IndraLab

Statements


USP49 affects Histone_H2B
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USP49 deubiquitinates Histone_H2B. 6 / 6
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"It has been reported that USP49 deubiquitinates histone H2B and regulates co-transcriptional pre-mRNA splicing; interestingly, p53 is also mainly localized to the nucleus."

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"Silencing Usp49 induces relatively small changes in gene expression, however alterations in H2B ubiquitination levels caused by Usp49 regulate U1A and U2B association with chromatin and binding to nascent pre-mRNA."

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"Usp49 in complex with RVB1 and SUG1 yeast homologues deubiquitinates H2B, this modification is required for efficient co-transcriptional splicing of a large set of exons."

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"Here we report the purification of ubiquitin specific peptidase 49 (USP49) as a histone H2B specific deubiquitinase and demonstrate that H2B deubiquitination by USP49 is required for efficient cotranscriptional splicing of a large set of exons."

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"USP49 deubiquitinates histone H2B and regulates cotranscriptional pre-mRNA splicing."

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"USP49 forms a complex with RuvB-like1 (RVB1) and SUG1 and specifically deubiquitinates histone H2B in vitro and in vivo."
USP49 affects TP53
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USP49 leads to the deubiquitination of TP53. 3 / 3
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"Investigation of the mechanism revealed that USP49 interacts with the N terminus of p53 and suppresses several types of p53 ubiquitination."

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"USP49 suppresses p53 ubiquitination."

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"To assess this, we co-transfected HA-p53, Myc-ubiquitin, and Flag-USP49 into 293T cells, and found that USP49 suppressed ubiquitination of HA-p53."
USP49 affects STING1
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USP49 deubiquitinates STING1. 3 / 3
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"Mechanistically, USP49 removes K63-linked ubiquitin chains from MITA after HSV-1 infection which inhibits the aggregation of MITA and the subsequent recruitment of TBK1 to the signaling complex."

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"USP49, a ubiquitin-specific protease, interacts with and deubiquitinates STING after HSV-1 infection."

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"Here, we report that USP49 interacts with and deubiquitinates MITA after HSV-1 infection, thereby turning down cellular antiviral responses."
USP49 affects FKBP4
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USP49 deubiquitinates FKBP4. 3 / 3
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"Here we report that a deubiquitinase, USP49, is a new regulator of the AKT pathway.| Mechanistically, USP49 deubiquitinates and stabilizes FKBP51, which in turn enhances PHLPP's capability to dephosphorylate AKT Furthermore, USP49 inhibited pancreatic cancer cell proliferation and enhanced cellular response to gemcitabine in a FKBP51-AKT-dependent manner."

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"Mechanistically, USP49 deubiquitinates and stabilizes FKBP51, which in turn enhances PHLPP 's capability to dephosphorylate AKT Furthermore, USP49 inhibited pancreatic cancer cell proliferation and enhanced cellular response to gemcitabine in a FKBP51-AKT-dependent manner."

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"Recent studies show that DUBs play essential roles in proliferation, motility, and chemoresistance of malignant cells through stabilizing critical proteins.5 For example, USP49 deubiquitinates FKBP51, which serves as a scaffold for dephosphorylating Ser473 residue at Akt, and further sensitizes pancreatic cancer cells to gemcitabine."
USP49 affects PAX9
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USP49 deubiquitinates PAX9. 2 / 2
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"We identify and demonstrate that USP49 interacts with and deubiquitinates PAX9 and MSX1, thereby extending their protein half-lives."

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"In sum, our results suggest that deubiquitination of PAX9 and MSX1 by USP49 stabilizes their protein levels to facilitate successful odontogenesis."
USP49 affects H2BC21
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USP49 deubiquitinates H2BC21. 2 / 2
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No evidence text available

"USP49 deubiquitinates histone H2B and regulates cotranscriptional pre-mRNA splicing."
USP49 affects gemcitabine
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USP49 deubiquitinates gemcitabine. 1 / 1
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"Recent studies show that DUBs play essential roles in proliferation, motility, and chemoresistance of malignant cells through stabilizing critical proteins.5 For example, USP49 deubiquitinates FKBP51, which serves as a scaffold for dephosphorylating Ser473 residue at Akt, and further sensitizes pancreatic cancer cells to gemcitabine."
USP49 affects PTEN
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USP49 deubiquitinates PTEN. 1 / 1
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"Further studies indicated that USP49 deubiquitinated PTEN and stabilized PTEN protein, which suggested that USP49 inhibited PI3K and AKT signaling by stabilizing PTEN in NSCLC cells."
USP49 affects MSX1
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USP49 deubiquitinates MSX1. 1 / 1
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"In sum, our results suggest that deubiquitination of PAX9 and MSX1 by USP49 stabilizes their protein levels to facilitate successful odontogenesis."
USP49 affects MDM2-p53 axis genes
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USP49 leads to the deubiquitination of MDM2-p53 axis genes. 1 / 1
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"Therefore, our findings indicated that USP49-mediated H2B deubiquitination controls the transcription of MDM2-p53 axis genes in the process of HCT116 cell proliferation."
USP49 affects H2BC10
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USP49 deubiquitinates H2BC10. 1 / 1
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"USP49 deubiquitinates histone H2B and regulates cotranscriptional pre-mRNA splicing"
USP49 affects H2AX
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USP49 leads to the deubiquitination of H2AX. 1 / 1
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"Over-expressed USP49 suppressed ubiquitylation of γH2AX in an enzymatic activity-dependent manner."
USP49 affects FKBP5
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USP49 deubiquitinates FKBP5. 1 / 1
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"Mechanistically, USP49 deubiquitinates and stabilizes FKBP51, which in turn enhances PHLPP's capability to dephosphorylate AKT Furthermore, USP49 inhibited pancreatic cancer cell proliferation and enhanced cellular response to gemcitabine in a FKBP51-AKT-dependent manner."
USP49 affects DUSP1
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USP49 deubiquitinates DUSP1. 1 / 1
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"Moreover, USP49 positively regulated DUSP1 expression through deubiquitinating DUSP1."
USP49 affects BAG2
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USP49 deubiquitinates BAG2. 1 / 1
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"Investigation of mechanisms unravels that USP49 deubiquitinates and stabilizes Bcl-2-Associated Athanogene 2 (BAG2), a well-known protein that antagonizes apoptosis and enables adaptive response of CRC cells."