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P19878 (NCF2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 167. 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·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length526 AA.
Sequence statusComplete.
Protein existenceEvidence 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). Ref.3

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. Interacts with NCF4. Interacts (via the C-terminal SH3 domain) with NCF1 (via C-terminus). Interacts with SYTL1 and RAC1. May interact with NOXO1. Interacts with S100A8 and calprotectin (S100A8/9). Ref.3 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.16

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.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26

Sequence similarities

Belongs to the NCF2/NOXA1 family.

Contains 1 OPR domain.

Contains 2 SH3 domains.

Contains 3 TPR repeats.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseChronic granulomatous disease
Disease mutation
   DomainRepeat
SH3 domain
TPR repeat
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaging

Inferred from electronic annotation. Source: Ensembl

antigen 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

cellular defense response

Traceable author statement Ref.1. Source: ProtInc

cellular response to hormone stimulus

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

positive regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

respiratory burst

Traceable author statement PubMed 7938008. Source: BHF-UCL

response to activity

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to glucose

Inferred from electronic annotation. Source: Ensembl

response to hyperoxia

Inferred from electronic annotation. Source: Ensembl

response to laminar fluid shear stress

Inferred from electronic annotation. Source: Ensembl

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

response to progesterone

Inferred from electronic annotation. Source: Ensembl

superoxide anion generation

Traceable author statement PubMed 7938008. Source: BHF-UCL

superoxide metabolic process

Traceable author statement PubMed 7938008. Source: BHF-UCL

   Cellular_componentNADPH oxidase complex

Traceable author statement PubMed 7938008. Source: BHF-UCL

acrosomal vesicle

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

nucleolus

Inferred from direct assay. Source: HPA

phagolysosome

Traceable author statement. Source: Reactome

   Molecular_functionelectron carrier activity

Traceable author statement Ref.1. Source: UniProtKB

protein C-terminus binding

Inferred from physical interaction PubMed 9365277. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 11483497Ref.16PubMed 15657040PubMed 16297854PubMed 16782902PubMed 19129478. Source: IntAct

Complete GO annotation...

Alternative products

This entry describes 4 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.
Isoform 4 (identifier: P19878-4)

The sequence of this isoform differs from the canonical sequence as follows:
     123-203: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 526526Neutrophil cytosol factor 2
PRO_0000106361

Regions

Repeat37 – 7034TPR 1
Repeat71 – 10434TPR 2
Repeat121 – 15434TPR 3
Domain240 – 29960SH3 1
Domain351 – 42979OPR
Domain457 – 51660SH3 2

