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    STAMBP STAM binding protein [ Homo sapiens (human) ]

    Gene ID: 10617, updated on 2-Nov-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Identification of STAM-binding protein as a target for the treatment of gemcitabine resistance pancreatic cancer in a nutrient-poor microenvironment.

    Identification of STAM-binding protein as a target for the treatment of gemcitabine resistance pancreatic cancer in a nutrient-poor microenvironment.
    Zhang W, Xu Z, Du Y, Liu T, Xiong Z, Hu J, Chen L, Peng X, Zhou F., Free PMC Article

    09/16/2024
    The expression and clinical significance of STAMBP in breast cancer.

    The expression and clinical significance of STAMBP in breast cancer.
    Li L, Yang X, He M, Xu X, Xuan X, Zhang J, Zhang L, Xu H, Li D.

    02/4/2023
    The deubiquitinating enzyme STAMBP is a newly discovered driver of triple-negative breast cancer progression that maintains RAI14 protein stability.

    The deubiquitinating enzyme STAMBP is a newly discovered driver of triple-negative breast cancer progression that maintains RAI14 protein stability.
    Yang Q, Yan D, Zou C, Xue Q, Lin S, Huang Q, Li X, Tang D, Chen X, Liu J., Free PMC Article

    12/17/2022
    STAM binding protein regulated by hsa_circ_0007334 exerts oncogenic potential in pancreatic cancer.

    STAM binding protein regulated by hsa_circ_0007334 exerts oncogenic potential in pancreatic cancer.
    Yu S, E C, Yang J.

    11/26/2022
    The deubiquitinase STAMBP modulates cytokine secretion through the NLRP3 inflammasome.

    The deubiquitinase STAMBP modulates cytokine secretion through the NLRP3 inflammasome.
    Bednash JS, Johns F, Patel N, Smail TR, Londino JD, Mallampalli RK., Free PMC Article

    01/22/2022
    STAMBP promotes lung adenocarcinoma metastasis by regulating the EGFR/MAPK signaling pathway.

    STAMBP promotes lung adenocarcinoma metastasis by regulating the EGFR/MAPK signaling pathway.
    Xu H, Yang X, Xuan X, Wu D, Zhang J, Xu X, Zhao Y, Ma C, Li D., Free PMC Article

    01/1/2022
    Structural and functional characterization of ubiquitin variant inhibitors for the JAMM-family deubiquitinases STAMBP and STAMBPL1.

    Structural and functional characterization of ubiquitin variant inhibitors for the JAMM-family deubiquitinases STAMBP and STAMBPL1.
    Guo Y, Liu Q, Mallette E, Caba C, Hou F, Fux J, LaPlante G, Dong A, Zhang Q, Zheng H, Tong Y, Zhang W., Free PMC Article

    11/27/2021
    Prediagnostic circulating inflammation biomarkers and esophageal squamous cell carcinoma: A case-cohort study in Japan.

    Prediagnostic circulating inflammation biomarkers and esophageal squamous cell carcinoma: A case-cohort study in Japan.
    Aversa J, Song M, Shimazu T, Inoue M, Charvat H, Yamaji T, Sawada N, Pfeiffer RM, Karimi P, Dawsey SM, Rabkin CS, Tsugane S, Camargo MC.

    03/13/2021
    the present study reported the first case of a Chinese patient with refractory epilepsy as an initial symptom of MIC-CAP. Additionally, novel pathogenic compound heterozygosity of the STAMBP was identified.

    Early‑onset epilepsy and microcephaly‑capillary malformation syndrome caused by a novel STAMBP mutation in a Chinese boy.
    Wu F, Dai Y, Wang J, Cheng M, Wang Y, Li X, Yuan P, Liao S, Jiang L, Chen J, Yan L, Zhong M., Free PMC Article

    04/4/2020
    these results indicate the importance of STAMBP in melanoma metastasis by regulating SLUG.

    STAM-binding protein regulates melanoma metastasis through SLUG stabilization.
    Iwakami Y, Yokoyama S, Watanabe K, Hayakawa Y.

    05/18/2019
    Contrary to previously reported STAMBP mutations, the Ser236Phe mutation did not lead to constitutive activation of the PI3K-AKT-mTOR pathway in patient-derived LCLs, as indicated by the expression of phosphorylated S6 ribosomal protein, suggesting that it is not the major pathomechanism underlying the disorder in this patient.

    A novel homozygous missense mutation in the SH3-binding motif of STAMBP causing microcephaly-capillary malformation syndrome.
    Hori I, Miya F, Negishi Y, Hattori A, Ando N, Boroevich KA, Okamoto N, Kato M, Tsunoda T, Yamasaki M, Kanemura Y, Kosaki K, Saitoh S.

    12/22/2018
    Targeting the deubiquitinase STAMBP inhibits NALP7 inflammasome activity.

    Targeting the deubiquitinase STAMBP inhibits NALP7 inflammasome activity.
    Bednash JS, Weathington N, Londino J, Rojas M, Gulick DL, Fort R, Han S, McKelvey AC, Chen BB, Mallampalli RK., Free PMC Article

    11/17/2018
    The authors propose a structural organization where the AMSH-SH3 binding motif interacts with the STAM2-SH3 domain and contributes to the correct positioning of AMSH prior to polyubiquitin chains' cleavage.

