DYRK1A Antibodies

Dual specificity tyrosine-phosphorylation-regulated kinase 1A (DYRK1A)

Dual-specificity kinase which possesses both serine/threonine and tyrosine kinase activities. May play a role in a signaling pathway regulating nuclear functions of cell regeneration.

Modulates alternative splicing by phosphorylating the splice factor SRSF6 (By similarity). Has pro-survival function and negatively regulates the apoptotic process.

Gene Information

Human
Gene Name:	DYRK1A
Uniprot:	Q13627
Entrez:	1859

Family

Belongs to:
protein kinase superfamily

Alternative Names

dual-specificity tyrosine-(Y)-phosphorylation regulated kinase 1A; DYRK1; DYRK1A; MNBEC 2.7.110EC 2.7.12; MNBH

Molecular Weight

Mass (kDA):
85.584 kDA

Genomic Context

Human
Location:	21q22.13
Sequence:	21; NC_000021.9 (37365573..37526358)

Tissue Specificity

Ubiquitous. Highest levels in skeletal muscle, testis, fetal lung and fetal kidney.

Subcellular Localizations

Nucleus. Nucleus speckle.

Diseases

• Down Syndrome
• Trisomy
• Alzheimer's Disease
• Malignant Neoplasms
• Neoplasms
• Neurofibrillary Tangles
• Neurodegenerative Disorders
• Nerve Degeneration
• Nervousness
• Dementia
• Partial Trisomy
• Microcephaly

• Memory Impairment
• Cell Transformation, Neoplastic
• Haploinsufficiency
• Leukemia
• Hypertrophy
• Neuropathology Disease

Interacting Proteins

• DCAF7
• LZTS2
• RB1
• RBL1
• TROAP

• YWHAB

Pathways

• Brain Development
• Neurogenesis
• Localization
• Pathogenesis
• Cell Cycle
• Cell Death
• Cell Proliferation
• Hyperphosphorylation
• Rna Interference
• Aging
• Translation
• Mitosis
• Senescence

• Cell Growth
• Cell Migration
• Cell Division
• Oocyte Maturation
• Endocytosis
• Clathrin-mediated Endocytosis
• Cell Differentiation

PTMs

• Phosphorylation
• Dephosphorylation
• Cleavage

• Deacetylation
• Acetylation
• Methylation

• Ubiquitination

Research Areas

• Protein Kinase

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/DYRK1A

Best Uses Of The DYRK1A Marker

This article will help you determine the gene based on its sequence. The DYRK1A gene encodes a member of the Dual-specificity tyrosine-phosphorylation-regulated kinase family. This gene interacts well other proteins, for instance, glycogen synthase. The sequence of the gene and its phosphorylation locations have been characterized, and then used to create pGEXDYRK1A.

DYRK1A is a member of the Dual-specificity tyrosine-phosphorylation-regulated kinase family

DYRK1A is a member the Dual-specificity, T-ph-regulated Kinase Family. It has a multitude of functions. It is responsible to phosphorylate Map1b at S1392 to prepare it for Gsk3 beta at 605004. It is responsible for regulating the microtubule's stability in developing cortical neurons.

DYRK1A inhibitors are a brand new area of research. A growing number of active molecules have been identified and are being tested. Becker and Sippl discuss the present status of DYRK1A inhibitions. Below are a few examples of the currently available inhibitors.

DYRK1A is an transcription factor that regulates a wide range of gene expression. Its gene product was found to be expressed in skeletal muscle and the heart tissue. A number of isoforms of DYRK1A have been identified and the PEST sequence is believed to be responsible for the rapid degradation of the protein. The most abundant transcript is isoform-1 that contains 763 amino acid.

It also phosphorylates glycogen synase

The ATP-dependent glycogen synthesis enzyme GSK-3 regulates glucose metabolism by activating the enzyme at Ser652 and Ser648 residues. This blocks glycogen synthase's activity which is vital for getting rid of excess glucose from cells. GSK-3 also inhibits the insulin receptor from phosphorylating IRS-1 on tyrosine residues.

GSK-3 regulates cellular glucose homeostasis and glycogen production in a variety of ways. It also functions as a suppressor of the Wnt signaling pathways and inhibits cell proliferation through the phosphorylation their serine-containing enzymes. It has been proven to regulate the levels of b-catenin , which plays an important role in the development of cancer.

