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Protein

Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1

Gene

NMNAT1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

ATP + nicotinamide ribonucleotide = diphosphate + NAD+.1 Publication
ATP + beta-nicotinate-D-ribonucleotide = diphosphate + deamido-NAD+.

Cofactori

Zn2+2 Publications, Mg2+2 PublicationsNote: Divalent metal cations. Zn(2+) confers higher activity as compared to Mg2+.2 Publications

Enzyme regulationi

Activity is strongly inhibited by galotannin. Inhibited by P1-(adenosine-5')-P4-(nicotinic-acid-riboside-5')-tetraphosphate (Nap4AD).1 Publication

Kineticsi

  1. KM=34 µM for NMN2 Publications
  2. KM=40 µM for ATP2 Publications
  3. KM=937 µM for PPi2 Publications
  4. KM=59 µM for NAD+2 Publications

Vmax=25 µmol/min/mg enzyme for NAD synthesis2 Publications

Vmax=60.5 µmol/min/µg enzyme for NAD+ cleavage2 Publications

Vmax=8.5 µmol/min/µg enzyme for NADH cleavage2 Publications

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei24 – 241ATPBy similarity
Binding sitei58 – 581ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi15 – 173ATPBy similarity1 Publication
Nucleotide bindingi156 – 1583ATPBy similarity
Nucleotide bindingi224 – 2274ATPBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. nicotinamide-nucleotide adenylyltransferase activity Source: UniProtKB
  3. nicotinate-nucleotide adenylyltransferase activity Source: UniProtKB

GO - Biological processi

  1. NAD biosynthetic process Source: UniProtKB
  2. NAD metabolic process Source: Reactome
  3. small molecule metabolic process Source: Reactome
  4. vitamin metabolic process Source: Reactome
  5. water-soluble vitamin metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

Pyridine nucleotide biosynthesis

Keywords - Ligandi

ATP-binding, Magnesium, NAD, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:HS10701-MONOMER.
BRENDAi2.7.7.1. 2681.
2.7.7.18. 2681.
ReactomeiREACT_11088. Nicotinate metabolism.
SABIO-RKQ9HAN9.
UniPathwayiUPA00253; UER00332.
UPA00253; UER00600.

Names & Taxonomyi

Protein namesi
Recommended name:
Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1Curated (EC:2.7.7.1, EC:2.7.7.18)
Short name:
NMN/NaMN adenylyltransferase 1
Alternative name(s):
Nicotinamide-nucleotide adenylyltransferase 1
Short name:
NMN adenylyltransferase 1
Nicotinate-nucleotide adenylyltransferase 1
Short name:
NaMN adenylyltransferase 1
Gene namesi
Name:NMNAT1
Synonyms:NMNAT
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Unplaced

Organism-specific databases

HGNCiHGNC:17877. NMNAT1.

Subcellular locationi

  1. Nucleus 4 Publications

GO - Cellular componenti

  1. nucleoplasm Source: Reactome
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Leber congenital amaurosis 9 (LCA9)4 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA severe dystrophy of the retina, typically becoming evident in the first years of life. Visual function is usually poor and often accompanied by nystagmus, sluggish or near-absent pupillary responses, photophobia, high hyperopia and keratoconus.

