HMGN2 Antibodies

Non-histone chromosomal protein HMG-17 (HMGN2)

Binds to the interior side of the nucleosomal DNA thus altering the interaction between the DNA and the histone octamer. May be involved in the process which maintains transcribable genes in a unique chromatin conformation (By similarity).

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Gene Information

Human
Gene Name:	HMGN2
Uniprot:	P05204
Entrez:	3151

Family

Belongs to:
HMGN family

Alternative Names

High mobility group nucleosome-binding domain-containing protein 2; high-mobility group (nonhistone chromosomal) protein 17; high-mobility group nucleosomal binding domain 2; HMG17high mobility group protein N2; MGC5629; MGC88718; non-histone chromosomal protein HMG-17; nonhistone chromosomal protein HMG-17

Molecular Weight

Mass (kDA):
9.393 kDA

Genomic Context

Human
Location:	1p36.11
Sequence:	1; NC_000001.11 (26472440..26476642)

Subcellular Localizations

Nucleus. Cytoplasm. Cytoplasmic enrichment upon phosphorylation.

Diseases

• Neoplasms
• Malignant Neoplasms
• Hepatitis B
• Hepatitis
• Cell Invasion
• Infective Disorder
• Cell Transformation, Neoplastic
• Pneumonia
• Prostatic Neoplasms
• Malignant Neoplasm Of Prostate
• Corneal Diseases
• Malignant Neoplasm Of Breast
• Alveolar Bone Loss

• Carcinoma
• Chronic Periodontitis
• Mammary Neoplasms
• Adenocarcinoma
• Malignant Paraganglionic Neoplasm
• Suppressor Mutation
• Inflammation

Interacting Proteins

• TERF2

Pathways

• Localization
• Chromatin Remodeling
• Mitosis
• Cell Cycle
• Dna Replication
• Dna Repair
• Metaphase
• Atp-dependent Chromatin Remodeling
• Methylation
• Translation
• Interphase
• Eye Development
• Receptor Transactivation

• Hair Follicle Development
• Oocyte Maturation
• Chondrocyte Differentiation
• Embryo Development
• Mismatch Repair
• Nucleosome Assembly
• Fermentation

PTMs

• Phosphorylation
• Acetylation

• Cleavage
• Methylation

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/HMGN2

Best Uses Of The HMGN2 Marker

In this article, you will learn about HMGN2 and its functions in gene regulation. In addition, you will discover why HMGNs bind to MNH3K27ac and how they influence cellular transcription profiles. Ultimately, your knowledge of HMGNs will help you to find the best applications for this marker. HMGNs are also associated with chromatin regulatory sites, which is why they can influence cell-type specific transcription factors.

HMGN2

HMGN2 is an oncoprotein that is found in the extracellular space. It is translocated from the nucleus to the cytoplasm before being released into the extracellular space. HMGN2 contains tumor-homing activity at its amino-terminus, and its carboxy-terminal region inhibits tumor invasion and metastasis. Its role in tumor growth is unclear, but it is a potential therapeutic target.

The binding sites of HMGNs are cell-type specific, and they are colocalized with epigenetic marks that identify regulatory sites in active chromatin. These colocalizations are a major advantage of HMGNs as a genetic tool. Furthermore, they are associated with gene expression. For example, a gene with high cell-specificity is likely to contain many copies of the HMGN2 gene.

HMGNs bind cell-type-specific enhancer elements, which are responsible for maintaining a cell's identity. They also oppose ATP-dependent chromatin remodeling, which is associated with chromatin compaction. This is due to dynamic interactions of cell-type-specific transcription factors with accessible chromatin regulatory sites. In this process, the HMGN2 marker is key to the maintenance of cell identity.

One of the most exciting uses of HMGN2 is as a genetic marker. Researchers can use HMGN2 to study gene function. Researchers have discovered that HMGN2 preserves transcriptional activation of RGC genes. This protein also contributes to global chromatin accessibility and promotes lateral cortical expansion. By preserving chromatin accessibility, HMGN2 can contribute to our understanding of how chromatin architecture can influence transcription.

HMGN2 is a highly conserved protein found in the human fetal cerebral cortex and the SVZ of the hippocampal dentate gyrus, two regions that are involved in neurogenesis. It is found in newborn neurons that express PSA-NCAM. This makes it an ideal marker to identify neurogenesis in the early stages of development. The use of HMGN2 in research is expanding rapidly.

The HMGN2 marker has been used to study somatic cell nuclear reprogramming. In mice, HMGN2 decreases the rate of cellular reprogramming, but despite this it does not alter the stable properties of reprogrammed cells. In addition, HMGN2 is essential in regulating the function of Postnikov and Bustin, which are essential for chromatin structure and function.

HMGNs regulate transcription

HMGNs regulate transcription by binding to nucleosomes and chromatin fragments that contain H3K27ac. However, the protein does not exhibit a preference for H3K27me3, the active chromatin mark. Instead, HMGNs are found in large quantities on transcribed chromatin and may be a direct target of RNA pol II polymerase. Here we will discuss some of the mechanisms by which HMGNs regulate transcription.

One of the key features of HMGNs is their intrinsic disorder, which limits their ability to affect transcription at high levels. As a result, doubling the number of HMGN proteins had a much greater impact on the cellular transcription profile than a total deletion. Because HMGNs are highly variable in their structural organization, their effects on transcription are likely influenced by multiple factors, including their intrinsic disorder. This disorder, along with the presence of multiple partners, may explain how the various HMGN variants regulate transcription in cells.

