P19878 (NCF2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Neutrophil cytosol factor 2
Short name=NCF-2

Alternative name(s):
67 kDa neutrophil oxidase factor
NADPH oxidase activator 2
Neutrophil NADPH oxidase factor 2
p67-phox

Gene names

Name:	NCF2
Synonyms:	NOXA2, P67PHOX

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	526 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	NCF2, NCF1, and a membrane bound cytochrome b558 are required for activation of the latent NADPH oxidase (necessary for superoxide production).
Subunit structure	Interacts with SYTL1 and RAC1. Interacts with NCF4. May interact with NOXO1. Interacts with S100A8 and calprotectin (S100A8/9). Ref.10 Ref.11 Ref.12 Ref.13
Subcellular location	Cytoplasm.
Domain	The OPR/PB1 domain mediates the association with NCF4/p40-PHOX. Ref.13
Involvement in disease	Granulomatous disease, chronic, cytochrome-b-positive 2, autosomal recessive (CGD2) [MIM:233710]: 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.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24
Sequence similarities	Belongs to the NCF2/NOXA1 family. Contains 1 OPR domain. Contains 2 SH3 domains. Contains 3 TPR repeats.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Chronic granulomatous disease Disease mutation
Domain	Repeat SH3 domain TPR repeat
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	aging Inferred from electronic annotation. Source: Compara antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent Traceable author statement. Source: Reactome cellular defense response Traceable author statement Ref.1. Source: ProtInc cellular response to hormone stimulus Inferred from electronic annotation. Source: Compara innate immune response Traceable author statement PubMed 7938008. Source: BHF-UCL interaction with host Traceable author statement. Source: Reactome phagosome maturation Traceable author statement. Source: Reactome positive regulation of blood pressure Inferred from electronic annotation. Source: Compara positive regulation of neuron apoptotic process Inferred from electronic annotation. Source: Compara respiratory burst Traceable author statement PubMed 7938008. Source: BHF-UCL response to activity Inferred from electronic annotation. Source: Compara response to drug Inferred from electronic annotation. Source: Compara response to glucose stimulus Inferred from electronic annotation. Source: Compara response to hyperoxia Inferred from electronic annotation. Source: Compara response to laminar fluid shear stress Inferred from electronic annotation. Source: Compara response to lipopolysaccharide Inferred from electronic annotation. Source: Compara response to progesterone stimulus Inferred from electronic annotation. Source: Compara superoxide anion generation Traceable author statement PubMed 7938008. Source: BHF-UCL
Cellular_component	NADPH oxidase complex Traceable author statement PubMed 7938008. Source: BHF-UCL acrosomal vesicle Inferred from electronic annotation. Source: Compara cytosol Traceable author statement. Source: Reactome nucleolus Inferred from direct assay. Source: HPA phagolysosome Traceable author statement. Source: Reactome
Molecular_function	electron carrier activity Traceable author statement Ref.1. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RAC1	P63000	2	EBI-489611,EBI-413628

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P19878-1)

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: P19878-2)

The sequence of this isoform differs from the canonical sequence as follows:
     123-203: Missing.
     502-526: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: P19878-3)

The sequence of this isoform differs from the canonical sequence as follows:
     123-167: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 526

526

Neutrophil cytosol factor 2

PRO_0000106361

Regions

Repeat

37 – 70

34

TPR 1

Repeat

71 – 104

34

TPR 2

Repeat

121 – 154

34

TPR 3

Domain

240 – 299

60

SH3 1

Domain

351 – 429

79

OPR

Domain

457 – 516

60

SH3 2

Natural variations

Alternative sequence

123 – 203

81

Missing in isoform 2.

VSP_045259

Alternative sequence

123 – 167

45

Missing in isoform 3.

VSP_045260

Alternative sequence

502 – 526

25

Missing in isoform 2.

VSP_045261

Natural variant

19 – 21

3

Missing in CGD2.

VAR_017387

Natural variant

42

1

N → S in CGD2. Ref.24
Corresponds to variant rs137854514 [ dbSNP | Ensembl ].

