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P58058

- NADK_MOUSE

UniProt

P58058 - NADK_MOUSE

Protein

NAD kinase

Gene

Nadk

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    ATP + NAD+ = ADP + NADP+.

    Cofactori

    Divalent metal cations.By similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. NAD+ kinase activity Source: UniProtKB

    GO - Biological processi

    1. NAD metabolic process Source: InterPro
    2. NADP biosynthetic process Source: InterPro

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Metal-binding, NAD, NADP, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_209575. Nicotinate metabolism.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NAD kinase (EC:2.7.1.23)
    Alternative name(s):
    Poly(P)/ATP NAD kinase
    Gene namesi
    Name:Nadk
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:2183149. Nadk.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: UniProtKB

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 439439NAD kinasePRO_0000120714Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei46 – 461PhosphoserineBy similarity
    Modified residuei48 – 481PhosphoserineBy similarity
    Modified residuei50 – 501PhosphoserineBy similarity
    Modified residuei64 – 641PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP58058.
    PaxDbiP58058.
    PRIDEiP58058.

    PTM databases

    PhosphoSiteiP58058.

    Expressioni

    Gene expression databases

    ArrayExpressiP58058.
    BgeeiP58058.
    CleanExiMM_NADK.
    GenevestigatoriP58058.

    Interactioni

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000030939.

    Structurei

    3D structure databases

    ProteinModelPortaliP58058.
    SMRiP58058. Positions 72-422.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi322 – 3298Poly-Ala

    Sequence similaritiesi

    Belongs to the NAD kinase family.Curated

    Phylogenomic databases

    eggNOGiCOG0061.
    GeneTreeiENSGT00390000013792.
    HOGENOMiHOG000176769.
    HOVERGENiHBG008249.
    InParanoidiQ3TCP7.
    KOiK00858.
    OMAiQTIMHIQ.
    OrthoDBiEOG7ZPNJT.
    TreeFamiTF324076.

    Family and domain databases

    Gene3Di2.60.200.30. 1 hit.
    3.40.50.10330. 1 hit.
    HAMAPiMF_00361. NAD_kinase.
    InterProiIPR017438. ATP-NAD_kinase_dom_1.
    IPR016064. ATP-NAD_kinase_PpnK-typ.
    IPR017437. ATP-NAD_kinase_PpnK-typ_all-b.
    IPR002504. PolyP/ATP_NADK.
    [Graphical view]
    PANTHERiPTHR20275. PTHR20275. 1 hit.
    PfamiPF01513. NAD_kinase. 1 hit.
    [Graphical view]
    SUPFAMiSSF111331. SSF111331. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P58058-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEMEQEKMNL SQELSADSAS YNCSACHGDE TWSYNHPIRG RAKSRSLSAS    50
    PALGSTKEFR RTRSLHGPCP VTTFGPKACV LQNPQTIMHI QDPASQRLTW 100
    NKSPKSVLVI KKIRDASLLQ PFKELCIYLM EENNMIVYVE KKVLEDPAIV 150
    SDENFGPVKK KFCTFREDYD DISNQIDFII CLGGDGTLLY ASSLFQGSVP 200
    PVMAFHLGSL GFLTPFNFEN FQSQVNQVIE GNAAVILRSR LKVRVVKEPR 250
    DKKTAIHNGL SENGLDTEGG KQAMQYQVLN EVVIDRGPSS YLSNVDVYLD 300
    GHLITTVQGD GVIVSTPTGS TAYAAAAGAS MVHPNVPAIM VTPICPHSLS 350
    FRPIVVPAGV ELKIMLSPEA RNTAWVSFDG RKRQEIRHGD SISITTSCYP 400
    LPSICVCDPV SDWFESLAQC LHWNVRKKQA HFPEDEEDS 439
    Length:439
    Mass (Da):48,597
    Last modified:July 27, 2011 - v2
    Checksum:iC3AFA7CDC3F0BF9C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti430 – 4301A → V in AAH04012. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK170095 mRNA. Translation: BAE41560.1.
    AK170608 mRNA. Translation: BAE41908.1.
    AK170960 mRNA. Translation: BAE42141.1.
    BC004012 mRNA. Translation: AAH04012.1.
    AL627405 Genomic DNA. Translation: CAM16741.1.
    CH466594 Genomic DNA. Translation: EDL15013.1.
    CCDSiCCDS19031.1.
    RefSeqiNP_001153109.1. NM_001159637.1.
    NP_619612.2. NM_138671.2.
    XP_006538725.1. XM_006538662.1.
    XP_006538726.1. XM_006538663.1.
    UniGeneiMm.28347.

