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Article

DYRK1A autophosphorylation on serine residue 520 modulates its kinase activity via 14-3-3 binding.

Molecular biology of the cell - 1 Apr 2007

Alvarez Mónica, Altafaj Xavier, Aranda Sergi, de la Luna Susana

Abstract excerpt

Dual-specificity tyrosine-phosphorylated and regulated kinase (DYRK) proteins are an evolutionarily conserved family of protein kinases, with members identified from yeast to humans, that participate in a variety of cellular processes. DYRKs are serine/threonine protein kinases that are activated...

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Identifiers

PMID: 17229891
DOI: 10.1091/mbc.e06-08-0668
PMCID: PMC1838983

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-17229891-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

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DYRK1A autophosphorylation on serine residue 520 modulates its kinase activity via 14-3-3 binding.PMID 17229891Read ↗

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DYRK1A binds to an evolutionarily conserved WD40-repeat protein WDR68 and induces its nuclear translocationSemantic proximity Read ↗

Cloning and Characterization of DYRK1B, a Novel Member of the DYRK Family of Protein KinasesSemantic proximity Read ↗

Phosphoproteomics identifies the DYRK1B protein kinase as a regulator of processing bodiesSemantic proximity Read ↗

Splice Variants of the Dual Specificity Tyrosine Phosphorylation-regulated Kinase 4 (DYRK4) Differ in Their Subcellular Localization and Catalytic ActivitySemantic proximity Read ↗

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Identification of FAM53C as a cytosolic-anchoring inhibitory binding protein of the kinase DYRK1ASemantic proximity Read ↗

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Proteasome regulation by reversible tyrosine phosphorylation at the membrane.Semantic proximity Read ↗

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