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    ANP32B acidic nuclear phosphoprotein 32 family member B [ Homo sapiens (human) ]

    Gene ID: 10541, updated on 27-Aug-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Structures of H5N1 influenza polymerase with ANP32B reveal mechanisms of genome replication and host adaptation.

    Structures of H5N1 influenza polymerase with ANP32B reveal mechanisms of genome replication and host adaptation.
    Staller E, Carrique L, Swann OC, Fan H, Keown JR, Sheppard CM, Barclay WS, Grimes JM, Fodor E., Free PMC Article

    08/8/2024
    ANP32B inhibition suppresses the growth of prostate cancer cells by regulating c-Myc signaling.

    ANP32B inhibition suppresses the growth of prostate cancer cells by regulating c-Myc signaling.
    Zhou C, Ma H, Yu W, Zhou Y, Zhang X, Meng Y, Chen C, Zhang J, Shi G.

    03/6/2024
    The histone chaperone ANP32B regulates chromatin incorporation of the atypical human histone variant macroH2A.

    The histone chaperone ANP32B regulates chromatin incorporation of the atypical human histone variant macroH2A.
    Mandemaker IK, Fessler E, Corujo D, Kotthoff C, Wegerer A, Rouillon C, Buschbeck M, Jae LT, Mattiroli F, Ladurner AG.

    11/8/2023
    ANP32B promotes lung cancer progression by regulating VDAC1.

    ANP32B promotes lung cancer progression by regulating VDAC1.
    Li T, Wang N, Li S, Yan H, Gao S, Gao W, Xu R.

    02/22/2023
    KPNA6 is a Cofactor of ANP32A/B in Supporting Influenza Virus Polymerase Activity.

    KPNA6 is a Cofactor of ANP32A/B in Supporting Influenza Virus Polymerase Activity.
    Yu M, Sun L, Zhang Z, Zhang Y, Zhang H, Na L, Wang X., Free PMC Article

    03/19/2022
    A natural variant in ANP32B impairs influenza virus replication in human cells.

    A natural variant in ANP32B impairs influenza virus replication in human cells.
    Staller E, Sheppard CM, Baillon L, Frise R, Peacock TP, Sancho-Shimizu V, Barclay WS., Free PMC Article

    11/6/2021
    Interaction of host cellular factor ANP32B with matrix proteins of different paramyxoviruses.

    Interaction of host cellular factor ANP32B with matrix proteins of different paramyxoviruses.
    Günther M, Bauer A, Müller M, Zaeck L, Finke S.

    08/13/2020
    ANP32A and ANP32B mediate the export of unspliced or partially spliced viral mRNA via interactions with Rev and CRM1.

    ANP32A and ANP32B are key factors in the Rev-dependent CRM1 pathway for nuclear export of HIV-1 unspliced mRNA.
    Wang Y, Zhang H, Na L, Du C, Zhang Z, Zheng YH, Wang X., Free PMC Article

    06/27/2020
    ANP32A and ANP32B from different species are powerful factors in the maintenance of viral polymerase activity. Human ANP32A and ANP32B contribute equally to support human influenza viral RNA replication.

    Fundamental Contribution and Host Range Determination of ANP32A and ANP32B in Influenza A Virus Polymerase Activity.
    Zhang H, Zhang Z, Wang Y, Wang M, Wang X, Zhang X, Ji S, Du C, Chen H, Wang X., Free PMC Article

    05/30/2020
    Human ANP32A and ANP32B homologues both support function of human-adapted influenza polymerase but do not support efficient activity of avian IAV polymerase which requires avian ANP32A.

    Species specific differences in use of ANP32 proteins by influenza A virus.
    Long JS, Idoko-Akoh A, Mistry B, Goldhill D, Staller E, Schreyer J, Ross C, Goodbourn S, Shelton H, Skinner MA, Sang H, McGrew MJ, Barclay W., Free PMC Article

    02/29/2020
    According to the cellular function of the characterized targets of ProTalpha, and the evolution in the composition of the diverse ProTalpha-complexes when proliferation activity was reduced or apoptosis induced, leads to hypothesized that ProTalpha interactions might be related to the proliferation activity and control of the cell survival.

