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Q96T66

- NMNA3_HUMAN

UniProt

Q96T66 - NMNA3_HUMAN

Protein

Nicotinamide mononucleotide adenylyltransferase 3

Gene

NMNAT3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 2 (17 Oct 2006)
      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. Can also use GTP and ITP as nucleotide donors. Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD+. For the pyrophosphorolytic activity, can use NAD (+), NADH, NAAD, nicotinic acid adenine dinucleotide phosphate (NHD), nicotinamide guanine dinucleotide (NGD) as substrates. Fails to cleave phosphorylated dinucleotides NADP+, NADPH and NAADP+. Protects against axonal degeneration following injury.2 Publications

    Catalytic activityi

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

    Cofactori

    Divalent metal cations. Magnesium confers the highest activity.1 Publication

    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=209 µM for NMN2 Publications
    2. KM=130 µM for NAD+2 Publications
    3. KM=29 µM for ATP2 Publications
    4. KM=390 µM for PPi2 Publications
    5. KM=276 µM for GTP2 Publications
    6. KM=350 µM for ITP2 Publications
    7. KM=111 µM for NaMN2 Publications
    8. KM=130 µM for NMNH2 Publications
    9. KM=2.01 µM for triazofurin monophosphate2 Publications

    Vmax=3.6 µmol/min/mg enzyme for NAD synthesis2 Publications

    Vmax=12.8 µmol/min/mg enzyme for pyrophosphorolytic NAD+ cleavage2 Publications

    Vmax=2.9 µmol/min/mg enzyme for pyrophosphorolytic NADH cleavage2 Publications

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei14 – 141Substrate
    Binding sitei53 – 531Substrate
    Binding sitei137 – 1371Substrate

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi13 – 2210ATPSequence Analysis
    Nucleotide bindingi201 – 2066ATPSequence Analysis

    GO - Molecular functioni

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

    GO - Biological processi

    1. NAD biosynthetic process Source: UniProtKB
    2. NAD metabolic process Source: Reactome
    3. response to wounding Source: Ensembl
    4. small molecule metabolic process Source: Reactome
    5. vitamin metabolic process Source: Reactome
    6. 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

    Enzyme and pathway databases

    BioCyciMetaCyc:HS08953-MONOMER.
    BRENDAi2.7.7.1. 2681.
    ReactomeiREACT_11088. Nicotinate metabolism.
    SABIO-RKQ96T66.
    UniPathwayiUPA00253; UER00600.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nicotinamide mononucleotide adenylyltransferase 3
    Short name:
    NMN adenylyltransferase 3
    Alternative name(s):
    Nicotinate-nucleotide adenylyltransferase 3 (EC:2.7.7.18)
    Short name:
    NaMN adenylyltransferase 3
    Pyridine nucleotide adenylyltransferase 3 (EC:2.7.7.1)
    Short name:
    PNAT-3
    Gene namesi
    Name:NMNAT3
    ORF Names:FKSG76
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:20989. NMNAT3.

    Subcellular locationi

    Mitochondrion 2 Publications

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. mitochondrion Source: UniProtKB

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134952303.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 252252Nicotinamide mononucleotide adenylyltransferase 3PRO_0000135016Add
    BLAST

    Proteomic databases

    MaxQBiQ96T66.
    PaxDbiQ96T66.
    PRIDEiQ96T66.

    PTM databases

    PhosphoSiteiQ96T66.

    Expressioni

    Tissue specificityi

    Expressed in lung and spleen with lower levels in placenta and kidney.2 Publications

    Gene expression databases

    ArrayExpressiQ96T66.
    BgeeiQ96T66.
    CleanExiHS_NMNAT3.
    GenevestigatoriQ96T66.

    Organism-specific databases

    HPAiHPA057402.

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Protein-protein interaction databases

    STRINGi9606.ENSP00000340523.

