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    ZDHHC17 zinc finger DHHC-type palmitoyltransferase 17 [ Homo sapiens (human) ]

    Gene ID: 23390, updated on 14-Nov-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Activation of JNK and p38 MAPK Mediated by ZDHHC17 Drives Glioblastoma Multiforme Development and Malignant Progression.

    Activation of JNK and p38 MAPK Mediated by ZDHHC17 Drives Glioblastoma Multiforme Development and Malignant Progression.
    Chen X, Hao A, Li X, Ye K, Zhao C, Yang H, Ma H, Hu L, Zhao Z, Hu L, Ye F, Sun Q, Zhang H, Wang H, Yao X, Fang Z., Free PMC Article

    04/13/2021
    Data reveal the structural basis of interaction between DHHC17, and SNAP25b, a canonical substrate. These results show the role of critical residues for substrate binding and palmitate transfer and the involvement of the same residues in binding Huntingtin, another important substrate of DHHC17.

    Structural Basis for Substrate Recognition by the Ankyrin Repeat Domain of Human DHHC17 Palmitoyltransferase.
    Verardi R, Kim JS, Ghirlando R, Banerjee A., Free PMC Article

    03/17/2018
    The large number of zDABM sequences within the human proteome suggests that zDHHC17 may be an interaction hub regulating many cellular processes.

    Peptide array-based screening reveals a large number of proteins interacting with the ankyrin-repeat domain of the zDHHC17 S-acyltransferase.
    Lemonidis K, MacLeod R, Baillie GS, Chamberlain LH., Free PMC Article

    10/28/2017
    CPj0783 might cause abnormal vesicle-mediated transport by interacting with HIP14.

    Chlamydia pneumoniae CPj0783 interaction with Huntingtin-protein14.
    Yanatori I, Yasui Y, Ouchi K, Kishi F.

    03/4/2017
    This suggests that altered HIP14-HTT and HIP14L-HTT interactions in the presence of the HD mutation reduces palmitoylation and promotes mislocalization of HTT and other HIP14/HIP14L substrates

    Aberrant palmitoylation in Huntington disease.
    Sanders SS, Hayden MR.

    01/2/2016
    Data show that deletion of huntingtin protein (HTT) amino acids 1-427 abolishes the interaction of HTT with palmitoyl acyltransferases huntingtin interacting protein 14 (HIP14) and huntingtin interacting protein 14-like (HIP14L).

    Identification of binding sites in Huntingtin for the Huntingtin Interacting Proteins HIP14 and HIP14L.
    Sanders SS, Mui KK, Sutton LM, Hayden MR., Free PMC Article

    06/27/2015
    HIP14 shares a high proportion of interactors with HTT resulting in defective palmitoylation of the target proteins which might be an important mechanism towards pathogenesis of Huntington's disease.

    The palmitoyl acyltransferase HIP14 shares a high proportion of interactors with huntingtin: implications for a role in the pathogenesis of Huntington's disease.
    Butland SL, Sanders SS, Schmidt ME, Riechers SP, Lin DT, Martin DD, Vaid K, Graham RK, Singaraja RR, Wanker EE, Conibear E, Hayden MR., Free PMC Article

    02/21/2015
    DHHC17 is a ClipR-59 palmitoyltransferase that modulates ClipR-59 plasma membrane binding.

    DHHC17 palmitoylates ClipR-59 and modulates ClipR-59 association with the plasma membrane.
    Ren W, Sun Y, Du K., Free PMC Article

    12/14/2013
    Low levels of human HIP14 are sufficient to rescue neuropathological, behavioural, and enzymatic defects due to loss of murine HIP14 in Hip14-/- mice.

    Low levels of human HIP14 are sufficient to rescue neuropathological, behavioural, and enzymatic defects due to loss of murine HIP14 in Hip14-/- mice.
    Young FB, Franciosi S, Spreeuw A, Deng Y, Sanders S, Tam NC, Huang K, Singaraja RR, Zhang W, Bissada N, Kay C, Hayden MR., Free PMC Article

    10/13/2012
    Immunohistochemical analysis of pancreatic sections demonstrated that HIP14 is almost exclusively expressed in insulin-positive cells in islets of Langerhans.

