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P14598

- NCF1_HUMAN

UniProt

P14598 - NCF1_HUMAN

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Protein

Neutrophil cytosol factor 1

Gene

NCF1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. SH3 domain binding Source: BHF-UCL
  5. 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
Complete GO annotation...

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

ReactomeiREACT_111174. Cross-presentation of particulate exogenous antigens (phagosomes).
REACT_121256. Phagosomal maturation (early endosomal stage).
REACT_228166. VEGFA-VEGFR2 Pathway.

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
Complete GO annotation...

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.2 Publications
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 – 3031Phosphoserine1 Publication
Modified residuei304 – 3041Phosphoserine1 Publication
Modified residuei320 – 3201Phosphoserine1 Publication
Modified residuei328 – 3281Phosphoserine1 Publication
Modified residuei345 – 3451Phosphoserine1 Publication
Modified residuei348 – 3481Phosphoserine1 Publication

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 – 1712Combined sources
Beta strandi19 – 213Combined sources
Beta strandi23 – 3210Combined sources
Beta strandi37 – 426Combined sources
Helixi44 – 5714Combined sources
Turni59 – 635Combined sources
Helixi67 – 693Combined sources
Helixi78 – 803Combined sources
Helixi84 – 10118Combined sources
Helixi106 – 1094Combined sources
Helixi112 – 1187Combined sources
Helixi122 – 1254Combined sources
Beta strandi137 – 1404Combined sources
Beta strandi153 – 1553Combined sources
Beta strandi159 – 1624Combined sources
Beta strandi171 – 1744Combined sources
Beta strandi182 – 1876Combined sources
Beta strandi195 – 1984Combined sources
Beta strandi202 – 2065Combined sources
Helixi207 – 2093Combined sources
Beta strandi210 – 2145Combined sources
Beta strandi229 – 2357Combined sources
Beta strandi241 – 2444Combined sources
Beta strandi252 – 2576Combined sources
Beta strandi262 – 2687Combined sources
Beta strandi271 – 2766Combined sources
Helixi277 – 2793Combined sources
Beta strandi280 – 2823Combined sources
Helixi287 – 2926Combined sources
Helixi302 – 3043Combined sources
Helixi321 – 3288Combined sources
Helixi371 – 3766Combined sources
Helixi380 – 3856Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00530000063010.
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

        10         20         30         40         50
MGDTFIRHIA LLGFEKRFVP SQHYVYMFLV KWQDLSEKVV YRRFTEIYEF
60 70 80 90 100
HKTLKEMFPI EAGAINPENR IIPHLPAPKW FDGQRAAENR QGTLTEYCGT
110 120 130 140 150
LMSLPTKISR CPHLLDFFKV RPDDLKLPTD NQTKKPETYL MPKDGKSTAT
160 170 180 190 200
DITGPIILQT YRAIANYEKT SGSEMALSTG DVVEVVEKSE SGWWFCQMKA
210 220 230 240 250
KRGWIPASFL EPLDSPDETE DPEPNYAGEP YVAIKAYTAV EGDEVSLLEG
260 270 280 290 300
EAVEVIHKLL DGWWVIRKDD VTGYFPSMYL QKSGQDVSQA QRQIKRGAPP
310 320 330 340 350
RRSSIRNAHS IHQRSRKRLS QDAYRRNSVR FLQQRRRQAR PGPQSPGSPL
360 370 380 390
EEERQTQRSK PQPAVPPRPS ADLILNRCSE STKRKLASAV
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.Curated
The sequence BAG54596.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

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:
EMBLi
GenBanki
DDBJi
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.
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
DrugBanki DB00514. Dextromethorphan.

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 .
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.
GeneTreei ENSGT00530000063010.
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).
REACT_228166. VEGFA-VEGFR2 Pathway.

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

« Hide 'large scale' publications
  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: INVOLVEMENT IN CGD1, VARIANT CGD1 GLN-42, VARIANT SER-262.
  31. "Clinical, functional, and genetic characterization of chronic granulomatous disease in 89 Turkish patients."
    Koeker M.Y., Camcioglu Y., van Leeuwen K., Kilic S.S., Barlan I., Yilmaz M., Metin A., de Boer M., Avcilar H., Patiroglu T., Yildiran A., Yegin O., Tezcan I., Sanal O., Roos D.
    J. Allergy Clin. Immunol. 132:1156-1163(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN CGD1.

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: November 26, 2014
This is version 179 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