See also OMIM:608553
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti9 – 91V → M in LCA9; does not affect nuclear localization; results in significantly reduced enzymatic activity. 1 Publication
VAR_068856
Natural varianti13 – 131A → T in LCA9. 3 Publications
Corresponds to variant rs138613460 [ dbSNP | Ensembl ].
VAR_068857
Natural varianti20 – 201I → N in LCA9. 1 Publication
VAR_068858
Natural varianti33 – 331D → G in LCA9. 1 Publication
VAR_068859
Natural varianti35 – 351M → T in LCA9. 1 Publication
VAR_068860
Natural varianti54 – 541A → V in LCA9. 1 Publication
VAR_068861
Natural varianti66 – 661R → W in LCA9; does not affect nuclear localization; results in significantly reduced enzymatic activity. 1 Publication
VAR_068862
Natural varianti67 – 671V → F in LCA9. 1 Publication
VAR_068863
Natural varianti69 – 691M → V in LCA9. 2 Publications
VAR_068864
Natural varianti72 – 721L → H in LCA9. 1 Publication
VAR_068865
Natural varianti98 – 981V → G in LCA9. 3 Publications
VAR_068866
Natural varianti147 – 1471A → P in LCA9. 1 Publication
VAR_068867
Natural varianti151 – 1511V → F in LCA9. 2 Publications
VAR_068868
Natural varianti153 – 1531L → P in LCA9. 1 Publication
VAR_068869
Natural varianti153 – 1531L → V in LCA9. 1 Publication
VAR_068870
Natural varianti156 – 1561G → R in LCA9. 1 Publication
VAR_068871
Natural varianti173 – 1731D → G in LCA9. 1 Publication
VAR_068872
Natural varianti178 – 1781V → M in LCA9. 1 Publication
VAR_068873
Natural varianti181 – 1811Y → C in LCA9. 1 Publication
VAR_068874
Natural varianti184 – 1841I → M in LCA9. 1 Publication
VAR_068875
Natural varianti207 – 2071R → W in LCA9; results in significantly reduced enzymatic activity. 2 Publications
Corresponds to variant rs142968179 [ dbSNP | Ensembl ].
VAR_068876
Natural varianti217 – 2171I → N in LCA9. 1 Publication
VAR_068877
Natural varianti237 – 2371R → C in LCA9; does not affect nuclear localization. 2 Publications
VAR_068878
Natural varianti237 – 2371R → L in LCA9. 1 Publication
VAR_068879
Natural varianti239 – 2391L → S in LCA9. 1 Publication
VAR_068880
Natural varianti251 – 2511H → P in LCA9. 1 Publication
VAR_068881
Natural varianti257 – 2571E → K in LCA9; results in significantly reduced enzymatic activity; the mutant localizes to the cytoplasm. 3 Publications
Corresponds to variant rs150726175 [ dbSNP | Ensembl ].
VAR_068882
Natural varianti273 – 2731N → D in LCA9; results in significantly reduced enzymatic activity. 2 Publications
VAR_068883

Keywords - Diseasei

Disease mutation, Leber congenital amaurosis

Organism-specific databases

MIMi608553. phenotype.
Orphaneti65. Leber congenital amaurosis.
PharmGKBiPA31660.

Polymorphism and mutation databases

BioMutaiNMNAT1.
DMDMi30580491.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 279279Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1PRO_0000135012Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei117 – 1171Phosphoserine1 Publication
Modified residuei119 – 1191Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9HAN9.
PaxDbiQ9HAN9.
PeptideAtlasiQ9HAN9.
PRIDEiQ9HAN9.

PTM databases

PhosphoSiteiQ9HAN9.

Expressioni

Tissue specificityi

Widely expressed with highest levels in skeletal muscle, heart and kidney. Also expressed in the liver pancreas and placenta. Widely expressed throughout the brain.2 Publications

Gene expression databases

BgeeiQ9HAN9.
CleanExiHS_NMNAT1.
ExpressionAtlasiQ9HAN9. baseline and differential.
GenevestigatoriQ9HAN9.

Organism-specific databases

HPAiHPA059447.

Interactioni

Subunit structurei

Homohexamer. Interacts with ADPRT/PARP1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CCNCP248633EBI-3917542,EBI-395261
KPNA2Q6NVW73EBI-3917542,EBI-9377406
SIRT1Q96EB63EBI-3917542,EBI-1802965

Protein-protein interaction databases

BioGridi122308. 24 interactions.
DIPiDIP-60881N.
IntActiQ9HAN9. 8 interactions.
STRINGi9606.ENSP00000366410.