    Structurei

    Secondary structure

    1
    252
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 139
    Helixi20 – 3516
    Beta strandi37 – 4812
    Beta strandi54 – 563
    Helixi61 – 7111
    Helixi72 – 743
    Beta strandi76 – 805
    Helixi83 – 864
    Beta strandi87 – 893
    Helixi93 – 10412
    Beta strandi129 – 1357
    Helixi136 – 1416
    Turni145 – 1473
    Helixi150 – 15910
    Beta strandi162 – 1654
    Helixi172 – 1787
    Helixi180 – 1845
    Helixi186 – 1883
    Beta strandi189 – 1924
    Helixi202 – 2109
    Helixi221 – 2299
    Turni230 – 2334

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1NUPX-ray1.90A/B1-252[»]
    1NUQX-ray1.90A/B1-252[»]
    1NURX-ray2.15A/B1-252[»]
    1NUSX-ray2.20A/B1-252[»]
    1NUTX-ray1.90A/B1-252[»]
    1NUUX-ray1.90A/B1-252[»]
    ProteinModelPortaliQ96T66.
    SMRiQ96T66. Positions 3-235.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ96T66.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1057.
    HOGENOMiHOG000216047.
    HOVERGENiHBG052640.
    InParanoidiQ96T66.
    KOiK06210.
    OMAiHNIYTEE.
    PhylomeDBiQ96T66.
    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.

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q96T66-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MKSRIPVVLL ACGSFNPITN MHLRMFEVAR DHLHQTGMYQ VIQGIISPVN    50
    DTYGKKDLAA SHHRVAMARL ALQTSDWIRV DPWESEQAQW METVKVLRHH 100
    HSKLLRSPPQ MEGPDHGKAL FSTPAAVPEL KLLCGADVLK TFQTPNLWKD 150
    AHIQEIVEKF GLVCVGRVGH DPKGYIAESP ILRMHQHNIH LAKEPVQNEI 200
    SATYIRRALG QGQSVKYLIP DAVITYIKDH GLYTKGSTWK GKSTQSTEGK 250
    TS 252
    Length:252
    Mass (Da):28,322
    Last modified:October 17, 2006 - v2
    Checksum:i6402CFB2FE789CF4
    GO
    Isoform 2 (identifier: Q96T66-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-37: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:215
    Mass (Da):24,119
    Checksum:i0E445A25C77E1800
    GO
    Isoform 3 (identifier: Q96T66-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         37-125: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:163
    Mass (Da):18,255
    Checksum:i0E9550BF1ADADFF2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti169 – 1691G → S in AAK52726. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3737Missing in isoform 2. 1 PublicationVSP_010267Add
    BLAST
    Alternative sequencei37 – 12589Missing in isoform 3. 1 PublicationVSP_043203Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF345564 mRNA. Translation: AAK52726.1.
    AK123208 mRNA. Translation: BAG53878.1.
    AC046134 Genomic DNA. No translation available.
    AC110716 Genomic DNA. No translation available.
    CH471052 Genomic DNA. Translation: EAW79023.1.
    CH471052 Genomic DNA. Translation: EAW79024.1.
    CH471052 Genomic DNA. Translation: EAW79025.1.
    CH471052 Genomic DNA. Translation: EAW79030.1.
    CH471052 Genomic DNA. Translation: EAW79031.1.
    BC034374 mRNA. Translation: AAH34374.1.
    CCDSiCCDS3111.1. [Q96T66-2]
    CCDS56282.1. [Q96T66-3]
    RefSeqiNP_001186976.1. NM_001200047.1. [Q96T66-3]
    NP_835471.1. NM_178177.3. [Q96T66-2]
    XP_006713691.1. XM_006713628.1. [Q96T66-1]
    XP_006713692.1. XM_006713629.1. [Q96T66-1]
    UniGeneiHs.208673.
    Hs.745268.

    Genome annotation databases

    EnsembliENST00000296202; ENSP00000296202; ENSG00000163864. [Q96T66-1]
    ENST00000339837; ENSP00000340523; ENSG00000163864. [Q96T66-2]
    ENST00000406164; ENSP00000384319; ENSG00000163864. [Q96T66-2]
    ENST00000413939; ENSP00000412953; ENSG00000163864. [Q96T66-3]
    GeneIDi349565.
    KEGGihsa:349565.
    UCSCiuc003etj.3. human. [Q96T66-1]
    uc010hul.3. human. [Q96T66-3]

