dbPTM

DYR1B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DYR1B_HUMAN
UniProt AC	Q9Y463
Protein Name	Dual specificity tyrosine-phosphorylation-regulated kinase 1B
Gene Name	DYRK1B
Organism	Homo sapiens (Human).
Sequence Length	629
Subcellular Localization	Nucleus.
Protein Description	Dual-specificity kinase which possesses both serine/threonine and tyrosine kinase activities. Enhances the transcriptional activity of TCF1/HNF1A and FOXO1. Inhibits epithelial cell migration. Mediates colon carcinoma cell survival in mitogen-poor environments. Inhibits the SHH and WNT1 pathways, thereby enhancing adipogenesis. In addition, promotes expression of the gluconeogenic enzyme glucose-6-phosphatase (G6PC)..
Protein Sequence	MAVPPGHGPFSGFPGPQEHTQVLPDVRLLPRRLPLAFRDATSAPLRKLSVDLIKTYKHINEVYYAKKKRRAQQAPPQDSSNKKEKKVLNHGYDDDNHDYIVRSGERWLERYEIDSLIGKGSFGQVVKAYDHQTQELVAIKIIKNKKAFLNQAQIELRLLELMNQHDTEMKYYIVHLKRHFMFRNHLCLVFELLSYNLYDLLRNTHFRGVSLNLTRKLAQQLCTALLFLATPELSIIHCDLKPENILLCNPKRSAIKIVDFGSSCQLGQRIYQYIQSRFYRSPEVLLGTPYDLAIDMWSLGCILVEMHTGEPLFSGSNEVDQMNRIVEVLGIPPAAMLDQAPKARKYFERLPGGGWTLRRTKELRKDYQGPGTRRLQEVLGVQTGGPGGRRAGEPGHSPADYLRFQDLVLRMLEYEPAARISPLGALQHGFFRRTADEATNTGPAGSSASTSPAPLDTCPSSSTASSISSSGGSSGSSSDNRTYRYSNRYCGGPGPPITDCEMNSPQVPPSQPLRPWAGGDVPHKTHQAPASASSLPGTGAQLPPQPRYLGRPPSPTSPPPPELMDVSLVGGPADCSPPHPAPAPQHPAASALRTRMTGGRPPLPPPDDPATLGPHLGLRGVPQSTAASS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
41	Phosphorylation	PLAFRDATSAPLRKL CCCCCCCCCCCHHHC	29.70	25072903
42	Phosphorylation	LAFRDATSAPLRKLS CCCCCCCCCCHHHCH	29.61	25072903
49	Phosphorylation	SAPLRKLSVDLIKTY CCCHHHCHHHHHHHH	19.34	20873877
57	Acetylation	VDLIKTYKHINEVYY HHHHHHHHHHHHHHH	43.15	22643183
63	Phosphorylation	YKHINEVYYAKKKRR HHHHHHHHHHHHHHH	7.48	28152594
64	Phosphorylation	KHINEVYYAKKKRRA HHHHHHHHHHHHHHH	19.68	28152594
66	2-Hydroxyisobutyrylation	INEVYYAKKKRRAQQ HHHHHHHHHHHHHHC	42.58	-
79	Phosphorylation	QQAPPQDSSNKKEKK HCCCCCCCCCHHHHH	30.48	24260401
92	Phosphorylation	KKVLNHGYDDDNHDY HHHHHCCCCCCCCCE	14.51	-
111	Phosphorylation	GERWLERYEIDSLIG CCHHHHHEECHHEEE	14.09	-
115	Phosphorylation	LERYEIDSLIGKGSF HHHEECHHEEECCCH	27.78	30576142
119	Ubiquitination	EIDSLIGKGSFGQVV ECHHEEECCCHHHHE	44.37	-
121	Phosphorylation	DSLIGKGSFGQVVKA HHEEECCCHHHHEEE	29.68	30576142
127	Ubiquitination	GSFGQVVKAYDHQTQ CCHHHHEEECCCCCC	42.23	-
129	Phosphorylation	FGQVVKAYDHQTQEL HHHHEEECCCCCCEE	14.29	-
171	Phosphorylation	QHDTEMKYYIVHLKR HCCHHHHHHHHHHHH	9.34	-
214	Phosphorylation	RGVSLNLTRKLAQQL CCCCHHHHHHHHHHH	25.37	22985185
256	Ubiquitination	NPKRSAIKIVDFGSS CCCCCCEEEEECCCC	36.07	-
262	Phosphorylation	IKIVDFGSSCQLGQR EEEEECCCCCHHHHH	28.12	23665168
263	Phosphorylation	KIVDFGSSCQLGQRI EEEECCCCCHHHHHH	13.28	29514088
271	Phosphorylation	CQLGQRIYQYIQSRF CHHHHHHHHHHHHHH	9.46	21945579
273	Phosphorylation	LGQRIYQYIQSRFYR HHHHHHHHHHHHHCC	5.51	19664994
276	Phosphorylation	RIYQYIQSRFYRSPE HHHHHHHHHHCCCHH	18.13	21945579
356	Phosphorylation	RLPGGGWTLRRTKEL CCCCCCCHHHCCHHH	17.42	29449344
360	Phosphorylation	GGWTLRRTKELRKDY CCCHHHCCHHHHHHC	23.57	29449344
401	Phosphorylation	PGHSPADYLRFQDLV CCCCHHHHHHHHHHH	11.24	-
421	Phosphorylation	YEPAARISPLGALQH CCCCCCCCCCHHHHH	14.44	24719451
446	Phosphorylation	TNTGPAGSSASTSPA CCCCCCCCCCCCCCC	25.49	27251275
447	Phosphorylation	NTGPAGSSASTSPAP CCCCCCCCCCCCCCC	25.89	27251275
449	Phosphorylation	GPAGSSASTSPAPLD CCCCCCCCCCCCCCC	31.22	27251275
450	Phosphorylation	PAGSSASTSPAPLDT CCCCCCCCCCCCCCC	38.15	27251275
451	Phosphorylation	AGSSASTSPAPLDTC CCCCCCCCCCCCCCC	19.30	27251275
485	Phosphorylation	SDNRTYRYSNRYCGG CCCCCEEECCCCCCC	10.41	-
486	Phosphorylation	DNRTYRYSNRYCGGP CCCCEEECCCCCCCC	13.06	-
554	Phosphorylation	RYLGRPPSPTSPPPP CCCCCCCCCCCCCCC	43.42	28348404
556	Phosphorylation	LGRPPSPTSPPPPEL CCCCCCCCCCCCCHH	59.19	28348404
557	Phosphorylation	GRPPSPTSPPPPELM CCCCCCCCCCCCHHC	38.50	28348404
576	Phosphorylation	VGGPADCSPPHPAPA CCCCCCCCCCCCCCC	41.85	28348404
594	Phosphorylation	PAASALRTRMTGGRP HHHHHHHHHHCCCCC	26.16	22210691
624	Phosphorylation	GLRGVPQSTAASS-- CCCCCCCHHCCCC--	17.59	26853621
625	Phosphorylation	LRGVPQSTAASS--- CCCCCCHHCCCC---	22.46	26853621