    Genome annotation databases

    EnsembliENSMUST00000030939; ENSMUSP00000030939; ENSMUSG00000029063.
    ENSMUST00000105613; ENSMUSP00000101238; ENSMUSG00000029063.
    GeneIDi192185.
    KEGGimmu:192185.
    UCSCiuc008wdt.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK170095 mRNA. Translation: BAE41560.1 .
    AK170608 mRNA. Translation: BAE41908.1 .
    AK170960 mRNA. Translation: BAE42141.1 .
    BC004012 mRNA. Translation: AAH04012.1 .
    AL627405 Genomic DNA. Translation: CAM16741.1 .
    CH466594 Genomic DNA. Translation: EDL15013.1 .
    CCDSi CCDS19031.1.
    RefSeqi NP_001153109.1. NM_001159637.1.
    NP_619612.2. NM_138671.2.
    XP_006538725.1. XM_006538662.1.
    XP_006538726.1. XM_006538663.1.
    UniGenei Mm.28347.

    3D structure databases

    ProteinModelPortali P58058.
    SMRi P58058. Positions 72-422.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000030939.

    PTM databases

    PhosphoSitei P58058.

    Proteomic databases

    MaxQBi P58058.
    PaxDbi P58058.
    PRIDEi P58058.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000030939 ; ENSMUSP00000030939 ; ENSMUSG00000029063 .
    ENSMUST00000105613 ; ENSMUSP00000101238 ; ENSMUSG00000029063 .
    GeneIDi 192185.
    KEGGi mmu:192185.
    UCSCi uc008wdt.2. mouse.

    Organism-specific databases

    CTDi 65220.
    MGIi MGI:2183149. Nadk.

    Phylogenomic databases

    eggNOGi COG0061.
    GeneTreei ENSGT00390000013792.
    HOGENOMi HOG000176769.
    HOVERGENi HBG008249.
    InParanoidi Q3TCP7.
    KOi K00858.
    OMAi QTIMHIQ.
    OrthoDBi EOG7ZPNJT.
    TreeFami TF324076.

    Enzyme and pathway databases

    Reactomei REACT_209575. Nicotinate metabolism.

    Miscellaneous databases

    ChiTaRSi NADK. mouse.
    NextBioi 371192.
    PROi P58058.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P58058.
    Bgeei P58058.
    CleanExi MM_NADK.
    Genevestigatori P58058.

    Family and domain databases

    Gene3Di 2.60.200.30. 1 hit.
    3.40.50.10330. 1 hit.
    HAMAPi MF_00361. NAD_kinase.
    InterProi IPR017438. ATP-NAD_kinase_dom_1.
    IPR016064. ATP-NAD_kinase_PpnK-typ.
    IPR017437. ATP-NAD_kinase_PpnK-typ_all-b.
    IPR002504. PolyP/ATP_NADK.
    [Graphical view ]
    PANTHERi PTHR20275. PTHR20275. 1 hit.
    Pfami PF01513. NAD_kinase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF111331. SSF111331. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: NOD.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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].
    5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiNADK_MOUSE
    AccessioniPrimary (citable) accession number: P58058
    Secondary accession number(s): Q3TCP7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 4, 2001
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 93 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3