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    PSMA3 proteasome 20S subunit alpha 3 [ Homo sapiens (human) ]

    Gene ID: 5684, updated on 17-Jun-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Immuno-oncological role of 20S proteasome alpha-subunit 3 in aggravating the progression of esophageal squamous cell carcinoma.

    Immuno-oncological role of 20S proteasome alpha-subunit 3 in aggravating the progression of esophageal squamous cell carcinoma.
    Liu J, Shao J, Zhang C, Qin G, Liu J, Li M, Wu P, Zhao X, Zhang Y.

    02/12/2022
    LncRNA PSMA3-AS1 promotes cell proliferation, migration, and invasion in ovarian cancer by activating the PI3K/Akt pathway via the miR-378a-3p/GALNT3 axis.

    LncRNA PSMA3-AS1 promotes cell proliferation, migration, and invasion in ovarian cancer by activating the PI3K/Akt pathway via the miR-378a-3p/GALNT3 axis.
    Xu Z, Jin H, Duan X, Liu H, Zhao X, Fan S, Wang Y, Yao T.

    11/22/2021
    Structural Fluctuations of the Human Proteasome alpha7 Homo-Tetradecamer Double Ring Imply the Proteasomal alpha-Ring Assembly Mechanism.

    Structural Fluctuations of the Human Proteasome α7 Homo-Tetradecamer Double Ring Imply the Proteasomal α-Ring Assembly Mechanism.
    Song C, Satoh T, Sekiguchi T, Kato K, Murata K., Free PMC Article

    06/5/2021
    Study identified that PSMA3 and PSMA3-AS1 in mesenchymal stem cells (MSCs) could be packaged into exosomes and transferred to myeloma cells, thus promoting proteasome inhibitor resistance through a novel exosomal PSMA3-AS1/PSMA3 signaling pathway. PSMA3-AS1 could form an RNA duplex with pre-PSMA3, which transcriptionally promoted PSMA3 expression by increasing its stability.

    Exosome-Transmitted PSMA3 and PSMA3-AS1 Promote Proteasome Inhibitor Resistance in Multiple Myeloma.
    Xu H, Han H, Song S, Yi N, Qian C, Qiu Y, Zhou W, Hong Y, Zhuang W, Li Z, Li B, Zhuang W.

    05/30/2020
    High PSMA3 expression is associated with cholangiocarcinoma.

    Secretomic profiling of cells from hollow fiber bioreactor reveals PSMA3 as a potential cholangiocarcinoma biomarker.
    Verathamjamras C, Weeraphan C, Chokchaichamnankit D, Watcharatanyatip K, Subhasitanont P, Diskul-Na-Ayudthaya P, Mingkwan K, Luevisadpaibul V, Chutipongtanate S, Champattanachai V, Svasti J, Srisomsap C.

    07/21/2018
    In thyroid hemiagenesis, genomic examinations revealed the presence of four recurrent defects (three deletions and one duplication) affecting highly conservative proteasome genes PSMA1, PSMA3, and PSMD3.

    Mutations in proteasome-related genes are associated with thyroid hemiagenesis.
    Budny B, Szczepanek-Parulska E, Zemojtel T, Szaflarski W, Rydzanicz M, Wesoly J, Handschuh L, Wolinski K, Piatek K, Niedziela M, Ziemnicka K, Figlerowicz M, Zabel M, Ruchala M., Free PMC Article

    09/30/2017
    Our results provide evidence on new T1DM-susceptible loci in the PSMA3, PSMA6 and PSMC6 proteasome genes and give a new insight into the T1DM pathogenesis

    Genetic variations in the PSMA3, PSMA6 and PSMC6 genes are associated with type 1 diabetes in Latvians and with expression level of number of UPS-related and T1DM-susceptible genes in HapMap individuals.
    Sjakste T, Paramonova N, Osina K, Dokane K, Sokolovska J, Sjakste N.

    08/13/2016
    Evidence of a sex-specific association of PSMA3 genetic variants with subtypes of juvenile idiopathic arthritis.

    Juvenile idiopathic arthritis subtype- and sex-specific associations with genetic variants in the PSMA6/PSMC6/PSMA3 gene cluster.
    Sjakste T, Paramonova N, Rumba-Rozenfelde I, Trapina I, Sugoka O, Sjakste N.

    05/7/2016
    Protein interaction between Ambn and Psma3 can facilitate redistribution of ameloblastin domains within forming enamel.

    Protein Interaction between Ameloblastin and Proteasome Subunit α Type 3 Can Facilitate Redistribution of Ameloblastin Domains within Forming Enamel.
    Geng S, White SN, Paine ML, Snead ML., Free PMC Article

    11/28/2015
    A combination of two-dimensional gel electrophoresis (2D-GE) and tandem mass-spectrometry revealed a large number of PSMA3-bound proteins that are involved in various aspects of mRNA metabolism, including splicing.

    Proteomic analysis of the 20S proteasome (PSMA3)-interacting proteins reveals a functional link between the proteasome and mRNA metabolism.
    Fedorova OA, Moiseeva TN, Nikiforov AA, Tsimokha AS, Livinskaya VA, Hodson M, Bottrill A, Evteeva IN, Ermolayeva JB, Kuznetzova IM, Turoverov KK, Eperon I, Barlev NA.

    02/25/2012
    Serum 20S proteasome concentration and percentage of lymphocytic apoptosis predicted survival and patient prognosis in critically ill patients.

    The value of correlation of serum 20S proteasome concentration and percentage of lymphocytic apoptosis in critically ill patients: a prospective observational study.
    Yousef AA, Suliman GA, Mabrouk MM., Free PMC Article

    01/28/2012
    Plasminogen activator inhibitor type 1 interacts with alpha3 subunit of proteasome and modulates its activity.

    Plasminogen activator inhibitor type 1 interacts with alpha3 subunit of proteasome and modulates its activity.
    Boncela J, Przygodzka P, Papiewska-Pajak I, Wyroba E, Osinska M, Cierniewski CS., Free PMC Article

    04/16/2011
    The authors propose that the full-length HCV F protein as well as the F protein initiating from codon 26 is degraded by an ubiquitin-independent pathway that is mediated by the proteasome subunit alpha3.

    Ubiquitin-independent degradation of hepatitis C virus F protein.
    Yuksek K, Chen WL, Chien D, Ou JH., Free PMC Article

    01/21/2010
    EBNA3C binds to human the C8/alpha7 subunit of the 20S proteasome; degraded by purified 20S proteasomes in vitro but, found to be very stable and apparently turned over at a very low rate in B cells infected latently with EBV

    Epstein-Barr virus EBNA3 proteins bind to the C8/alpha7 subunit of the 20S proteasome and are degraded by 20S proteasomes in vitro, but are very stable in latently infected B cells.
    Touitou R, O'Nions J, Heaney J, Allday MJ.

    01/21/2010
    Aurora-B might undergo degradation by binding to HC8 in a proteasome-dependent manner during mitosis

    Human aurora-B binds to a proteasome alpha-subunit HC8 and undergoes degradation in a proteasome-dependent manner.
    Shu F, Guo S, Dang Y, Qi M, Zhou G, Guo Z, Zhang Y, Wu C, Zhao S, Yu L.

    01/21/2010
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