dbPTM

NQO1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NQO1_HUMAN
UniProt AC	P15559
Protein Name	NAD(P)H dehydrogenase [quinone] 1
Gene Name	NQO1
Organism	Homo sapiens (Human).
Sequence Length	274
Subcellular Localization	Cytoplasm.
Protein Description	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..
Protein Sequence	MVGRRALIVLAHSERTSFNYAMKEAAAAALKKKGWEVVESDLYAMNFNPIISRKDITGKLKDPANFQYPAESVLAYKEGHLSPDIVAEQKKLEAADLVIFQFPLQWFGVPAILKGWFERVFIGEFAYTYAAMYDKGPFRSKKAVLSITTGGSGSMYSLQGIHGDMNVILWPIQSGILHFCGFQVLEPQLTYSIGHTPADARIQILEGWKKRLENIWDETPLYFAPSSLFDLNFQAGFLMKKEVQDEEKNKKFGLSVGHHLGKSIPTDNQIKARK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
13	Phosphorylation	ALIVLAHSERTSFNY EEEEEECCCCCCHHH	24.14	23312004
20	Phosphorylation	SERTSFNYAMKEAAA CCCCCHHHHHHHHHH	13.18	22817900
23	Ubiquitination	TSFNYAMKEAAAAAL CCHHHHHHHHHHHHH	35.71	21906983
23	2-Hydroxyisobutyrylation	TSFNYAMKEAAAAAL CCHHHHHHHHHHHHH	35.71	-
31	Ubiquitination	EAAAAALKKKGWEVV HHHHHHHHHCCCEEE	47.95	21906983
31	Acetylation	EAAAAALKKKGWEVV HHHHHHHHHCCCEEE	47.95	19811543
31	2-Hydroxyisobutyrylation	EAAAAALKKKGWEVV HHHHHHHHHCCCEEE	47.95	-
33	Ubiquitination	AAAALKKKGWEVVES HHHHHHHCCCEEEEC	68.61	21906983
40	Phosphorylation	KGWEVVESDLYAMNF CCCEEEECCEEEEEC	22.70	-
43	Phosphorylation	EVVESDLYAMNFNPI EEEECCEEEEECCCC	14.59	-
45	Sulfoxidation	VESDLYAMNFNPIIS EECCEEEEECCCCCC	3.57	30846556
54	Ubiquitination	FNPIISRKDITGKLK CCCCCCCCCCCCCCC	46.84	21906983
59	Acetylation	SRKDITGKLKDPANF CCCCCCCCCCCCCCC	43.65	19608861
59	Ubiquitination	SRKDITGKLKDPANF CCCCCCCCCCCCCCC	43.65	21906983
61	2-Hydroxyisobutyrylation	KDITGKLKDPANFQY CCCCCCCCCCCCCCC	66.21	-
61	Ubiquitination	KDITGKLKDPANFQY CCCCCCCCCCCCCCC	66.21	21906983
61	Acetylation	KDITGKLKDPANFQY CCCCCCCCCCCCCCC	66.21	26051181
68	Phosphorylation	KDPANFQYPAESVLA CCCCCCCCCHHHHHH	10.56	28152594
72	Phosphorylation	NFQYPAESVLAYKEG CCCCCHHHHHHHHCC	25.24	28152594
76	Phosphorylation	PAESVLAYKEGHLSP CHHHHHHHHCCCCCH	12.86	23312004
77	Acetylation	AESVLAYKEGHLSPD HHHHHHHHCCCCCHH	52.17	26051181
77	Ubiquitination	AESVLAYKEGHLSPD HHHHHHHHCCCCCHH	52.17	21906983
77	2-Hydroxyisobutyrylation	AESVLAYKEGHLSPD HHHHHHHHCCCCCHH	52.17	-
82	Phosphorylation	AYKEGHLSPDIVAEQ HHHCCCCCHHHHHHH	18.17	29255136
90	Malonylation	PDIVAEQKKLEAADL HHHHHHHHHHHHCCE	51.32	26320211
90	2-Hydroxyisobutyrylation	PDIVAEQKKLEAADL HHHHHHHHHHHHCCE	51.32	-
90	Ubiquitination	PDIVAEQKKLEAADL HHHHHHHHHHHHCCE	51.32	906983
91	Ubiquitination	DIVAEQKKLEAADLV HHHHHHHHHHHCCEE	51.78	-
127	Phosphorylation	VFIGEFAYTYAAMYD HHHHHHHHHHHHHHC	12.95	-
128	Phosphorylation	FIGEFAYTYAAMYDK HHHHHHHHHHHHHCC	11.85	-
129	Phosphorylation	IGEFAYTYAAMYDKG HHHHHHHHHHHHCCC	4.62	-
133	Phosphorylation	AYTYAAMYDKGPFRS HHHHHHHHCCCCCCC	15.13	-
135	Ubiquitination	TYAAMYDKGPFRSKK HHHHHHCCCCCCCCE	51.50	-
171	Ubiquitination	DMNVILWPIQSGILH CCEEEEEECCCCCCH	15.99	19608861
171	Acetylation	DMNVILWPIQSGILH CCEEEEEECCCCCCH	15.99	19608861
174	Phosphorylation	VILWPIQSGILHFCG EEEEECCCCCCHHCC	28.64	26074081
175	Ubiquitination	ILWPIQSGILHFCGF EEEECCCCCCHHCCC	15.31	19608861
175	Acetylation	ILWPIQSGILHFCGF EEEECCCCCCHHCCC	15.31	19608861
