dbPTM

DYR1A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DYR1A_HUMAN
UniProt AC	Q13627
Protein Name	Dual specificity tyrosine-phosphorylation-regulated kinase 1A
Gene Name	DYRK1A
Organism	Homo sapiens (Human).
Sequence Length	763
Subcellular Localization	Nucleus . 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 (By similarity)..
Protein Sequence	MHTGGETSACKPSSVRLAPSFSFHAAGLQMAGQMPHSHQYSDRRQPNISDQQVSALSYSDQIQQPLTNQVMPDIVMLQRRMPQTFRDPATAPLRKLSVDLIKTYKHINEVYYAKKKRRHQQGQGDDSSHKKERKVYNDGYDDDNYDYIVKNGEKWMDRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHFMFRNHLCLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPELSIIHCDLKPENILLCNPKRSAIKIVDFGSSCQLGQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHILDQAPKARKFFEKLPDGTWNLKKTKDGKREYKPPGTRKLHNILGVETGGPGGRRAGESGHTVADYLKFKDLILRMLDYDPKTRIQPYYALQHSFFKKTADEGTNTSNSVSTSPAMEQSQSSGTTSSTSSSSGGSSGTSNSGRARSDPTHQHRHSGGHFTAAVQAMDCETHSPQVRQQFPAPLGWSGTEAPTQVTVETHPVQETTFHVAPQQNALHHHHGNSSHHHHHHHHHHHHHGQQALGNRTRPRVYNSPTNSSSTQDSMEVGHSHHSMTSLSSSTTSSSTSSSSTGNQGNQAYQNRPVAANTLDFGQNGAMDVNLTVYSNPRQETGIAGHPTYQFSANTGPAHYMTEGHLTMRQGADREESPMTGVCVQQSPVASS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
7	Phosphorylation	-MHTGGETSACKPSS -CCCCCCCCCCCCCC	25.54	29083192
8	Phosphorylation	MHTGGETSACKPSSV CCCCCCCCCCCCCCC	27.63	29083192
11	Acetylation	GGETSACKPSSVRLA CCCCCCCCCCCCCCC	47.88	25953088
11	Methylation	GGETSACKPSSVRLA CCCCCCCCCCCCCCC	47.88	23644510
11	Ubiquitination	GGETSACKPSSVRLA CCCCCCCCCCCCCCC	47.88	-
14	Phosphorylation	TSACKPSSVRLAPSF CCCCCCCCCCCCCCC	21.56	23186163
20	Phosphorylation	SSVRLAPSFSFHAAG CCCCCCCCCEEEHHH	28.10	28348404
22	Phosphorylation	VRLAPSFSFHAAGLQ CCCCCCCEEEHHHCH	22.06	27251275
57	Phosphorylation	DQQVSALSYSDQIQQ HHHHHHHCCHHHCCC	23.47	29438985
58	Phosphorylation	QQVSALSYSDQIQQP HHHHHHCCHHHCCCC	19.67	29438985
67	Phosphorylation	DQIQQPLTNQVMPDI HHCCCCCCCCCCCHH	30.23	29438985
96	Acetylation	ATAPLRKLSVDLIKT CCCCHHHCCHHHHHH	4.95	19608861
97	Phosphorylation	TAPLRKLSVDLIKTY CCCHHHCCHHHHHHH	19.34	23312004
105	Acetylation	VDLIKTYKHINEVYY HHHHHHHHHHHHHHH	43.15	23749302
111	Phosphorylation	YKHINEVYYAKKKRR HHHHHHHHHHHHHHH	7.48	28152594
112	Phosphorylation	KHINEVYYAKKKRRH HHHHHHHHHHHHHHH	19.68	28152594
127	Phosphorylation	QQGQGDDSSHKKERK CCCCCCCCCCHHCHH	38.80	28985074
134	Ubiquitination	SSHKKERKVYNDGYD CCCHHCHHCCCCCCC	50.60	-
136	Phosphorylation	HKKERKVYNDGYDDD CHHCHHCCCCCCCCC	15.57	17016520
140	Phosphorylation	RKVYNDGYDDDNYDY HHCCCCCCCCCCCCE	21.04	19060867
145	Phosphorylation	DGYDDDNYDYIVKNG CCCCCCCCCEEEECC	19.67	19605366
147	Phosphorylation	YDDDNYDYIVKNGEK CCCCCCCEEEECCCC	9.39	21878370
150	Ubiquitination	DNYDYIVKNGEKWMD CCCCEEEECCCCEEC	50.07	-
159	Phosphorylation	GEKWMDRYEIDSLIG CCCEECCEECHHHCC	16.99	22817900
167	Ubiquitination	EIDSLIGKGSFGQVV ECHHHCCCCCHHHHH	44.37	-
177	Phosphorylation	FGQVVKAYDRVEQEW HHHHHHHHHHHHHEE	9.88	23665168
194	Acetylation	IKIIKNKKAFLNQAQ EEEHHCCHHHHHHHH	54.48	26051181
219	Phosphorylation	KHDTEMKYYIVHLKR HCCCHHHHHHHHHHH	9.34	-
262	Phosphorylation	RGVSLNLTRKFAQQM CCCCCHHHHHHHHHH	30.64	22985185
304	Ubiquitination	NPKRSAIKIVDFGSS CCCCCCEEEEECCCC	36.07	-
310	Phosphorylation	IKIVDFGSSCQLGQR EEEEECCCCCHHHHH	28.12	23665168
311	Phosphorylation	KIVDFGSSCQLGQRI EEEECCCCCHHHHHH	13.28	29514088
