UBE2K Antibodies

Ubiquitin-conjugating enzyme E2 K (UBE2K)

Accepts ubiquitin in the E1 complex and catalyzes its covalent attachment to other proteins. In vitro, in the presence or in the absence of BRCA1-BARD1 E3 ubiquitin-protein ligase complex, catalyzes the synthesis of 'Lys-48'-linked polyubiquitin chains.

Does not transfer ubiquitin directly to but elongates monoubiquitinated substrate protein. Mediates the selective degradation of short-lived and abnormal proteins, like the endoplasmic reticulum-associated degradation (ERAD) of misfolded lumenal proteins.

Gene Information

Human
Gene Name:	UBE2K
Uniprot:	P61086
Entrez:	3093

Family

Belongs to:
ubiquitin-conjugating enzyme family

Alternative Names

E2(25K); E225K; E2-25K; EC 6.3.2.19; Hip2; HIP-2; huntingtin interacting protein 2; Huntingtin-interacting protein 2; HYPG; LIG; UbcH1; UBE2K; UBE2K-25K; ubiquitin carrier protein; ubiquitin-conjugating enzyme E2 K; Ubiquitin-conjugating enzyme E2(25K); Ubiquitin-conjugating enzyme E2-25 kDa; Ubiquitin-conjugating enzyme E2-25K; ubiquitin-conjugating enzyme E2K (UBC1 homolog, yeast); ubiquitin-protein ligase

Molecular Weight

Mass (kDA):
22.407 kDA

Genomic Context

Human
Location:	4p14
Sequence:	4; NC_000004.12 (39698136..39782792)

Tissue Specificity

Expressed in all tissues tested, including spleen, thymus, prostate, testis, ovary, small intestine, colon, peripheral blood leukocytes, T-lymphocytes, monocytes, granulocytes and bone marrow mononuclear cells. Highly expressed in brain, with highest levels found in cortex and striatum and at lower levels in cerebellum and brainstem.

Subcellular Localizations

Cytoplasm.

Diseases

• Huntington Disease
• Neurotoxicity Syndromes
• Alzheimer's Disease
• Neuroaxonal Dystrophies
• Nerve Degeneration
• Schizophrenia
• Pathological Dilatation
• Atherosclerosis
• Malignant Tumor Of Cervix
• Dystrophy
• Psychotic Disorders
• Parkinson Disease

• Retinoblastoma
• Malignant Neoplasms
• Cytomegalovirus Infections
• Dislocations
• Neoplasms
• Arteriosclerosis
• Machado-joseph Disease

Interacting Proteins

• CCNB1
• DDI1
• DTX3
• HTT
• MIPOL1

• REL
• RNF138
• RNF5
• SIAH1
• TRIM27

• TRIM39

Pathways

• Cell Death
• Pathogenesis
• Conjugation
• Cell Cycle
• Protein Phosphorylation
• Transport
• S Phase
• G1 Phase

• Proteolysis
• Localization
• Autophagy

PTMs

• Ubiquitination
• Phosphorylation

• Cleavage
• Acetylation

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/UBE2K

Best Uses Of The UBE2K Marker

The UBE2K gene is involved in ubiquitination and proteasomal degradation of histone H3. It regulates the levels of SETDB1 and H3K9me3 in distinct genes. If you want to know more about the gene, you can read this article. It will help you determine the best uses of this marker. It can be used in various types of studies, including epigenetics, cell biology, immunohistochemistry, and ELISA.

UBE2K modulates ubiquitination and proteasomal degradation of histone H3

This study examined the effects of siRNA against UBE2K on histone H3 in mouse fibroblasts. RNA-sequencing analysis was conducted using hESCs expressing a control or UBE2K shRNA. RNA-sequencing spectra were homogenized, centrifuged, and digested with trypsin at a ratio of 1:100 w/w. The protein samples were cleared one day after treatment.

A subunit of UBE2K, Hip2, is a ubiquitin-conjugating enzyme that interacts with a polyubiquitin-conjugating enzyme called E3-ubiquitin ligase. This enzyme plays an essential role in the UPS-mediated degradation of proteins. During the degradation process, the enzymes of the proteasome elongate the monoubiquitinated substrate protein. Consequently, UBE2K plays a critical role in cell-cycle regulation of histone levels.

The worm orthologue of UBE2K, ubc-20, regulates the levels of histone H3 and H3K9me3 in Caenorhabditis elegans germ cells. UBE2K mediated ubiquitination and proteasomal degradation of histone H3 influences the stability of germ cells and total protein levels.

A knockdown of UBE2K in hESCs impairs the ability to generate mature NPCs. These cells expressed reduced levels of neuronal markers and did not produce neuronal extensions, synaptic proteins, or neurites. In addition, knockdown of UBE2K does not affect the ability to differentiate hESCs to neuroectoderm.

Knockdown of UBE2K inhibits ubiquitination and proteasomasomal degradation of histone H3 and impairs the induction of distinct neural genes. Moreover, altered UBE2K levels impair neurogenesis. This study demonstrates the importance of UBE2K in neuronal differentiation.

The bacterial cloned in E. coli (OP50)73 was used to produce plasmids containing UBE2K. The clones that were resistant to puromycin were further expanded for further experiments. Once clones were produced, UBE2K was transiently expressed in human fibroblasts.