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
271	Y	Phosphorylation	Kinase	DYR1B	Q9Y463	PhosphoELM
273	Y	Phosphorylation	Kinase	DYR1B	Q9Y463	PhosphoELM
421	S	Phosphorylation	Kinase	DYRK1B	Q9Y463	PSP
421	S	Phosphorylation	Kinase	MAPK1	P28482	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of DYR1B_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 DYR1B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RANB9_HUMAN	RANBP9	physical	14500717
HDAC5_HUMAN	HDAC5	physical	15546868
DCAF7_HUMAN	DCAF7	physical	20940704
DCAF7_HUMAN	DCAF7	physical	21777625
RBL1_HUMAN	RBL1	physical	23602568
RB_HUMAN	RB1	physical	23602568
LZTS2_HUMAN	LZTS2	physical	23602568
TROAP_HUMAN	TROAP	physical	23602568
CDN2A_HUMAN	CDKN2A	physical	23602568
ARF_HUMAN	CDKN2A	physical	23602568
AKA11_HUMAN	AKAP11	physical	23602568
KAP0_HUMAN	PRKAR1A	physical	23602568
RBL2_HUMAN	RBL2	physical	23602568
CBP_HUMAN	CREBBP	physical	23602568
EP300_HUMAN	EP300	physical	23602568
SKI_HUMAN	SKI	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
SI1L1_HUMAN	SIPA1L1	physical	23602568
WDR6_HUMAN	WDR6	physical	23602568
ATD3B_HUMAN	ATAD3B	physical	23602568
SI1L3_HUMAN	SIPA1L3	physical	23602568
SI1L2_HUMAN	SIPA1L2	physical	23602568
ICE1_HUMAN	ICE1	physical	23602568
K0232_HUMAN	KIAA0232	physical	23602568
ZN516_HUMAN	ZNF516	physical	23602568
ENAH_HUMAN	ENAH	physical	23602568
LZTS3_HUMAN	LZTS3	physical	23602568
TEBP_HUMAN	PTGES3	physical	23602568
DDB1_HUMAN	DDB1	physical	23602568
MS3L1_HUMAN	MSL3	physical	23602568
ICE2_HUMAN	ICE2	physical	23602568
KAT8_HUMAN	KAT8	physical	23602568
FOXK1_HUMAN	FOXK1	physical	23602568
BMAL1_HUMAN	ARNTL	physical	23602568
CCNA2_HUMAN	CCNA2	physical	23602568
EP400_HUMAN	EP400	physical	23602568
CTBP2_HUMAN	CTBP2	physical	23602568
TCAL1_HUMAN	TCEAL1	physical	23602568
KAPCA_HUMAN	PRKACA	physical	23602568
PPR3F_HUMAN	PPP1R3F	physical	23602568
TECR_HUMAN	TECR	physical	23602568
IMB1_HUMAN	KPNB1	physical	23602568
CHIP_HUMAN	STUB1	physical	23602568
UBP11_HUMAN	USP11	physical	23602568
ID2_HUMAN	ID2	physical	26735018
DYR1B_HUMAN	DYRK1B	physical	26735018
DCAF7_HUMAN	DCAF7	physical	27307198

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615812	Abdominal obesity-metabolic syndrome 3 (AOMS3)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of DYR1B_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-57, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-273, AND MASSSPECTROMETRY.	19369195 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-273, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-271 AND TYR-273, ANDMASS SPECTROMETRY.	18220336 [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-273, 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-273, AND MASSSPECTROMETRY.	17389395 [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-273, AND MASSSPECTROMETRY.	18083107 [Abstract]