dbPTM

NQO2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NQO2_HUMAN
UniProt AC	P16083
Protein Name	Ribosyldihydronicotinamide dehydrogenase [quinone]
Gene Name	NQO2
Organism	Homo sapiens (Human).
Sequence Length	231
Subcellular Localization	Cytoplasm.
Protein Description	The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinones 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	MAGKKVLIVYAHQEPKSFNGSLKNVAVDELSRQGCTVTVSDLYAMNLEPRATDKDITGTLSNPEVFNYGVETHEAYKQRSLASDITDEQKKVREADLVIFQFPLYWFSVPAILKGWMDRVLCQGFAFDIPGFYDSGLLQGKLALLSVTTGGTAEMYTKTGVNGDSRYFLWPLQHGTLHFCGFKVLAPQISFAPEIASEEERKGMVAAWSQRLQTIWKEEPIPCTAHWHFGQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
16	Ubiquitination	VYAHQEPKSFNGSLK EEECCCCCCCCCCCC	67.91	21890473
16	Ubiquitination	VYAHQEPKSFNGSLK EEECCCCCCCCCCCC	67.91	21890473
21	Phosphorylation	EPKSFNGSLKNVAVD CCCCCCCCCCEEHHH	36.96	27251275
23	Ubiquitination	KSFNGSLKNVAVDEL CCCCCCCCEEHHHHH	51.58	21890473
31	Phosphorylation	NVAVDELSRQGCTVT EEHHHHHHHCCCEEE	22.10	17192257
54	Ubiquitination	LEPRATDKDITGTLS CCCCCCCCCCCCCCC	46.83	21890473
77	Ubiquitination	VETHEAYKQRSLASD CCCHHHHHHHHHHCC	46.40	21890473
80	Phosphorylation	HEAYKQRSLASDITD HHHHHHHHHHCCCCH	26.29	22817900
83	Phosphorylation	YKQRSLASDITDEQK HHHHHHHCCCCHHHH	34.53	26437602
90	Ubiquitination	SDITDEQKKVREADL CCCCHHHHHHHHCCE	51.71	21890473
133	Phosphorylation	AFDIPGFYDSGLLQG EEECCCCCCCCHHCC	18.34	20068231
135	Phosphorylation	DIPGFYDSGLLQGKL ECCCCCCCCHHCCCE	21.69	20068231
146	Phosphorylation	QGKLALLSVTTGGTA CCCEEEEEEECCCCE	20.47	20068231
148	Phosphorylation	KLALLSVTTGGTAEM CEEEEEEECCCCEEE	19.15	20068231
149	Phosphorylation	LALLSVTTGGTAEMY EEEEEEECCCCEEEE	31.30	20068231
152	Phosphorylation	LSVTTGGTAEMYTKT EEEECCCCEEEEECC	22.31	20068231
156	Phosphorylation	TGGTAEMYTKTGVNG CCCCEEEEECCCCCC	9.15	20068231
157	Phosphorylation	GGTAEMYTKTGVNGD CCCEEEEECCCCCCC	22.33	20068231
158	Ubiquitination	GTAEMYTKTGVNGDS CCEEEEECCCCCCCC	26.29	21890473
197	Phosphorylation	SFAPEIASEEERKGM ECCHHHCCHHHHHCH	51.72	8182056
217	Ubiquitination	QRLQTIWKEEPIPCT HHHHHHHHCCCCCCC	48.64	-

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
Oops, there are no upstream regulatory protein records of NQO2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of NQO2_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 NQO2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GORS2_HUMAN	GORASP2	physical	16189514
NQO2_HUMAN	NQO2	physical	9367528
LRRC7_HUMAN	LRRC7	physical	25416956

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
DB06695	Dabigatran etexilate
DB03147	Flavin adenine dinucleotide
DB01065	Melatonin
DB00170	Menadione
DB01087	Primaquine

Regulatory Network of NQO2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-197, AND MASSSPECTROMETRY.	19369195 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, AND MASSSPECTROMETRY.	18691976 [Abstract]