190	Phosphorylation	QVLEPQLTYSIGHTP EEECCEEEEECCCCC	15.24	26074081
191	Phosphorylation	VLEPQLTYSIGHTPA EECCEEEEECCCCCH	13.59	26074081
192	Phosphorylation	LEPQLTYSIGHTPAD ECCEEEEECCCCCHH	19.50	26074081
196	Phosphorylation	LTYSIGHTPADARIQ EEEECCCCCHHHHHH	18.24	26074081
209	Acetylation	IQILEGWKKRLENIW HHHHHHHHHHHHHCC	38.58	19608861
209	Ubiquitination	IQILEGWKKRLENIW HHHHHHHHHHHHHCC	38.58	21906983
209	2-Hydroxyisobutyrylation	IQILEGWKKRLENIW HHHHHHHHHHHHHCC	38.58	-
210	Acetylation	QILEGWKKRLENIWD HHHHHHHHHHHHCCC	56.56	19814811
210	Ubiquitination	QILEGWKKRLENIWD HHHHHHHHHHHHCCC	56.56	-
224	Acetylation	DETPLYFAPSSLFDL CCCCCEECCCHHHCC	6.90	19608861
224	Ubiquitination	DETPLYFAPSSLFDL CCCCCEECCCHHHCC	6.90	19608861
228	Ubiquitination	LYFAPSSLFDLNFQA CEECCCHHHCCCHHH	4.55	19608861
228	Acetylation	LYFAPSSLFDLNFQA CEECCCHHHCCCHHH	4.55	19608861
241	Ubiquitination	QAGFLMKKEVQDEEK HHEEEEEEEECCHHH	49.50	21906983
248	Ubiquitination	KEVQDEEKNKKFGLS EEECCHHHHHHCCCC	72.52	21906983
250	Sumoylation	VQDEEKNKKFGLSVG ECCHHHHHHCCCCHH	61.62	28112733
251	Sumoylation	QDEEKNKKFGLSVGH CCHHHHHHCCCCHHH	54.80	-
251	Ubiquitination	QDEEKNKKFGLSVGH CCHHHHHHCCCCHHH	54.80	-
251	Acetylation	QDEEKNKKFGLSVGH CCHHHHHHCCCCHHH	54.80	26051181
251	Malonylation	QDEEKNKKFGLSVGH CCHHHHHHCCCCHHH	54.80	26320211
251	Sumoylation	QDEEKNKKFGLSVGH CCHHHHHHCCCCHHH	54.80	28112733
255	Phosphorylation	KNKKFGLSVGHHLGK HHHHCCCCHHHHCCC	26.82	20873877
262	Ubiquitination	SVGHHLGKSIPTDNQ CHHHHCCCCCCCCCC	52.12	2190698
262	Acetylation	SVGHHLGKSIPTDNQ CHHHHCCCCCCCCCC	52.12	23954790
262	2-Hydroxyisobutyrylation	SVGHHLGKSIPTDNQ CHHHHCCCCCCCCCC	52.12	-
263	Phosphorylation	VGHHLGKSIPTDNQI HHHHCCCCCCCCCCH	31.81	28348404
266	Phosphorylation	HLGKSIPTDNQIKAR HCCCCCCCCCCHHCC	46.01	20873877
271	Malonylation	IPTDNQIKARK---- CCCCCCHHCCC----	32.16	32601280
271	Ubiquitination	IPTDNQIKARK---- CCCCCCHHCCC----	32.16	21906983
271	2-Hydroxyisobutyrylation	IPTDNQIKARK---- CCCCCCHHCCC----	32.16	-
271	Sumoylation	IPTDNQIKARK---- CCCCCCHHCCC----	32.16	-
271	Sumoylation	IPTDNQIKARK---- CCCCCCHHCCC----	32.16	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
-	K	Ubiquitination	E3 ubiquitin ligase	STUB1	Q9UNE7	PMID:21220432

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of NQO1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of NQO1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HSP74_HUMAN	HSPA4	physical	11821413
NQO1_HUMAN	NQO1	physical	10543876
CHIP_HUMAN	STUB1	physical	21220432
PDIP3_HUMAN	POLDIP3	physical	22939629
YTHD1_HUMAN	YTHDF1	physical	22939629
RS19_HUMAN	RPS19	physical	22939629
PARP1_HUMAN	PARP1	physical	24140708
NF2L2_HUMAN	NFE2L2	physical	24140708
NDKA_HUMAN	NME1	physical	26344197
P53_HUMAN	TP53	physical	26540344

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00958	Carboplatin
DB00515	Cisplatin
DB00266	Dicoumarol
DB00997	Doxorubicin
DB03147	Flavin adenine dinucleotide
DB00170	Menadione
DB00526	Oxaliplatin
DB00163	Vitamin E

Regulatory Network of NQO1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-59 AND LYS-262, AND MASSSPECTROMETRY.	19608861 [Abstract]