UniProt ID | DYRK3_MOUSE | |
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UniProt AC | Q922Y0 | |
Protein Name | Dual specificity tyrosine-phosphorylation-regulated kinase 3 | |
Gene Name | Dyrk3 {ECO:0000312|MGI:MGI:1330300} | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 586 | |
Subcellular Localization | Nucleus . Cytoplasmic granule . Shuttles between cytoplasm and stress granules. Localized predominantly on distinct speckles distributed throughout the cytoplasm of the cell. At low concentration, showns a homogeneous distribution throughout the cyto | |
Protein Description | Dual-specificity kinase which possesses both serine/threonine and tyrosine kinase activities. Negative regulator of EPO-dependent erythropoiesis, may place an upper limit on red cell production during stress erythropoiesis. Inhibits cell death due to cytokine withdrawal in hematopoietic progenitor cells (By similarity). May act by regulating CREB/CRE signaling. [PubMed: 12356771 Stabilizes and prevents stress granule disassembly thereby regulating mTORC1 signaling during cellular stress. During stressful conditions, DYRK3 partitions to the stress granule from the cytosol, as well as mTORC1 components, which prevents mTORC1 signaling. When stress signals are gone, the kinase activity of DYRK3 is required for the dissolution of stress granule and mTORC1 relocation to the cytosol, and promotes the phosphorylation of the mTORC1 inhibitor, AKT1S1, allowing full reactivation of mTORC1 signaling. Promotes cell survival upon genotoxic stress through phosphorylation of SIRT1. This in turn inhibits TP53 activity and apoptosis (By similarity] | |
Protein Sequence | MGGAARDRGRKDAALPGAGLPPQQRRLGDGVYDTFMMIDETKGPPYSDTFSNPSEAPVSRRLNITTEPLTRGHTQHFVNGSEMKVEQLFQEFGNRRSNTLQSDGISNSEKSSPASQGKSSESLSAVKCNLSSRPSKVLPLTPEQALKQYKHHLTAYEKLEIVSYPEIYFVGPNAKKRQGVIGGPNNGGYDDADGAYIHVPRDHLAYRYEVLKIIGKGSFGQVARVYDHKLRQYVALKMVRNEKRFHRQAAEEIRILEHLKKQDKTGSMNVIHMLESFTFRNHVCMAFELLSIDLYELIKKNKFQGFSVQLVRKFAQSILQSLDALHKNKIIHCDLKPENILLKHHGRSATKVIDFGSSCFEYQKLYTYIQSRFYRAPEIILGCRYSTPIDIWSFGCILAELLTGQPLFPGEDEGDQLACMIELLGMPPQKLLEQSKRAKYFINSKGLPRYCSVSTQTDGRVVLLGGRSRRGKKRGPPGSKDWATALKGCGDYLFIEFLKRCLQWDPSARLTPAQALRHPWISKSTPKPLTMDKVPGKRVVNPTNAFQGLGSKLPPVVGIASKLKANLMSETSGSIPLCSVLPKLIS | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
208 | Phosphorylation | RDHLAYRYEVLKIIG CHHHHHHHEEHHHHC | 9.56 | 22817900 | |
317 | Phosphorylation | LVRKFAQSILQSLDA HHHHHHHHHHHHHHH | 23.10 | 17203969 | |
366 | Phosphorylation | CFEYQKLYTYIQSRF HHHHHHHHHHHHHHH | 12.44 | 28066266 | |
367 | Phosphorylation | FEYQKLYTYIQSRFY HHHHHHHHHHHHHHH | 25.28 | 22499769 | |
368 | Phosphorylation | EYQKLYTYIQSRFYR HHHHHHHHHHHHHHC | 5.38 | 22499769 | |
371 | Phosphorylation | KLYTYIQSRFYRAPE HHHHHHHHHHHCCCH | 18.13 | 22499769 | |
525 | Phosphorylation | HPWISKSTPKPLTMD CCCCCCCCCCCCCCC | 38.78 | 26239621 | |
530 | Phosphorylation | KSTPKPLTMDKVPGK CCCCCCCCCCCCCCC | 31.67 | 26239621 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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368 | Y | Phosphorylation | Kinase | DYRK3 | Q922Y0 | PSP |
Modified Location | Modified Residue | Modification | Function | Reference | ||
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Oops, there are no descriptions of PTM sites of DYRK3_MOUSE !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
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Oops, there are no SNP-PTM records of DYRK3_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
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Oops, there are no PPI records of DYRK3_MOUSE !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry."; Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.; J. Proteome Res. 6:250-262(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-317, AND MASSSPECTROMETRY. | |
"DYRK3 activation, engagement of protein kinase A/cAMP responseelement-binding protein, and modulation of progenitor cell survival."; Li K., Zhao S., Karur V., Wojchowski D.M.; J. Biol. Chem. 277:47052-47060(2002). Cited for: FUNCTION, AND MUTAGENESIS OF LYS-237; TYR-366 AND TYR-368. |