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    SPRTN SprT-like N-terminal domain [ Homo sapiens (human) ]

    Gene ID: 83932, updated on 10-Aug-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    SPRTN is involved in hepatocellular carcinoma development through the ER stress response.

    SPRTN is involved in hepatocellular carcinoma development through the ER stress response.
    Batel A, Polović M, Glumac M, Šuman O, Jadrijević S, Lozić B, Petrović M, Samardžija B, Bradshaw NJ, Skube K, Palada V, Acman M, Marinović Terzić I.

    03/18/2024
    SPRTN patient variants cause global-genome DNA-protein crosslink repair defects.

    SPRTN patient variants cause global-genome DNA-protein crosslink repair defects.
    Weickert P, Li HY, Götz MJ, Dürauer S, Yaneva D, Zhao S, Cordes J, Acampora AC, Forne I, Imhof A, Stingele J., Free PMC Article

    03/10/2023
    Ubiquitin-directed AAA+ ATPase p97/VCP unfolds stable proteins crosslinked to DNA for proteolysis by SPRTN.

    Ubiquitin-directed AAA+ ATPase p97/VCP unfolds stable proteins crosslinked to DNA for proteolysis by SPRTN.
    Kröning A, van den Boom J, Kracht M, Kueck AF, Meyer H., Free PMC Article

    07/2/2022
    The protease SPRTN and SUMOylation coordinate DNA-protein crosslink repair to prevent genome instability.

    The protease SPRTN and SUMOylation coordinate DNA-protein crosslink repair to prevent genome instability.
    Ruggiano A, Vaz B, Kilgas S, Popović M, Rodriguez-Berriguete G, Singh AN, Higgins GS, Kiltie AE, Ramadan K., Free PMC Article

    02/19/2022
    Replication-dependent cytotoxicity and Spartan-mediated repair of trapped PARP1-DNA complexes.

    Replication-dependent cytotoxicity and Spartan-mediated repair of trapped PARP1-DNA complexes.
    Saha LK, Murai Y, Saha S, Jo U, Tsuda M, Takeda S, Pommier Y., Free PMC Article

    12/18/2021
    SPRTN protease-cleaved MRE11 decreases DNA repair and radiosensitises cancer cells.

    SPRTN protease-cleaved MRE11 decreases DNA repair and radiosensitises cancer cells.
    Na J, Newman JA, Then CK, Syed J, Vendrell I, Torrecilla I, Ellermann S, Ramadan K, Fischer R, Kiltie AE., Free PMC Article

    09/18/2021
    USP11 mediates repair of DNA-protein cross-links by deubiquitinating SPRTN metalloprotease.

    USP11 mediates repair of DNA-protein cross-links by deubiquitinating SPRTN metalloprotease.
    Perry M, Biegert M, Kollala SS, Mallard H, Su G, Kodavati M, Kreiling N, Holbrook A, Ghosal G., Free PMC Article

    09/11/2021
    A ubiquitin switch controls autocatalytic inactivation of the DNA-protein crosslink repair protease SPRTN.

    A ubiquitin switch controls autocatalytic inactivation of the DNA-protein crosslink repair protease SPRTN.
    Zhao S, Kieser A, Li HY, Reinking HK, Weickert P, Euteneuer S, Yaneva D, Acampora AC, Götz MJ, Feederle R, Stingele J., Free PMC Article

    02/6/2021
    DNA Structure-Specific Cleavage of DNA-Protein Crosslinks by the SPRTN Protease.

    DNA Structure-Specific Cleavage of DNA-Protein Crosslinks by the SPRTN Protease.
    Reinking HK, Kang HS, Götz MJ, Li HY, Kieser A, Zhao S, Acampora AC, Weickert P, Fessler E, Jae LT, Sattler M, Stingele J., Free PMC Article

    10/24/2020
    TEX264 recognises both unmodified and SUMO1-modifed TOP1 and initiates TOP1cc repair by recruiting p97 and SPRTN.

    TEX264 coordinates p97- and SPRTN-mediated resolution of topoisomerase 1-DNA adducts.
    Fielden J, Wiseman K, Torrecilla I, Li S, Hume S, Chiang SC, Ruggiano A, Narayan Singh A, Freire R, Hassanieh S, Domingo E, Vendrell I, Fischer R, Kessler BM, Maughan TS, El-Khamisy SF, Ramadan K., Free PMC Article

    07/4/2020
    the ZBD contributes to the ssDNA specificity of SPRTN, restricts the access of globular substrates, and positions DPCs, which may need to be partially unfolded, for optimal cleavage.

    Structural Insight into DNA-Dependent Activation of Human Metalloprotease Spartan.
    Li F, Raczynska JE, Chen Z, Yu H.

    05/2/2020
    e show that SPRTN is a DNA-dependent mammalian protease required for resolving cytotoxic DNA-protein crosslinks (DPCs)- a function that had only been attributed to the metalloprotease Wss1 in budding yeast. We provide genetic evidence that SPRTN and Wss1 function distinctly in vivo to resolve DPCs

    SPRTN is a mammalian DNA-binding metalloprotease that resolves DNA-protein crosslinks.
    Lopez-Mosqueda J, Maddi K, Prgomet S, Kalayil S, Marinovic-Terzic I, Terzic J, Dikic I., Free PMC Article

    11/26/2017
    SPRTN protease represents a specialized DNA replication-coupled DPC repair pathway essential for DNA replication progression and genome stability.

