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P14598 (NCF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 175. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:NCF1
Synonyms:NOXO2, SH3PXD1A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length390 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

NCF2, NCF1, and a membrane bound cytochrome b558 are required for activation of the latent NADPH oxidase (necessary for superoxide production). Ref.1 Ref.3 Ref.22

Subunit structure

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. Ref.1 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.24 Ref.26 Ref.28 Ref.29

Subcellular location

Cytoplasmcytosol. Membrane; Peripheral membrane protein; Cytoplasmic side Ref.1 Ref.17 Ref.25.

Tissue specificity

Detected in peripheral blood monocytes and neutrophils (at protein level). Ref.1 Ref.3

Domain

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. Ref.25 Ref.26

Post-translational modification

Phosphorylated by PRKCD; phosphorylation induces activation of NCF1 and NADPH oxidase activity. Ref.15 Ref.22

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.13 Ref.30

Sequence similarities

Contains 1 PX (phox homology) domain.

Contains 2 SH3 domains.

Sequence caution

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.

Ontologies

Keywords
   Cellular componentCytoplasm
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseChronic granulomatous disease
Disease mutation
   DomainRepeat
SH3 domain
   LigandLipid-binding
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processantigen processing and presentation of exogenous peptide antigen via MHC class I

Traceable author statement. Source: Reactome

antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent

Traceable author statement. Source: Reactome

antigen processing and presentation of peptide antigen via MHC class I

Traceable author statement. Source: Reactome

apoptotic process

Inferred from electronic annotation. Source: Ensembl

cell proliferation

Inferred from electronic annotation. Source: Ensembl

cellular defense response

Traceable author statement PubMed 2848318. Source: ProtInc

hydrogen peroxide biosynthetic process

Inferred from electronic annotation. Source: Ensembl

inflammatory response

Inferred from electronic annotation. Source: Ensembl

innate immune response

Traceable author statement PubMed 7938008. Source: BHF-UCL

interaction with host

Traceable author statement. Source: Reactome

leukotriene metabolic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of smooth muscle contraction

Inferred from electronic annotation. Source: Ensembl

neutrophil mediated killing of fungus

Inferred from electronic annotation. Source: Ensembl

neutrophil mediated killing of gram-positive bacterium

Inferred from electronic annotation. Source: Ensembl

oxidation-reduction process

Inferred from mutant phenotype Ref.3. Source: GOC

phagosome maturation

Traceable author statement. Source: Reactome

protein targeting to membrane

Inferred from direct assay Ref.25. Source: UniProtKB

respiratory burst

Traceable author statement PubMed 7938008. Source: BHF-UCL

respiratory burst involved in defense response

Inferred from electronic annotation. Source: Ensembl

response to yeast

Inferred from electronic annotation. Source: Ensembl

superoxide anion generation

Inferred from mutant phenotype Ref.3. Source: UniProtKB

superoxide metabolic process

Traceable author statement PubMed 7938008. Source: BHF-UCL

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Ensembl

NADPH oxidase complex

Inferred from direct assay Ref.1. Source: UniProtKB

cytosol

Inferred from direct assay Ref.1. Source: UniProtKB

dendrite

Inferred from electronic annotation. Source: Ensembl

extrinsic component of membrane

Inferred from direct assay Ref.25. Source: UniProtKB

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

phagolysosome

Traceable author statement. Source: Reactome

rough endoplasmic reticulum

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionSH3 domain binding

Inferred from physical interaction PubMed 7938008. Source: BHF-UCL

electron carrier activity

Traceable author statement PubMed 2848318. Source: UniProtKB

phosphatidylinositol binding

Inferred from direct assay Ref.25. Source: UniProtKB

phosphatidylinositol-3,4-bisphosphate binding

Inferred from direct assay Ref.25. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 11094157. Source: UniProtKB

superoxide-generating NADPH oxidase activity

Inferred from mutant phenotype Ref.3. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P14598-1)

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.
Isoform 2 (identifier: P14598-2)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 390390Neutrophil cytosol factor 1
PRO_0000096762

