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p47phox (human)

Overview p47phox the 47-kilodalton cytosolic subunit of the multi-protein complex known as NADPH oxidase found in neutrophils. The holo-oxidase produces a burst of superoxide which is delivered to the lumen of the neutrophil phagosome. Contains 2 SH2 domains. Mutations in NCF1, as well as in other NADPH oxidase subunits, can result in chronic granulomatous disease. Note: This description may include information from UniProtKB. Protein type: EC 1.-.-.-; Oxidoreductase Cellular Component: cytosol; NADPH oxidase complex Molecular Function: GTPase activity; protein binding; electron carrier activity; GTP binding; superoxide-generating NADPH oxidase activity; SH3 domain binding; phosphoinositide binding Biological Process: respiratory burst; respiratory burst during defense response; interaction with host; superoxide metabolic process; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; leukotriene metabolic process; cell proliferation; antigen processing and presentation of peptide antigen via MHC class I; GTP catabolic process; negative regulation of smooth muscle contraction; antigen processing and presentation of exogenous peptide antigen via MHC class I; cellular defense response; innate immune response; cell communication; response to yeast; protein targeting to membrane; inflammatory response; superoxide release; hydrogen peroxide biosynthetic process Reference #:  P14598 (UniProtKB) Alt. Names/Synonyms: 47 kDa autosomal chronic granulomatous disease protein; 47 kDa neutrophil oxidase factor; FLJ79451; NADPH oxidase organizer 2; NCF-1; NCF-47K; NCF1; NCF1A; Neutrophil cytosol factor 1; neutrophil cytosolic factor 1; Neutrophil NADPH oxidase factor 1; Nox organizer 2; Nox-organizing protein 2; NOXO2; p47-phox; p47phox; SH3 and PX domain-containing protein 1A; SH3PXD1A Gene Symbols: NCF1 Molecular weight: 44,652 Da Basal Isoelectric point: 9.2  Predict pI for various phosphorylation states Protein-Specific Antibodies or siRNAs from Cell Signaling Technology®

Select Structure to View Below p47phox 1GD5 - A=1-128 (human) 1K4U - P=359-390 (human) 1KQ6 - A=1-141 (human) 1NG2 - A=156-340 (human) 1O7K - A/B/C=1-123 (human) 1OV3 - A/B=156-285 (human) 1UEC - A=149-340 (human) 1W70 - C/D=359-372 (human) 1WLP - B=151-286 (human)

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB 1GD5 1K4U 1KQ6 1NG2 1O7K 1OV3 1UEC 1W70 1WLP  |  Phospho3D  |  DISEASE 233700 608512  |  Source  |  InnateDB  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene

	Sites Implicated In
activation: S303‑p, S304‑p, S345‑p, S359‑p, S370‑p enzymatic activity, induced: S303‑p, S304‑p, S328‑p, S359‑p, S370‑p intracellular localization: S304‑p, S359‑p, S370‑p, S379‑p molecular association, regulation: S303‑p, S304‑p, S315‑p, S320‑p, S328‑p, S359‑p, S370‑p, S379‑p phosphorylation: S359‑p, S370‑p

	Modification Sites and Domains

	Modification Sites in Parent Protein, Orthologs, and Isoforms

SS  SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.	MS  MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.			human
0	3		Y41-p	DLSEKVVyRRFtEIy
0	1		T45-p	KVVyRRFtEIyEFHK
0	13		Y48-p	yRRFtEIyEFHKTLK
0	1		T133-p	KLPTDNQtKKPEtyL
1	0		T138-p	NQtKKPEtyLMPKDG
0	1		Y139-p	QtKKPEtyLMPKDGK
1	0		T153-p	KSTATDItGPIILQT
1	0		S208-p	KRGWIPAsFLEPLDS
1	0		Y279-p	TGYFPSMyLQKsGQD
1	0		S283-p	PSMyLQKsGQDVsQA
0	1		S288-p	QKsGQDVsQAQRQIK
5	0		S303-p	RGAPPRRssIRNAHs
8	0		S304-p	GAPPRRssIRNAHsI
1	0		S310-p	ssIRNAHsIHQRsRK
6	0		S315-p	AHsIHQRsRKRLsQD
7	13		S320-p	QRsRKRLsQDAYRRN
9	0		S328-p	QDAYRRNsVRFLQQR
8	4		S345-p	QARPGPQsPGsPLEE
7	4		S348-p	PGPQsPGsPLEEERQ
0	1		T356-p	PLEEERQtQRsKPQP
8	0		S359-p	EERQtQRsKPQPAVP
8	0		S370-p	PAVPPRPsADLILNR
7	0		S379-p	DLILNRCsESTKRKL

	mouse
Y41	DLSEKVVYRKFTEIY
T45	KVVYRKFTEIYEFHK
Y48	YRKFTEIYEFHKMLK
A133	KLPTDSQAKKPETYL
T138	SQAKKPETYLVPKDG
Y139	QAKKPETYLVPKDGK
T153	KNNVADITGPIILQT
S208	KRGWVPASYLEPLDS
Y279	TGYFPSMYLQKAGEE
A283	PSMYLQKAGEEITQA
T288	QKAGEEITQAQRQIR
S304	RGAPPRRSTIRNAQS
T305	GAPPRRSTIRNAQSI
S311	STIRNAQSIHQRSRK
S316	AQSIHQRSRKRLsQD
S321-p	QRSRKRLsQDTYRRN
S329	QDTYRRNSVRFLQQR
S346	PGRPGPLSTDGTKDN
G349	PGPLSTDGTKDNPST
T356	GTKDNPSTPRVKPQP
V359	DNPSTPRVKPQPAVP
S370	PAVPPRPSSDLILHR
T379	DLILHRCTESTKRKL

	rat
Y41	DLSEKVVYRKFTEIY
T45	KVVYRKFTEIYEFHK
Y48	YRKFTEIYEFHKMLK
V133	KLPNDSQVKKPETYL
T138	SQVKKPETYLTAKDG
Y139	QVKKPETYLTAKDGK
M153	KNNVADIMGPIILQT
S208	KRGWVPASYLEPLDS
Y279	TGYFPSMYLQKAGEE
A283	PSMYLQKAGEEITQA
T288	QKAGEEITQAQRQIR
S304	RGAPPRRSTIRNAQS
T305	GAPPRRSTIRNAQSI
S311	STIRNAQSIHQRSRK
S316	AQSIHQRSRKRLSQD
S321	QRSRKRLSQDTYRRN
S329	QDTYRRNSVRFLQQR
S346	PARPGPQSPDSKDNP
S349	PGPQSPDSKDNPSTP
T355	DSKDNPSTPRAKPQP
A358	DNPSTPRAKPQPAVP
S369	PAVPPRPSSDLILHR
T378	DLILHRCTESTKRKL

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