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Q9HAN9

- NMNA1_HUMAN

UniProt

Q9HAN9 - NMNA1_HUMAN

Protein

Nicotinamide mononucleotide adenylyltransferase 1

Gene

NMNAT1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    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

    Divalent metal cations. Zinc confers higher activity as compared to magnesium.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 sitei16 – 161SubstrateBy similarity
    Binding sitei55 – 551SubstrateBy similarity
    Binding sitei158 – 1581SubstrateBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi15 – 2410ATPSequence Analysis
    Nucleotide bindingi222 – 2276ATPSequence Analysis

    GO - Molecular functioni

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

    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.
    ReactomeiREACT_11088. Nicotinate metabolism.
    SABIO-RKQ9HAN9.
    UniPathwayiUPA00253; UER00600.

    Names & Taxonomyi

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

    Organism-specific databases

    HGNCiHGNC:17877. NMNAT1.

    Subcellular locationi

    Nucleus 4 Publications

    GO - Cellular componenti

    1. nucleoplasm Source: Reactome
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Leber congenital amaurosis 9 (LCA9) [MIM:608553]: A 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.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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.

    PTM / Processingi

    Molecule processing

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

    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

    ArrayExpressiQ9HAN9.
    BgeeiQ9HAN9.
    CleanExiHS_NMNAT1.
    GenevestigatoriQ9HAN9.

    Organism-specific databases

    HPAiHPA059447.

    Interactioni

    Subunit structurei

    Homohexamer. Interacts with ADPRT/PARP1.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SIRT1Q96EB63EBI-3917542,EBI-1802965

    Protein-protein interaction databases

    BioGridi122308. 8 interactions.
    DIPiDIP-60881N.
    IntActiQ9HAN9. 6 interactions.
    STRINGi9606.ENSP00000366410.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    Motif

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

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1057.
    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

    MENSEKTEVV LLACGSFNPI TNMHLRLFEL AKDYMNGTGR YTVVKGIISP    50
    VGDAYKKKGL IPAYHRVIMA ELATKNSKWV EVDTWESLQK EWKETLKVLR 100
    HHQEKLEASD CDHQQNSPTL ERPGRKRKWT ETQDSSQKKS LEPKTKAVPK 150
    VKLLCGADLL ESFAVPNLWK SEDITQIVAN YGLICVTRAG NDAQKFIYES 200
    DVLWKHRSNI HVVNEWIAND ISSTKIRRAL RRGQSIRYLV PDLVQEYIEK 250
    HNLYSSESED RNAGVILAPL QRNTAEAKT 279
    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:
    EMBL
    GenBank
    DDBJ
    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_073624.2. NM_022787.3.
    XP_006710887.1. XM_006710824.1.
    UniGeneiHs.633762.

    Genome annotation databases

    EnsembliENST00000377205; ENSP00000366410; ENSG00000173614.
    ENST00000462686; ENSP00000435134; ENSG00000173614.
    GeneIDi64802.
    KEGGihsa:64802.
    UCSCiuc001aqp.3. human.

    Polymorphism databases

    DMDMi30580491.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS108.1.
    RefSeqi NP_073624.2. NM_022787.3.
    XP_006710887.1. XM_006710824.1.
    UniGenei Hs.633762.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GZU X-ray 2.90 A/B/C 2-279 [» ]
    1KKU X-ray 2.50 A 1-279 [» ]
    1KQN X-ray 2.20 A/B/C/D/E/F 1-279 [» ]
    1KQO X-ray 2.50 A/B/C/D/E/F 1-279 [» ]
    1KR2 X-ray 2.30 A/B/C/D/E/F 1-279 [» ]
    ProteinModelPortali Q9HAN9.
    SMRi Q9HAN9. Positions 6-275.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122308. 8 interactions.
    DIPi DIP-60881N.
    IntActi Q9HAN9. 6 interactions.
    STRINGi 9606.ENSP00000366410.

    PTM databases

    PhosphoSitei Q9HAN9.

    Polymorphism databases

    DMDMi 30580491.

    Proteomic databases

    MaxQBi Q9HAN9.
    PaxDbi Q9HAN9.
    PeptideAtlasi Q9HAN9.
    PRIDEi Q9HAN9.

    Protocols and materials databases

    DNASUi 64802.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000377205 ; ENSP00000366410 ; ENSG00000173614 .
    ENST00000462686 ; ENSP00000435134 ; ENSG00000173614 .
    GeneIDi 64802.
    KEGGi hsa:64802.
    UCSCi uc001aqp.3. human.

    Organism-specific databases

    CTDi 64802.
    GeneCardsi GC01P010003.
    GeneReviewsi NMNAT1.
    HGNCi HGNC:17877. NMNAT1.
    HPAi HPA059447.
    MIMi 608553. phenotype.
    608700. gene.
    neXtProti NX_Q9HAN9.
    Orphaneti 65. Leber congenital amaurosis.
    PharmGKBi PA31660.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1057.
    HOGENOMi HOG000216047.
    HOVERGENi HBG052640.
    InParanoidi Q9HAN9.
    KOi K06210.
    OMAi HRVAMCQ.
    PhylomeDBi Q9HAN9.
    TreeFami TF315035.

    Enzyme and pathway databases

    UniPathwayi UPA00253 ; UER00600 .
    BioCyci MetaCyc:HS10701-MONOMER.
    BRENDAi 2.7.7.1. 2681.
    Reactomei REACT_11088. Nicotinate metabolism.
    SABIO-RK Q9HAN9.

    Miscellaneous databases

    ChiTaRSi NMNAT1. human.
    EvolutionaryTracei Q9HAN9.
    GeneWikii NMNAT1.
    GenomeRNAii 64802.
    NextBioi 66892.
    PROi Q9HAN9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9HAN9.
    Bgeei Q9HAN9.
    CleanExi HS_NMNAT1.
    Genevestigatori Q9HAN9.

    Family and domain databases

    Gene3Di 3.40.50.620. 1 hit.
    InterProi IPR004821. Cyt_trans-like.
    IPR005248. NAMN_adtrnsfrase.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view ]
    PANTHERi PTHR12039. PTHR12039. 1 hit.
    Pfami PF01467. CTP_transf_2. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR00482. TIGR00482. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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. "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.
    14. "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).
    15. "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).
    16. Cited for: VARIANTS LCA9 THR-35; GLY-98; PHE-151; VAL-153; LYS-257 AND ASP-273.
    17. 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.
    18. 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: October 1, 2014
    This is version 120 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