| Tag |
Content |
LipidDB ID |
LipidDB-9606-01304 |
Entry Name |
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UniProt Accession |
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Theoretical PI |
6.59 |
Molecular Weight |
34438.63 |
Genbank Protein ID |
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Genbank Nucleotide ID |
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Protein Name |
Nicotinamide mononucleotide adenylyltransferase 2 |
Protein Synonyms/Alias |
NMN adenylyltransferase 2; 2.7.7.1; Nicotinate-nucleotide adenylyltransferase 2; NaMN adenylyltransferase 2; 2.7.7.18; |
Gene Name |
NMNAT2 |
Gene Synonyms/Alias |
C1orf15; KIAA0479; |
Created Date |
09-MAY-2003 |
| Lipid Modification Sites |
| Position |
Sequence Form |
Peptide |
References |
Modification Type |
164 | Canonical | GESLSRICCVRPPVE | [1][2] | S-Palmitoylation | 165 | Canonical | ESLSRICCVRPPVER | [1][2] | S-Palmitoylation |
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Organism |
Homo sapiens (Human) |
NCBI Taxa ID |
9606 |
Reference |
[1] Lau C, Dölle C, Gossmann TI, Agledal L, Niere M, Ziegler M. Isoform-specifictargeting and interaction domains in human nicotinamide mononucleotideadenylyltransferases. J Biol Chem. 2010 Jun 11;285(24):18868-76. doi:10.1074/jbc.M110.107631. Epub 2010 Apr 13.[ PMID:20388704]
[2] Mayer PR, Huang N, Dewey CM, Dries DR, Zhang H, Yu G. Expression,localization, and biochemical characterization of nicotinamide mononucleotideadenylyltransferase 2. J Biol Chem. 2010 Dec 17;285(51):40387-96. doi:10.1074/jbc.M110.178913. Epub 2010 Oct 13.[ PMID:20943658]
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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 but with a lower efficiency. Cannot use triazofurin monophosphate (TrMP) as substrate. Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+). For the pyrophosphorolytic activity prefers NAD(+), NADH and NAAD as substrates and degrades nicotinic acid adenine dinucleotide phosphate (NHD) less effectively. Fails to cleave phosphorylated dinucleotides NADP(+), NADPH and NAADP(+). |
Sequence Annotation |
Nucleotide-binding: 15 24 ATP. Nucleotide-binding: 269 274 ATP. Binding site: 16 16 Substrate. Binding site: 55 55 Substrate. Binding site: 202 202 Substrate.
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Protein Length |
307 AA. |
Protein Sequence (Canonical) |
MTETTKTHVI LLACGSFNPI TKGHIQMFER ARDYLHKTGR FIVIGGIVSP VHDSYGKQGL 60
VSSRHRLIMC QLAVQNSDWI RVDPWECYQD TWQTTCSVLE HHRDLMKRVT GCILSNVNTP 120
SMTPVIGQPQ NETPQPIYQN SNVATKPTAA KILGKVGESL SRICCVRPPV ERFTFVDENA 180
NLGTVMRYEE IELRILLLCG SDLLESFCIP GLWNEADMEV IVGDFGIVVV PRDAADTDRI 240
MNHSSILRKY KNNIMVVKDD INHPMSVVSS TKSRLALQHG DGHVVDYLSQ PVIDYILKSQ 300
LYINASG 307
|
FASTA (Canonical) |
>LipidDB-9606-01304|Q9BZQ4
MTETTKTHVILLACGSFNPITKGHIQMFERARDYLHKTGRFIVIGGIVSPVHDSYGKQGL
VSSRHRLIMCQLAVQNSDWIRVDPWECYQDTWQTTCSVLEHHRDLMKRVTGCILSNVNTP
SMTPVIGQPQNETPQPIYQNSNVATKPTAAKILGKVGESLSRICCVRPPVERFTFVDENA
NLGTVMRYEEIELRILLLCGSDLLESFCIPGLWNEADMEVIVGDFGIVVVPRDAADTDRI
MNHSSILRKYKNNIMVVKDDINHPMSVVSSTKSRLALQHGDGHVVDYLSQPVIDYILKSQ
LYINASG
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Gene Ontology |
GO:0005794; C:Golgi apparatus; IDA:UniProtKB GO:0000139; C:Golgi membrane; TAS:Reactome GO:0005770; C:late endosome; IEA:Ensembl GO:0045202; C:synapse; IEA:Ensembl GO:0005802; C:trans-Golgi network; IEA:Ensembl GO:0005524; F:ATP binding; IEA:UniProtKB-KW GO:0000309; F:nicotinamide-nucleotide adenylyltransferase activity; TAS:Reactome GO:0004515; F:nicotinate-nucleotide adenylyltransferase activity; IDA:UniProtKB GO:0009435; P:NAD biosynthetic process; IC:UniProtKB GO:0019674; P:NAD metabolic process; TAS:Reactome GO:0044281; P:small molecule metabolic process; TAS:Reactome GO:0006766; P:vitamin metabolic process; TAS:Reactome GO:0006767; P:water-soluble vitamin metabolic process; TAS:Reactome |
Interpro |
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Pfam |
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SMART |
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PROSITE |
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PRINTS |
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