dbPTM

VRK3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	VRK3_HUMAN
UniProt AC	Q8IV63
Protein Name	Inactive serine/threonine-protein kinase VRK3
Gene Name	VRK3
Organism	Homo sapiens (Human).
Sequence Length	474
Subcellular Localization	Nucleus .
Protein Description	Inactive kinase that suppresses ERK activity by promoting phosphatase activity of DUSP3 which specifically dephosphorylates and inactivates ERK in the nucleus..
Protein Sequence	MISFCPDCGKSIQAAFKFCPYCGNSLPVEEHVGSQTFVNPHVSSFQGSKRGLNSSFETSPKKVKWSSTVTSPRLSLFSDGDSSESEDTLSSSERSKGSGSRPPTPKSSPQKTRKSPQVTRGSPQKTSCSPQKTRQSPQTLKRSRVTTSLEALPTGTVLTDKSGRQWKLKSFQTRDNQGILYEAAPTSTLTCDSGPQKQKFSLKLDAKDGRLFNEQNFFQRAAKPLQVNKWKKLYSTPLLAIPTCMGFGVHQDKYRFLVLPSLGRSLQSALDVSPKHVLSERSVLQVACRLLDALEFLHENEYVHGNVTAENIFVDPEDQSQVTLAGYGFAFRYCPSGKHVAYVEGSRSPHEGDLEFISMDLHKGCGPSRRSDLQSLGYCMLKWLYGFLPWTNCLPNTEDIMKQKQKFVDKPGPFVGPCGHWIRPSETLQKYLKVVMALTYEEKPPYAMLRNNLEALLQDLRVSPYDPIGLPMVP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MISFCPDCGK -----CCEECCCCCH	21.35	25002506
11	Phosphorylation	FCPDCGKSIQAAFKF ECCCCCHHHHHHHHH	12.76	25002506
50	Methylation	SSFQGSKRGLNSSFE HHCCCCCCCCCCCCC	57.43	115919865
54	Phosphorylation	GSKRGLNSSFETSPK CCCCCCCCCCCCCCC	41.25	22167270
55	Phosphorylation	SKRGLNSSFETSPKK CCCCCCCCCCCCCCC	26.48	23401153
58	Phosphorylation	GLNSSFETSPKKVKW CCCCCCCCCCCCCCC	48.60	30266825
59	Phosphorylation	LNSSFETSPKKVKWS CCCCCCCCCCCCCCC	27.76	19664994
66	Phosphorylation	SPKKVKWSSTVTSPR CCCCCCCCCCCCCCC	15.48	26853621
67	Phosphorylation	PKKVKWSSTVTSPRL CCCCCCCCCCCCCCE	26.28	30576142
68	Phosphorylation	KKVKWSSTVTSPRLS CCCCCCCCCCCCCEE	23.45	26853621
70	Phosphorylation	VKWSSTVTSPRLSLF CCCCCCCCCCCEEEC	32.85	25159151
71	Phosphorylation	KWSSTVTSPRLSLFS CCCCCCCCCCEEECC	12.04	25159151
71	O-linked_Glycosylation	KWSSTVTSPRLSLFS CCCCCCCCCCEEECC	12.04	30379171
75	Phosphorylation	TVTSPRLSLFSDGDS CCCCCCEEECCCCCC	28.75	22115753
78	Phosphorylation	SPRLSLFSDGDSSES CCCEEECCCCCCCCC	46.08	25159151
82	Phosphorylation	SLFSDGDSSESEDTL EECCCCCCCCCCCCC	41.35	25159151
83	Phosphorylation	LFSDGDSSESEDTLS ECCCCCCCCCCCCCC	50.29	25159151
85	Phosphorylation	SDGDSSESEDTLSSS CCCCCCCCCCCCCHH	42.60	30278072
88	Phosphorylation	DSSESEDTLSSSERS CCCCCCCCCCHHHHC	25.20	22115753
90	Phosphorylation	SESEDTLSSSERSKG CCCCCCCCHHHHCCC	33.63	19690332
91	Phosphorylation	ESEDTLSSSERSKGS CCCCCCCHHHHCCCC	39.05	23403867
92	Phosphorylation	SEDTLSSSERSKGSG CCCCCCHHHHCCCCC	33.38	23403867
95	Phosphorylation	TLSSSERSKGSGSRP CCCHHHHCCCCCCCC	37.00	24719451
98	Phosphorylation	SSERSKGSGSRPPTP HHHHCCCCCCCCCCC	37.01	23403867
100	Phosphorylation	ERSKGSGSRPPTPKS HHCCCCCCCCCCCCC	43.22	23403867
104	Phosphorylation	GSGSRPPTPKSSPQK CCCCCCCCCCCCCCC	46.13	22617229
107	Phosphorylation	SRPPTPKSSPQKTRK CCCCCCCCCCCCCCC	48.75	23403867
107	O-linked_Glycosylation	SRPPTPKSSPQKTRK CCCCCCCCCCCCCCC	48.75	30379171
108	Phosphorylation	RPPTPKSSPQKTRKS CCCCCCCCCCCCCCC	37.16	23403867
112	Phosphorylation	PKSSPQKTRKSPQVT CCCCCCCCCCCCCCC	37.77	28111955
115	Phosphorylation	SPQKTRKSPQVTRGS CCCCCCCCCCCCCCC	19.78	22617229
119	Phosphorylation	TRKSPQVTRGSPQKT CCCCCCCCCCCCCCC	24.86	25159151
