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Q15080 (NCF4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 151. 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·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:NCF4
Synonyms:SH3PXD4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length339 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1

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. NCF4 interacts primarily with NCF2 to form a complex with NCF1. Ref.1 Ref.12 Ref.13

Subcellular location

Cytoplasmcytosol. Endosome membrane; Peripheral membrane protein; Cytoplasmic side. Membrane; Peripheral membrane protein Ref.1 Ref.11.

Tissue specificity

Expression is restricted to hematopoietic cells.

Domain

The OPR/PB1 domain mediates the association with NCF2/p67-PHOX. Ref.11 Ref.14

The PX domain mediates interaction with membranes enriched in phosphatidylnositol 3-phosphate. Ref.11 Ref.14

Involvement in disease

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. Ref.15

Sequence similarities

Contains 1 OPR domain.

Contains 1 PX (phox homology) domain.

Contains 1 SH3 domain.

Ontologies

Keywords
   Cellular componentCytoplasm
Endosome
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseChronic granulomatous disease
Disease mutation
   DomainSH3 domain
   LigandLipid-binding
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
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

immune response

Traceable author statement Ref.1. Source: UniProtKB

interaction with host

Traceable author statement. Source: Reactome

oxidation-reduction process

Traceable author statement Ref.2. Source: UniProtKB

phagosome maturation

Traceable author statement. Source: Reactome

positive regulation of catalytic activity

Inferred from mutant phenotype Ref.1. Source: GOC

   Cellular_componentNADPH oxidase complex

Inferred from direct assay Ref.1. Source: UniProtKB

cytosol

Inferred from direct assay Ref.1. Source: UniProtKB

endosome membrane

Inferred from direct assay Ref.11. Source: UniProtKB

membrane

Inferred from direct assay Ref.1. Source: UniProtKB

phagolysosome

Traceable author statement. Source: Reactome

   Molecular_functionphosphatidylinositol-3-phosphate binding

Inferred from direct assay Ref.11. Source: UniProtKB

protein dimerization activity

Traceable author statement Ref.1. Source: UniProtKB

superoxide-generating NADPH oxidase activator activity

Inferred from mutant phenotype Ref.1. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q15080-1)

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: Q15080-2)

The sequence of this isoform differs from the canonical sequence as follows:
     254-339: DIAVEEDLSS...DNYRVYNTMP → SVAWEGGACP...WRKISAALPY
Isoform 3 (identifier: Q15080-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 339339Neutrophil cytosol factor 4
PRO_0000096764

Regions

Domain19 – 140122PX
Domain170 – 22960SH3
Domain237 – 32993OPR
Region58 – 603Phosphatidylinositol 3-phosphate binding
Region92 – 943Phosphatidylinositol 3-phosphate binding

Amino acid modifications

Modified residue1541Phosphothreonine Ref.10
Modified residue3151Phosphoserine Ref.10

Natural variations

Alternative sequence254 – 33986DIAVE…YNTMP → SVAWEGGACPAFLPSLRPPP LTSPSHGSLSHSKAPSGSQM SHNAVTSHQRPGWPGQPHSP FPHPTPHFQPDASLLQPVTP LGTSRWRKISAALPY in isoform 2.
VSP_004328
Alternative sequence254 – 33986DIAVE…YNTMP → SVAWEGGACPAFLPSLRPLP LTSPSHGSLSHSKAPSGSQM SHNAVTSHQRPGWPGQPHSP FPHPTPHFQPDASLLQPVTP LGTSRWRKISAALPY in isoform 3.
VSP_042681
Natural variant1051R → 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. Ref.15
VAR_065949
Natural variant1471L → I. Ref.1 Ref.2
VAR_009314
Natural variant1531R → H.
Corresponds to variant rs35160112 [ dbSNP | Ensembl ].
VAR_034136

Experimental info

Mutagenesis581R → Q: Abolishes interaction with membranes enriched in phosphatidylinositol 3-phosphate. Ref.11
Mutagenesis601R → A: Strongly reduces interaction with membranes enriched in phosphatidylinositol 3-phosphate. Ref.11
Mutagenesis921K → A: Abolishes interaction with membranes enriched in phosphatidylinositol 3-phosphate. Ref.11
Mutagenesis941Y → A: Slightly reduces interaction with membranes enriched in phosphatidylinositol 3-phosphate. Ref.11
Mutagenesis1051R → A: Abolishes interaction with membranes enriched in phosphatidylinositol 3-phosphate. Ref.11
Mutagenesis1541T → A: Reduces phosphorylation. Ref.10
Mutagenesis2111T → A: No effect on phosphorylation. Ref.10
Mutagenesis2511T → A: No effect on phosphorylation. Ref.10
Mutagenesis2741T → A: No effect on phosphorylation. Ref.10
Mutagenesis3151S → A: Reduces phosphorylation. Ref.10
Mutagenesis3271T → A: No effect on phosphorylation. Ref.10

Secondary structure

.................................................. 339
Helix Strand Turn

Details...