Structurei

Secondary structure

1
279
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 159Combined sources
Helixi22 – 3716Combined sources
Beta strandi39 – 5012Combined sources
Helixi53 – 553Combined sources
Helixi63 – 7311Combined sources
Turni74 – 763Combined sources
Beta strandi78 – 825Combined sources
Helixi86 – 883Combined sources
Helixi95 – 10612Combined sources
Beta strandi150 – 1567Combined sources
Helixi157 – 1626Combined sources
Turni166 – 1683Combined sources
Helixi171 – 18010Combined sources
Beta strandi183 – 1886Combined sources
Helixi190 – 1989Combined sources
Helixi201 – 2055Combined sources
Helixi206 – 2094Combined sources
Beta strandi210 – 2145Combined sources
Beta strandi217 – 2193Combined sources
Helixi223 – 2319Combined sources
Helixi242 – 25110Combined sources
Helixi256 – 2594Combined sources
Turni260 – 2645Combined sources
Helixi268 – 2747Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GZUX-ray2.90A/B/C2-279[»]
1KKUX-ray2.50A1-279[»]
1KQNX-ray2.20A/B/C/D/E/F1-279[»]
1KQOX-ray2.50A/B/C/D/E/F1-279[»]
1KR2X-ray2.30A/B/C/D/E/F1-279[»]
ProteinModelPortaliQ9HAN9.
SMRiQ9HAN9. Positions 6-275.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9HAN9.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni55 – 573Substrate binding1 Publication
Regioni92 – 954Substrate binding2 Publications
Regioni168 – 1692Substrate binding2 Publications

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi123 – 1297Nuclear localization signalSequence Analysis