    NMR Reveals the Interplay among the AMSH SH3 Binding Motif, STAM2, and Lys63-Linked Diubiquitin.
    Hologne M, Cantrelle FX, Riviere G, Guillière F, Trivelli X, Walker O.

    06/24/2017
    The VHS domain of STAM2 directs AMSH to cleave longer Lys63-linked ubiquitin chains

    The Vps27/Hrs/STAM (VHS) Domain of the Signal-transducing Adaptor Molecule (STAM) Directs Associated Molecule with the SH3 Domain of STAM (AMSH) Specificity to Longer Ubiquitin Chains and Dictates the Position of Cleavage.
    Baiady N, Padala P, Mashahreh B, Cohen-Kfir E, Todd EA, Du Pont KE, Berndsen CE, Wiener R., Free PMC Article

    08/27/2016
    Two siblings with classic features of MIC-CAP syndrome that harbor a novel predicted splice mutation in STAMBP

    Novel STAMBP mutation and additional findings in an Arabic family.
    Faqeih EA, Bastaki L, Rosti RO, Spencer EG, Zada AP, Saleh MA, Um K, Gleeson JG.

    12/19/2015
    associated molecule with the SH3 domain of STAM-mediated deubiquitination of connexin 43 protects Gap junctions from degradation

    AMSH-mediated deubiquitination of Cx43 regulates internalization and degradation of gap junctions.
    Ribeiro-Rodrigues TM, Catarino S, Marques C, Ferreira JV, Martins-Marques T, Pereira P, Girão H.

    01/31/2015
    Recognition of the proximal ubiquitin is imperative for the linkage specificity and catalytic efficiency of AMSH.

    Mechanism of recruitment and activation of the endosome-associated deubiquitinase AMSH.
    Davies CW, Paul LN, Das C., Free PMC Article

    01/18/2014
    Mutations in STAMBP, encoding a deubiquitinating enzyme, cause microcephaly-capillary malformation syndrome.

    Mutations in STAMBP, encoding a deubiquitinating enzyme, cause microcephaly-capillary malformation syndrome.
    McDonell LM, Mirzaa GM, Alcantara D, Schwartzentruber J, Carter MT, Lee LJ, Clericuzio CL, Graham JM Jr, Morris-Rosendahl DJ, Polster T, Acsadi G, Townshend S, Williams S, Halbert A, Isidor B, David A, Smyser CD, Paciorkowski AR, Willing M, Woulfe J, Das S, Beaulieu CL, Marcadier J, FORGE Canada Consortium, Geraghty MT, Frey BJ, Majewski J, Bulman DE, Dobyns WB, O'Driscoll M, Boycott KM., Free PMC Article

    06/22/2013
    AMSH efficiently removes ubiquitin from the activated EGFR.

    Recycling of EGFR and ErbB2 is associated with impaired Hrs tyrosine phosphorylation and decreased deubiquitination by AMSH.
    Meijer IM, van Rotterdam W, van Zoelen EJ, van Leeuwen JE.

    01/12/2013
    tight coupling of ESCRT-III CHMP3 and AMSH functions and provide insight into the regulation of ESCRT-III

    Structural basis for ESCRT-III CHMP3 recruitment of AMSH.
    Solomons J, Sabin C, Poudevigne E, Usami Y, Hulsik DL, Macheboeuf P, Hartlieb B, Göttlinger H, Weissenhorn W., Free PMC Article

    12/3/2011
    Studies indicate that USP8/Ubpy and AMSH interact with ESCRT components to modulate the ubiquitination status of receptors and relevant sorting proteins.

    Regulation of endocytic sorting by ESCRT-DUB-mediated deubiquitination.
    Wright MH, Berlin I, Nash PD.

    10/22/2011
    AMSH interacts with ESCRT-0 to regulate the stability and trafficking of CXCR4.

    AMSH interacts with ESCRT-0 to regulate the stability and trafficking of CXCR4.
    Sierra MI, Wright MH, Nash PD., Free PMC Article

    05/31/2010
    Data suggest that AMSH and UBPY are essential for trafficking and down-regulation of PAR(2) but not for regulating PAR(2) dissociation from beta-arrestin2 or PAR(2)-mediated ERK2 activation.

    Endosomal deubiquitinating enzymes control ubiquitination and down-regulation of protease-activated receptor 2.
    Hasdemir B, Murphy JE, Cottrell GS, Bunnett NW., Free PMC Article

    01/21/2010
    crystal structures of the human AMSH-LP DUB domain alone and in complex with a Lys 63-linked di-ubiquitin at 1.2 A and 1.6 A resolutions, respectively

    Structural basis for specific cleavage of Lys 63-linked polyubiquitin chains.
    Sato Y, Yoshikawa A, Yamagata A, Mimura H, Yamashita M, Ookata K, Nureki O, Iwai K, Komada M, Fukai S.

    01/21/2010
    UBPY MIT domain and another ubiquitin isopeptidase, AMSH, reveals common interactions with CHMP1A and CHMP1B but a distinct selectivity of AMSH for CHMP3/VPS24, a core subunit of the ESCRT-III complex, and UBPY for CHMP7.

    The MIT domain of UBPY constitutes a CHMP binding and endosomal localization signal required for efficient epidermal growth factor receptor degradation.
    Row PE, Liu H, Hayes S, Welchman R, Charalabous P, Hofmann K, Clague MJ, Sanderson CM, Urbé S.

    01/21/2010
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