nunoi H., Sumimoto H.
      J. Biol. Chem. 278:25234-25246(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NOXA1.
    19. "TRAF4 acts as a silencer in TLR-mediated signaling through the association with TRAF6 and TRIF."
      Takeshita F., Ishii K.J., Kobiyama K., Kojima Y., Coban C., Sasaki S., Ishii N., Klinman D.M., Okuda K., Akira S., Suzuki K.
      Eur. J. Immunol. 35:2477-2485(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRAF4.
    20. "Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening."
      Voss M., Lettau M., Janssen O.
      BMC Immunol. 10:53-53(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FASLG.
    21. "Alternative splicing of ADAM15 regulates its interactions with cellular SH3 proteins."
      Kleino I., Ortiz R.M., Yritys M., Huovila A.P., Saksela K.
      J. Cell. Biochem. 108:877-885(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ADAM15.
    22. "Regulation of TNF-induced oxygen radical production in human neutrophils: role of delta-PKC."
      Kilpatrick L.E., Sun S., Li H., Vary T.C., Korchak H.M.
      J. Leukoc. Biol. 87:153-164(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION.
    23. "Solution structure of the PX domain, a target of the SH3 domain."
      Hiroaki H., Ago T., Ito T., Sumimoto H., Kohda D.
      Nat. Struct. Biol. 8:526-530(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-128.
    24. "Diverse recognition of non-PxxP peptide ligands by the SH3 domains from p67(phox), Grb2 and Pex13p."
      Kami K., Takeya R., Sumimoto H., Kohda D.
      EMBO J. 21:4268-4276(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 359-390 IN COMPLEX WITH NCF2, INTERACTION WITH NCF2.
    25. "Binding of the PX domain of p47(phox) to phosphatidylinositol 3,4-bisphosphate and phosphatidic acid is masked by an intramolecular interaction."
      Karathanassis D., Stahelin R.V., Bravo J., Perisic O., Pacold C.M., Cho W., Williams R.L.
      EMBO J. 21:5057-5068(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-123, DOMAIN, LIPID-BINDING, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-43; TRP-263; SER-303; SER-304; SER-328; SER-359 AND SER-370.
    26. "Molecular basis of phosphorylation-induced activation of the NADPH oxidase."
      Groemping Y., Lapouge K., Smerdon S.J., Rittinger K.
      Cell 113:343-355(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 156-340, DOMAIN, INTERACTION WITH CYBA.
    27. "A molecular mechanism for autoinhibition of the tandem SH3 domains of p47phox, the regulatory subunit of the phagocyte NADPH oxidase."
      Yuzawa S., Suzuki N.N., Fujioka Y., Ogura K., Sumimoto H., Inagaki F.
      Genes Cells 9:443-456(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 151-340.
    28. "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 360-372 IN COMPLEX WITH NCF4, SUBUNIT.
    29. "NMR solution structure of the tandem Src homology 3 domains of p47phox complexed with a p22phox-derived proline-rich peptide."
      Ogura K., Nobuhisa I., Yuzawa S., Takeya R., Torikai S., Saikawa K., Sumimoto H., Inagaki F.
      J. Biol. Chem. 281:3660-3668(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 151-286 IN COMPLEX WITH CYBA, INTERACTION WITH CYBA.
    30. "Autosomal recessive chronic granulomatous disease caused by defects in NCF1, the gene encoding the phagocyte p47-phox: mutations not arising in the NCF1 pseudogenes."
      Noack D., Rae J., Cross A.R., Ellis B.A., Newburger P.E., Curnutte J.T., Heyworth P.G.
      Blood 97:305-311(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CGD1 GLN-42, VARIANT SER-262.

    Entry informationi

    Entry nameiNCF1_HUMAN
    AccessioniPrimary (citable) accession number: P14598
    Secondary accession number(s): A6NEH2
    , A8K7S9, O43842, Q2PP07, Q53FR5, Q9BU90, Q9BXI7, Q9BXI8, Q9UDV9, Q9UMU2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: March 8, 2011
    Last modified: October 1, 2014
    This is version 177 of the entry and version 3 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, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: 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