122	Phosphorylation	SPQVTRGSPQKTSCS CCCCCCCCCCCCCCC	22.37	28355574
126	Phosphorylation	TRGSPQKTSCSPQKT CCCCCCCCCCCCCCC	29.71	28450419
127	Phosphorylation	RGSPQKTSCSPQKTR CCCCCCCCCCCCCCC	21.45	28450419
129	Phosphorylation	SPQKTSCSPQKTRQS CCCCCCCCCCCCCCC	30.08	28450419
133	Phosphorylation	TSCSPQKTRQSPQTL CCCCCCCCCCCCCHH	28.79	23403867
136	Phosphorylation	SPQKTRQSPQTLKRS CCCCCCCCCCHHHHH	18.71	30266825
139	Phosphorylation	KTRQSPQTLKRSRVT CCCCCCCHHHHHHCC	37.32	30266825
143	Phosphorylation	SPQTLKRSRVTTSLE CCCHHHHHHCCCCEE	29.52	26270265
146	Phosphorylation	TLKRSRVTTSLEALP HHHHHHCCCCEECCC	15.01	26270265
147	Phosphorylation	LKRSRVTTSLEALPT HHHHHCCCCEECCCC	28.58	26270265
148	Phosphorylation	KRSRVTTSLEALPTG HHHHCCCCEECCCCC	18.17	26270265
154	Phosphorylation	TSLEALPTGTVLTDK CCEECCCCCCEEECC	46.46	26270265
156	Phosphorylation	LEALPTGTVLTDKSG EECCCCCCEEECCCC	18.15	26270265
159	Phosphorylation	LPTGTVLTDKSGRQW CCCCCEEECCCCCEE	36.72	26270265
161	Ubiquitination	TGTVLTDKSGRQWKL CCCEEECCCCCEEEE	49.96	-
161	Acetylation	TGTVLTDKSGRQWKL CCCEEECCCCCEEEE	49.96	25953088
169	Ubiquitination	SGRQWKLKSFQTRDN CCCEEEEEEEECCCC	45.56	-
179	Ubiquitination	QTRDNQGILYEAAPT ECCCCCCEEEEECCC	2.39	21890473
197	Ubiquitination	TCDSGPQKQKFSLKL ECCCCCCCCCEEEEE	59.60	-
199	Ubiquitination	DSGPQKQKFSLKLDA CCCCCCCCEEEEEEC	43.91	-
223	Ubiquitination	NFFQRAAKPLQVNKW CHHHHHCCCCCCCHH	45.32	-
225	Ubiquitination	FQRAAKPLQVNKWKK HHHHCCCCCCCHHHH	9.77	21890473
229 (in isoform 2)	Ubiquitination	-	62.63	21890473
229 (in isoform 1)	Ubiquitination	-	62.63	21890473
229	Ubiquitination	AKPLQVNKWKKLYST CCCCCCCHHHHHHCC	62.63	21890473
232	Ubiquitination	LQVNKWKKLYSTPLL CCCCHHHHHHCCCEE	52.09	-
268	Phosphorylation	SLGRSLQSALDVSPK HHCHHHHHHHCCCHH	35.77	30622161
273	Phosphorylation	LQSALDVSPKHVLSE HHHHHCCCHHHHCCH	28.09	30622161
275 (in isoform 1)	Ubiquitination	-	38.55	21890473
275	Acetylation	SALDVSPKHVLSERS HHHCCCHHHHCCHHH	38.55	23749302
275 (in isoform 2)	Ubiquitination	-	38.55	21890473
275	Ubiquitination	SALDVSPKHVLSERS HHHCCCHHHHCCHHH	38.55	21890473
338	Ubiquitination	FRYCPSGKHVAYVEG EEECCCCCEEEEEEC	38.96	-
348	Phosphorylation	AYVEGSRSPHEGDLE EEEECCCCCCCCCCE	32.10	20873877
410	Ubiquitination	QKQKFVDKPGPFVGP HHHHHCCCCCCCCCC	46.72	-
411 (in isoform 2)	Phosphorylation	-	51.75	21406692
439	Phosphorylation	LKVVMALTYEEKPPY HHHHHHHHCCCCCCH	21.24	29449344
440	Phosphorylation	KVVMALTYEEKPPYA HHHHHHHCCCCCCHH	23.96	29449344

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
108	S	Phosphorylation	Kinase	CDK5	Q00535	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of VRK3_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 VRK3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
TWF2_HUMAN	TWF2	physical	17353931

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 VRK3_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 SER-59; SER-82; SER-83 ANDSER-90, AND MASS SPECTROMETRY.	19690332 [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 SER-59, AND MASSSPECTROMETRY.	19413330 [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 SER-55 AND SER-59, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136, AND MASSSPECTROMETRY.	18187866 [Abstract]