    Polymorphism databases

    DMDMi116242680.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF345564 mRNA. Translation: AAK52726.1 .
    AK123208 mRNA. Translation: BAG53878.1 .
    AC046134 Genomic DNA. No translation available.
    AC110716 Genomic DNA. No translation available.
    CH471052 Genomic DNA. Translation: EAW79023.1 .
    CH471052 Genomic DNA. Translation: EAW79024.1 .
    CH471052 Genomic DNA. Translation: EAW79025.1 .
    CH471052 Genomic DNA. Translation: EAW79030.1 .
    CH471052 Genomic DNA. Translation: EAW79031.1 .
    BC034374 mRNA. Translation: AAH34374.1 .
    CCDSi CCDS3111.1. [Q96T66-2 ]
    CCDS56282.1. [Q96T66-3 ]
    RefSeqi NP_001186976.1. NM_001200047.1. [Q96T66-3 ]
    NP_835471.1. NM_178177.3. [Q96T66-2 ]
    XP_006713691.1. XM_006713628.1. [Q96T66-1 ]
    XP_006713692.1. XM_006713629.1. [Q96T66-1 ]
    UniGenei Hs.208673.
    Hs.745268.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1NUP X-ray 1.90 A/B 1-252 [» ]
    1NUQ X-ray 1.90 A/B 1-252 [» ]
    1NUR X-ray 2.15 A/B 1-252 [» ]
    1NUS X-ray 2.20 A/B 1-252 [» ]
    1NUT X-ray 1.90 A/B 1-252 [» ]
    1NUU X-ray 1.90 A/B 1-252 [» ]
    ProteinModelPortali Q96T66.
    SMRi Q96T66. Positions 3-235.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000340523.

    PTM databases

    PhosphoSitei Q96T66.

    Polymorphism databases

    DMDMi 116242680.

    Proteomic databases

    MaxQBi Q96T66.
    PaxDbi Q96T66.
    PRIDEi Q96T66.

    Protocols and materials databases

    DNASUi 349565.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000296202 ; ENSP00000296202 ; ENSG00000163864 . [Q96T66-1 ]
    ENST00000339837 ; ENSP00000340523 ; ENSG00000163864 . [Q96T66-2 ]
    ENST00000406164 ; ENSP00000384319 ; ENSG00000163864 . [Q96T66-2 ]
    ENST00000413939 ; ENSP00000412953 ; ENSG00000163864 . [Q96T66-3 ]
    GeneIDi 349565.
    KEGGi hsa:349565.
    UCSCi uc003etj.3. human. [Q96T66-1 ]
    uc010hul.3. human. [Q96T66-3 ]

    Organism-specific databases

    CTDi 349565.
    GeneCardsi GC03M139279.
    HGNCi HGNC:20989. NMNAT3.
    HPAi HPA057402.
    MIMi 608702. gene.
    neXtProti NX_Q96T66.
    PharmGKBi PA134952303.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1057.
    HOGENOMi HOG000216047.
    HOVERGENi HBG052640.
    InParanoidi Q96T66.
    KOi K06210.
    OMAi HNIYTEE.
    PhylomeDBi Q96T66.
    TreeFami TF315035.

    Enzyme and pathway databases

    UniPathwayi UPA00253 ; UER00600 .
    BioCyci MetaCyc:HS08953-MONOMER.
    BRENDAi 2.7.7.1. 2681.
    Reactomei REACT_11088. Nicotinate metabolism.
    SABIO-RK Q96T66.

    Miscellaneous databases

    EvolutionaryTracei Q96T66.
    GenomeRNAii 349565.
    NextBioi 99518.
    PROi Q96T66.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96T66.
    Bgeei Q96T66.
    CleanExi HS_NMNAT3.
    Genevestigatori Q96T66.

    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. "Identification of FKSG76, a novel gene encoding a NMN adenylyltransferase."
      Wang Y.-G., Gong L.
      Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "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] (ISOFORM 3).
      Tissue: Brain cortex.
    3. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORM 2).
      Tissue: Colon and Kidney.
    6. "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: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    7. "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.
    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: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH NMN; NAD AND ATP ANALOG, SUBCELLULAR LOCATION, SUBUNIT, TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiNMNA3_HUMAN
    AccessioniPrimary (citable) accession number: Q96T66
    Secondary accession number(s): B3KVR6
    , D3DNF2, D3DNF3, Q8N4G1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 10, 2004
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 110 of the entry and version 2 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, Reference proteome

    Documents

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

    External Data

    Dasty 3