Regions

Domain4 – 125122PX
Domain156 – 21560SH3 1
Domain226 – 28560SH3 2
Compositional bias211 – 25444Asp/Glu-rich (highly acidic)
Compositional bias292 – 39099Arg/Lys-rich (highly basic)

Amino acid modifications

Modified residue3031Phosphoserine Ref.15
Modified residue3041Phosphoserine Ref.15
Modified residue3201Phosphoserine Ref.15
Modified residue3281Phosphoserine Ref.15
Modified residue3451Phosphoserine Ref.15
Modified residue3481Phosphoserine Ref.15

Natural variations

Alternative sequence1931W → QTSHLTGLLPLVLRNPQPQA PCQGSGSLAPGRTPALLGAL NVLPTLWVAFCLSVHPVVAV GICAWQAGAGHVCVFCLDGY GTVCSL in isoform 2.
VSP_035032
Alternative sequence194 – 390197Missing in isoform 2.
VSP_035033
Natural variant421R → Q in CGD1. Ref.30
VAR_012476
Natural variant901R → H.
Corresponds to variant rs13447 [ dbSNP | Ensembl ].
VAR_014735
Natural variant991G → S. Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.11
Corresponds to variant rs17856077 [ dbSNP | Ensembl ].
VAR_018479
Natural variant1601T → S.
VAR_012477
Natural variant1661N → D. Ref.3 Ref.4 Ref.7 Ref.14
Corresponds to variant rs4868 [ dbSNP | Ensembl ].
VAR_012478
Natural variant2581K → E. Ref.7
VAR_018476
Natural variant2621G → S. Ref.30
VAR_012479
Natural variant3081A → V.
Corresponds to variant rs13739 [ dbSNP | Ensembl ].
VAR_012480

Experimental info

Mutagenesis431R → Q: Reduces affinity for membranes enriched in phosphatidylinositol 3,4-bisphosphate. Ref.25
Mutagenesis901R → A: Reduces affinity for membranes enriched in phosphatidylinositol 3,4-bisphosphate.
Mutagenesis2631W → R: Abolishes autoinhibition and promotes phospholipid binding. Ref.25
Mutagenesis3031S → E: Abolishes autoinhibition and promotes phospholipid binding; when associated with E-304; E-328; E-359 and E-370. Ref.25
Mutagenesis3041S → E: Abolishes autoinhibition and promotes phospholipid binding; when associated with E-303; E-328; E-359 and E-370. Ref.25
Mutagenesis3281S → E: Abolishes autoinhibition and promotes phospholipid binding; when associated with E-303; E-304; E-359 and E-370. Ref.25
Mutagenesis3591S → E: Abolishes autoinhibition and promotes phospholipid binding; when associated with E-303; E-304; E-328 and E-370. Ref.25
Mutagenesis3701S → E: Abolishes autoinhibition and promotes phospholipid binding; when associated with E-303; E-304; E-328 and E-359. Ref.25
Sequence conflict2001A → T in AAK19516. Ref.7

Secondary structure

............................................................... 390
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 8, 2011. Version 3.
Checksum: 5A0F9F0EF101D2DB

FASTA39044,652
        10         20         30         40         50         60 
MGDTFIRHIA LLGFEKRFVP SQHYVYMFLV KWQDLSEKVV YRRFTEIYEF HKTLKEMFPI 

        70         80         90        100        110        120 
EAGAINPENR IIPHLPAPKW FDGQRAAENR QGTLTEYCGT LMSLPTKISR CPHLLDFFKV 

       130        140        150        160        170        180 
RPDDLKLPTD NQTKKPETYL MPKDGKSTAT DITGPIILQT YRAIANYEKT SGSEMALSTG 

       190        200        210        220        230        240 
DVVEVVEKSE SGWWFCQMKA KRGWIPASFL EPLDSPDETE DPEPNYAGEP YVAIKAYTAV 

       250        260        270        280        290        300 
EGDEVSLLEG EAVEVIHKLL DGWWVIRKDD VTGYFPSMYL QKSGQDVSQA QRQIKRGAPP 

       310        320        330        340        350        360 
RRSSIRNAHS IHQRSRKRLS QDAYRRNSVR FLQQRRRQAR PGPQSPGSPL EEERQTQRSK 

       370        380        390 
PQPAVPPRPS ADLILNRCSE STKRKLASAV 

« Hide

Isoform 2 [UniParc].