VAR_065002

Natural variant

44

1

G → C in CGD2. Ref.24
Corresponds to variant rs137854510 [ dbSNP | Ensembl ].

VAR_065003

Natural variant

44

1

G → R in CGD2. Ref.20 Ref.22
Corresponds to variant rs137854510 [ dbSNP | Ensembl ].

VAR_065004

Natural variant

58

1

Missing in CGD2. Ref.24

VAR_065005

Natural variant

77

1

R → Q in CGD2. Ref.19 Ref.24
Corresponds to variant rs119103275 [ dbSNP | Ensembl ].

VAR_017388

Natural variant

78

1

G → E in CGD2. Ref.16
Corresponds to variant rs137854519 [ dbSNP | Ensembl ].

VAR_008904

Natural variant

79

1

M → V. Ref.18
Corresponds to variant rs137854512 [ dbSNP | Ensembl ].

VAR_065006

Natural variant

93

1

D → E in CGD2. Ref.23
Corresponds to variant rs137854507 [ dbSNP | Ensembl ].

VAR_065007

Natural variant

96

1

Missing in CGD2. Ref.24

VAR_065008

Natural variant

102

1

R → P in CGD2. Ref.24
Corresponds to variant rs137854515 [ dbSNP | Ensembl ].

VAR_065009

Natural variant

108

1

D → V in CGD2. Ref.22
Corresponds to variant rs137854509 [ dbSNP | Ensembl ].

VAR_065010

Natural variant

128

1

A → V in CGD2. Ref.19
Corresponds to variant rs119103274 [ dbSNP | Ensembl ].

VAR_017389

Natural variant

137

1

W → R in CGD2. Ref.24
Corresponds to variant rs137854516 [ dbSNP | Ensembl ].

VAR_065011

Natural variant

140

1

A → D in CGD2. Ref.24
Corresponds to variant rs137854520 [ dbSNP | Ensembl ].

VAR_065012

Natural variant

160 – 161

2

DK → EV in CGD2.

VAR_017390

Natural variant

169

1

Q → E in CGD2. Ref.24
Corresponds to variant rs137854517 [ dbSNP | Ensembl ].

VAR_065013

Natural variant

181

1

K → R. Ref.3 Ref.4 Ref.5 Ref.8 Ref.9 Ref.18 Ref.19
Corresponds to variant rs2274064 [ dbSNP | Ensembl ].

VAR_018477

Natural variant

184

1

R → P in CGD2. Ref.24
Corresponds to variant rs137854518 [ dbSNP | Ensembl ].

VAR_065014

Natural variant

196

1

Missing in CGD2. Ref.24

VAR_065015

Natural variant

202

1

A → V in CGD2. Ref.23
Corresponds to variant rs137854508 [ dbSNP | Ensembl ].

VAR_065016

Natural variant

279

1

T → M.
Corresponds to variant rs13306581 [ dbSNP | Ensembl ].

VAR_034129

Natural variant

297

1

V → A.
Corresponds to variant rs35937854 [ dbSNP | Ensembl ].

VAR_034130

Natural variant

328

1

R → K. Ref.3 Ref.18
Corresponds to variant rs137854511 [ dbSNP | Ensembl ].

VAR_018478

Natural variant

369

1

G → R. Ref.19
Corresponds to variant rs137854513 [ dbSNP | Ensembl ].

VAR_065017

Natural variant

389

1

H → Q. Ref.3 Ref.4 Ref.18 Ref.19
Corresponds to variant rs17849502 [ dbSNP | Ensembl ].

VAR_052620

Natural variant

395

1

R → W. Ref.18
Corresponds to variant rs13306575 [ dbSNP | Ensembl ].

VAR_008905

Natural variant

419

1

N → I in CGD2. Ref.21 Ref.24
Corresponds to variant rs35012521 [ dbSNP | Ensembl ].

VAR_052621

Secondary structure

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526

Helix Strand Turn

Details...

