UniProt Accession

 NMNA1_HUMAN; Q9HAN9; B1AN63; Q8TAE9; Q9H247; Q9H6B6 

Genbank Protein ID

 AF314163; AF312734; AF459819; AF459823; AF459820; AF459821; AF459822; AK026065; AK315640; AL603962; AL357140; AL357140; AL603962; CH471130; BC014943 

Genbank Nucleotide ID

 AAG33632.1; AAG33629.1; AAL76934.1; AAL76935.1; AAL76935.1; AAL76935.1; AAL76935.1; BAB15345.1; BAG38007.1; CAI16813.1; CAI16813.1; CAI16889.1; CAI16889.1; EAW71635.1; AAH14943.1 

Protein Name

 Nicotinamide mononucleotide adenylyltransferase 1 

Protein Synonyms/Alias

 NMN adenylyltransferase 1; Nicotinate-nucleotide adenylyltransferase 1; NaMN adenylyltransferase 1 

Gene Name

 NMNAT1 

Gene Synonyms/Alias

 NMNAT 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
250	LVQEYIEKHNLYSSE	ubiquitination	[1]

Reference

 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983] 

Functional Description

 Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate with the same efficiency. Can use triazofurin monophosphate (TrMP) as substrate. Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+). For the pyrophosphorolytic activity, prefers NAD(+) and NAAD as substrates and degrades NADH, nicotinic acid adenine dinucleotide phosphate (NHD) and nicotinamide guanine dinucleotide (NGD) less effectively. Fails to cleave phosphorylated dinucleotides NADP(+), NADPH and NAADP(+). Protects against axonal degeneration following mechanical or toxic insults. 

Sequence Annotation

 NP_BIND 15 24 ATP (Potential).
 NP_BIND 222 227 ATP (Potential).
 MOTIF 123 129 Nuclear localization signal (Potential).
 BINDING 16 16 Substrate (By similarity).
 BINDING 55 55 Substrate (By similarity).
 BINDING 158 158 Substrate (By similarity).  

Keyword

 3D-structure; ATP-binding; Complete proteome; Direct protein sequencing; Disease mutation; Leber congenital amaurosis; Magnesium; NAD; Nucleotide-binding; Nucleotidyltransferase; Nucleus; Phosphoprotein; Pyridine nucleotide biosynthesis; Reference proteome; Transferase; Zinc. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 279 AA 

Protein Sequence

Gene Ontology

 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0000309; F:nicotinamide-nucleotide adenylyltransferase activity; IDA:UniProtKB.
 GO:0004515; F:nicotinate-nucleotide adenylyltransferase activity; IDA:UniProtKB.
 GO:0009435; P:NAD biosynthetic process; IC:UniProtKB.
 GO:0009611; P:response to wounding; IEA:Compara.
 GO:0006767; P:water-soluble vitamin metabolic process; TAS:Reactome. 

Interpro

 IPR004821; Cyt_trans-like.
 IPR005248; NAMN_adtrnsfrase.
 IPR014729; Rossmann-like_a/b/a_fold. 

Pfam

 PF01467; CTP_transf_2 

SMART

  

PROSITE

  

PRINTS