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Description

Dual specificity tyrosine-phosphorylation-regulated kinase 1A (UniProt: Q13627, also known as EC 2.7.12.1, Dual specificity YAK1-related kinase, DYRK1A, HP86, Protein kinase minibrain homolog, MNBH, hMNB) is encoded by the DYRK1A (also known as DYRK, MNB, MNBH) gene (Gene ID: 1859) in human. DYRK1A is a dual-specificity kinase that possesses both serine/threonine and tyrosine kinase activities and plays a role in a signaling pathway regulating nuclear functions of cell proliferation. DYRK family members share a conserved kinase domain and an adjacent DYRK-homology domain or DH-box (DDDNXDY), while differing in their N- and C-terminal regions. DYRK1A is ubiquitous in its distribution and highest levels are observed in skeletal muscle, testis, fetal lung, and fetal kidney. It is also expressed in the developing central nervous system. DYRK1A is regulated by autophosphorylation on serine, threonine, and tyrosine residues, but catalyzes phosphorylation of a broad-range of substrates only on serine/threonine residues within the RPX(S/T)P motif with a preference for proline at position P+1 and arginine at position P-3. The ATP binding region of DYRK1A is localized to amino acids 165-173 and 238-241. Its protein kinase domain is localized to amino acids 159-479. Five isoforms of DYRK1A have been described that are produced by alternative splicing. Mutations in DYRK1A gene are known to cause autosomal dominant mental retardation that is characterized by primary microcephaly, severe mental retardation without speech, and anxious autistic behavior.