Q15080 (NCF4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	NCF4
Synonyms:	SH3PXD4

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	339 AA.
Sequence status	Complete.
Protein existence	Evidence 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.
Subunit structure	p40-PHOX associates primarily with p67-PHOX to form a complex with p47-PHOX.
Subcellular location	Cytoplasm.
Tissue specificity	Expression is restricted to hematopoietic cells.
Domain	The OPR/PB1 domain mediates the association with NCF2/p67-PHOX. 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 component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Chronic granulomatous disease Disease mutation
Domain	SH3 domain
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent Traceable author statement. Source: Reactome cell communication Inferred from electronic annotation. Source: InterPro 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
Cellular_component	NADPH oxidase complex Inferred from direct assay Ref.1. Source: UniProtKB cytosol Inferred from direct assay Ref.1. Source: UniProtKB phagolysosome Traceable author statement. Source: Reactome
Molecular_function	phosphatidylinositol binding Inferred from electronic annotation. Source: InterPro protein dimerization activity Traceable author statement Ref.1. Source: UniProtKB
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 339

339

Neutrophil cytosol factor 4

PRO_0000096764

Regions

Domain

19 – 140

122

PX

Domain

170 – 229

60

SH3

Domain

237 – 329

93

OPR

Amino acid modifications

Modified residue

154

1

Phosphothreonine Ref.10

Modified residue

315

1

Phosphoserine Ref.10

Natural variations

Alternative sequence

254 – 339

86

DIAVE…YNTMP → SVAWEGGACPAFLPSLRPPP LTSPSHGSLSHSKAPSGSQM SHNAVTSHQRPGWPGQPHSP FPHPTPHFQPDASLLQPVTP LGTSRWRKISAALPY in isoform 2.

VSP_004328

Alternative sequence

254 – 339

86

DIAVE…YNTMP → SVAWEGGACPAFLPSLRPLP LTSPSHGSLSHSKAPSGSQM SHNAVTSHQRPGWPGQPHSP FPHPTPHFQPDASLLQPVTP LGTSRWRKISAALPY in isoform 3.

VSP_042681

Natural variant

105

1

R → 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 variant

147

1

L → I. Ref.1 Ref.2

VAR_009314

Natural variant

153

1

R → H.
Corresponds to variant rs35160112 [ dbSNP | Ensembl ].

VAR_034136

Experimental info

Mutagenesis

154

1

T → A: Reduces phosphorylation. Ref.10

Mutagenesis

211

1

T → A: No effect on phosphorylation. Ref.10

Mutagenesis

251

1

T → A: No effect on phosphorylation. Ref.10

Mutagenesis

274

1

T → A: No effect on phosphorylation. Ref.10

Mutagenesis

315

1

S → A: Reduces phosphorylation. Ref.10

Mutagenesis

327

1

T → A: No effect on phosphorylation. Ref.10

Secondary structure

1

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339

Helix Strand Turn

Details...

Helix

3 – 15

13

Beta strand

21 – 32

12

Beta strand

34 – 36

3

Beta strand

38 – 47

10

Beta strand

52 – 58

7

Helix

59 – 73

15

Helix

80 – 82

3

Helix

98 – 116

19

Helix

121 – 124

4

Helix

127 – 133

7

Helix

137 – 140

4

Beta strand

174 – 179

6

Beta strand

184 – 188

5

Beta strand

196 – 202

7

Beta strand

204 – 212

9

Beta strand

215 – 220

6

Helix

221 – 223

3

Beta strand

224 – 226

3

Beta strand

238 – 246

9

Beta strand

249 – 257

9

Helix

267 – 278

12

Beta strand

281 – 288

8

Beta strand

290 – 292

3

Beta strand

294 – 296

3

Helix

300 – 309

10

Beta strand

324 – 328

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 30, 2006. Version 2. Checksum: D82FE9E5BA12890B	FASTA	339	39,032
	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
	Isoform 2 [UniParc]. Checksum: 49393E82583B7ADD	FASTA	348	39,001
	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 TIKSVAWEGG ACPAFLPSLR PPPLTSPSHG SLSHSKAPSG SQMSHNAVTS 310 320 330 340 HQRPGWPGQP HSPFPHPTPH FQPDASLLQP VTPLGTSRWR KISAALPY
	Isoform 3 [UniParc]. Checksum: 0C787E82434C16C6	FASTA	348	39,017
	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 TIKSVAWEGG ACPAFLPSLR PLPLTSPSHG SLSHSKAPSG SQMSHNAVTS 310 320 330 340 HQRPGWPGQP HSPFPHPTPH FQPDASLLQP VTPLGTSRWR KISAALPY

References

	« Hide 'large scale' referencesShow '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), 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. , 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.
[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.
[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.
[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 , 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.

IPI

IPI00014338.
IPI00297156.
IPI00877642.

PIR

S39768.

RefSeq

NP_000622.2. NM_000631.4.
NP_038202.2. NM_013416.3.

UniGene

Hs.474781.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q15080.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-17019N.

IntAct

Q15080. 3 interactions.

MINT

MINT-206126.

STRING

9606.ENSP00000337605.

PTM databases

PhosphoSite

Q15080.

Polymorphism databases

DMDM

108884815.

Proteomic databases

PaxDb

Q15080.

PRIDE

Q15080.

Protocols and materials databases

DNASU

4689.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000248899; ENSP00000248899; ENSG00000100365.
ENST00000397147; ENSP00000380334; ENSG00000100365.

GeneID

4689.

KEGG

hsa:4689.

UCSC

uc003apy.4. human.

Organism-specific databases

CTD

4689.

GeneCards

GC22P037257.

HGNC

HGNC:7662. NCF4.

HPA

CAB010146.

MIM

601488. gene.
613960. phenotype.

neXtProt

NX_Q15080.

Orphanet

379. Chronic granulomatous disease.

PharmGKB

PA31465.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG297760.

HOGENOM

HOG000013076.

HOVERGEN

HBG006452.

KO

K08012.

OMA

LFPWKLH.

Enzyme and pathway databases

Reactome

REACT_116125. Disease.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

Q15080.

Bgee

Q15080.

CleanEx

HS_NCF4.

Genevestigator

Q15080.

GermOnline

ENSG00000100365. Homo sapiens.

Family and domain databases

Gene3D

3.30.1520.10. 1 hit.

InterPro

IPR000919. NCF_P40.
IPR000270. OPR_PB1.
IPR001683. Phox.
IPR001452. SH3_domain.
[Graphical view]

PANTHER

PTHR15552. PTHR15552. 1 hit.

Pfam

PF00564. PB1. 1 hit.
PF00787. PX. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]

PRINTS

PR00497. P40PHOX.

SMART

SM00666. PB1. 1 hit.
SM00312. PX. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]

SUPFAM

SSF64268. PX. 1 hit.
SSF50044. SH3. 1 hit.

PROSITE

PS50195. PX. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q15080.

GenomeRNAi

4689.

NextBio

18080.

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Entry information

Entry name

NCF4_HUMAN

Accession

Primary (citable) accession number: Q15080
Secondary accession number(s): A8K4F9 , O60808, Q86U56, Q9BU98, Q9NP45

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	May 30, 2006
Last modified:	May 1, 2013
This is version 143 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.