319	Phosphorylation	CQLGQRIYQYIQSRF CHHHHHHHHHHHHHH	9.46	21945579
321	Phosphorylation	LGQRIYQYIQSRFYR HHHHHHHHHHHHHCC	5.51	19664994
324	Phosphorylation	RIYQYIQSRFYRSPE HHHHHHHHHHCCCHH	18.13	21945579
402	Phosphorylation	FEKLPDGTWNLKKTK HHCCCCCCCCEEECC	20.68	23665168
406	Acetylation	PDGTWNLKKTKDGKR CCCCCCEEECCCCCC	56.00	25953088
444 (in isoform 2)	Ubiquitination	-	26.84	21890473
449	Phosphorylation	SGHTVADYLKFKDLI CCCCHHHHHHHHHHH	11.31	23665168
453	Ubiquitination	VADYLKFKDLILRML HHHHHHHHHHHHHHH	50.46	21890473
453 (in isoform 1)	Ubiquitination	-	50.46	21890473
453 (in isoform 3)	Ubiquitination	-	50.46	21890473
453 (in isoform 4)	Ubiquitination	-	50.46	21890473
453 (in isoform 5)	Ubiquitination	-	50.46	21890473
453	Malonylation	VADYLKFKDLILRML HHHHHHHHHHHHHHH	50.46	26320211
466	Phosphorylation	MLDYDPKTRIQPYYA HHCCCCCCCCCCHHH	38.09	24719451
482	Phosphorylation	QHSFFKKTADEGTNT HHHHCCCCCCCCCCC	39.67	23186163
487	Phosphorylation	KKTADEGTNTSNSVS CCCCCCCCCCCCCCC	33.02	23186163
489	Phosphorylation	TADEGTNTSNSVSTS CCCCCCCCCCCCCCC	29.17	23186163
490	Phosphorylation	ADEGTNTSNSVSTSP CCCCCCCCCCCCCCC	29.22	23186163
492	Phosphorylation	EGTNTSNSVSTSPAM CCCCCCCCCCCCCHH	19.74	23186163
494	Phosphorylation	TNTSNSVSTSPAMEQ CCCCCCCCCCCHHHC	24.00	23186163
495	Phosphorylation	NTSNSVSTSPAMEQS CCCCCCCCCCHHHCH	36.25	23186163
496	Phosphorylation	TSNSVSTSPAMEQSQ CCCCCCCCCHHHCHH	11.80	24275569
502	Phosphorylation	TSPAMEQSQSSGTTS CCCHHHCHHCCCCCC	20.80	28985074
504	Phosphorylation	PAMEQSQSSGTTSST CHHHCHHCCCCCCCC	35.66	23186163
505	Phosphorylation	AMEQSQSSGTTSSTS HHHCHHCCCCCCCCC	32.30	23186163
507	Phosphorylation	EQSQSSGTTSSTSSS HCHHCCCCCCCCCCC	26.00	23186163
508	Phosphorylation	QSQSSGTTSSTSSSS CHHCCCCCCCCCCCC	24.97	23186163
509	Phosphorylation	SQSSGTTSSTSSSSG HHCCCCCCCCCCCCC	31.30	23186163
510	Phosphorylation	QSSGTTSSTSSSSGG HCCCCCCCCCCCCCC	30.16	23186163
511	Phosphorylation	SSGTTSSTSSSSGGS CCCCCCCCCCCCCCC	32.18	23186163
512	Phosphorylation	SGTTSSTSSSSGGSS CCCCCCCCCCCCCCC	30.12	23186163
513	Phosphorylation	GTTSSTSSSSGGSSG CCCCCCCCCCCCCCC	28.72	23186163
514	Phosphorylation	TTSSTSSSSGGSSGT CCCCCCCCCCCCCCC	32.54	23186163
515	Phosphorylation	TSSTSSSSGGSSGTS CCCCCCCCCCCCCCC	49.47	23186163
519	Phosphorylation	SSSSGGSSGTSNSGR CCCCCCCCCCCCCCC	49.73	17229891
529	Phosphorylation	SNSGRARSDPTHQHR CCCCCCCCCCCCCCC	47.13	27794612
532	Phosphorylation	GRARSDPTHQHRHSG CCCCCCCCCCCCCCC	38.88	20068231
538	Phosphorylation	PTHQHRHSGGHFTAA CCCCCCCCCCHHHHE	46.56	30175587
543	Phosphorylation	RHSGGHFTAAVQAMD CCCCCHHHHEEEEEC	14.18	30108239
553	Phosphorylation	VQAMDCETHSPQVRQ EEEECCCCCCHHHHH	33.70	30576142
555	Phosphorylation	AMDCETHSPQVRQQF EECCCCCCHHHHHHC	25.17	20873877
705	Phosphorylation	MDVNLTVYSNPRQET EEEEEEEECCCCCCC	9.48	-
706	Phosphorylation	DVNLTVYSNPRQETG EEEEEEECCCCCCCC	35.70	-
738	Phosphorylation	YMTEGHLTMRQGADR EECCCCEEECCCCCC	12.48	26074081
748	Phosphorylation	QGADREESPMTGVCV CCCCCCCCCCCCEEE	18.41	22617229
751	Phosphorylation	DREESPMTGVCVQQS CCCCCCCCCEEEECC	29.82	22115753
758	Phosphorylation	TGVCVQQSPVASS-- CCEEEECCCCCCC--	12.30	30278072
762	Phosphorylation	VQQSPVASS------ EECCCCCCC------	36.49	21712546
763	Phosphorylation	QQSPVASS------- ECCCCCCC-------	34.21	21712546

