VRK1_HUMAN - dbPTM
VRK1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VRK1_HUMAN
UniProt AC Q99986
Protein Name Serine/threonine-protein kinase VRK1
Gene Name VRK1
Organism Homo sapiens (Human).
Sequence Length 396
Subcellular Localization Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, spindle. Dispersed throughout the cell but not located on mitotic spindle or chromatids during mitosis.
Protein Description Serine/threonine kinase involved in Golgi disassembly during the cell cycle: following phosphorylation by PLK3 during mitosis, required to induce Golgi fragmentation. Acts by mediating phosphorylation of downstream target protein. Phosphorylates 'Thr-18' of p53/TP53 and may thereby prevent the interaction between p53/TP53 and MDM2. Phosphorylates casein and histone H3. Phosphorylates BANF1: disrupts its ability to bind DNA, reduces its binding to LEM domain-containing proteins and causes its relocalization from the nucleus to the cytoplasm. Phosphorylates ATF2 which activates its transcriptional activity..
Protein Sequence MPRVKAAQAGRQSSAKRHLAEQFAVGEIITDMAKKEWKVGLPIGQGGFGCIYLADMNSSESVGSDAPCVVKVEPSDNGPLFTELKFYQRAAKPEQIQKWIRTRKLKYLGVPKYWGSGLHDKNGKSYRFMIMDRFGSDLQKIYEANAKRFSRKTVLQLSLRILDILEYIHEHEYVHGDIKASNLLLNYKNPDQVYLVDYGLAYRYCPEGVHKEYKEDPKRCHDGTIEFTSIDAHNGVAPSRRGDLEILGYCMIQWLTGHLPWEDNLKDPKYVRDSKIRYRENIASLMDKCFPEKNKPGEIAKYMETVKLLDYTEKPLYENLRDILLQGLKAIGSKDDGKLDLSVVENGGLKAKTITKKRKKEIEESKEPGVEDTEWSNTQTEEAIQTRSRTRKRVQK
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 Orthologous
Protein Cluster
5Sumoylation---MPRVKAAQAGRQ
---CCHHHHHHCCCH		39.01-
5Sumoylation---MPRVKAAQAGRQ
---CCHHHHHHCCCH		39.01-
5Ubiquitination---MPRVKAAQAGRQ
---CCHHHHHHCCCH		39.0129967540
5Methylation---MPRVKAAQAGRQ
---CCHHHHHHCCCH		39.0181424245
13PhosphorylationAAQAGRQSSAKRHLA
HHHCCCHHHHHHHHH		30.7926074081
14PhosphorylationAQAGRQSSAKRHLAE
HHCCCHHHHHHHHHH		29.4826074081
16UbiquitinationAGRQSSAKRHLAEQF
CCCHHHHHHHHHHHH		42.1521906983
18UbiquitinationRQSSAKRHLAEQFAV
CHHHHHHHHHHHHHH		28.7822817900
342-HydroxyisobutyrylationEIITDMAKKEWKVGL
HHHHHHHHHCCCCCC		44.58-
34UbiquitinationEIITDMAKKEWKVGL
HHHHHHHHHCCCCCC		44.5832015554
35UbiquitinationIITDMAKKEWKVGLP
HHHHHHHHCCCCCCC		60.30-
71UbiquitinationSDAPCVVKVEPSDNG
CCCCEEEEEECCCCC		22.0829967540
71SumoylationSDAPCVVKVEPSDNG