The elution of the peptides was performed by incubating the hESCs or HEK293 cells in a binding buffer of 10 mM EDTA and 1% Triton X-100. Inhibitors were added to the elution buffer. Finally, hESCs and HEK293 cells were scraped from the plates and stained using the Boster Bio UBE2K.

All studies performed on mice were conducted on these two strains of histone H3 fusion proteins were statistically significant. A positive score was deemed significant if a t-test was more than four points. Overall, the results show that UBE2K is a potent inhibitor of histone H3 fusion proteins.

The results also showed that hip2 knockdown decreased the frequency of BrdU positive cells in MKN45 and AGS cell lines. In addition, GC cells with hip2 knockdowns displayed reduced migration and invasion when compared to controls. This suggests that hip2 knockdowns inhibit cancer cell invasion and growth. These findings also suggest that ubiquitination and degradation of histone H3 are potent therapeutic agents in the fight against cancer.

Similarly, a high level of hip2 expression correlates with a poor prognosis. For example, in a study of patients with GC, Hip2 expression correlated with the overall survival rate. The findings were based on data obtained from patients with STAD and enrolled in the TCGA database. However, there was no correlation between hip2 expression and gender.

It regulates SETDB1 levels

SETDB1 is a cancer-related gene. The gene has many roles in tumorigenesis, including the regulation of the epithelial-mesenchymal transition (EMT). Moreover, SETDB1 methylation inhibited Smad3/4-mediated H3K9 acetylation of the SNAI1 promoter, leading to inhibition of EMT. Additionally, SETDB1 methylation was involved in the oncogenic activation of Akt.

SETDB1 has three SUMO-interacting motifs. In addition to its role in repressing transcription, it is involved in a methyltransferase activity on H3K9, which controls gene silencing. To date, few biological assays have been developed based on the activity of SETDB1 in human cancers. Boster Bio has developed an antibody for SETDB1 that reacts with a wide variety of animal samples, including mouse and rabbit. SETDB1 methylates Lys-9 on histone H3 and coordinates this activity with DNA methylation.

SETDB1 stabilizes the gain-of-function mutant p53 R249S. Mutant p53 is methylated at K370, resulting in enhanced cell proliferation and migration. Knockdown of SETDB1 results in decreased levels of K370me2 in HCCLM3 cells. SETDB1 has important roles in tumor progression.

This UBE2K marker controls SETDB1 levels in human tumors. Compared with other UBE2K inhibitors, it inhibits tumor growth and increases cell differentiation. The inhibitors of SETDB1 also inhibited the expression of TP53, a gene that controls the expression of SETDB1.

Moreover, the gene regulates the activity of the Wnt signaling pathway. SETDB1 is a candidate oncogene in PCa and has tremendous therapeutic potential. These findings provide evidence for SETDB1 inhibition. However, further studies are required to confirm these findings. So far, the UBE2K marker is a promising candidate for cancer research. There is considerable interest in this tumor suppressor.

SETDB1 inhibits the activity of five transcription factors, including CDX2, ELF3, HNF4G, and VDR. Hence, knockdown of SETDB1 decreases the expression of the oncogene Myc and promotes the differentiation of colon epithelial cells. In addition, patients with BRC with high SETDB1 expression had poorer survival.

It modulates H3K9me3 levels in distinct genes

UBE2K is a multifunctional protein that regulates H3K9me3 levels in distinct gene regions. It is also a critical regulator of H3K9 trimethylation, and is essential for the maintenance of the histone chromatin structure in ESCs and immortal germ cells. In fact, its expression regulates H3K9me3 levels in more than 60 genes, and can be utilized for gene targeting and drug discovery.

The UBE2K marker, which is found in the gene ubc-20, regulates the levels of histone H3 and H3K9me3 in distinct gene regions. It is a versatile and highly sensitive tool for identifying alterations in histone H3 levels. Furthermore, it is compatible with the genome-wide sequence of human cancer genes.

In addition to its ability to target specific genes, UBE2K also regulates the ubiquitin-proteasome system. It has been found that ectopic expression of UBE2K reduced H3 levels and reduced H3K9me3 in human HEK293 cells. In addition, it was found that a proteasome inhibitor, MG-132, significantly reduced UBE2K's effect on histone H3.

Loss of UBE2K increases global H3K9 trimethylation, while loss of the UBE2K protein inhibits the induction of distinct genes. Consequently, UBE2K is required for commitment of hESCs to neuroectoderm fate, although a role in neurogenesis is still unknown. For now, the UBE2K marker is a valuable tool to help scientists study the role of UBE2K in neural differentiation.

The Boster Bio UBE2K Marker is a powerful gene therapy for cancer and other inflammatory disorders. The UBE2K protein is found in many tissues and has been shown to reduce the expression of multiple genes. The results of the Boster Bio UBE2K Marker in cancer cell lines are promising. The data obtained from the study will provide valuable information for drug development.

MG-132, along with other small molecules, binds to a particular protein called H3F3A, and induces ubiquitination of the protein. This is a highly effective drug, as it binds to H3K9me3 sites on DNA and RNA, and regulates the activity of various genes in the body.