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Q15080

- NCF4_HUMAN

UniProt

Q15080 - NCF4_HUMAN

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Protein
Neutrophil cytosol factor 4
Gene
NCF4, SH3PXD4
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

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

GO - Biological processi

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

Names & Taxonomyi

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

Organism-specific databases

HGNCiHGNC:7662. NCF4.

Subcellular locationi

Cytoplasmcytosol. Endosome membrane; Peripheral membrane protein; Cytoplasmic side. Membrane; Peripheral membrane protein 2 Publications

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Endosome, Membrane

Pathology & Biotechi

Involvement in diseasei

Granulomatous disease, chronic, cytochrome-b-positive 3, autosomal recessive (CGD3) [MIM:613960]: A disorder characterized by the inability of neutrophils and phagocytes to kill microbes that they have ingested. Patients suffer from life-threatening bacterial/fungal infections.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti105 – 1051R → Q in CGD3; the protein remains cytosolic, does not localize to phagosomes or endosomes and is unable to bind phosphatidylinositol 3-phosphate (PtdIns(3)P) in a lipid-binding assay; unable to rescue the NADPH-oxidase defect of NCF4 functionally null cells. 1 Publication
VAR_065949

Mutagenesis

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

Keywords - Diseasei

Chronic granulomatous disease, Disease mutation

Organism-specific databases

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

PTM / Processingi

Molecule processing

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

Amino acid modifications

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ15080.
PaxDbiQ15080.
PRIDEiQ15080.

PTM databases

PhosphoSiteiQ15080.

Expressioni

Tissue specificityi

Expression is restricted to hematopoietic cells.

Gene expression databases

ArrayExpressiQ15080.
BgeeiQ15080.
CleanExiHS_NCF4.
GenevestigatoriQ15080.

Organism-specific databases

HPAiCAB010146.
HPA036156.

Interactioni

Subunit structurei

Component of an NADPH oxidase complex composed of a heterodimer formed by the membrane proteins CYBA and CYBB and the cytosolic subunits NCF1, NCF2 and NCF4. NCF4 interacts primarily with NCF2 to form a complex with NCF1.3 Publications

Binary interactionsi

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

Protein-protein interaction databases

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

Structurei

Secondary structure

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

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ15080.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 140122PX
Add
BLAST
Domaini170 – 22960SH3
Add
BLAST
Domaini237 – 32993OPR
Add
BLAST

Region

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

Domaini

The OPR/PB1 domain mediates the association with NCF2/p67-PHOX.2 Publications
The PX domain mediates interaction with membranes enriched in phosphatidylnositol 3-phosphate.2 Publications

Sequence similaritiesi

Contains 1 OPR domain.
Contains 1 SH3 domain.

Keywords - Domaini

SH3 domain

Phylogenomic databases

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

Family and domain databases

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

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

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

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

« Hide

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

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

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

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

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

Natural variant

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei254 – 33986DIAVE…YNTMP → SVAWEGGACPAFLPSLRPPP LTSPSHGSLSHSKAPSGSQM SHNAVTSHQRPGWPGQPHSP FPHPTPHFQPDASLLQPVTP LGTSRWRKISAALPY in isoform 2.
VSP_004328Add
BLAST
Alternative sequencei254 – 33986DIAVE…YNTMP → SVAWEGGACPAFLPSLRPLP LTSPSHGSLSHSKAPSGSQM SHNAVTSHQRPGWPGQPHSP FPHPTPHFQPDASLLQPVTP LGTSRWRKISAALPY in isoform 3.
VSP_042681Add
BLAST

Sequence databases

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

Genome annotation databases

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

Polymorphism databases

DMDMi108884815.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

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

3D structure databases

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

Protein-protein interaction databases

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

PTM databases

PhosphoSitei Q15080.

Polymorphism databases

DMDMi 108884815.

Proteomic databases

MaxQBi Q15080.
PaxDbi Q15080.
PRIDEi Q15080.

Protocols and materials databases

DNASUi 4689.
Structural Biology Knowledgebase Search...