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1057.
GeneTreeiENSGT00530000063189.
HOGENOMiHOG000216047.
HOVERGENiHBG052640.
InParanoidiQ9HAN9.
KOiK06210.
OMAiHRVAMCQ.
PhylomeDBiQ9HAN9.
TreeFamiTF315035.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
InterProiIPR004821. Cyt_trans-like.
IPR005248. NAMN_adtrnsfrase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERiPTHR12039. PTHR12039. 1 hit.
PfamiPF01467. CTP_transf_2. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00482. TIGR00482. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9HAN9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MENSEKTEVV LLACGSFNPI TNMHLRLFEL AKDYMNGTGR YTVVKGIISP
60 70 80 90 100
VGDAYKKKGL IPAYHRVIMA ELATKNSKWV EVDTWESLQK EWKETLKVLR
110 120 130 140 150
HHQEKLEASD CDHQQNSPTL ERPGRKRKWT ETQDSSQKKS LEPKTKAVPK
160 170 180 190 200
VKLLCGADLL ESFAVPNLWK SEDITQIVAN YGLICVTRAG NDAQKFIYES
210 220 230 240 250
DVLWKHRSNI HVVNEWIAND ISSTKIRRAL RRGQSIRYLV PDLVQEYIEK
260 270
HNLYSSESED RNAGVILAPL QRNTAEAKT
Length:279
Mass (Da):31,932
Last modified:March 1, 2001 - v1
Checksum:i740DE872CD9C22E7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti20 – 201I → F in AAL76934 (PubMed:11027696).Curated
Sequence conflicti20 – 201I → F in AAL76935 (PubMed:11027696).Curated
Sequence conflicti217 – 2171I → F in AAG33629 (PubMed:11891043).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti9 – 91V → M in LCA9; does not affect nuclear localization; results in significantly reduced enzymatic activity. 1 Publication
VAR_068856
Natural varianti13 – 131A → T in LCA9. 3 Publications
Corresponds to variant rs138613460 [ dbSNP | Ensembl ].
VAR_068857
Natural varianti20 – 201I → N in LCA9. 1 Publication
VAR_068858
Natural varianti33 – 331D → G in LCA9. 1 Publication
VAR_068859
Natural varianti35 – 351M → T in LCA9. 1 Publication
VAR_068860
Natural varianti54 – 541A → V in LCA9. 1 Publication
VAR_068861
Natural varianti66 – 661R → W in LCA9; does not affect nuclear localization; results in significantly reduced enzymatic activity. 1 Publication
VAR_068862
Natural varianti67 – 671V → F in LCA9. 1 Publication
VAR_068863
Natural varianti69 – 691M → V in LCA9. 2 Publications
VAR_068864
Natural varianti72 – 721L → H in LCA9. 1 Publication
VAR_068865
Natural varianti98 – 981V → G in LCA9. 3 Publications
VAR_068866
Natural varianti147 – 1471A → P in LCA9. 1 Publication
VAR_068867
Natural varianti151 – 1511V → F in LCA9. 2 Publications
VAR_068868
Natural varianti153 – 1531L → P in LCA9. 1 Publication
VAR_068869
Natural varianti153 – 1531L → V in LCA9. 1 Publication
VAR_068870
Natural varianti156 – 1561G → R in LCA9. 1 Publication
VAR_068871
Natural varianti173 – 1731D → G in LCA9. 1 Publication
VAR_068872
Natural varianti178 – 1781V → M in LCA9. 1 Publication
VAR_068873
Natural varianti181 – 1811Y → C in LCA9. 1 Publication
VAR_068874
Natural varianti184 – 1841I → M in LCA9. 1 Publication
VAR_068875
Natural varianti207 – 2071R → W in LCA9; results in significantly reduced enzymatic activity. 2 Publications
Corresponds to variant rs142968179 [ dbSNP | Ensembl ].
VAR_068876
Natural varianti217 – 2171I → N in LCA9. 1 Publication
VAR_068877
Natural varianti237 – 2371R → C in LCA9; does not affect nuclear localization. 2 Publications
VAR_068878
Natural varianti237 – 2371R → L in LCA9. 1 Publication
VAR_068879
Natural varianti239 – 2391L → S in LCA9. 1 Publication
VAR_068880
Natural varianti251 – 2511H → P in LCA9. 1 Publication
VAR_068881
Natural varianti257 – 2571E → K in LCA9; results in significantly reduced enzymatic activity; the mutant localizes to the cytoplasm. 3 Publications
Corresponds to variant rs150726175 [ dbSNP | Ensembl ].
VAR_068882
Natural varianti273 – 2731N → D in LCA9; results in significantly reduced enzymatic activity. 2 Publications
VAR_068883

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF314163 mRNA. Translation: AAG33632.1.
AF312734 mRNA. Translation: AAG33629.1.
AF459819 mRNA. Translation: AAL76934.1.
AF459823
, AF459820, AF459821, AF459822 Genomic DNA. Translation: AAL76935.1.
AK026065 mRNA. Translation: BAB15345.1.
AK315640 mRNA. Translation: BAG38007.1.
AL603962, AL357140 Genomic DNA. Translation: CAI16813.1.
AL357140, AL603962 Genomic DNA. Translation: CAI16889.1.
CH471130 Genomic DNA. Translation: EAW71635.1.
BC014943 mRNA. Translation: AAH14943.1.
CCDSiCCDS108.1.
RefSeqiNP_001284707.1. NM_001297778.1.
NP_073624.2. NM_022787.3.
UniGeneiHs.633762.

Genome annotation databases

GeneIDi64802.
KEGGihsa:64802.
UCSCiuc001aqp.3. human.

