NMNA1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NMNA1_HUMAN
• UniProt AC: Q9HAN9
• Protein Name: Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1 {ECO:0000305}
• Gene Name: NMNAT1
• Organism: Homo sapiens (Human).
• Sequence Length: 279
• Subcellular Localization: Nucleus .
• Protein Description: Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. [PubMed: 17402747 Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate with the same efficiency]
• Protein Sequence: MENSEKTEVVLLACGSFNPITNMHLRLFELAKDYMNGTGRYTVVKGIISPVGDAYKKKGLIPAYHRVIMAELATKNSKWVEVDTWESLQKEWKETLKVLRHHQEKLEASDCDHQQNSPTLERPGRKRKWTETQDSSQKKSLEPKTKAVPKVKLLCGADLLESFAVPNLWKSEDITQIVANYGLICVTRAGNDAQKFIYESDVLWKHRSNIHVVNEWIANDISSTKIRRALRRGQSIRYLVPDLVQEYIEKHNLYSSESEDRNAGVILAPLQRNTAEAKT

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
7	Phosphorylation	-MENSEKTEVVLLAC -CCCCCCCEEEEEEC	29.93	24719451
34	Phosphorylation	LFELAKDYMNGTGRY HHHHHHHHHCCCCCE	7.56	22210691
41	Phosphorylation	YMNGTGRYTVVKGII HHCCCCCEEEEEEEE	12.77	-
42	Phosphorylation	MNGTGRYTVVKGIIS HCCCCCEEEEEEEEE	19.91	22210691
55	Phosphorylation	ISPVGDAYKKKGLIP EECCCHHHHHCCCHH	28.25	-
64	Phosphorylation	KKGLIPAYHRVIMAE HCCCHHHHHHHHHHH	5.70	-
90	Ubiquitination	DTWESLQKEWKETLK CHHHHHHHHHHHHHH	71.48	-
109	Phosphorylation	HQEKLEASDCDHQQN HHHHHHHHCCCCCCC	29.42	29255136
117	Phosphorylation	DCDHQQNSPTLERPG CCCCCCCCCCCCCCC	18.22	29255136
119	Phosphorylation	DHQQNSPTLERPGRK CCCCCCCCCCCCCCC	40.86	30266825
128	Ubiquitination	ERPGRKRKWTETQDS CCCCCCCCCCCCCCC	62.60	-
130	Phosphorylation	PGRKRKWTETQDSSQ CCCCCCCCCCCCCHH	31.99	28985074
135	Phosphorylation	KWTETQDSSQKKSLE CCCCCCCCHHHHCCC	25.50	21815630
136	Phosphorylation	WTETQDSSQKKSLEP CCCCCCCHHHHCCCC	55.07	25159151
208	Phosphorylation	DVLWKHRSNIHVVNE HCEEECCCCEEECCH	39.60	17322306
222	Phosphorylation	EWIANDISSTKIRRA HHHHHCCCHHHHHHH	34.51	27251275
223	Phosphorylation	WIANDISSTKIRRAL HHHHCCCHHHHHHHH	33.77	27251275
250	Ubiquitination	LVQEYIEKHNLYSSE HHHHHHHHCCCCCCC	28.38	-
261	Methylation	YSSESEDRNAGVILA CCCCCCCCCCCEEEE	30.74	115485213

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
136	S	Phosphorylation	Kinase	PRKCA	P17252	GPS

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of NMNA1_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 NMNA1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
NTRK2_HUMAN	NTRK2	physical	21988832
SIK1_HUMAN	SIK1	physical	21988832
NMNA1_HUMAN	NMNAT1	physical	25416956
SIR1_HUMAN	SIRT1	physical	19478080
PCY1A_HUMAN	PCYT1A	physical	26186194
CDC5L_HUMAN	CDC5L	physical	26186194
NMNA1_HUMAN	NMNAT1	physical	21516116
PCY1A_HUMAN	PCYT1A	physical	28514442

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 608553: Leber congenital amaurosis 9 (LCA9)
• 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

Phosphorylation

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117, AND MASSSPECTROMETRY.
PubMed: 19413330

"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-119, AND MASSSPECTROMETRY.
PubMed: 17081983