Genome annotation databases

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

Organism-specific databases

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

Phylogenomic databases

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

Enzyme and pathway databases

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

Miscellaneous databases

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

Gene expression databases

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

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "p40phox, a third cytosolic component of the activation complex of the NADPH oxidase to contain src homology 3 domains."
    Wientjes F.B., Hsuan J.J., Totty N.F., Segal A.W.
    Biochem. J. 296:557-561(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, VARIANT ILE-147, PARTIAL PROTEIN SEQUENCE.
  2. "Genomic structure, chromosomal localization, start of transcription, and tissue expression of the human p40-phox, a new component of the nicotinamide adenine dinucleotide phosphate-oxidase complex."
    Zhan S., Vazquez N., Zhan S., Wientjes F.B., Budarf M.L., Schrock E., Ried T., Green E.D., Chanock S.J.
    Blood 88:2714-2721(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ILE-147.
  3. "Identification of a splice variant mRNA of p40phox, an NADPH oxidase component of phagocytes."
    Hasebe T., Someya A., Nagaoka I.
    FEBS Lett. 455:257-261(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  5. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
  7. NHLBI resequencing and genotyping service (RS&G)
    Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  8. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Lymph.
  10. "p40(phox) is phosphorylated on threonine 154 and serine 315 during activation of the phagocyte NADPH oxidase. Implication of a protein kinase c-type kinase in the phosphorylation process."
    Bouin A.-P., Grandvaux N., Vignais P.V., Fuchs A.
    J. Biol. Chem. 273:30097-30103(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-154 AND SER-315, MUTAGENESIS OF THR-154; THR-211; THR-251; THR-274; SER-315 AND THR-327.
  11. "The crystal structure of the PX domain from p40(phox) bound to phosphatidylinositol 3-phosphate."
    Bravo J., Karathanassis D., Pacold C.M., Pacold M.E., Ellson C.D., Anderson K.E., Butler P.J.G., Lavenir I., Perisic O., Hawkins P.T., Stephens L., Williams R.L.
    Mol. Cell 8:829-839(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 2-144 IN COMPLEX WITH PHOSPHATIDYLINOSITOL 3-PHOSPHATE, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF ARG-58; ARG-60; LYS-92; TYR-94 AND ARG-105, LIPID-BINDING.
  12. "PB1 domain-mediated heterodimerization in NADPH oxidase and signaling complexes of atypical protein kinase C with Par6 and p62."
    Wilson M.I., Gill D.J., Perisic O., Quinn M.T., Williams R.L.
    Mol. Cell 12:39-50(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 237-339 IN COMPLEX WITH NCF2, INTERACTION WITH NCF2.
  13. "Effects of p47phox C terminus phosphorylations on binding interactions with p40phox and p67phox. Structural and functional comparison of p40phox and p67phox SH3 domains."
    Massenet C., Chenavas S., Cohen-Addad C., Dagher M.-C., Brandolin G., Pebay-Peyroula E., Fieschi F.
    J. Biol. Chem. 280:13752-13761(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.46 ANGSTROMS) OF 174-228 IN COMPLEX WITH NCF1, INTERACTION WITH NCF1.
  14. "Full-length p40phox structure suggests a basis for regulation mechanism of its membrane binding."
    Honbou K., Minakami R., Yuzawa S., Takeya R., Suzuki N.N., Kamakura S., Sumimoto H., Inagaki F.
    EMBO J. 26:1176-1186(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS), DOMAIN OPR/PB1.
  15. "A new genetic subgroup of chronic granulomatous disease with autosomal recessive mutations in p40 phox and selective defects in neutrophil NADPH oxidase activity."
    Matute J.D., Arias A.A., Wright N.A., Wrobel I., Waterhouse C.C., Li X.J., Marchal C.C., Stull N.D., Lewis D.B., Steele M., Kellner J.D., Yu W., Meroueh S.O., Nauseef W.M., Dinauer M.C.
    Blood 114:3309-3315(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CGD3 GLN-105, CHARACTERIZATION OF VARIANT CGD3 GLN-105.

Entry informationi

Entry nameiNCF4_HUMAN
AccessioniPrimary (citable) accession number: Q15080
Secondary accession number(s): A8K4F9
, O60808, Q86U56, Q9BU98, Q9NP45
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2006
Last modified: September 3, 2014
This is version 155 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

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

Documents

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

External Data

Dasty 3

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