ArticleJournal of molecular biology2008
Different requirements of the kinase and UHM domains of KIS for its nuclear localization and binding to splicing factors.
Article in Journal of molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
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Who cites it
22 citing papers in PubMed, 43 citations in OpenAlex.
- Integrative CRISPR Screening and RNA Analyses Discover an Essential Role for PUF60 Interactions with 3' Splice Sites in Cancer Progression.Cancer research · 2026Article
- U2AF2 controls alternative splicing in speckle-proximal regions in an RS domain-dependent manner.Nucleic acids research · 2026Article
- UHMK1 Promotes Prostate Cancer Progression through a Positive Feedback Loop with MTHFD2.Oncology research · 2025Article
- KIS, a target of SOX4, regulates the ID1-mediated enhancement of β-catenin to facilitate lung adenocarcinoma cell proliferation and metastasis.Journal of cancer research and clinical oncology · 2024Article
- Article
- UHMK1 promotes lung adenocarcinoma oncogenesis by regulating the PI3K/AKT/mTOR signaling pathway.Thoracic cancer · 2023Article
- UHMK1 aids colorectal cancer cell proliferation and chemoresistance through augmenting IL-6/STAT3 signaling.Cell death & disease · 2022Article
- Adaptive translational reprogramming of metabolism limits the response to targeted therapy in BRAFNature communications · 2022Article
- UHMK1-dependent phosphorylation of Cajal body protein coilin alters 5-FU sensitivity in colon cancer cells.Cell communication and signaling : CCS · 2022Article
- UHMK1 Is a Novel Marker for Personalized Prediction of Pancreatic Cancer Prognosis.Frontiers in oncology · 2022Article
- Identification of phenothiazine derivatives as UHM-binding inhibitors of early spliceosome assembly.Nature communications · 2020Article
- UHMK1 promotes gastric cancer progression through reprogramming nucleotide metabolism.The EMBO journal · 2020Article
- U2AFEMBO reports · 2019Article
- SF1 Phosphorylation Enhances Specific Binding to U2AFBiophysical journal · 2016Article
- Unmasking the U2AF homology motif family: a bona fide protein-protein interaction motif in disguise.RNA (New York, N.Y.) · 2016Review
- Toxic gain of function from mutant FUS protein is crucial to trigger cell autonomous motor neuron loss.The EMBO journal · 2016Article
- Structural basis for regulation of RNA-binding proteins by phosphorylation.ACS chemical biology · 2015Review
- Cancer-relevant splicing factor CAPERα engages the essential splicing factor SF3b155 in a specific ternary complex.The Journal of biological chemistry · 2014Article
- Structure of phosphorylated SF1 bound to U2AF⁶⁵ in an essential splicing factor complex.Structure (London, England : 1993) · 2013Article
- The protein kinase KIS impacts gene expression during development and fear conditioning in adult mice.PloS one · 2012Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
Abstract
The protein kinase KIS is made by the juxtaposition of a unique kinase domain and a C-terminal domain with a U2AF homology motif (UHM), a sequence motif for protein interaction initially identified in the heterodimeric pre-mRNA splicing factor U2AF. This domain of KIS is closely related to the C-terminal UHM domain of the U2AF large subunit, U2AF(65). KIS phosphorylates the splicing factor SF1, which in turn enhances SF1 binding to U2AF(65) and the 3' splice site, an event known to take place at an early step of spliceosome assembly. Here, the analysis of the subcellular localization of mutated forms of KIS indicates that the kinase domain of KIS is the necessary domain for its nuclear localization. As in the case of U2AF(65), the UHM-containing C-terminal domain of KIS is required for binding to the splicing factors SF1 and SF3b155. The efficiency of KIS binding to SF1 and SF3b155 is similar to that of U2AF(65) in pull-down assays. These results further support the functional link of KIS with splicing factors. Interestingly, when compared to other UHM-containing proteins, KIS presents a different specificity for the UHM docking sites that are present in the N-terminal region of SF3b155, thus providing a new insight into the variety of interactions mediated by UHM domains.
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Registered trials
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