U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination
    • Showing Current items.

    OS9 OS9 endoplasmic reticulum lectin [ Homo sapiens (human) ]

    Gene ID: 10956, updated on 3-Nov-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Monochorionic twins with selective fetal growth restriction: insight from placental whole-transcriptome analysis.

    Monochorionic twins with selective fetal growth restriction: insight from placental whole-transcriptome analysis.
    Li W, Chung CYL, Wang CC, Chan TF, Leung MBW, Chan OK, Wu L, Appiah K, Chaemsaithong P, Cheng YKY, Poon LCY, Leung TY.

    12/5/2020
    The relative expression of OS9 and XTP3B and the distribution of glycan and non-glycan degrons within the same protein contribute to the fidelity.

    Redundant and Antagonistic Roles of XTP3B and OS9 in Decoding Glycan and Non-glycan Degrons in ER-Associated Degradation.
    van der Goot AT, Pearce MMP, Leto DE, Shaler TA, Kopito RR., Free PMC Article

    01/26/2019
    The endoplasmic reticulum-associated protein, OS-9, behaves as a lectin in targeting the immature calcium-sensing receptor.

    The endoplasmic reticulum-associated protein, OS-9, behaves as a lectin in targeting the immature calcium-sensing receptor.
    Ward BK, Rea SL, Magno AL, Pedersen B, Brown SJ, Mullin S, Arulpragasam A, Ingley E, Conigrave AD, Ratajczak T.

    10/14/2017
    OS-9 up-regulates occludin and claudin-1 by activating the MAP kinase (MAPK) pathway, and thus protects the epithelial barrier function of Caco-2 monolayer under hypoxia condition.

    A Novel Role of OS-9 in the Maintenance of Intestinal Barrier Function from Hypoxia-induced Injury via p38-dependent Pathway.
    Sun L, Xu C, Chen G, Yu M, Yang S, Qiu Y, Peng K, Wang W, Xiao W, Yang H., Free PMC Article

    04/16/2016
    EDEM2 and OS-9 are required for ER-associated degradation of non-glycosylated sonic hedgehog

    EDEM2 and OS-9 are required for ER-associated degradation of non-glycosylated sonic hedgehog.
    Tang HY, Huang CH, Zhuang YH, Christianson JC, Chen X., Free PMC Article

    06/20/2015
    Unique regions mediate the interaction between OS-9 and GRP94.

    OS-9 facilitates turnover of nonnative GRP94 marked by hyperglycosylation.
    Dersh D, Jones SM, Eletto D, Christianson JC, Argon Y., Free PMC Article

    04/4/2015
    It delivers mutant neuroserpin to ERAD by recognition of glycan side chains and provide the first in vivo proof of involvement of ERAD in degradation of mutant neuroserpin.

    Lectin OS-9 delivers mutant neuroserpin to endoplasmic reticulum associated degradation in familial encephalopathy with neuroserpin inclusion bodies.
    Schipanski A, Oberhauser F, Neumann M, Lange S, Szalay B, Krasemann S, van Leeuwen FW, Galliciotti G, Glatzel M.

    02/14/2015
    long non-coding RNA ENST00000480739 suppresses tumour cell invasion by regulating OS-9 and HIF-1alpha in pancreatic ductal adenocarcinoma.

    A novel long non-coding RNA ENST00000480739 suppresses tumour cell invasion by regulating OS-9 and HIF-1α in pancreatic ductal adenocarcinoma.
    Sun YW, Chen YF, Li J, Huo YM, Liu DJ, Hua R, Zhang JF, Liu W, Yang JY, Fu XL, Yan T, Hong J, Cao H., Free PMC Article

    01/31/2015
    Data indicate that the interaction of OS-9 and XTP3-B with CD147(CG) was inhibited by mutations to conserved residues in their lectin domains.

