DYR1A_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: DYR1A_MOUSE
• UniProt AC: Q61214
• Protein Name: Dual specificity tyrosine-phosphorylation-regulated kinase 1A
• Gene Name: Dyrk1a
• Organism: Mus musculus (Mouse).
• Sequence Length: 763
• Subcellular Localization: Nucleus speckle .
• Protein Description: Dual-specificity kinase which possesses both serine/threonine and tyrosine kinase activities. May play a role in a signaling pathway regulating nuclear functions of cell proliferation. Modulates alternative splicing by phosphorylating the splice factor SRSF6 (By similarity). Exhibits a substrate preference for proline at position P+1 and arginine at position P-3. Has pro-survival function and negatively regulates the apoptotic process. Promotes cell survival upon genotoxic stress through phosphorylation of SIRT1. This in turn inhibits TP53 activity and apoptosis. [PubMed: 20167603]
• Protein Sequence: MHTGGETSACKPSSVRLAPSFSFHAAGLQMAAQMPHSHQYSDRRQPSISDQQVSALPYSDQIQQPLTNQVMPDIVMLQRRMPQTFRDPATAPLRKLSVDLIKTYKHINEVYYAKKKRRHQQGQGDDSSHKKERKVYNDGYDDDNYDYIVKNGEKWMDRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHFMFRNHLCLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPELSIIHCDLKPENILLCNPKRSAIKIVDFGSSCQLGQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHILDQAPKARKFFEKLPDGTWSLKKTKDGKREYKPPGTRKLHNILGVETGGPGGRRAGESGHTVADYLKFKDLILRMLDYDPKTRIQPYYALQHSFFKKTADEGTNTSNSVSTSPAMEQSQSSGTTSSTSSSSGGSSGTSNSGRARSDPTHQHRHSGGHFAAAVQAMDCETHSPQVRQQFPAPLGWSGTEAPTQVTVETHPVQETTFHVAPQQNALHHHHGNSSHHHHHHHHHHHHHGQQALGNRTRPRVYNSPTNSSSTQDSMEVGHSHHSMTSLSSSTTSSSTSSSSTGNQGNQAYQNRPVAANTLDFGQNGAMDVNLTVYSNPRQETGIAGHPTYQFSANTGPAHYMTEGHLAMRQGADREESPMTGVCVQQSPVASS

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
14	Phosphorylation	TSACKPSSVRLAPSF CCCCCCCCCCCCCCC	21.56	-
22	Phosphorylation	VRLAPSFSFHAAGLQ CCCCCCCEEEHHHHH	22.06	22322096
47	Phosphorylation	YSDRRQPSISDQQVS CCCCCCCCCCHHHHH	26.79	30352176
49	Phosphorylation	DRRQPSISDQQVSAL CCCCCCCCHHHHHCC	33.43	29895711
59	Phosphorylation	QVSALPYSDQIQQPL HHHCCCCCHHCCCCC	22.54	29895711
67	Phosphorylation	DQIQQPLTNQVMPDI HHCCCCCCCCCCCHH	30.23	29895711
111	Phosphorylation	YKHINEVYYAKKKRR HHHHHHHHHHHHHHH	7.48	22817900
136	Phosphorylation	HKKERKVYNDGYDDD CHHCHHCCCCCCCCC	15.57	25195567
140	Phosphorylation	RKVYNDGYDDDNYDY HHCCCCCCCCCCCCE	21.04	22499769
145	Phosphorylation	DGYDDDNYDYIVKNG CCCCCCCCCEEEECC	19.67	25177544
147	Phosphorylation	YDDDNYDYIVKNGEK CCCCCCCEEEECCCC	9.39	22499769
159	Phosphorylation	GEKWMDRYEIDSLIG CCCEECCEECHHHCC	16.99	-
177	Phosphorylation	FGQVVKAYDRVEQEW HHHHHHHHHHHHHEE	9.88	-
219	Phosphorylation	KHDTEMKYYIVHLKR HCCCHHHHHHHHHHH	9.34	-
310	Phosphorylation	IKIVDFGSSCQLGQR EEEEECCCCCHHHHH	28.12	-
319	Phosphorylation	CQLGQRIYQYIQSRF CHHHHHHHHHHHHHH	9.46	27742792
321	Phosphorylation	LGQRIYQYIQSRFYR HHHHHHHHHHHHHCC	5.51	18388127
324	Phosphorylation	RIYQYIQSRFYRSPE HHHHHHHHHHCCCHH	18.13	25177544
402	Phosphorylation	FEKLPDGTWSLKKTK HHCCCCCCCCEEECC	21.18	-
449	Phosphorylation	SGHTVADYLKFKDLI CCCCHHHHHHHHHHH	11.31	-
453	Ubiquitination	VADYLKFKDLILRML HHHHHHHHHHHHHHH	50.46	-
466	Phosphorylation	MLDYDPKTRIQPYYA HHCCCCCCCCCCHHH	38.09	-
511	Phosphorylation	SSGTTSSTSSSSGGS CCCCCCCCCCCCCCC	32.18	25338131
529	Phosphorylation	SNSGRARSDPTHQHR CCCCCCCCCCCCCCC	47.13	25266776
532	Phosphorylation	GRARSDPTHQHRHSG CCCCCCCCCCCCCCC	38.88	30635358
538	Phosphorylation	PTHQHRHSGGHFAAA CCCCCCCCCCHHHHH	46.56	27742792
553	Phosphorylation	VQAMDCETHSPQVRQ HHHHCCCCCCHHHHH	33.70	25266776
555	Phosphorylation	AMDCETHSPQVRQQF HHCCCCCCHHHHHHC	25.17	25266776
748	Phosphorylation	QGADREESPMTGVCV CCCCCCCCCCCCEEE	18.41	27087446
750	Oxidation	ADREESPMTGVCVQQ CCCCCCCCCCEEEEC	7.68	17242355
751	Phosphorylation	DREESPMTGVCVQQS CCCCCCCCCEEEECC	29.82	25619855
758	Phosphorylation	TGVCVQQSPVASS-- CCEEEECCCCCCC--	12.30	25521595
762	Phosphorylation	VQQSPVASS------ EECCCCCCC------	36.49	25619855
763	Phosphorylation	QQSPVASS------- ECCCCCCC-------	34.21	25619855

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
321	Y	Phosphorylation	Kinase	DYRK1A	Q61214	GPS

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of DYR1A_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of DYR1A_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ARIP4_MOUSE	Rad54l2	physical	15199138

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-145, AND MASSSPECTROMETRY.
PubMed: 18034455

"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-321, AND MASSSPECTROMETRY.
PubMed: 15592455

"Profiling of tyrosine phosphorylation pathways in human cells usingmass spectrometry.";
Salomon A.R., Ficarro S.B., Brill L.M., Brinker A., Phung Q.T.,Ericson C., Sauer K., Brock A., Horn D.M., Schultz P.G., Peters E.C.;
Proc. Natl. Acad. Sci. U.S.A. 100:443-448(2003).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-321, AND MASSSPECTROMETRY.
PubMed: 12522270