    Metalloprotease SPRTN/DVC1 Orchestrates Replication-Coupled DNA-Protein Crosslink Repair.
    Vaz B, Popovic M, Newman JA, Fielden J, Aitkenhead H, Halder S, Singh AN, Vendrell I, Fischer R, Torrecilla I, Drobnitzky N, Freire R, Amor DJ, Lockhart PJ, Kessler BM, McKenna GW, Gileadi O, Ramadan K., Free PMC Article

    09/2/2017
    Loss of SPRTN results in failure to repair DNA-protein crosslinks (DPCs) and hypersensitivity to DPC-inducing agents.

    Mechanism and Regulation of DNA-Protein Crosslink Repair by the DNA-Dependent Metalloprotease SPRTN.
    Stingele J, Bellelli R, Alte F, Hewitt G, Sarek G, Maslen SL, Tsutakawa SE, Borg A, Kjær S, Tainer JA, Skehel JM, Groll M, Boulton SJ., Free PMC Article

    09/2/2017
    Spartan has a DNA-dependent protease activity degrading certain proteins bound to DNA.

    DNA-dependent protease activity of human Spartan facilitates replication of DNA-protein crosslink-containing DNA.
    Mórocz M, Zsigmond E, Tóth R, Enyedi MZ, Pintér L, Haracska L., Free PMC Article

    08/26/2017
    DNA binding by SPARTAN regulates the targeting of Poleta to damage sites after UV exposure, and this function contributes highly to its DNA-damage tolerance function.

    The DNA-binding box of human SPARTAN contributes to the targeting of Polη to DNA damage sites.
    Toth A, Hegedus L, Juhasz S, Haracska L, Burkovics P.

    07/29/2017
    These findings offer new insights into the determinants of PIP box for PCNA binding.

    Crystal structure of human PCNA in complex with the PIP box of DVC1.
    Wang Y, Xu M, Jiang T.

    05/13/2017
    USP1, p21 and Spartan are translesion DNA synthesis regulators. (Review)

    The identification of translesion DNA synthesis regulators: Inhibitors in the spotlight.
    Bertolin AP, Mansilla SF, Gottifredi V., Free PMC Article

    04/30/2016
    Mutations in SPRTN cause early onset hepatocellular carcinoma, genomic instability and progeroid features.

    Mutations in SPRTN cause early onset hepatocellular carcinoma, genomic instability and progeroid features.
    Lessel D, Vaz B, Halder S, Lockhart PJ, Marinovic-Terzic I, Lopez-Mosqueda J, Philipp M, Sim JC, Smith KR, Oehler J, Cabrera E, Freire R, Pope K, Nahid A, Norris F, Leventer RJ, Delatycki MB, Barbi G, von Ameln S, Högel J, Degoricija M, Fertig R, Burkhalter MD, Hofmann K, Thiele H, Altmüller J, Nürnberg G, Nürnberg P, Bahlo M, Martin GM, Aalfs CM, Oshima J, Terzic J, Amor DJ, Dikic I, Ramadan K, Kubisch C., Free PMC Article

    01/24/2015
    The results suggest that Spartan negatively regulates POLD3 function in Rev1/Pol zeta-dependent translesion synthesis.

    Regulation of error-prone translesion synthesis by Spartan/C1orf124.
    Kim MS, Machida Y, Vashisht AA, Wohlschlegel JA, Pang YP, Machida YJ., Free PMC Article

    04/20/2013
    Spartan is recruited to sites of stalled replication via ubiquitinated PCNA and plays an important role to prevent mutations associated with replication of damaged DNA.

    Spartan/C1orf124 is important to prevent UV-induced mutagenesis.
    Machida Y, Kim MS, Machida YJ., Free PMC Article

    02/9/2013
    Authors propose that Spartan promotes genomic stability by regulating the choice of rescue of stalled replication fork, whose mechanism includes its interaction with ubiquitin-conjugated PCNA and protection against PCNA deubiquitylation.

    Characterization of human Spartan/C1orf124, an ubiquitin-PCNA interacting regulator of DNA damage tolerance.
    Juhasz S, Balogh D, Hajdu I, Burkovics P, Villamil MA, Zhuang Z, Haracska L., Free PMC Article

    02/2/2013
    DVC1 (C1orf124) recruits the p97 protein segregase to sites of DNA damage.

    DVC1 (C1orf124) recruits the p97 protein segregase to sites of DNA damage.
    Davis EJ, Lachaud C, Appleton P, Macartney TJ, Näthke I, Rouse J.

    01/26/2013
    DVC1 (C1orf124) is a DNA damage-targeting p97 adaptor that promotes ubiquitin-dependent responses to replication blocks.

    DVC1 (C1orf124) is a DNA damage-targeting p97 adaptor that promotes ubiquitin-dependent responses to replication blocks.
    Mosbech A, Gibbs-Seymour I, Kagias K, Thorslund T, Beli P, Povlsen L, Nielsen SV, Smedegaard S, Sedgwick G, Lukas C, Hartmann-Petersen R, Lukas J, Choudhary C, Pocock R, Bekker-Jensen S, Mailand N.

    01/26/2013
    C1orf124 acts at multiple steps in TLS, stabilizes RAD18 and ubiquitinated PCNA at damage sites, and facilitates the switch from replicative to TLS polymerase to bypass DNA lesion.

    Proliferating cell nuclear antigen (PCNA)-binding protein C1orf124 is a regulator of translesion synthesis.
    Ghosal G, Leung JW, Nair BC, Fong KW, Chen J., Free PMC Article

    01/5/2013
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