Natural variations

Alternative sequence123 – 20381Missing in isoform 2 and isoform 4.
VSP_045259
Alternative sequence123 – 16745Missing in isoform 3.
VSP_045260
Alternative sequence502 – 52625Missing in isoform 2.
VSP_045261
Natural variant19 – 213Missing in CGD2.
VAR_017387
Natural variant421N → S in CGD2. Ref.26
Corresponds to variant rs137854514 [ dbSNP | Ensembl ].
VAR_065002
Natural variant441G → C in CGD2. Ref.26
Corresponds to variant rs137854510 [ dbSNP | Ensembl ].
VAR_065003
Natural variant441G → R in CGD2. Ref.22 Ref.24
Corresponds to variant rs137854510 [ dbSNP | Ensembl ].
VAR_065004
Natural variant581Missing in CGD2. Ref.26
VAR_065005
Natural variant771R → Q in CGD2. Ref.21 Ref.26
Corresponds to variant rs119103275 [ dbSNP | Ensembl ].
VAR_017388
Natural variant781G → E in CGD2. Ref.18
Corresponds to variant rs137854519 [ dbSNP | Ensembl ].
VAR_008904
Natural variant791M → V. Ref.20
Corresponds to variant rs137854512 [ dbSNP | Ensembl ].
VAR_065006
Natural variant931D → E in CGD2. Ref.25
Corresponds to variant rs137854507 [ dbSNP | Ensembl ].
VAR_065007
Natural variant961Missing in CGD2. Ref.26
VAR_065008
Natural variant1021R → P in CGD2. Ref.26
Corresponds to variant rs137854515 [ dbSNP | Ensembl ].
VAR_065009
Natural variant1081D → V in CGD2. Ref.24
Corresponds to variant rs137854509 [ dbSNP | Ensembl ].
VAR_065010
Natural variant1281A → V in CGD2. Ref.21
Corresponds to variant rs119103274 [ dbSNP | Ensembl ].
VAR_017389
Natural variant1371W → R in CGD2. Ref.26
Corresponds to variant rs137854516 [ dbSNP | Ensembl ].
VAR_065011
Natural variant1401A → D in CGD2. Ref.26
Corresponds to variant rs137854520 [ dbSNP | Ensembl ].
VAR_065012
Natural variant160 – 1612DK → EV in CGD2.
VAR_017390
Natural variant1691Q → E in CGD2. Ref.26
Corresponds to variant rs137854517 [ dbSNP | Ensembl ].
VAR_065013
Natural variant1811K → R. Ref.3 Ref.4 Ref.5 Ref.8 Ref.9 Ref.20 Ref.21
Corresponds to variant rs2274064 [ dbSNP | Ensembl ].
VAR_018477
Natural variant1841R → P in CGD2. Ref.26
Corresponds to variant rs137854518 [ dbSNP | Ensembl ].
VAR_065014
Natural variant1961Missing in CGD2. Ref.26
VAR_065015
Natural variant2021A → V in CGD2. Ref.25
Corresponds to variant rs137854508 [ dbSNP | Ensembl ].
VAR_065016
Natural variant2791T → M.
Corresponds to variant rs13306581 [ dbSNP | Ensembl ].
VAR_034129
Natural variant2971V → A.
Corresponds to variant rs35937854 [ dbSNP | Ensembl ].
VAR_034130
Natural variant3281R → K. Ref.3 Ref.20
Corresponds to variant rs137854511 [ dbSNP | Ensembl ].
VAR_018478
Natural variant3691G → R. Ref.21
Corresponds to variant rs137854513 [ dbSNP | Ensembl ].
VAR_065017
Natural variant3891H → Q. Ref.3 Ref.4 Ref.20 Ref.21
Corresponds to variant rs17849502 [ dbSNP | Ensembl ].
VAR_052620
Natural variant3951R → W Impairs interaction with NCF4. Ref.16 Ref.20
Corresponds to variant rs13306575 [ dbSNP | Ensembl ].
VAR_008905
Natural variant4191N → I in CGD2. Ref.23 Ref.26
Corresponds to variant rs35012521 [ dbSNP | Ensembl ].
VAR_052621

Secondary structure

..................................................................... 526
Helix Strand Turn

Details...

Sequences

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

Last modified February 1, 1996. Version 2.
Checksum: EC136766E1915376

FASTA52659,762
        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 

« Hide

Isoform 2 [UniParc].

Checksum: D45BFF944F0CE53C
Show »

FASTA42047,515
Isoform 3 [UniParc].

Checksum: 4A15D34EA01887D6
Show »

FASTA48154,446
Isoform 4 [UniParc].

Checksum: 88E274CACEDFFBC7
Show »

FASTA44550,337

References

« Hide '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), FUNCTION, SUBUNIT, 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. 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] (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. expand/collapse author list , 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. expand/collapse author list , 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]"Diverse recognition of non-PxxP peptide ligands by the SH3 domains from p67(phox), Grb2 and Pex13p."
Kami K., Takeya R., Sumimoto H., Kohda D.
EMBO J. 21:4268-4276(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 455-516 IN COMPLEX WITH NCF1, INTERACTION WITH NCF1.
[16]"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 352-429 IN COMPLEX WITH NCF4, SUBUNIT, CHARACTERIZATION OF VARIANT TRP-395, INTERACTION WITH NCF4.
[17]"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.
[18]"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.
[19]"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.
[20]"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.
[21]"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.
[22]"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.
[23]"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.
[24]"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.
[25]"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.
[26]"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