    Unassembled CD147 is an endogenous endoplasmic reticulum-associated degradation substrate.
    Tyler RE, Pearce MM, Shaler TA, Olzmann JA, Greenblatt EJ, Kopito RR., Free PMC Article

    06/8/2013
    OS-9 plays no direct functional role in HIF degradation since physical interaction of OS-9 with oxygen sensing HIF prolyl hydroxylases cannot occur in vivo due to their different subcellular localization

    The function of hypoxia-inducible factor (HIF) is independent of the endoplasmic reticulum protein OS-9.
    Brockmeier U, Platzek C, Schneider K, Patak P, Bernardini A, Fandrey J, Metzen E., Free PMC Article

    12/3/2011
    It regulates endoplasmic reticulum-associated degradation. (review)

    [OS-9 and XTP3-B: lectins that regulate endoplasmic reticulum-associated degradation (ERAD)].
    Hosokawa N.

    08/27/2011
    The OS-9 specifically recognizes Manalpha1,6Manalpha1,6Man residues on the processed C-arm through the continuous double tryptophan (WW) motif.

    Structural basis for oligosaccharide recognition of misfolded glycoproteins by OS-9 in ER-associated degradation.
    Satoh T, Chen Y, Hu D, Hanashima S, Yamamoto K, Yamaguchi Y.

    01/29/2011
    Observational study and genome-wide association study of gene-disease association. (HuGE Navigator)

    Genome-wide searching of rare genetic variants in WTCCC data.
    Feng T, Zhu X., Free PMC Article

    09/15/2010
    The sugar-binding ability of human OS-9 and its involvement in ER-associated degradation

    The sugar-binding ability of human OS-9 and its involvement in ER-associated degradation.
    Mikami K, Yamaguchi D, Tateno H, Hu D, Qin SY, Kawasaki N, Yamada M, Matsumoto N, Hirabayashi J, Ito Y, Yamamoto K.

    07/5/2010
    model for mannose trimming and the requirement for OS-9 lectin activity in glycoprotein ERAD in which N-glycans lacking the terminal mannose from the C branch are recognized by OS-9 and targeted for degradation

    Human OS-9, a lectin required for glycoprotein endoplasmic reticulum-associated degradation, recognizes mannose-trimmed N-glycans.
    Hosokawa N, Kamiya Y, Kamiya D, Kato K, Nagata K., Free PMC Article

    01/21/2010
    OS9 is critically involved in the modulation of ER-to-Golgi transport of DC-STAMP in response to TLR triggering, suggesting a novel role for OS9 in myeloid differentiation and cell fusion.

    OS9 interacts with DC-STAMP and modulates its intracellular localization in response to TLR ligation.
    Jansen BJ, Eleveld-Trancikova D, Sanecka A, van Hout-Kuijer M, Hendriks IA, Looman MG, Leusen JH, Adema GJ.

    01/21/2010
    OS-9 recognises terminally misfolded proteins via polypeptide-based rather than glycan-based signals, but is only required for transferring those bearing N-glycans to the ubiquitination machinery.

    Mammalian OS-9 is upregulated in response to endoplasmic reticulum stress and facilitates ubiquitination of misfolded glycoproteins.
    Alcock F, Swanton E.

    01/21/2010
    Xbp1-responsive OS-9 variants in the mammalian endoplasmic reticulum inhibit secretion of misfolded protein conformers and enhancing their disposal

    A dual task for the Xbp1-responsive OS-9 variants in the mammalian endoplasmic reticulum: inhibiting secretion of misfolded protein conformers and enhancing their disposal.
    Bernasconi R, Pertel T, Luban J, Molinari M., Free PMC Article

    01/21/2010
    OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD

    OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD.
    Christianson JC, Shaler TA, Tyler RE, Kopito RR., Free PMC Article

    01/21/2010
    OS-9 regulates the secretory transport of TRPV4 and appears to protect TRPV4 subunits from the precocious ubiquitination and ER-associated degradation.

    OS-9 regulates the transit and polyubiquitination of TRPV4 in the endoplasmic reticulum.
    Wang Y, Fu X, Gaiser S, Köttgen M, Kramer-Zucker A, Walz G, Wegierski T.

    01/21/2010
    Identification of a peptide, resulting from a point mutation in gene OS-9, recognized by cytolytic T lymphocytes on a human melanoma.

    Identification of a new peptide recognized by autologous cytolytic T lymphocytes on a human melanoma.
    Vigneron N, Ooms A, Morel S, Degiovanni G, Van Den Eynde BJ.

    01/21/2010
    firstprevious page of 1 nextlast