Checksum: AB0F8221EE55FCAF
Show »

FASTA27830,781

References

« Hide 'large scale' references
[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]"Genomic structure of the human p47-phox (NCF1) gene."
Chanock S.J., Roesler J., Zhan S., Hopkins P., Lee P., Barrett D.T., Christensen B.L., Curnutte J.T., Goerlach A.
Blood Cells Mol. Dis. 26:37-46(2000) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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]"Comparison of the positional cloning methods used to isolate the BRCA1 gene."
Harshman K., Bell R., Rosenthal J., Katcher H., Miki Y., Swenson J., Gholami Z., Frye C., Ding W., Dayananth P., Eddington K., Norris F.H., Bristow P.K., Phelps R., Hattier T., Stone S., Shaffer D., Bayer S. expand/collapse author list , Hussey C., Tran T., Lai M., Rosteck P.R. Jr., Skolnick M.H., Shattuck-Eidens D., Kamb A.
Hum. Mol. Genet. 4:1259-1266(1995) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

NCF1base

NCF1 deficiency database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS34657.1. [P14598-1]
PIRA39249. A35926.
RefSeqNP_000256.4. NM_000265.5.
UniGeneHs.647047.
Hs.648940.
Hs.655201.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP14598.
SMRP14598. Positions 2-141, 157-332, 359-390.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid575724. 36 interactions.
DIPDIP-126N.
IntActP14598. 14 interactions.
MINTMINT-139338.

Chemistry

BindingDBP14598.

PTM databases

PhosphoSiteP14598.

Polymorphism databases

DMDM325511390.

Proteomic databases

PaxDbP14598.
PRIDEP14598.

Protocols and materials databases

DNASU653361.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000289473; ENSP00000289473; ENSG00000158517. [P14598-1]
ENST00000573351; ENSP00000459675; ENSG00000261919.
GeneID653361.
KEGGhsa:653361.
UCSCuc003ubb.3. human. [P14598-1]
uc010lbs.1. human. [P14598-2]

Organism-specific databases

CTD653361.
GeneCardsGC07P074188.
GeneReviewsNCF1.
H-InvDBHIX0033553.
HGNCHGNC:7660. NCF1.
HPACAB004524.
HPA047836.
HPA052095.
MIM233700. phenotype.
608512. gene.
neXtProtNX_P14598.
Orphanet379. Chronic granulomatous disease.
PharmGKBPA31463.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG326975.
HOVERGENHBG002055.
InParanoidP14598.
KOK08011.
OMASAYITTH.
PhylomeDBP14598.
TreeFamTF329347.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
REACT_6900. Immune System.

Gene expression databases

BgeeP14598.
GenevestigatorP14598.

Family and domain databases

Gene3D3.30.1520.10. 1 hit.
InterProIPR015039. NADPH_oxidase_p47Phox_C.
IPR001655. P47PHOX.
IPR001683. Phox.
IPR001452. SH3_domain.
[Graphical view]
PfamPF08944. p47_phox_C. 1 hit.
PF00787. PX. 1 hit.
PF00018. SH3_1. 2 hits.
[Graphical view]
PRINTSPR00498. P47PHOX.
SMARTSM00312. PX. 1 hit.
SM00326. SH3. 2 hits.
[Graphical view]
SUPFAMSSF50044. SSF50044. 2 hits.
SSF64268. SSF64268. 1 hit.
PROSITEPS50195. PX. 1 hit.
PS50002. SH3. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP14598.
GeneWikiNeutrophil_cytosolic_factor_1.
GenomeRNAi653361.
NextBio123127.
PROP14598.
SOURCESearch...

Entry information

Entry nameNCF1_HUMAN
AccessionPrimary (citable) accession number: P14598
Secondary accession number(s): A6NEH2 expand/collapse secondary AC list , A8K7S9, O43842, Q2PP07, Q53FR5, Q9BU90, Q9BXI7, Q9BXI8, Q9UDV9, Q9UMU2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: March 8, 2011
Last modified: July 9, 2014
This is version 175 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM