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NQO1 (human)

Overview NQO1 The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinons involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis. Homodimer. By dioxin. Inhibited by dicoumarol. Belongs to the NAD(P)H dehydrogenase (quinone) family. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB. Protein type: Oxidoreductase; EC 1.6.5.2 Cellular Component: cytoplasm; cytosol Molecular Function: protein binding; NAD(P)H dehydrogenase (quinone) activity; cytochrome-b5 reductase activity Biological Process: xenobiotic metabolic process; positive regulation of neuron apoptosis; response to toxin; negative regulation of catalytic activity; response to oxidative stress; nitric oxide biosynthetic process; regulation of amino acid metabolic process; synaptic transmission, cholinergic Reference #:  P15559 (UniProtKB) Alt. Names/Synonyms: Azoreductase; DHQU; DIA4; diaphorase (NADH/NADPH) (cytochrome b-5 reductase); diaphorase-4; dioxin-inducible 1; DT-diaphorase; DTD; Menadione reductase; NAD(P)H dehydrogenase [quinone] 1; NAD(P)H dehydrogenase, quinone 1; NAD(P)H:menadione oxidoreductase 1; NAD(P)H:Quinone acceptor oxidoreductase type 1; NAD(P)H:quinone oxidoreductase 1; NAD(P)H:quinone oxireductase; NMOR1; NMORI; NQO1; Phylloquinone reductase; QR1; Quinone reductase 1 Gene Symbols: NQO1 Molecular weight: 30,868 Da Basal Isoelectric point: 8.91  Predict pI for various phosphorylation states Protein-Specific Antibodies or siRNAs from Cell Signaling Technology®

Select Structure to View Below NQO1 1D4A - A/B/C/D=2-274 (human) 1DXO - A/B/C/D=2-274 (human) 1GG5 - A/B/C/D=2-274 (human) 1H66 - A/B/C/D=3-274 (human) 1H69 - A/B/C/D=3-274 (human) 1KBO - A/B/C/D=2-274 (human) 1KBQ - A/B/C/D=2-274 (human) 1QBG - A/B/C/D=4-274 (human) 2F1O - A/B/C/D/E/F/G/H=2-274 (human) 3JSX - F/A/E/B/H/C/D/G=2-274 (human) 1DXQ - A/B/C/D=1-274 (mouse) 1QRD - A/B=1-273 (rat)

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB 1D4A 1DXO 1GG5 1H66 1H69 1KBO 1KBQ 1QBG 2F1O 3JSX  |  ENZYME  |  Phospho3D  |  DISEASE  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene

	Modification Sites and Domains	Show Modification Legend
Click here to view phosphorylation modifications only

	Modification Sites in Parent Protein, Orthologs, and Isoforms	Show Modification Legend

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 ► Hide Isoforms
0	16		Y20-p	SERTSFNyAMkEAAA
0	1		K23-u	TSFNyAMkEAAAAAL
0	1		K31-a	EAAAAALkKkGWEVV
0	3		K31-u	EAAAAALkKkGWEVV
0	2		K33-u	AAAALkKkGWEVVEs
0	1		S40-p	kGWEVVEsDLyAMNF
0	1		Y43-p	EVVEsDLyAMNFNPI
0	1		K54-u	FNPIISRkDITGkLk
0	1		K59-a	SRkDITGkLkDPANF
0	2		K59-u	SRkDITGkLkDPANF
0	3		K61-u	kDITGkLkDPANFQy
0	2		Y68-p	kDPANFQyPAESVLA
0	1		Y76-p	PAESVLAykEGHLsP
0	4		K77-a	AESVLAykEGHLsPD
0	2		K77-u	AESVLAykEGHLsPD
0	1		S82-p	AykEGHLsPDIVAEQ
0	3		K90-u	PDIVAEQkkLEAADL
0	2		K91-u	DIVAEQkkLEAADLV
0	1		Y127-p	VFIGEFAyTyAAMyD
0	1		Y129-p	IGEFAyTyAAMyDKG
0	1		Y133-p	AyTyAAMyDKGPFRS
0	1		K141	DKGPFRSKKAVLSIT
0	11		K209-a	IQILEGWkkRLENIW
0	3		K209-u	IQILEGWkkRLENIW
0	1		K210-a	QILEGWkkRLENIWD
0	3		K210-u	QILEGWkkRLENIWD
0	1		K241-u	QAGFLMKkEVQDEEk
0	1		K248-u	kEVQDEEkNKkFGLS
0	1		K251-u	QDEEkNKkFGLSVGH
0	1		K262-a	SVGHHLGkSIPTDNQ
0	1		K262-u	SVGHHLGkSIPTDNQ
0	3		K271-u	IPTDNQIkARK____

	NQO1 iso3
Y20	SERTSFNYAMKEAAA
K23	TSFNYAMKEAAAAAL
K31	EAAAAALKKKGWEVV
K31	EAAAAALKKKGWEVV
K33	AAAALKKKGWEVVES
S40	KGWEVVESDLYAMNF
Y43	EVVESDLYAMNFNPI
K54	FNPIISRKDITGKLK
K59	SRKDITGKLKDPANF
K59	SRKDITGKLKDPANF
K61	KDITGKLKDPANFQY
Y68	KDPANFQYPAESVLA
Y76	PAESVLAYKEGHLSP
K77	AESVLAYKEGHLSPD
K77	AESVLAYKEGHLSPD
S82	AYKEGHLSPDIVAEQ
K90	PDIVAEQKkLEAADL
K91-u	DIVAEQKkLEAADLV
-	gap
-	gap
-	gap
K103-u	DLVIFQSkKAVLSIT
K171	IQILEGWKKRLENIW
K171	IQILEGWKKRLENIW
K172	QILEGWKKRLENIWD
K172	QILEGWKKRLENIWD
K203	QAGFLMKKEVQDEEK
K210	KEVQDEEKNKKFGLS
K213	QDEEKNKKFGLSVGH
K224	SVGHHLGKSIPTDNQ
K224	SVGHHLGKSIPTDNQ
K233	IPTDNQKKKKKKKKK

	mouse
Y20	SEKTSFNYAMKEAAV
K23	TSFNYAMKEAAVEAL
K31	EAAVEALKKRGWEVL
K31	EAAVEALKKRGWEVL
R33	AVEALKKRGWEVLES
S40	RGWEVLESDLYAMNF
Y43	EVLESDLYAMNFNPI
N54	FNPIISRNDITGELK
E59	SRNDITGELKDSKNF
E59	SRNDITGELKDSKNF
K61	NDITGELKDSKNFQY
Y68	KDSKNFQYPSESSLA
Y76	PSESSLAYkEGRLSP
K77	SESSLAYKEGRLSPD
K77-u	SESSLAYkEGRLSPD
S82	AYkEGRLSPDIVAEH
K90	PDIVAEHKKLEAADL
K91	DIVAEHKKLEAADLV
Y127	VLVAGFAYTYAAMYD
Y129	VAGFAYTYAAMYDNG
Y133	AYTYAAMYDNGPFQN
K141	DNGPFQNKKTLLSIT
K209	MQILEGWKKRLETVW
K209	MQILEGWKKRLETVW
K210	QILEGWKKRLETVWE
K210	QILEGWKKRLETVWE
K241	QAGFLMKKEVQEEQK
K248	KEVQEEQKKNKFGLS
K251	QEEQKKNKFGLSVGH
K262	SVGHHLGKSIPADNQ
K262	SVGHHLGKSIPADNQ
K271	IPADNQIKARK____

	rat
Y20	AERTSFNYAMKEAAV
K23	TSFNYAMKEAAVEAL
K31	EAAVEALKKKGWEVV
K31	EAAVEALKKKGWEVV
K33	AVEALKKKGWEVVES
S40	KGWEVVESDLYAMNF
Y43	EVVESDLYAMNFNPL
N54	FNPLISRNDITGEPK
E59	SRNDITGEPKDSENF
E59	SRNDITGEPKDSENF
K61	NDITGEPKDSENFQY
Y68	KDSENFQYPVESSLA
Y76	PVESSLAYKEGRLsP
K77	VESSLAYKEGRLsPD
K77	VESSLAYKEGRLsPD
S82-p	AYKEGRLsPDIVAEQ
K90	PDIVAEQKKLEAADL
K91	DIVAEQKKLEAADLV
Y127	VLVAGFAYTYATMYD
Y129	VAGFAYTYATMYDKG
Y133	AYTYATMYDKGPFQN
K141	DKGPFQNKKTLLSIT
K209	VQVLEGWKKRLETVW
K209	VQVLEGWKKRLETVW
K210	QVLEGWKKRLETVWE
K210	QVLEGWKKRLETVWE
K241	QAGFLLKKEVQEEQK
K248	KEVQEEQKKNKFGLS
K251	QEEQKKNKFGLSVGH
K262	SVGHHLGKSIPADNQ
K262	SVGHHLGKSIPADNQ
K271	IPADNQIKARK____

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