Polymorphism and mutation databases

BioMutaiNMNAT1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF314163 mRNA. Translation: AAG33632.1.
AF312734 mRNA. Translation: AAG33629.1.
AF459819 mRNA. Translation: AAL76934.1.
AF459823
, AF459820, AF459821, AF459822 Genomic DNA. Translation: AAL76935.1.
AK026065 mRNA. Translation: BAB15345.1.
AK315640 mRNA. Translation: BAG38007.1.
AL603962, AL357140 Genomic DNA. Translation: CAI16813.1.
AL357140, AL603962 Genomic DNA. Translation: CAI16889.1.
CH471130 Genomic DNA. Translation: EAW71635.1.
BC014943 mRNA. Translation: AAH14943.1.
CCDSiCCDS108.1.
RefSeqiNP_001284707.1. NM_001297778.1.
NP_073624.2. NM_022787.3.
UniGeneiHs.633762.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GZUX-ray2.90A/B/C2-279[»]
1KKUX-ray2.50A1-279[»]
1KQNX-ray2.20A/B/C/D/E/F1-279[»]
1KQOX-ray2.50A/B/C/D/E/F1-279[»]
1KR2X-ray2.30A/B/C/D/E/F1-279[»]
ProteinModelPortaliQ9HAN9.
SMRiQ9HAN9. Positions 6-275.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122308. 24 interactions.
DIPiDIP-60881N.
IntActiQ9HAN9. 8 interactions.
STRINGi9606.ENSP00000366410.

PTM databases

PhosphoSiteiQ9HAN9.

Polymorphism and mutation databases

BioMutaiNMNAT1.
DMDMi30580491.

Proteomic databases

MaxQBiQ9HAN9.
PaxDbiQ9HAN9.
PeptideAtlasiQ9HAN9.
PRIDEiQ9HAN9.

Protocols and materials databases

DNASUi64802.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi64802.
KEGGihsa:64802.
UCSCiuc001aqp.3. human.

Organism-specific databases

CTDi64802.
GeneCardsiGC01P010003.
GeneReviewsiNMNAT1.
HGNCiHGNC:17877. NMNAT1.
HPAiHPA059447.
MIMi608553. phenotype.
608700. gene.
neXtProtiNX_Q9HAN9.
Orphaneti65. Leber congenital amaurosis.
PharmGKBiPA31660.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1057.
GeneTreeiENSGT00530000063189.
HOGENOMiHOG000216047.
HOVERGENiHBG052640.
InParanoidiQ9HAN9.
KOiK06210.
OMAiHRVAMCQ.
PhylomeDBiQ9HAN9.
TreeFamiTF315035.

Enzyme and pathway databases

UniPathwayiUPA00253; UER00332.
UPA00253; UER00600.
BioCyciMetaCyc:HS10701-MONOMER.
BRENDAi2.7.7.1. 2681.
2.7.7.18. 2681.
ReactomeiREACT_11088. Nicotinate metabolism.
SABIO-RKQ9HAN9.

