dbPTM

DYRK3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DYRK3_HUMAN
UniProt AC	O43781
Protein Name	Dual specificity tyrosine-phosphorylation-regulated kinase 3
Gene Name	DYRK3
Organism	Homo sapiens (Human).
Sequence Length	588
Subcellular Localization	Nucleus . Cytoplasmic granule . Shuttles between cytoplasm and stress granules. Localized predominantly on distinct speckles distributed throughout the cytoplasm of the cell (PubMed:20167603). At low concentration, showns a homogeneous distribution t
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. [PubMed: 10779429 May act by regulating CREB/CRE signaling (By similarity 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]
Protein Sequence	MGGTARGPGRKDAGPPGAGLPPQQRRLGDGVYDTFMMIDETKCPPCSNVLCNPSEPPPPRRLNMTTEQFTGDHTQHFLDGGEMKVEQLFQEFGNRKSNTIQSDGISDSEKCSPTVSQGKSSDCLNTVKSNSSSKAPKVVPLTPEQALKQYKHHLTAYEKLEIINYPEIYFVGPNAKKRHGVIGGPNNGGYDDADGAYIHVPRDHLAYRYEVLKIIGKGSFGQVARVYDHKLRQYVALKMVRNEKRFHRQAAEEIRILEHLKKQDKTGSMNVIHMLESFTFRNHVCMAFELLSIDLYELIKKNKFQGFSVQLVRKFAQSILQSLDALHKNKIIHCDLKPENILLKHHGRSSTKVIDFGSSCFEYQKLYTYIQSRFYRAPEIILGSRYSTPIDIWSFGCILAELLTGQPLFPGEDEGDQLACMMELLGMPPPKLLEQSKRAKYFINSKGIPRYCSVTTQADGRVVLVGGRSRRGKKRGPPGSKDWGTALKGCDDYLFIEFLKRCLHWDPSARLTPAQALRHPWISKSVPRPLTTIDKVSGKRVVNPASAFQGLGSKLPPVVGIANKLKANLMSETNGSIPLCSVLPKLIS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
66	Phosphorylation	PRRLNMTTEQFTGDH CCCCCCCEEEECCCC	19.61	23532336
74	Phosphorylation	EQFTGDHTQHFLDGG EEECCCCCHHHCCCC	28.60	23532336
106	Phosphorylation	TIQSDGISDSEKCSP CCCCCCCCCCCCCCC	40.38	25627689
108	Ubiquitination	QSDGISDSEKCSPTV CCCCCCCCCCCCCCC	31.97	29967540
128	Ubiquitination	SDCLNTVKSNSSSKA CHHHHHHCCCCCCCC	41.71	29967540
131	Ubiquitination	LNTVKSNSSSKAPKV HHHHCCCCCCCCCCE	42.98	29967540
142	Phosphorylation	APKVVPLTPEQALKQ CCCEECCCHHHHHHH	20.79	30622161
148	Ubiquitination	LTPEQALKQYKHHLT CCHHHHHHHHHHHCH	55.38	29967540
151	Ubiquitination	EQALKQYKHHLTAYE HHHHHHHHHHCHHHH	23.27	29967540
197	Ubiquitination	YDDADGAYIHVPRDH CCCCCCCEEEECCHH	9.33	29967540
209	Phosphorylation	RDHLAYRYEVLKIIG CHHHHHHHEEHHHHC	9.56	22817900
217	Ubiquitination	EVLKIIGKGSFGQVA EEHHHHCCCCHHHHH	40.76	29967540
308	Phosphorylation	KNKFQGFSVQLVRKF HCCCCCCCHHHHHHH	18.77	29083192
310	Ubiquitination	KFQGFSVQLVRKFAQ CCCCCCHHHHHHHHH	32.80	29967540
330	Ubiquitination	LDALHKNKIIHCDLK HHHHHHCCEEECCCC	48.09	29967540
350	Phosphorylation	LKHHGRSSTKVIDFG EEECCCCCCEEEECC	30.77	29634919
351	Phosphorylation	KHHGRSSTKVIDFGS EECCCCCCEEEECCC	30.49	-
367	Phosphorylation	CFEYQKLYTYIQSRF HHHHHHHHHHHHHHH	12.44	28152594
368	Phosphorylation	FEYQKLYTYIQSRFY HHHHHHHHHHHHHHH	25.28	28152594
369	Phosphorylation	EYQKLYTYIQSRFYR HHHHHHHHHHHHHHC	5.38	27273156
372	Phosphorylation	KLYTYIQSRFYRAPE HHHHHHHHHHHCCCH	18.13	28152594
388	Phosphorylation	ILGSRYSTPIDIWSF HCCCCCCCCHHHHHH	18.48	24719451
446	Ubiquitination	AKYFINSKGIPRYCS HHHHHCCCCCCCEEE	57.27	-
451	Phosphorylation	NSKGIPRYCSVTTQA CCCCCCCEEEEEECC	5.45	-
453	Phosphorylation	KGIPRYCSVTTQADG CCCCCEEEEEECCCC	17.35	-
455	Phosphorylation	IPRYCSVTTQADGRV CCCEEEEEECCCCEE	9.26	-
456	Phosphorylation	PRYCSVTTQADGRVV CCEEEEEECCCCEEE	21.43	-
469	Phosphorylation	VVLVGGRSRRGKKRG EEEECCCCCCCCCCC	29.60	-
480	Phosphorylation	KKRGPPGSKDWGTAL CCCCCCCCCCHHHHH	32.96	24719451
481	Acetylation	KRGPPGSKDWGTALK CCCCCCCCCHHHHHC	64.51	11688115
485	Phosphorylation	PGSKDWGTALKGCDD CCCCCHHHHHCCCCH	25.27	24719451
488	Acetylation	KDWGTALKGCDDYLF CCHHHHHCCCCHHHH	55.84	11688127
493	Phosphorylation	ALKGCDDYLFIEFLK HHCCCCHHHHHHHHH	7.11	24719451
504	Ubiquitination	EFLKRCLHWDPSARL HHHHHHHCCCCCCCC	30.44	29967540
524	Ubiquitination	LRHPWISKSVPRPLT HCCCCCCCCCCCCCC	46.46	29967540
532	Phosphorylation	SVPRPLTTIDKVSGK CCCCCCCCCHHHCCC	34.56	-
537	Phosphorylation	LTTIDKVSGKRVVNP CCCCHHHCCCEECCH	44.32	-
554	Ubiquitination	AFQGLGSKLPPVVGI HHCCCCCCCCCHHHH	64.31	-
564	Ubiquitination	PVVGIANKLKANLMS CHHHHHHHHHHHHHH	42.20	-
566	Ubiquitination	VGIANKLKANLMSET HHHHHHHHHHHHHCC	36.52	-

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
Oops, there are no upstream regulatory protein records of DYRK3_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
350	S	Phosphorylation		29634919
Autophosphorylation at Ser-350 stabilizes the protein and enhances the protein kinase activity.

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
SORL_HUMAN	SORL1	physical	23602568
SIR1_MOUSE	Sirt1	physical	20167603

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of DYRK3_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-369, AND MASSSPECTROMETRY.	19534553 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-369, AND MASSSPECTROMETRY.	18083107 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-209, AND MASSSPECTROMETRY.	15592455 [Abstract]

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