Helix

3 – 18

16

Helix

22 – 30

9

Beta strand

32 – 34

3

Helix

37 – 49

13

Helix

53 – 66

14

Helix

71 – 83

13

Helix

87 – 99

13

Turn

100 – 103

4

Beta strand

105 – 108

4

Helix

110 – 112

3

Beta strand

117 – 119

3

Helix

120 – 133

14

Helix

137 – 148

12

Helix

154 – 157

4

Helix

158 – 167

10

Helix

187 – 191

5

Beta strand

243 – 247

5

Beta strand

255 – 258

4

Beta strand

266 – 269

4

Beta strand

274 – 276

3

Beta strand

278 – 282

5

Beta strand

285 – 289

5

Beta strand

294 – 296

3

Beta strand

352 – 366

15

Helix

372 – 382

11

Helix

387 – 389

3

Beta strand

392 – 394

3

Turn

407 – 409

3

Helix

410 – 414

5

Beta strand

421 – 426

6

Beta strand

460 – 463

4

Beta strand

472 – 475

4

Beta strand

483 – 493

11

Beta strand

495 – 498

4

Beta strand

503 – 506

4

Helix

508 – 510

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 1, 1996. Version 2. Checksum: EC136766E1915376	FASTA	526	59,762
	10 20 30 40 50 60 MSLVEAISLW NEGVLAADKK DWKGALDAFS AVQDPHSRIC FNIGCMYTIL KNMTEAEKAF 70 80 90 100 110 120 TRSINRDKHL AVAYFQRGML YYQTEKYDLA IKDLKEALIQ LRGNQLIDYK ILGLQFKLFA 130 140 150 160 170 180 CEVLYNIAFM YAKKEEWKKA EEQLALATSM KSEPRHSKID KAMECVWKQK LYEPVVIPVG 190 200 210 220 230 240 KLFRPNERQV AQLAKKDYLG KATVVASVVD QDSFSGFAPL QPQAAEPPPR PKTPEIFRAL 250 260 270 280 290 300 EGEAHRVLFG FVPETKEELQ VMPGNIVFVL KKGNDNWATV MFNGQKGLVP CNYLEPVELR 310 320 330 340 350 360 IHPQQQPQEE SSPQSDIPAP PSSKAPGRPQ LSPGQKQKEE PKEVKLSVPM PYTLKVHYKY 370 380 390 400 410 420 TVVMKTQPGL PYSQVRDMVS KKLELRLEHT KLSYRPRDSN ELVPLSEDSM KDAWGQVKNY 430 440 450 460 470 480 CLTLWCENTV GDQGFPDEPK ESEKADANNQ TTEPQLKKGS QVEALFSYEA TQPEDLEFQE 490 500 510 520 GDIILVLSKV NEEWLEGECK GKVGIFPKVF VEDCATTDLE STRREV
	Isoform 2 [UniParc]. Checksum: D45BFF944F0CE53C	FASTA	420	47,515
	10 20 30 40 50 60 MSLVEAISLW NEGVLAADKK DWKGALDAFS AVQDPHSRIC FNIGCMYTIL KNMTEAEKAF 70 80 90 100 110 120 TRSINRDKHL AVAYFQRGML YYQTEKYDLA IKDLKEALIQ LRGNQLIDYK ILGLQFKLFA 130 140 150 160 170 180 CEVVASVVDQ DSFSGFAPLQ PQAAEPPPRP KTPEIFRALE GEAHRVLFGF VPETKEELQV 190 200 210 220 230 240 MPGNIVFVLK KGNDNWATVM FNGQKGLVPC NYLEPVELRI HPQQQPQEES SPQSDIPAPP 250 260 270 280 290 300 SSKAPGRPQL SPGQKQKEEP KEVKLSVPMP YTLKVHYKYT VVMKTQPGLP YSQVRDMVSK 310 320 330 340 350 360 KLELRLEHTK LSYRPRDSNE LVPLSEDSMK DAWGQVKNYC LTLWCENTVG DQGFPDEPKE 370 380 390 400 410 420 SEKADANNQT TEPQLKKGSQ VEALFSYEAT QPEDLEFQEG DIILVLSKVN EEWLEGECKG
	Isoform 3 [UniParc]. Checksum: 4A15D34EA01887D6	FASTA	481	54,446
	10 20 30 40 50 60 MSLVEAISLW NEGVLAADKK DWKGALDAFS AVQDPHSRIC FNIGCMYTIL KNMTEAEKAF 70 80 90 100 110 120 TRSINRDKHL AVAYFQRGML YYQTEKYDLA IKDLKEALIQ LRGNQLIDYK ILGLQFKLFA 130 140 150 160 170 180 CEKQKLYEPV VIPVGKLFRP NERQVAQLAK KDYLGKATVV ASVVDQDSFS GFAPLQPQAA 190 200 210 220 230 240 EPPPRPKTPE IFRALEGEAH RVLFGFVPET KEELQVMPGN IVFVLKKGND NWATVMFNGQ 250 260 270 280 290 300 KGLVPCNYLE PVELRIHPQQ QPQEESSPQS DIPAPPSSKA PGRPQLSPGQ KQKEEPKEVK 310 320 330 340 350 360 LSVPMPYTLK VHYKYTVVMK TQPGLPYSQV RDMVSKKLEL RLEHTKLSYR PRDSNELVPL 370 380 390 400 410 420 SEDSMKDAWG QVKNYCLTLW CENTVGDQGF PDEPKESEKA DANNQTTEPQ LKKGSQVEAL 430 440 450 460 470 480 FSYEATQPED LEFQEGDIIL VLSKVNEEWL EGECKGKVGI FPKVFVEDCA TTDLESTRRE V

