DYRK1A

This gene encodes a member of the Dual-specificity tyrosine phosphorylation-regulated kinase (DYRK) family. This member contains a nuclear targeting signal sequence, a protein kinase domain, a leucine zipper motif, and a highly conservative 13-consecutive-histidine repeat. It catalyzes its autophosphorylation on serine/threonine and tyrosine residues. It may play a significant role in a signaling pathway regulating cell proliferation and may be involved in brain development. This gene is a homolog of Drosophila mnb (minibrain) gene and rat Dyrk gene. It is localized in the Down syndrome critical region of chromosome 21, and is considered to be a strong candidate gene for learning defects associated with Down syndrome. Alternative splicing of this gene generates several transcript variants differing from each other either in the 5' UTR or in the 3' coding region. These variants encode at least five different isoforms. [provided by RefSeq, Jul 2008]

Dual Specificity Tyrosine Phosphorylation Regulated Kinase 1A

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 proliferation. Modulates alternative splicing by phosphorylating the splice factor SRSF6 (By similarity).

Exhibits a substrate preference for proline at position P+1 and arginine at position P-3. Has pro-survival function and negatively regulates the apoptotic process. Promotes cell survival upon genotoxic stress through phosphorylation of SIRT1. This in turn inhibits TP53 activity and apoptosis (By similarity).

Amyloid-beta formation Source: ARUK-UCL
Circadian rhythm Source: UniProtKB
Negative regulation of DNA damage response, signal transduction by p53 class mediator Source: BHF-UCL
Negative regulation of microtubule polymerization Source: ARUK-UCL
Negative regulation of mRNA splicing, via spliceosome Source: Ensembl
Nervous system development Source: ProtInc
Peptidyl-serine autophosphorylation Source: ARUK-UCL
Peptidyl-serine phosphorylation Source: ARUK-UCL
Peptidyl-threonine phosphorylation Source: BHF-UCL
Peptidyl-tyrosine autophosphorylation Source: ARUK-UCL
Peptidyl-tyrosine phosphorylation Source: MGI
Positive regulation of protein deacetylation Source: BHF-UCL
Positive regulation of RNA splicing Source: ARUK-UCL
Positive regulation of transcription, DNA-templated Source: GO_Central
Protein autophosphorylation Source: UniProtKB
Protein phosphorylation Source: UniProtKB
Regulation of alternative mRNA splicing, via spliceosome Source: Ensembl

Nucleus; Nucleus speckle

Mental retardation, autosomal dominant 7 (MRD7):
A disease characterized by primary microcephaly, severe mental retardation without speech, anxious autistic behavior, and dysmorphic features, including bitemporal narrowing, deep-set eyes, large simple ears, and a pointed nasal tip. Mental retardation is characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period.

Autophosphorylated on numerous tyrosine residues. Can also autophosphorylate on serine and threonine residues (in vitro).