Sequences

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

Last modified May 30, 2006. Version 2.
Checksum: D82FE9E5BA12890B

FASTA33939,032
        10         20         30         40         50         60 
MAVAQQLRAE SDFEQLPDDV AISANIADIE EKRGFTSHFV FVIEVKTKGG SKYLIYRRYR 

        70         80         90        100        110        120 
QFHALQSKLE ERFGPDSKSS ALACTLPTLP AKVYVGVKQE IAEMRIPALN AYMKSLLSLP 

       130        140        150        160        170        180 
VWVLMDEDVR IFFYQSPYDS EQVPQALRRL RPRTRKVKSV SPQGNSVDRM AAPRAEALFD 

       190        200        210        220        230        240 
FTGNSKLELN FKAGDVIFLL SRINKDWLEG TVRGATGIFP LSFVKILKDF PEEDDPTNWL 

       250        260        270        280        290        300 
RCYYYEDTIS TIKDIAVEED LSSTPLLKDL LELTRREFQR EDIALNYRDA EGDLVRLLSD 

       310        320        330 
EDVALMVRQA RGLPSQKRLF PWKLHITQKD NYRVYNTMP 

« Hide

Isoform 2 [UniParc].

Checksum: 49393E82583B7ADD
Show »

FASTA34839,001
Isoform 3 [UniParc].

Checksum: 0C787E82434C16C6
Show »

FASTA34839,017

References

« Hide 'large scale' references
[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]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
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. 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 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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X77094 mRNA. Translation: CAA54372.1.
U50729 expand/collapse EMBL AC list , 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.
PIRS39768.
RefSeqNP_000622.2. NM_000631.4.
NP_038202.2. NM_013416.3.
UniGeneHs.474781.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalQ15080.
SMRQ15080. Positions 2-339.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110769. 7 interactions.
DIPDIP-17019N.
IntActQ15080. 5 interactions.
MINTMINT-206126.
STRING9606.ENSP00000337605.

PTM databases

PhosphoSiteQ15080.

Polymorphism databases

DMDM108884815.

Proteomic databases

PaxDbQ15080.
PRIDEQ15080.

Protocols and materials databases

DNASU4689.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000248899; ENSP00000248899; ENSG00000100365. [Q15080-1]
ENST00000397147; ENSP00000380334; ENSG00000100365. [Q15080-3]
GeneID4689.
KEGGhsa:4689.
UCSCuc003apy.4. human. [Q15080-1]
uc003apz.4. human. [Q15080-3]

Organism-specific databases

CTD4689.
GeneCardsGC22P037257.
HGNCHGNC:7662. NCF4.
HPACAB010146.
HPA036156.
MIM601488. gene.
613960. phenotype.
neXtProtNX_Q15080.
Orphanet379. Chronic granulomatous disease.
206. Crohn disease.
PharmGKBPA31465.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG297760.
HOGENOMHOG000013076.
HOVERGENHBG006452.
KOK08012.
OMALFPWKLH.
PhylomeDBQ15080.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressQ15080.
BgeeQ15080.
CleanExHS_NCF4.
GenevestigatorQ15080.

Family and domain databases

Gene3D3.30.1520.10. 1 hit.
InterProIPR000919. NCF_P40.
IPR000270. OPR_PB1.
IPR001683. Phox.
IPR001452. SH3_domain.
[Graphical view]
PANTHERPTHR15552. PTHR15552. 1 hit.
PfamPF00564. PB1. 1 hit.
PF00787. PX. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSPR00497. P40PHOX.
SMARTSM00666. PB1. 1 hit.
SM00312. PX. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
SSF64268. SSF64268. 1 hit.
PROSITEPS50195. PX. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ15080.
GenomeRNAi4689.
NextBio18080.
PROQ15080.
SOURCESearch...

Entry information

Entry nameNCF4_HUMAN
AccessionPrimary (citable) accession number: Q15080
Secondary accession number(s): A8K4F9 expand/collapse secondary AC list , O60808, Q86U56, Q9BU98, Q9NP45
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2006
Last modified: April 16, 2014
This is version 151 of the entry and version 2 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 22

Human chromosome 22: entries, gene names and cross-references to MIM