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of a 67-kD neutrophil oxidase factor with similarity to a noncatalytic region of p60c-src." Leto T.L., Lomax K.J., Volpp B.D., Nunoi H., Sechler J.M.G., Nauseef W.M., Clark R.A., Gallin J.I., Malech H.L. Science 248:727-730(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Characterization of the p67phox gene: genomic organization and restriction fragment length polymorphism analysis for prenatal diagnosis in chronic granulomatous disease." Kenney R.T., Malech H.L., Epstein N.D., Roberts R.L., Leto T.L. Blood 82:3739-3744(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Expression of a p67(phox) homolog in Caco-2 cells giving O(2)(-)-reconstituting ability to cytochrome b(558) together with recombinant p47(phox)." Yoshida L.S., Nishida S., Shimoyama T., Kawahara T., Rokutan K., Tsunawaki S. Biochem. Biophys. Res. Commun. 296:1322-1328(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ARG-181; LYS-328 AND GLN-389. Tissue: Colon adenocarcinoma.
[4]	"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 1), VARIANTS ARG-181 AND GLN-389.
[5]	"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] (ISOFORMS 1; 2 AND 3), VARIANT ARG-181. Tissue: Umbilical cord blood.
[6]	NHLBI resequencing and genotyping service (RS&G) Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ARG-181.
[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 1), VARIANT ARG-181. Tissue: Lymphoma.
[10]	"JFC1, a novel tandem C2 domain-containing protein associated with the leukocyte NADPH oxidase." McAdara Berkowitz J.K., Catz S.D., Johnson J.L., Ruedi J.M., Thon V., Babior B.M. J. Biol. Chem. 276:18855-18862(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SYTL1.
[11]	"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 NOXO1.
[12]	"The arachidonic acid-binding protein S100A8/A9 promotes NADPH oxidase activation by interaction with p67phox and Rac-2." Kerkhoff C., Nacken W., Benedyk M., Dagher M.C., Sopalla C., Doussiere J. FASEB J. 19:467-469(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH S100A8 AND CALPROTECTIN.
[13]	"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: INTERACTION WITH NCF4, DOMAIN OPR/PB1.
[14]	"Structure of the TPR domain of p67phox in complex with Rac.GTP." Lapouge K., Smith S.J., Walker P.A., Gamblin S.J., Smerdon S.J., Rittinger K. Mol. Cell 6:899-907(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-203 IN COMPLEX WITH RAC1.
[15]	"Solution structure of the 1st SH3 domain from human neutrophil cytosol factor 2 (NCF-2)." RIKEN structural genomics initiative (RSGI) Submitted (MAY-2006) to the PDB data bank Cited for: STRUCTURE BY NMR OF 242-297.
[16]	"Autosomal recessive chronic granulomatous disease with absence of the 67-kD cytosolic NADPH oxidase component: identification of mutation and detection of carriers." de Boer M., Hilarius-Stokman P.M., Hossle J.P., Verhoeven A.J., Graf N., Kenney R.T., Seger R., Roos D. Blood 83:531-536(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CGD2 GLU-78.