Miscellaneous databases

ChiTaRSiNMNAT1. human.
EvolutionaryTraceiQ9HAN9.
GeneWikiiNMNAT1.
GenomeRNAii64802.
NextBioi66892.
PROiQ9HAN9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9HAN9.
CleanExiHS_NMNAT1.
ExpressionAtlasiQ9HAN9. baseline and differential.
GenevestigatoriQ9HAN9.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
InterProiIPR004821. Cyt_trans-like.
IPR005248. NAMN_adtrnsfrase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERiPTHR12039. PTHR12039. 1 hit.
PfamiPF01467. CTP_transf_2. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00482. TIGR00482. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of recombinant human nicotinamide mononucleotide adenylyl transferase (NMNAT), a nuclear enzyme essential for NAD synthesis."
    Schweiger M., Hennig K., Lerner F., Niere M., Hirsch-Kauffmann M., Specht T., Weise C., Oei S.L., Ziegler M.
    FEBS Lett. 492:95-100(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 208-225 AND 262-272, SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH ADPRT.
  2. "Molecular cloning, chromosomal localization, tissue mRNA levels, bacterial expression, and enzymatic properties of human NMN adenylyltransferase."
    Emanuelli M., Carnevali F., Saccucci F., Pierella F., Amici A., Raffaelli N., Magni G.
    J. Biol. Chem. 276:406-412(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 238-250 AND 262-272, COFACTOR, TISSUE SPECIFICITY.
    Tissue: Placenta.
  3. "Human homologue of a gene mutated in the slow Wallerian degeneration (C57BL/Wld(s)) mouse."
    Fernando F.S., Conforti L., Tosi S., Smith A.D., Coleman M.P.
    Gene 284:23-29(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Synovium.
  5. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Eye.
  8. "Structural characterization of a human cytosolic NMN/NaMN adenylyltransferase and implication in human NAD biosynthesis."
    Zhang X., Kurnasov O.V., Karthikeyan S., Grishin N.V., Osterman A.L., Zhang H.
    J. Biol. Chem. 278:13503-13511(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  9. "Subcellular compartmentation and differential catalytic properties of the three human nicotinamide mononucleotide adenylyltransferase isoforms."
    Berger F., Lau C., Dahlmann M., Ziegler M.
    J. Biol. Chem. 280:36334-36341(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION.
  10. "Initial-rate kinetics of human NMN-adenylyltransferases: substrate and metal ion specificity, inhibition by products and multisubstrate analogues, and isozyme contributions to NAD+ biosynthesis."
    Sorci L., Cimadamore F., Scotti S., Petrelli R., Cappellacci L., Franchetti P., Orsomando G., Magni G.
    Biochemistry 46:4912-4922(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, COFACTOR.
  11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: SUBCELLULAR LOCATION, VARIANTS LCA9 THR-13; PHE-67; GLY-98; PHE-151; TRP-207; LEU-237; LYS-257 AND ASP-273, CHARACTERIZATION OF VARIANTS LCA9 TRP-207; LYS-257 AND ASP-273.
  13. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117 AND THR-119, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  14. "Crystal structure of human nicotinamide mononucleotide adenylyltransferase in complex with NMN."
    Werner E., Ziegler M., Lerner F., Schweiger M., Heinemann U.
    FEBS Lett. 516:239-244(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 5-278 IN COMPLEX WITH SUBSTRATE NMN.
  15. "Structure of human NMN adenylyltransferase. A key nuclear enzyme for NAD homeostasis."
    Garavaglia S., D'Angelo I., Emanuelli M., Carnevali F., Pierella F., Magni G., Rizzi M.
    J. Biol. Chem. 277:8524-8530(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
  16. "Structure of human nicotinamide/nicotinic acid mononucleotide adenylyltransferase. Basis for the dual substrate specificity and activation of the oncolytic agent tiazofurin."
    Zhou T., Kurnasov O., Tomchick D.R., Binns D.D., Grishin N.V., Marquez V.E., Osterman A.L., Zhang H.
    J. Biol. Chem. 277:13148-13154(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH PRODUCTS NAD AND NAAD.
  17. Cited for: VARIANTS LCA9 THR-35; GLY-98; PHE-151; VAL-153; LYS-257 AND ASP-273.
  18. Cited for: VARIANTS LCA9 THR-13; VAL-69; PRO-147; PRO-153; GLY-173; MET-178; CYS-181; TRP-207; ASN-217; CYS-237; SER-239 AND PRO-251.
  19. Cited for: VARIANTS LCA9 MET-9; THR-13; ASN-20; GLY-33; VAL-54; TRP-66; VAL-69; HIS-72; GLY-98; ARG-156; MET-184; CYS-237 AND LYS-257, CHARACTERIZATION OF VARIANTS LCA9 MET-9; TRP-66 AND CYS-237.

Entry informationi

Entry nameiNMNA1_HUMAN
AccessioniPrimary (citable) accession number: Q9HAN9
Secondary accession number(s): B1AN63
, Q8TAE9, Q9H247, Q9H6B6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 9, 2003
Last sequence update: March 1, 2001
Last modified: April 29, 2015
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.