NNRD_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NNRD_HUMAN
• UniProt AC: Q8IW45
• Protein Name: ATP-dependent (S)-NAD(P)H-hydrate dehydratase {ECO:0000255|HAMAP-Rule:MF_03157}
• Gene Name: NAXD {ECO:0000312|HGNC:HGNC:25576}
• Organism: Homo sapiens (Human).
• Sequence Length: 347
• Subcellular Localization: Mitochondrion .
• Protein Description: Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ATP, which is converted to ADP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration..
• Protein Sequence: MVTRAGAGTAVAGAVVVALLSAALALYGPPLDAVLERAFSLRKAHSIKDMENTLQLVRNIIPPLSSTKHKGQDGRIGVVGGCQEYTGAPYFAAISALKVGADLSHVFCASAAAPVIKAYSPELIVHPVLDSPNAVHEVEKWLPRLHALVVGPGLGRDDALLRNVQGILEVSKARDIPVVIDADGLWLVAQQPALIHGYRKAVLTPNHVEFSRLYDAVLRGPMDSDDSHGSVLRLSQALGNVTVVQKGERDILSNGQQVLVCSQEGSSRRCGGQGDLLSGSLGVLVHWALLAGPQKTNGSSPLLVAAFGACSLTRQCNHQAFQKHGRSTTTSDMIAEVGAAFSKLFET

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
46	Phosphorylation	FSLRKAHSIKDMENT HHHHHHCCCCCHHHH	35.87	23312004
65	Phosphorylation	RNIIPPLSSTKHKGQ HHHCCCCCCCCCCCC	41.56	-
67	Phosphorylation	IIPPLSSTKHKGQDG HCCCCCCCCCCCCCC	33.52	-
68	Ubiquitination	IPPLSSTKHKGQDGR CCCCCCCCCCCCCCC	45.31	-
85	Phosphorylation	VVGGCQEYTGAPYFA EECCCCCCCCCCCHH	5.65	27273156
86	Phosphorylation	VGGCQEYTGAPYFAA ECCCCCCCCCCCHHH	26.56	27259358
90	Phosphorylation	QEYTGAPYFAAISAL CCCCCCCCHHHHHHH	12.81	26356563
115 (in isoform 3)	Ubiquitination	-	6.34	21906983
140	Acetylation	NAVHEVEKWLPRLHA CHHHHHHHHHHHCCE	60.24	25038526
171	Phosphorylation	VQGILEVSKARDIPV HHHHHHHHCCCCCCE	15.95	22777824
172	Ubiquitination	QGILEVSKARDIPVV HHHHHHHCCCCCCEE	53.25	-
172 (in isoform 2)	Ubiquitination	-	53.25	-
200	Ubiquitination	ALIHGYRKAVLTPNH CCCCCCHHCCCCCCC	34.07	-
200 (in isoform 2)	Ubiquitination	-	34.07	-
222	Sulfoxidation	DAVLRGPMDSDDSHG HHHHCCCCCCCCCCH	9.55	21406390
224	Phosphorylation	VLRGPMDSDDSHGSV HHCCCCCCCCCCHHH	36.75	28857561
227	Phosphorylation	GPMDSDDSHGSVLRL CCCCCCCCCHHHHHH	34.44	28258704
230	Phosphorylation	DSDDSHGSVLRLSQA CCCCCCHHHHHHHHH	16.74	28258704
240	N-linked_Glycosylation	RLSQALGNVTVVQKG HHHHHHCCEEEEECC	27.43	19159218
246	Ubiquitination	GNVTVVQKGERDILS CCEEEEECCCEECCC	51.64	2190698
246 (in isoform 2)	Ubiquitination	-	51.64	21906983
246 (in isoform 1)	Ubiquitination	-	51.64	21906983
297	N-linked_Glycosylation	LAGPQKTNGSSPLLV HHCCCCCCCCCCHHH	56.22	UniProtKB CARBOHYD
306 (in isoform 2)	Phosphorylation	-	8.91	-
323 (in isoform 2)	Phosphorylation	-	41.39	-
331	Phosphorylation	HGRSTTTSDMIAEVG HCCCCCHHHHHHHHH	24.08	30576142
342	Phosphorylation	AEVGAAFSKLFET-- HHHHHHHHHHHCC--	24.59	30576142
347	Phosphorylation	AFSKLFET------- HHHHHHCC-------	36.25	30576142

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of NNRD_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of NNRD_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
KR107_HUMAN	KRTAP10-7	physical	25416956
KR109_HUMAN	KRTAP10-9	physical	25416956
KR108_HUMAN	KRTAP10-8	physical	25416956
KR103_HUMAN	KRTAP10-3	physical	25416956
NT2NL_HUMAN	NOTCH2NL	physical	25416956
GRHPR_HUMAN	GRHPR	physical	26344197
SIAS_HUMAN	NANS	physical	26344197
PRDX2_HUMAN	PRDX2	physical	26344197
SGTA_HUMAN	SGTA	physical	21516116
PPT2_HUMAN	PPT2	physical	28514442
KMCP1_HUMAN	SLC25A30	physical	28514442
MKLN1_HUMAN	MKLN1	physical	28514442
NEUFC_HUMAN	CYB5D2	physical	28514442
1A02_HUMAN	HLA-A	physical	28514442
1A03_HUMAN	HLA-A	physical	28514442
1A01_HUMAN	HLA-A	physical	28514442
1A26_HUMAN	HLA-A	physical	28514442
ERD23_HUMAN	KDELR3	physical	28514442

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
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-240, AND MASSSPECTROMETRY.
PubMed: 19159218

Phosphorylation

"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-85, AND MASSSPECTROMETRY.
PubMed: 19534553

"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-85, AND MASSSPECTROMETRY.
PubMed: 18083107