The multifunctional GSK-3I2 is involved in a variety of physiological processes, and its function in glycogen metabolism is well-documented. GSK-3I2 plays a role in many physiological processes, including glycogen metabolism. It also regulates gene expression, cell cycle and tau-protein. It is also linked to various other diseases and is thought to be a potential therapeutic target for 15 forms of cancer. This makes GSK-3I2 among the most intriguing targets for the development and development of selective, potent inhibitors.

It interacts with HAN11

We recently discovered that the DYRK1A marker is able to interact with HAN11 which is a protein that is expressed in the cytosol of normal cells. However, we're not certain if this interaction transient or regulated by the cell type. The DYRK1A gene is mostly cytosolic in physiological conditions however it is found in the nucleus of ectopically expressed cells. We have developed a pipeline to address this issue. It takes into account the effectiveness of DYRK1A enrichment as well as the molecular weights of the interactions.

Our results suggest that DYRK1A assists in the repair of a subset of DSBs induced by IR, but it may not play a part in overall cell survival. Our results also suggest that DYRK1A could be a weak predictor during the DNA damage reaction. We believe that DYRK1A could be involved in the process of promoting repair of a subset of DSBs that trigger IR and IR, this repair might not have a significant effect on the survival of cells.

Adult mice have DYRK1A genes that are expressed in a variety of brain areas. It is also associated with GABAergic neurons and glutamatergic synapses. The interaction between DYRK1A and HAN11 has implications in various clinical scenarios. The interplay between DYRK1A and HAN11 expression levels within human cells suggests that genes associated with dysregulation HAN11 could be related to the development of the brain.

The E3 ubiquitin ligase RNF169 is one of the proteins that was interacted with DYRK1A. The AP-MS analysis also revealed DYRK1A. This protein is involved in the response to DNA damage, and it limits the activity of the p53-binding protein. Both proteins are highly enriched in categories related to DNA damage.

Many different cellular and molecular pathways have been implicated in the function of DYRK1A. DYRK1A has been implicated in the interaction between many substrates and proteins. The list of DYRK1A targets will continue to grow. As we continue to discover more about the DYRK1A gene, it will be important to observe its role in these processes.

It was used to create pGEX DYRK1A

The cDNA that encodes DYRK1A was cloned into a pBEN-SGC vector, which contains an Strep-tag(r) II sequence at the N-terminus the catalytic domain. PGK-Neo selection cassettes are used to insert an loxP downstream site upstream of exon 5 and downstream of exon 6. The mutants were then bred with mouse strains C57BL/6NJ.

Transfection of the DYRK1AK188R-derived plasmid resulted in stable cell lines expressing this gene. The cells expressed neurites that were three to four times larger than the body of the cell after two days of NGF treatment. Similar patterns of neurites were seen in cells transfected with vectors. DYRK1A stimulates the growth of neurites in PC12 cells, regardless of its kinase activity.

In a later study, it was discovered that downregulation of DYRK1A caused an increase in SF3b1's phosphorylation at the Thr434 (a residue found within SF3b1). This study did not include DYRK1A coexpression. It was found that pGEX -DYRK1A decreased the phosphorylation level at Thr434 in SF3b1. This suggests that DYRK1A can be phosphorylated by other residues of SF3b1 (the exogenous phosphatase).

The DYRK1A CDNA was isolated using PCR from a human fetal kidney CDNA library. The DYRK1A DNA was inserted into an NheI site, which was then blunted using T4 DNA polymerase. The DYRK1A cDNA was then transformed into pGEX-DYRK1A vector using site-directed mutagenesis.

The tyrosine-autophosphorylation of DYRK1A proteins is not performed in a temporary state during the process of translation. It takes place quickly during transcription in vitro. The protein is autophosphorylated on a few tyrosine residues, including Y321 (the tyrosine residue responsible for tyrosine autophosphorylation). However, mature DYRK1A does not undergo autophosphorylation in the activation loop.

The serine/threonine-kinase structures are stabilized by autophosphorylation of Y321 while the activation loop's activation loop's protein phosphotyrosine determine the selectivity for CMGC Kinases. The absence of phosphate-moiety the catalytic domain of DYRK1A causes the protein to lose its specific target recognition.