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	Q13627	GPS
529	S	Phosphorylation	Kinase	DYRK1A	Q13627	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of DYR1A_HUMAN !!

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 DYR1A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SRSF4_HUMAN	SRSF4	physical	14623875
CCNL2_HUMAN	CCNL2	physical	14623875
SRSF5_HUMAN	SRSF5	physical	14623875
CLASR_HUMAN	CLASRP	physical	14623875
SRSF1_HUMAN	SRSF1	physical	14623875
DYN1_HUMAN	DNM1	physical	11877424
H2B1B_HUMAN	HIST1H2BB	physical	10644696
H31_HUMAN	HIST1H3A	physical	10644696
DYN1_HUMAN	DNM1	physical	19722700
CLH1_HUMAN	CLTC	physical	19722700
AMPH_HUMAN	AMPH	physical	16733250
DCAF7_HUMAN	DCAF7	physical	20940704
DCAF7_HUMAN	DCAF7	physical	21777625
LIN52_HUMAN	LIN52	physical	21498571
M3K5_HUMAN	MAP3K5	physical	22110360
SYUA_HUMAN	SNCA	physical	16959772
A4_HUMAN	APP	physical	21832049
RBL1_HUMAN	RBL1	physical	23602568
RB_HUMAN	RB1	physical	23602568
LZTS2_HUMAN	LZTS2	physical	23602568
TROAP_HUMAN	TROAP	physical	23602568
CCNA2_HUMAN	CCNA2	physical	23602568
KAP0_HUMAN	PRKAR1A	physical	23602568
RBL2_HUMAN	RBL2	physical	23602568
CBP_HUMAN	CREBBP	physical	23602568
EP300_HUMAN	EP300	physical	23602568
F117B_HUMAN	FAM117B	physical	23602568
DCAF7_HUMAN	DCAF7	physical	23602568
GLCI1_HUMAN	GLCCI1	physical	23602568
FA53C_HUMAN	FAM53C	physical	23602568
F117A_HUMAN	FAM117A	physical	23602568
RN169_HUMAN	RNF169	physical	23602568
DYL1_HUMAN	DYNLL1	physical	23602568
ABCD3_HUMAN	ABCD3	physical	23602568
DYL2_HUMAN	DYNLL2	physical	23602568
SI1L1_HUMAN	SIPA1L1	physical	23602568
FNTA_HUMAN	FNTA	physical	23602568
FNTB_HUMAN	FNTB	physical	23602568
PPR3F_HUMAN	PPP1R3F	physical	23602568
K0232_HUMAN	KIAA0232	physical	23602568
CCDC8_HUMAN	CCDC8	physical	23602568
SIR1_MOUSE	Sirt1	physical	20167603
DCAF7_HUMAN	DCAF7	physical	25342745
ID2_HUMAN	ID2	physical	26735018
DYR1A_HUMAN	DYRK1A	physical	26735018
PRKN_HUMAN	PARK2	physical	25963095
DCAF7_HUMAN	DCAF7	physical	27307198

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614104	Mental retardation, autosomal dominant 7 (MRD7)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of DYR1A_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-145; TYR-321 ANDSER-324, AND MASS SPECTROMETRY.	19690332 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-321; SER-748 ANDSER-758, AND MASS SPECTROMETRY.	18691976 [Abstract]
"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-321, AND MASSSPECTROMETRY.	19534553 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-321, AND MASSSPECTROMETRY.	19413330 [Abstract]
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-321, AND MASSSPECTROMETRY.	18088087 [Abstract]
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks."; Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.; Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-321, AND MASSSPECTROMETRY.	17389395 [Abstract]
"Proteomics analysis of protein kinases by target class-selectiveprefractionation and tandem mass spectrometry."; Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R.,Keri G., Wehland J., Daub H.; Mol. Cell. Proteomics 6:537-547(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-321, AND MASSSPECTROMETRY.	17192257 [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-145, 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-145 AND TYR-321, ANDMASS SPECTROMETRY.	15592455 [Abstract]