ArticleMolecular and cellular biology2004
Nizp1, a novel multitype zinc finger protein that interacts with the NSD1 histone lysine methyltransferase through a unique C2HR motif.
Article in Molecular and cellular biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 48 citations in OpenAlex.
- Research status of small molecule inhibitors, probes, and degraders of NSDs: a comprehensive review.Future medicinal chemistry · 2025Review
- Article
- The sotos syndrome gene Nsd1 safeguards developmental gene enhancers poised for transcription by maintaining the precise deposition of histone methylation.The Journal of biological chemistry · 2025Article
- Functional characterization of plant specific Indeterminate Domain (IDD) transcription factors in tomato (Solanum lycopersicum L.).Scientific reports · 2024Article
- NSD1: A Lysine Methyltransferase between Developmental Disorders and Cancer.Life (Basel, Switzerland) · 2021Review
- Structure, Activity and Function of the NSD3 Protein Lysine Methyltransferase.Life (Basel, Switzerland) · 2021Review
- Functional Interplay between Methyltransferases and Inflammasomes in Inflammatory Responses and Diseases.International journal of molecular sciences · 2021Review
- Article
- Role of the zinc finger and SCAN domain-containing transcription factors in cancer.American journal of cancer research · 2019Review
- Review
- The Role of Nuclear Receptor-Binding SET Domain Family Histone Lysine Methyltransferases in Cancer.Cold Spring Harbor perspectives in medicine · 2017Review
- Intrinsic protein disorder in histone lysine methylation.Biology direct · 2016Article
- Structural basis for PHDVC5HCHNSD1-C2HRNizp1 interaction: implications for Sotos syndrome.Nucleic acids research · 2016Article
- Examining the impact of gene variants on histone lysine methylation.Biochimica et biophysica acta · 2014Review
- KRAB-Zinc Finger Proteins: A Repressor Family Displaying Multiple Biological Functions.Current genomics · 2013Article
- Genetic syndromes caused by mutations in epigenetic genes.Human genetics · 2013Review
- The methyltransferase NSD3 has chromatin-binding motifs, PHD5-C5HCH, that are distinct from other NSD (nuclear receptor SET domain) family members in their histone H3 recognition.The Journal of biological chemistry · 2013Article
- Article
- Jarid2 (Jumonji, AT rich interactive domain 2) regulates NOTCH1 expression via histone modification in the developing heart.The Journal of biological chemistry · 2012Article
- Endothelial Jarid2/Jumonji is required for normal cardiac development and proper Notch1 expression.The Journal of biological chemistry · 2011Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Haploinsufficiency of the NSD1 gene is a hallmark of Sotos syndrome, and rearrangements of this gene by translocation can cause acute myeloid leukemia. The NSD1 gene product is a SET-domain histone lysine methyltransferase that has previously been shown to interact with nuclear receptors. We describe here a novel NSD1-interacting protein, Nizp1, that contains a SCAN box, a KRAB-A domain, and four consensus C2H2-type zinc fingers preceded by a unique finger derivative, referred to herein as the C2HR motif. The C2HR motif functions to mediate protein-protein interaction with the cysteine-rich (C5HCH) domain of NSD1 in a Zn(II)-dependent fashion, and when tethered to RNA polymerase II promoters, represses transcription in an NSD1-dependent manner. Mutations of the cysteine or histidine residues in the C2HR motif abolish the interaction of Nizp1 with NSD1 and compromise the ability of Nizp1 to repress transcription. Interestingly, converting the C2HR motif into a canonical C2H2 zinc finger has a similar effect. Thus, Nizp1 contains a novel type of zinc finger motif that functions as a docking site for NSD1 and is more than just a degenerate evolutionary remnant of a C2H2 motif.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.