DYRK3_MOUSE - dbPTM
DYRK3_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DYRK3_MOUSE
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
208PhosphorylationRDHLAYRYEVLKIIG
CHHHHHHHEEHHHHC
9.5622817900
317PhosphorylationLVRKFAQSILQSLDA
HHHHHHHHHHHHHHH
23.1017203969
366PhosphorylationCFEYQKLYTYIQSRF
HHHHHHHHHHHHHHH
12.4428066266
367PhosphorylationFEYQKLYTYIQSRFY
HHHHHHHHHHHHHHH
25.2822499769
368PhosphorylationEYQKLYTYIQSRFYR
HHHHHHHHHHHHHHC
5.3822499769
371PhosphorylationKLYTYIQSRFYRAPE
HHHHHHHHHHHCCCH
18.1322499769
525PhosphorylationHPWISKSTPKPLTMD
CCCCCCCCCCCCCCC
38.7826239621
530PhosphorylationKSTPKPLTMDKVPGK
CCCCCCCCCCCCCCC
31.6726239621

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
368YPhosphorylationKinaseDYRK3Q922Y0
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DYRK3_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of DYRK3_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of DYRK3_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DYRK3_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.

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