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 expand/collapse EMBL AC list , 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.
CCDSCCDS1356.1. [P19878-1]
CCDS53446.1. [P19878-4]
CCDS53447.1. [P19878-3]
PIRA34855.
RefSeqNP_000424.2. NM_000433.3. [P19878-1]
NP_001121123.1. NM_001127651.2. [P19878-1]
NP_001177718.1. NM_001190789.1. [P19878-4]
NP_001177723.1. NM_001190794.1. [P19878-3]
UniGeneHs.587558.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1E96X-ray2.40B1-203[»]
1HH8X-ray1.80A1-213[»]
1K4UNMR-S455-516[»]
1OEYX-ray2.00A/B/C/D352-429[»]
1WM5X-ray1.95A1-203[»]
2DMONMR-A243-297[»]
ProteinModelPortalP19878.
SMRP19878. Positions 2-185, 242-297, 352-428, 455-516.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110768. 16 interactions.
DIPDIP-76N.
IntActP19878. 8 interactions.
MINTMINT-151560.
STRING9606.ENSP00000356505.

PTM databases

PhosphoSiteP19878.

Polymorphism databases

DMDM1346669.

Proteomic databases

MaxQBP19878.
PaxDbP19878.
PRIDEP19878.

Protocols and materials databases

DNASU4688.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000367535; ENSP00000356505; ENSG00000116701. [P19878-1]
ENST00000367536; ENSP00000356506; ENSG00000116701. [P19878-1]
ENST00000413720; ENSP00000399294; ENSG00000116701. [P19878-3]
ENST00000418089; ENSP00000407217; ENSG00000116701. [P19878-4]
GeneID4688.
KEGGhsa:4688.
UCSCuc001gqj.4. human. [P19878-1]

Organism-specific databases

CTD4688.
GeneCardsGC01M183524.
GeneReviewsNCF2.
HGNCHGNC:7661. NCF2.
HPACAB022160.
HPA002327.
HPA006040.
MIM233710. phenotype.
608515. gene.
neXtProtNX_P19878.
Orphanet379. Chronic granulomatous disease.
PharmGKBPA31464.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG248396.
HOGENOMHOG000237312.
HOVERGENHBG001521.
KOK08010.
OMAYSQVRDM.
OrthoDBEOG7G1V62.
PhylomeDBP19878.
TreeFamTF329087.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressP19878.
BgeeP19878.
CleanExHS_NCF2.
GenevestigatorP19878.

Family and domain databases

Gene3D1.25.40.10. 1 hit.
InterProIPR000270. OPR_PB1.
IPR001452. SH3_domain.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
[Graphical view]
PfamPF00564. PB1. 1 hit.
PF00018. SH3_1. 2 hits.
PF00515. TPR_1. 2 hits.
[Graphical view]
PRINTSPR00452. SH3DOMAIN.
SMARTSM00666. PB1. 1 hit.
SM00326. SH3. 2 hits.
SM00028. TPR. 3 hits.
[Graphical view]
SUPFAMSSF50044. SSF50044. 2 hits.
PROSITEPS50002. SH3. 2 hits.
PS50005. TPR. 3 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNCF2. human.
EvolutionaryTraceP19878.
GeneWikiNeutrophil_cytosolic_factor_2.
GenomeRNAi4688.
NextBio18076.
PROP19878.
SOURCESearch...

Entry information

Entry nameNCF2_HUMAN
AccessionPrimary (citable) accession number: P19878
Secondary accession number(s): B2R6Q1 expand/collapse secondary AC list , 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: July 9, 2014
This is version 167 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 1

Human chromosome 1: entries, gene names and cross-references to MIM