[17]	"Identification of a double mutation (D160V-K161E) (sic) in the p67phox gene of a chronic granulomatous disease patient." Bonizzato A., Russo M.P., Donini M., Dusi S. Biochem. Biophys. Res. Commun. 231:861-863(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CGD2 160-GLU-VAL-161.
[18]	"Molecular characterization of autosomal recessive chronic granulomatous disease caused by a defect of the nicotinamide adenine dinucleotide phosphate (reduced form) oxidase component p67-phox." Patino P.J., Rae J., Noack D., Erickson R., Ding J., Garcia de Olarte D., Curnutte J.T. Blood 94:2505-2514(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CGD2 19-LYS--ASP-21 DEL, VARIANTS VAL-79; ARG-181; LYS-328; GLN-389 AND TRP-395.
[19]	"Autosomal recessive chronic granulomatous disease caused by novel mutations in NCF-2, the gene encoding the p67-phox component of phagocyte NADPH oxidase." Noack D., Rae J., Cross A.R., Munoz J., Salmen S., Mendoza J.A., Rossi N., Curnutte J.T., Heyworth P.G. Hum. Genet. 105:460-467(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CGD2 GLN-77 AND VAL-128, VARIANTS ARG-181; ARG-369 AND GLN-389.
[20]	"Hematologically important mutations: the autosomal recessive forms of chronic granulomatous disease (first update)." Cross A.R., Noack D., Rae J., Curnutte J.T., Heyworth P.G. Blood Cells Mol. Dis. 26:561-565(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CGD2 ARG-44.
[21]	"Genetic and mutational heterogeneity of autosomal recessive chronic granulomatous disease in Tunisia." El Kares R., Barbouche M.R., Elloumi-Zghal H., Bejaoui M., Chemli J., Mellouli F., Tebib N., Abdelmoula M.S., Boukthir S., Fitouri Z., M'Rad S., Bouslama K., Touiri H., Abdelhak S., Dellagi M.K. J. Hum. Genet. 51:887-895(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CGD2 ILE-419.
[22]	"Focus on FOCIS: the continuing diagnostic challenge of autosomal recessive chronic granulomatous disease." Yu G., Hong D.K., Dionis K.Y., Rae J., Heyworth P.G., Curnutte J.T., Lewis D.B. Clin. Immunol. 128:117-126(2008) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CGD2 ARG-44 AND VAL-108.
[23]	"Four different NCF2 mutations in six families from Turkey and an overview of NCF2 gene mutations." Koker M.Y., Sanal O., van Leeuwen K., de Boer M., Metin A., Patiroglu T., Ozgur T.T., Tezcan I., Roos D. Eur. J. Clin. Invest. 39:942-951(2009) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CGD2 GLU-93 AND VAL-202.
[24]	"Hematologically important mutations: the autosomal recessive forms of chronic granulomatous disease (second update)." Roos D., Kuhns D.B., Maddalena A., Bustamante J., Kannengiesser C., de Boer M., van Leeuwen K., Koker M.Y., Wolach B., Roesler J., Malech H.L., Holland S.M., Gallin J.I., Stasia M.J. Blood Cells Mol. Dis. 44:291-299(2010) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CGD2 SER-42; CYS-44; LYS-58 DEL; GLN-77; GLU-96 DEL; PRO-102; ARG-137; ASP-140; GLU-169; PRO-184; LYS-196 DEL AND ILE-419.
+	Additional computationally mapped references.