    Huntingtin-interacting protein 14 is a type 1 diabetes candidate protein regulating insulin secretion and beta-cell apoptosis.
    Berchtold LA, Størling ZM, Ortis F, Lage K, Bang-Berthelsen C, Bergholdt R, Hald J, Brorsson CA, Eizirik DL, Pociot F, Brunak S, Størling J., Free PMC Article

    11/12/2011
    Novel peptides have been developed that target the jun N-terminus kinase (JNK)-interacting motif on zD17 to selectively block enhancement of the zD17-Jun N terminus kinase (JNK) interaction and the activation of JNK isoforms 2 and 3.

    Palmitoyl acyltransferase zD17 mediates neuronal responses in acute ischemic brain injury by regulating JNK activation in a signaling module.
    Yang G, Cynader MS., Free PMC Article

    10/15/2011
    a subset of DHHCs controls STREX palmitoylation and function; DHHC17 may preferentially target cysteine-rich domains

    Multiple palmitoyltransferases are required for palmitoylation-dependent regulation of large conductance calcium- and voltage-activated potassium channels.
    Tian L, McClafferty H, Jeffries O, Shipston MJ., Free PMC Article

    09/20/2010
    Coexpression of an independent palmitoyl acyltransferase (HIP14) with the GODZ-DHHS mutant also rescued Ca(2+) transport.

    Golgi-specific DHHC zinc finger protein GODZ mediates membrane Ca2+ transport.
    Hines RM, Kang R, Goytain A, Quamme GA., Free PMC Article

    05/31/2010
    The ankyrin repeat domain of Huntingtin interacting protein 14 contains a surface aromatic cage, a potential site for methyl-lysine binding.

    The ankyrin repeat domain of Huntingtin interacting protein 14 contains a surface aromatic cage, a potential site for methyl-lysine binding.
    Gao T, Collins RE, Horton JR, Zhang X, Zhang R, Dhayalan A, Tamas R, Jeltsch A, Cheng X., Free PMC Article

    01/21/2010
    huntingtin interacting protein genes, HIP14 and HIP14L, encode Mg2+ transport proteins that are regulated by their innate palmitoyl acyltransferases thus fulfilling the characteristics of "chanzymes."

    Huntingtin-interacting proteins, HIP14 and HIP14L, mediate dual functions, palmitoyl acyltransferase and Mg2+ transport.
    Goytain A, Hines RM, Quamme GA., Free PMC Article

    01/21/2010
    Observational study of gene-disease association. (HuGE Navigator)

    Genetic analysis of candidate genes modifying the age-at-onset in Huntington's disease.
    Metzger S, Bauer P, Tomiuk J, Laccone F, Didonato S, Gellera C, Mariotti C, Lange HW, Weirich-Schwaiger H, Wenning GK, Seppi K, Melegh B, Havasi V, Balikó L, Wieczorek S, Zaremba J, Hoffman-Zacharska D, Sulek A, Basak AN, Soydan E, Zidovska J, Kebrdlova V, Pandolfo M, Ribaï P, Kadasi L, Kvasnicova M, Weber BH, Kreuz F, Dose M, Stuhrmann M, Riess O.

    03/13/2008
    has the ability to induce colony formation in cell culture, anchorage-independent growth, and tumors in mice

    Huntingtin interacting protein 14 is an oncogenic human protein: palmitoyl acyltransferase.
    Ducker CE, Stettler EM, French KJ, Upson JJ, Smith CD, Ducker CE, Stettler EM, French KJ, Upson JJ, Smith CD., Free PMC Articles: PMC2908390, PMC2908390

    01/21/2010
    HIP14 is a protein: palmitoyl acyltransferase

    Huntingtin interacting protein 14 is an oncogenic human protein: palmitoyl acyltransferase.
    Ducker CE, Stettler EM, French KJ, Upson JJ, Smith CD, Ducker CE, Stettler EM, French KJ, Upson JJ, Smith CD., Free PMC Articles: PMC2908390, PMC2908390

    06/3/2005
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