Moreover, loss of HMGN decreases the binding of Brd3 and p300 to chromatin. This result is consistent with earlier findings in other systems. This study highlights the important role of HMGNs in regulating transcription. The binding sites of TFs and HMGNs are directly associated with chromatin and thus affect the transcription process in ESCs. The role of HMGN in transcription is largely unclear, but the findings suggest that the protein may act as a key regulator of gene expression.

HMGNs are protein sequence-specific regulatory factors that influence transcription by interacting with proteins that modify chromatin. Furthermore, these proteins affect the levels of histone modification and regulate chromatin remodeling. These proteins are highly conserved and have a high degree of similarity, making them potentially similar for regulation. In vitro biochemical studies show that the HMGNs regulate transcription by interacting with specific components of chromatin.

Interestingly, HMGNs have a limited impact on the transcription of a cell. HMGN5S17,21E and HMGN3a have no effect on transcription, but the effects of swap mutants differ from those of HMGN1. These findings suggest that the functional specificity of HMGN variants is dependent on the overall structure of the protein. These results have implications for drug development. If you are concerned about how HMGNs regulate transcription, it would be in your best interests to consider genetically-modified MEFs.

HMGNs bind to nucleosomes

HMGNs are a family of transcription factors that preferentially bind to chromatin, including enhancers and promoters. Loss of HMGNs decreases the occupancy of p300 and Brd3 on chromatin. Furthermore, loss of HMGNs affects the occupancy of bromodomain-containing proteins Brd3 and acetyltransferase p300, though not always.

HMGNs bind to nucleomes and interact with chromatin dynamically. The proteins bind to nucleosomes with a low degree of specificity toward DNA sequence, and are able to dissociate from nucleosome-chromatin binding sites rapidly. The proteins also alter interactions between linker histone h2 and chromatin, reducing chromatin compaction.

In addition, HMGNs preferentially bind to rMNH3K27ac, which is a mark of transcriptionally silent chromatin. The data from these experiments support the idea that HMGNs may hinder the activity of transcription factors by limiting the access to chromatin. If you're interested in finding out whether or not HMGNs bind to nucleosomes, you should read on!

The occupancy of HMGN at transcription start sites is directly related to gene expression. The most highly expressed genes have the highest HMGN occupancy, while the least expressed ones are the lowest. Therefore, it is likely that HMGNs influence cell identity and function through their binding to nucleosomes. In addition, HMGNs are involved in the dynamic establishment of cell type-specific chromatin epigenetic landscapes.

At the onset of reprogramming, HMGNs are present in MEF super-enhancers. However, their occupancy decreases during the reprogramming process. In addition, they are localized at ESC super-enhancers in fully reprogrammed cells. The HMGN organization in iPSCs and ESCs is similar. HMGNs gradually relocate from MEFs-specific chromatin regulatory sites to ESCs-specific ones.

HMGN proteins are expressed in nearly every vertebrate cell and the amino acid sequences have remained conserved throughout evolution. The level of HMGN protein varies according to developmental stage, and changes in HMGN levels are associated with altered cellular phenotypes. They are essential for the proper functioning of the genome, and alterations in their levels affect many aspects of cellular behavior.

HMGNs bind to MNH3K27ac

In this study, we show that HMGNs preferentially bind to MNH3K27a and MNH3K27me3, demonstrating the potential for HMGNs to interact with these two histone modifications. These results were confirmed by a two-color mobility shift assay. These results also demonstrate that HMGNs can modulate the binding of H3K27me3 to H3K27ac.

These findings are consistent with previous studies showing that HMGNs are essential for oligodendrocyte differentiation. Knockout mice lacking HMGN1&2 have a reduced population of oligodendrocytes compared to wild-type animals. Furthermore, knockout mice of both HMGN1 and HMGN2 do not exhibit reduced numbers of oligodendrocytes in spinal tissues. However, ChIP-seq analysis revealed that HMGN1 and HMGN2 bind to nucleosomes. Further, HMGN3 is found to have a high level of expression in adult mice, mainly in the inner nuclear cells and ganglion cells. Moreover, the protein is distributed unevenly in pre-fated cells.

HMGN1 and HMGN2 colocalize with H3K27ac in mouse ESCs, rBs, and effs. Their co-localization with H3K27ac is significantly associated with their respective gene expression levels. Furthermore, loss of HMGNs increases H3K27ac levels in the cells and promotes increased H3K27me3 occupancy.

Although acetylation does not constitute a major HMGN binding site, it is a key determinant in the preferred binding of HMGN to MNH3K27ac. In addition to acetylation, HMGNs also colocalize with MNH3K27ac. Interestingly, the acetyl moiety is not a major determinant in the binding of HMGNs to MNH3K27ac.

HMGNs are ubiquitous nuclear proteins that bind dynamically to chromatin without preference to DNA sequence. They colocalize with H3K27ac and are known to bind to specific genomic regions, including super-enhancers. In addition, HMGNs also localize to genomic regions with high H3K27ac content. These findings will provide more insight into the molecular mechanism by which HMGNs control gene expression.

HMGNs preferentially bind to chromatin fragments with MNH3K27ac, while they do not show preference for other active chromatin marks, such as H3K27me3 (a mark of transcriptionally silent compact chromosomes).