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    CALML5 calmodulin like 5 [ Homo sapiens (human) ]

    Gene ID: 51806, updated on 7-Apr-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Identification of lactylation gene CALML5 and its correlated lncRNAs in cutaneous melanoma by machine learning.

    Identification of lactylation gene CALML5 and its correlated lncRNAs in cutaneous melanoma by machine learning.
    Feng H, Chen W, Zhang C., Free PMC Article

    12/1/2023
    CALML5 is a novel diagnostic marker for differentiating thymic squamous cell carcinoma from type B3 thymoma.

    CALML5 is a novel diagnostic marker for differentiating thymic squamous cell carcinoma from type B3 thymoma.
    Kanamori K, Suina K, Shukuya T, Takahashi F, Hayashi T, Hara K, Saito T, Mitsuishi Y, Shimamura SS, Winardi W, Tajima K, Ko R, Mimori T, Asao T, Itoh M, Kawaji H, Suehara Y, Takamochi K, Suzuki K, Takahashi K., Free PMC Article

    04/28/2023
    Identification of calmodulin-like protein 5 as tumor-suppressor gene silenced during early stage of carcinogenesis in squamous cell carcinoma of uterine cervix.

    Identification of calmodulin-like protein 5 as tumor-suppressor gene silenced during early stage of carcinogenesis in squamous cell carcinoma of uterine cervix.
    Kitazawa S, Takaoka Y, Ueda Y, Kitazawa R.

    09/18/2021
    The authors results suggest that CLSP may function as a senescence-suppressing factor in keratinocytes.

    Calmodulin-like skin protein suppresses the increase in senescence-associated β-galactosidase induced by hydrogen peroxide or ultraviolet irradiation in keratinocytes.
    Takahara Y, Miyachi N, Nawa M, Matsuoka M.

    10/26/2019
    CALML5 interacts with SFN in suprabasal epidermis, cocontrols 13% of late differentiation genes, and modulates interaction of SFN to some of its binding partners.

    CALML5 is a ZNF750- and TINCR-induced protein that binds stratifin to regulate epidermal differentiation.
    Sun BK, Boxer LD, Ransohoff JD, Siprashvili Z, Qu K, Lopez-Pajares V, Hollmig ST, Khavari PA., Free PMC Article

    02/27/2016
    CLSP is increased in the upper epidermis in exacerbated atopic dermatitis as compared to non-exacerbated atopic dermatitis and normal skin, revealing a role in re-establishing the epidermal barrier

    Calmodulin-like skin protein level increases in the differentiated epidermal layers in atopic dermatitis.
    Donovan M, Ambach A, Thomas-Collignon A, Prado C, Bernard D, Jammayrac O, Gollnick H, de Lacharriere O.

    07/19/2014
    Ubiquitination of CALML5 in the nucleus is involved in the carcinogenesis of breast cancer in premenopausal women.

    Specific expression of k63-linked ubiquitination of calmodulin-like protein 5 in breast cancer of premenopausal patients.
    Debald M, Schildberg FA, Linke A, Walgenbach K, Kuhn W, Hartmann G, Walgenbach-Brünagel G.

    01/25/2014
    CLSP is a physiological heterotrimeric humanin receptor agonist.

    Secreted calmodulin-like skin protein inhibits neuronal death in cell-based Alzheimer's disease models via the heterotrimeric Humanin receptor.
    Hashimoto Y, Nawa M, Kurita M, Tokizawa M, Iwamatsu A, Matsuoka M., Free PMC Article

    08/31/2013
    An investigation of the cation-binding properties of CLSP and the ensuing conformational changes finds that, with its high- and low-affinity Ca+2+-binding sites and a pronounced effect of Mg2+, CLSP is more similar to troponin C than to calmodulin.

    Cation- and peptide-binding properties of human calmodulin-like skin protein.
    Durussel I, Méhul B, Bernard D, Schmidt R, Cox JA.

    01/21/2010
    abnormal elevated levels of CLSP, characteristic of psoriatic epidermis, were probably not due to an overexpression of the protein, but most likely the result of its non-degradation

    Influence of calcium on the proteolytic degradation of the calmodulin-like skin protein (calmodulin-like protein 5) in psoriatic epidermis.
    Méhul B, Bernard D, Brouard M, Delattre C, Schmidt R.

    01/21/2010
    The structure and dynamics of human calmodulin-like skin protein (CLSP) have been characterized by NMR spectroscopy.

    A structural and dynamic characterization of the EF-hand protein CLSP.
    Babini E, Bertini I, Capozzi F, Chirivino E, Luchinat C.

    01/21/2010
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