CCCCEEEEEECCCCC		22.0828112733
75PhosphorylationCVVKVEPSDNGPLFT
EEEEEECCCCCCCCC		30.15-
85AcetylationGPLFTELKFYQRAAK
CCCCCEEEHHHHCCC		35.4725953088
85UbiquitinationGPLFTELKFYQRAAK
CCCCCEEEHHHHCCC		35.4729967540
92UbiquitinationKFYQRAAKPEQIQKW
EHHHHCCCHHHHHHH		48.3729967540
92SumoylationKFYQRAAKPEQIQKW
EHHHHCCCHHHHHHH		48.37-
92SumoylationKFYQRAAKPEQIQKW
EHHHHCCCHHHHHHH		48.37-
98AcetylationAKPEQIQKWIRTRKL
CCHHHHHHHHHHCCC		46.3323749302
98UbiquitinationAKPEQIQKWIRTRKL
CCHHHHHHHHHHCCC		46.3332015554
100UbiquitinationPEQIQKWIRTRKLKY
HHHHHHHHHHCCCHH		4.0922505724
106UbiquitinationWIRTRKLKYLGVPKY
HHHHCCCHHCCCCCC		41.2729967540
106AcetylationWIRTRKLKYLGVPKY
HHHHCCCHHCCCCCC		41.2725953088
112SumoylationLKYLGVPKYWGSGLH
CHHCCCCCCCCCCCC		51.75-
112SumoylationLKYLGVPKYWGSGLH
CHHCCCCCCCCCCCC		51.75-
112UbiquitinationLKYLGVPKYWGSGLH
CHHCCCCCCCCCCCC		51.7522817900
112AcetylationLKYLGVPKYWGSGLH
CHHCCCCCCCCCCCC		51.7525953088
114UbiquitinationYLGVPKYWGSGLHDK
HCCCCCCCCCCCCCC		10.7021890473
121UbiquitinationWGSGLHDKNGKSYRF
CCCCCCCCCCCEEEE		57.7729967540
124UbiquitinationGLHDKNGKSYRFMIM
CCCCCCCCEEEEEEE		54.42-
140UbiquitinationRFGSDLQKIYEANAK
CCCHHHHHHHHHHHH		55.33-
140AcetylationRFGSDLQKIYEANAK
CCCHHHHHHHHHHHH		55.3325953088
142PhosphorylationGSDLQKIYEANAKRF
CHHHHHHHHHHHHHC		18.9429496907
147UbiquitinationKIYEANAKRFSRKTV
HHHHHHHHHCCHHHH		54.5024816145
147AcetylationKIYEANAKRFSRKTV
HHHHHHHHHCCHHHH		54.5025953088
149UbiquitinationYEANAKRFSRKTVLQ
HHHHHHHCCHHHHHH		9.0324816145
152UbiquitinationNAKRFSRKTVLQLSL
HHHHCCHHHHHHHHH		41.61-
152SumoylationNAKRFSRKTVLQLSL
HHHHCCHHHHHHHHH		41.61-
152SumoylationNAKRFSRKTVLQLSL
HHHHCCHHHHHHHHH		41.61-
153PhosphorylationAKRFSRKTVLQLSLR
HHHCCHHHHHHHHHH		25.9119664994
158PhosphorylationRKTVLQLSLRILDIL
HHHHHHHHHHHHHHH		11.5719664994
188UbiquitinationSNLLLNYKNPDQVYL
HHEECCCCCCCCEEE		62.0121906983
190UbiquitinationLLLNYKNPDQVYLVD
EECCCCCCCCEEEEE		29.2921963094
211AcetylationYCPEGVHKEYKEDPK
CCCCCCCHHHHCCCC		61.4023749302
211UbiquitinationYCPEGVHKEYKEDPK
CCCCCCCHHHHCCCC		61.4024816145
213UbiquitinationPEGVHKEYKEDPKRC
CCCCCHHHHCCCCCC		25.2024816145
269SumoylationEDNLKDPKYVRDSKI
CCCCCCCHHHCCCCC		67.52-
269UbiquitinationEDNLKDPKYVRDSKI
CCCCCCCHHHCCCCC		67.5229967540
269SumoylationEDNLKDPKYVRDSKI
CCCCCCCHHHCCCCC		67.52-
275SumoylationPKYVRDSKIRYRENI