    Prothymosin α interacts with SET, ANP32A and ANP32B and other cytoplasmic and mitochondrial proteins in proliferating cells.
    Barbeito P, Sarandeses CS, Díaz-Jullien C, Muras J, Covelo G, Moreira D, Freire-Cobo C, Freire M.

    12/2/2017
    ANP32B modulates Bad phosphorylation as well as Bak and Bax expression, resulting in regulation of apoptosis in HCC. These findings indicate the potential value of ANP32B as a therapeutic target for HCC

    Downregulation of ANP32B exerts anti-apoptotic effects in hepatocellular carcinoma.
    Ohno Y, Koizumi M, Nakayama H, Watanabe T, Hirooka M, Tokumoto Y, Kuroda T, Abe M, Fukuda S, Higashiyama S, Kumagi T, Hiasa Y., Free PMC Article

    09/30/2017
    Caspase-3-resistant uncleavable form of acidic leucine-rich nuclear phosphoprotein 32B potentiates leukemic cell apoptosis.

    Caspase-3-resistant uncleavable form of acidic leucine-rich nuclear phosphoprotein 32B potentiates leukemic cell apoptosis.
    Li CX, Shen SM, Wang LS, Yu Y.

    10/3/2015
    ANP32B is a nuclear target of henipavirus M proteins.

    ANP32B is a nuclear target of henipavirus M proteins.
    Bauer A, Neumann S, Karger A, Henning AK, Maisner A, Lamp B, Dietzel E, Kwasnitschka L, Balkema-Buschmann A, Keil GM, Finke S., Free PMC Article

    01/3/2015
    this is the first demonstration that ANP32B expression was down-regulated during differentiation induction of leukemic cells by all-trans retinoic acid.

    Acidic leucine-rich nuclear phosphoprotein 32 family member B (ANP32B) contributes to retinoic acid-induced differentiation of leukemic cells.
    Yu Y, Shen SM, Zhang FF, Wu ZX, Han B, Wang LS.

    10/27/2012
    the interaction of ANP32B with the core histones H3-H4 occurs on its concave side, and both the acidic and hydrophobic residues that compose the concave surface are critical for histone binding.

    Solution structure of histone chaperone ANP32B: interaction with core histones H3-H4 through its acidic concave domain.
    Tochio N, Umehara T, Munemasa Y, Suzuki T, Sato S, Tsuda K, Koshiba S, Kigawa T, Nagai R, Yokoyama S.

    08/16/2010
    ANP32B is a direct substrate of caspase-3. It is cleaved at the sequence of Ala-Glu-Val-Asp, after Asp-163. The reduced expression of endogenous ANP32B by specific siRNA enhances caspase-3 activation & apoptosis induction by NSC606985 & etoposide.

    Downregulation of ANP32B, a novel substrate of caspase-3, enhances caspase-3 activation and apoptosis induction in myeloid leukemic cells.
    Shen SM, Yu Y, Wu YL, Cheng JK, Wang LS, Chen GQ.

    04/19/2010
    The CK2 alpha' phosphorylates APRIL and therefore is responsible for the regulation of the nucleocytoplasmic translocation of CD83 mRNA.

    Phosphorylation of the HuR ligand APRIL by casein kinase 2 regulates CD83 expression.
    Chemnitz J, Pieper D, Grüttner C, Hauber J.

    01/21/2010
    recruitment of ANP32B onto the promoter region requires KLF5 and results in promoter region-specific histone incorporation and inhibition of histone acetylation by ANP32B

    Promoter region-specific histone incorporation by the novel histone chaperone ANP32B and DNA-binding factor KLF5.
    Munemasa Y, Suzuki T, Aizawa K, Miyamoto S, Imai Y, Matsumura T, Horikoshi M, Nagai R., Free PMC Article

    01/21/2010
    regulatory roles of oncoprotein ProT and tumor suppressor PHAP in apoptosis

    Distinctive roles of PHAP proteins and prothymosin-alpha in a death regulatory pathway.
    Jiang X, Kim HE, Shu H, Zhao Y, Zhang H, Kofron J, Donnelly J, Burns D, Ng SC, Rosenberg S, Wang X.

    01/21/2010
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