UBP1

Last update 08 May 2025

Basic Info

Synonyms

LBP-1a, LBP1, Transcription factor LBP-1

+ [3]

Introduction

Functions as a transcriptional activator in a promoter context-dependent manner. Modulates the placental expression of CYP11A1. Involved in regulation of the alpha-globin gene in erythroid cells. Activation of the alpha-globin promoter in erythroid cells is via synergistic interaction with TFCP2 (By similarity). Involved in regulation of the alpha-globin gene in erythroid cells. Binds strongly to sequences around the HIV-1 initiation site and weakly over the TATA-box. Represses HIV-1 transcription by inhibiting the binding of TFIID to the TATA-box.

100 Clinical Results associated with UBP1

100 Translational Medicine associated with UBP1

0 Patents (Medical) associated with UBP1

139

Literatures (Medical) associated with UBP1

01 May 2025·International Journal of Biological Macromolecules

Upstream-binding protein-1 promotes breast tumorigenesis by inducing NRG2-mediated metastasis, plasticity, and macrophage polarization

Article

Author: Negi, Manorma ; Kaushik, Nagendra Kumar ; Jaiswal, Apurva ; Choi, Eun Ha ; Kaushik, Neha

Upstream binding protein 1 (UBP1) is a transcription factor (TF) of the CP2/grainyhead family involved in various biological processes, including cancer cell proliferation, differentiation, and embryonic development. While other mammalian grainyhead-like TFs have been linked to different cancers, including breast cancer (BC), the role of UBP1 in BC remains unexplored. In this study, we provide a preliminary investigation into the novel functions of UBP1 in BC. Using online database screening, we first demonstrated that elevated UBP1 levels in breast carcinoma are associated with poor prognosis and adverse clinical outcomes. We further showed that UBP1 promotes epithelial-mesenchymal transition (EMT) and stemness in BC cells while regulating key signaling pathways, including the PI3K-Akt. Additionally, UBP1 modulates tumor metastasis by influencing tumor-associated macrophage (TAM) polarization, promoting an immunosuppressive macrophage phenotype, and driving tumor progression. Our findings highlight UBP1's pivotal role in BC progression through multiple mechanisms, including EMT induction, stemness maintenance, and macrophage polarization via activation of the NRG2/Akt axis. Moreover, higher UBP1 expression correlates with lower overall and recurrence-free survival, underscoring its potential as a prognostic marker and therapeutic target for aggressive BC.

01 Mar 2025·Journal of Biological Chemistry

Drug resistance–associated mutations in Plasmodium UBP-1 disrupt its essential deubiquitinating activity

Article

Author: Ascher, David B ; Lee, Marcus C S ; Henrici, Ryan ; Artavanis-Tsakonas, Katerina ; Hoshizaki, Johanna ; Ansbro, Megan R ; Karpiyevich, Maryia ; Smith, Cameron J ; van der Heden van Noort, Gerbrand J ; Eavis, Heledd ; Briggs, Carla ; Sutherland, Colin J

Deubiquitinating enzymes function to cleave ubiquitin (Ub) moieties from modified proteins, serving to maintain the pool of free Ub in the cell while simultaneously impacting the fate and function of a target protein. Like all eukaryotes, Plasmodium parasites rely on the dynamic addition and removal of Ub for their own growth and survival. While humans possess around 100 deubiquitinases, Plasmodium contains ∼20 putative Ub hydrolases, many of which bear little to no resemblance to those of other organisms. In this study, we characterize Plasmodium falciparum UBP-1, a large Ub hydrolase unique to Plasmodium spp., which has been linked to endocytosis and drug resistance. We demonstrate its Ub activity, linkage specificity, and assess the repercussions of point mutations associated with drug resistance on catalytic activity and parasite fitness. We confirm that the deubiquitinating activity of UBP-1 is essential for parasite survival, implicating an important role for Ub signaling in endocytosis.

08 Feb 2025·Nucleic Acids Research

Ubiquitin protease Ubp1 cooperates with Ubp10 and Ubp12 to revert lysine-164 PCNA ubiquitylation at replication forks

Article

Author: Sacristán, María P ; Rodríguez, Sergio ; Muñoz, Sofía ; Zamarreño, Javier ; Bueno, Avelino

AbstractProliferating cell nuclear antigen (PCNA) is essential for the faithful duplication of eukaryotic genomes. PCNA also orchestrates events necessary to address threats to genomic integrity, such as the DNA damage tolerance (DDT) response, a mechanism by which eukaryotic cells bypass replication-blocking lesions to maintain replisome stability. DDT is regulated by the ubiquitylation of PCNA and the consequent recruitment of specialized polymerases that ensure replication continuity. We have recently described that the deubiquitylases Ubp10 and Ubp12 modulate DDT events by reverting the ubiquitylation of PCNA in Saccharomyces cerevisiae. This study identifies Ubp1 as a novel PCNA deubiquitylase that cooperates with Ubp10 and Ubp12 in the regulation of DDT during DNA replication. Ubp1, previously known as a cytoplasmic protein, also localizes to the nucleus, where it associates with DNA replication forks. Additionally, Ubp1 interacts with and deubiquitylates PCNA. Here, we provide evidence that Ubp1 collaborates with Ubp10 and Ubp12 to facilitate DNA replication by efficiently reverting PCNAK164 ubiquitylation at replication forks under conditions free from exogenous perturbations. Consequently, the deletion of UBP1, UBP10, and UBP12 leads to persistent ubiquitylation of PCNAK164 and a marked delay in S phase progression.

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UBP1

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