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    NAGK N-acetylglucosamine kinase [ Homo sapiens (human) ]

    Gene ID: 55577, updated on 2-Nov-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    The Immunometabolic Gene N-Acetylglucosamine Kinase Is Uniquely Involved in the Heritability of Multiple Sclerosis Severity.

    The Immunometabolic Gene N-Acetylglucosamine Kinase Is Uniquely Involved in the Heritability of Multiple Sclerosis Severity.
    Nataf S, Guillen M, Pays L., Free PMC Article

    05/21/2024
    N-Acetylglucosamine Kinase-Small Nuclear Ribonucleoprotein Polypeptide N Interaction Promotes Axodendritic Branching in Neurons via Dynein-Mediated Microtubule Transport.

    N-Acetylglucosamine Kinase-Small Nuclear Ribonucleoprotein Polypeptide N Interaction Promotes Axodendritic Branching in Neurons via Dynein-Mediated Microtubule Transport.
    Timalsina B, Choi HJ, Moon IS., Free PMC Article

    08/3/2023
    Glutamine deprivation triggers NAGK-dependent hexosamine salvage.

    Glutamine deprivation triggers NAGK-dependent hexosamine salvage.
    Campbell S, Mesaros C, Izzo L, Affronti H, Noji M, Schaffer BE, Tsang T, Sun K, Trefely S, Kruijning S, Blenis J, Blair IA, Wellen KE., Free PMC Article

    12/18/2021
    Implementation of the plasma MYCN/NAGK ratio to detect MYCN amplification in patients with neuroblastoma.

    Implementation of the plasma MYCN/NAGK ratio to detect MYCN amplification in patients with neuroblastoma.
    Su Y, Wang L, Zhao Q, Yue Z, Zhao W, Wang X, Duan C, Jin M, Zhang D, Chen S, Yin J, Qiu L, Cheng X, Xu Z, Ma X., Free PMC Article

    11/13/2021
    N-Acetyl-D-Glucosamine Kinase Interacts with NudC and Lis1 in Dynein Motor Complex and Promotes Cell Migration.

    N-Acetyl-D-Glucosamine Kinase Interacts with NudC and Lis1 in Dynein Motor Complex and Promotes Cell Migration.
    Islam MA, Choi HJ, Dash R, Sharif SR, Oktaviani DF, Seog DH, Moon IS., Free PMC Article

    09/18/2021
    In a screen for human kinases that regulate Xenopus laevis embryogenesis, we identified Nagk and other components of the UDP-GlcNAc glycosylation salvage pathway as regulators of anteroposterior patterning and Wnt signaling.

    Developmental regulation of Wnt signaling by Nagk and the UDP-GlcNAc salvage pathway.
    Neitzel LR, Spencer ZT, Nayak A, Cselenyi CS, Benchabane H, Youngblood CQ, Zouaoui A, Ng V, Stephens L, Hann T, Patton JG, Robbins D, Ahmed Y, Lee E., Free PMC Article

    08/24/2019
    results indicate that the NAGK-dynein interaction with the involvements of Lis1 and NudE1 plays an important role in prophase nuclear envelope breakdown (NEB) and metaphase MT-KT attachment during eukaryotic cell division.

    N-Acetyl-D-Glucosamine Kinase Interacts with Dynein-Lis1-NudE1 Complex and Regulates Cell Division.
    Sharif SR, Islam A, Moon IS., Free PMC Article

    04/29/2017
    Data shows associations between NAGK, speckle, paraspeckle and general transcription factor suggesting its regulatory roles in gene expression.

    N-acetyl-D-glucosamine kinase is a component of nuclear speckles and paraspeckles.
    Sharif SR, Lee H, Islam MA, Seog DH, Moon IS., Free PMC Article

    03/19/2016
    Participants with homozygous mutations in the N-acetylmannosamine kinase (GNK) domain have an earlier disease onset than heterozygous participants with mutations in the uridine diphosphate-N-acetylglucosamine 2-epimerase (GNE) and GNK domains.

    Heterozygous UDP-GlcNAc 2-epimerase and N-acetylmannosamine kinase domain mutations in the GNE gene result in a less severe GNE myopathy phenotype compared to homozygous N-acetylmannosamine kinase domain mutations.
    Mori-Yoshimura M, Monma K, Suzuki N, Aoki M, Kumamoto T, Tanaka K, Tomimitsu H, Nakano S, Sonoo M, Shimizu J, Sugie K, Nakamura H, Oya Y, Hayashi YK, Malicdan MC, Noguchi S, Murata M, Nishino I.

    03/30/2013
    Phosphorylation of Tyr205 may modulate GlcNAc kinase activity and/or specificity.

    Structures of human N-Acetylglucosamine kinase in two complexes with N-Acetylglucosamine and with ADP/glucose: insights into substrate specificity and regulation.
    Weihofen WA, Berger M, Chen H, Saenger W, Hinderlich S.

    01/21/2010
    The cell-free system was validated for MNK activity, and it revealed that mutations in one enzymatic domain (in MNK, A631V, M712T) affected not only that domain's enzyme activity, but also the activity of the other domain.

    Use of a cell-free system to determine UDP-N-acetylglucosamine 2-epimerase and N-acetylmannosamine kinase activities in human hereditary inclusion body myopathy.
    Sparks SE, Ciccone C, Lalor M, Orvisky E, Klootwijk R, Savelkoul PJ, Dalakas MC, Krasnewich DM, Gahl WA, Huizing M.

    01/21/2010
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