Web resources

NCF2base

NCF2 deficiency database

GeneReviews

Mendelian genes neutrophil cytosolic factor 2 (NCF2)

Leiden Open Variation Database (LOVD)

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M32011 mRNA. Translation: AAA36379.1.
U00788 , U00776, U00777, U00778, U00779, U00780, U00781, U00782, U00783, U00784, U00785, U00786, U00787 Genomic DNA. Translation: AAB60320.1.
AF527950 mRNA. Translation: AAM89263.1.
BT007439 mRNA. Translation: AAP36107.1.
AK296672 mRNA. Translation: BAG59269.1.
AK298713 mRNA. Translation: BAG60869.1.
AK312666 mRNA. Translation: BAG35548.1.
DQ314879 Genomic DNA. Translation: ABC40738.1.
AL137800 Genomic DNA. Translation: CAC19686.1.
CH471067 Genomic DNA. Translation: EAW91160.1.
BC001606 mRNA. Translation: AAH01606.1.

IPI

IPI00021070.
IPI00641875.
IPI00910100.

PIR

A34855.

RefSeq

NP_000424.2. NM_000433.3.
NP_001121123.1. NM_001127651.2.
NP_001177718.1. NM_001190789.1.
NP_001177723.1. NM_001190794.1.

UniGene

Hs.587558.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1E96	X-ray	2.40	B	1-203	[»]
1HH8	X-ray	1.80	A	1-213	[»]
1K4U	NMR	-	S	455-516	[»]
1OEY	X-ray	2.00	A/B/C/D	352-429	[»]
1WM5	X-ray	1.95	A	1-203	[»]
2DMO	NMR	-	A	243-297	[»]

ProteinModelPortal

P19878.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-76N.

IntAct

P19878. 6 interactions.

MINT

MINT-151560.

STRING

9606.ENSP00000356505.

PTM databases

PhosphoSite

P19878.

Polymorphism databases

DMDM

1346669.

Proteomic databases

PaxDb

P19878.

PRIDE

P19878.

Protocols and materials databases

DNASU

4688.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000367535; ENSP00000356505; ENSG00000116701.
ENST00000367536; ENSP00000356506; ENSG00000116701.
ENST00000413720; ENSP00000399294; ENSG00000116701.

GeneID

4688.

KEGG

hsa:4688.

UCSC

uc001gqj.4. human.

Organism-specific databases

CTD

4688.

GeneCards

GC01M183524.

HGNC

HGNC:7661. NCF2.

HPA

CAB022160.
HPA002327.
HPA006040.

MIM

233710. phenotype.
608515. gene.

neXtProt

NX_P19878.

Orphanet

379. Chronic granulomatous disease.

PharmGKB

PA31464.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG248396.

HOGENOM

HOG000237312.

HOVERGEN

HBG001521.

KO

K08010.

PhylomeDB

P19878.

Enzyme and pathway databases

Reactome

REACT_116125. Disease.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P19878.

Bgee

P19878.

CleanEx

HS_NCF2.

Genevestigator

P19878.

GermOnline

ENSG00000116701. Homo sapiens.

Family and domain databases

Gene3D

1.25.40.10. 1 hit.

InterPro

IPR000270. OPR_PB1.
IPR000108. p67phox.
IPR001452. SH3_domain.
IPR001440. TPR-1.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR019734. TPR_repeat.
[Graphical view]

Pfam

PF00564. PB1. 1 hit.
PF00018. SH3_1. 2 hits.
PF00515. TPR_1. 2 hits.
[Graphical view]

PRINTS

PR00499. P67PHOX.
PR00452. SH3DOMAIN.

SMART

SM00666. PB1. 1 hit.
SM00326. SH3. 2 hits.
SM00028. TPR. 3 hits.
[Graphical view]

SUPFAM

SSF50044. SH3. 2 hits.

PROSITE

PS50002. SH3. 2 hits.
PS50005. TPR. 3 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

NCF2. human.

EvolutionaryTrace

P19878.

GenomeRNAi

4688.

NextBio

18076.

SOURCE

Search...

Entry information

Entry name

NCF2_HUMAN

Accession

Primary (citable) accession number: P19878
Secondary accession number(s): B2R6Q1 , B4DKQ7, B4DQA7, E9PHJ2, E9PHX3, Q2PP06, Q8NFC7, Q9BV51

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	February 1, 1996
Last modified:	May 1, 2013
This is version 154 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.