CHHHCCCCCCHHHHH		35.18-
275SumoylationPKYVRDSKIRYRENI
CHHHCCCCCCHHHHH		35.18-
288UbiquitinationNIASLMDKCFPEKNK
HHHHHHHHHCCCCCC		24.6629967540
288AcetylationNIASLMDKCFPEKNK
HHHHHHHHHCCCCCC		24.6625953088
293AcetylationMDKCFPEKNKPGEIA
HHHHCCCCCCCCHHH		71.1923749302
293UbiquitinationMDKCFPEKNKPGEIA
HHHHCCCCCCCCHHH		71.1929967540
295UbiquitinationKCFPEKNKPGEIAKY
HHCCCCCCCCHHHHH		66.5229967540
301AcetylationNKPGEIAKYMETVKL
CCCCHHHHHHHHHHH		51.2825953088
301UbiquitinationNKPGEIAKYMETVKL
CCCCHHHHHHHHHHH		51.2821963094
302PhosphorylationKPGEIAKYMETVKLL
CCCHHHHHHHHHHHH		7.3723663014
303UbiquitinationPGEIAKYMETVKLLD
CCHHHHHHHHHHHHC		3.2521890473
305PhosphorylationEIAKYMETVKLLDYT
HHHHHHHHHHHHCCC		13.3523663014
307SumoylationAKYMETVKLLDYTEK
HHHHHHHHHHCCCCC		51.24-
307UbiquitinationAKYMETVKLLDYTEK
HHHHHHHHHHCCCCC		51.2429967540
307SumoylationAKYMETVKLLDYTEK
HHHHHHHHHHCCCCC		51.24-
314AcetylationKLLDYTEKPLYENLR
HHHCCCCCCHHHCHH		32.3026051181
314UbiquitinationKLLDYTEKPLYENLR
HHHCCCCCCHHHCHH		32.3029967540
329AcetylationDILLQGLKAIGSKDD
HHHHHHHHHHCCCCC		44.7925953088
329UbiquitinationDILLQGLKAIGSKDD
HHHHHHHHHHCCCCC		44.7922817900
331UbiquitinationLLQGLKAIGSKDDGK
HHHHHHHHCCCCCCC		6.4721890473
333PhosphorylationQGLKAIGSKDDGKLD
HHHHHHCCCCCCCCC		27.1421955146
334UbiquitinationGLKAIGSKDDGKLDL
HHHHHCCCCCCCCCE		55.4122817900
334AcetylationGLKAIGSKDDGKLDL
HHHHHCCCCCCCCCE		55.4123749302
336UbiquitinationKAIGSKDDGKLDLSV
HHHCCCCCCCCCEEE		60.9222817900
338AcetylationIGSKDDGKLDLSVVE
HCCCCCCCCCEEEEE		45.9126051181
338SumoylationIGSKDDGKLDLSVVE
HCCCCCCCCCEEEEE		45.91-
338UbiquitinationIGSKDDGKLDLSVVE
HCCCCCCCCCEEEEE		45.9129967540
338SumoylationIGSKDDGKLDLSVVE
HCCCCCCCCCEEEEE		45.91-
342PhosphorylationDDGKLDLSVVENGGL
CCCCCCEEEEECCCC		24.6330266825
350UbiquitinationVVENGGLKAKTITKK
EEECCCCCEEECCHH		51.6232015554
350SumoylationVVENGGLKAKTITKK
EEECCCCCEEECCHH		51.62-
350SumoylationVVENGGLKAKTITKK
EEECCCCCEEECCHH		51.62-
355PhosphorylationGLKAKTITKKRKKEI
CCCEEECCHHHHHHH		35.4322817900
365PhosphorylationRKKEIEESKEPGVED
HHHHHHHHCCCCCCC		29.5422167270
373PhosphorylationKEPGVEDTEWSNTQT
CCCCCCCCCCCCHHH		26.3322167270
376PhosphorylationGVEDTEWSNTQTEEA
CCCCCCCCCHHHHHH		24.6222167270
378PhosphorylationEDTEWSNTQTEEAIQ
CCCCCCCHHHHHHHH		31.2123401153
380PhosphorylationTEWSNTQTEEAIQTR
CCCCCHHHHHHHHHH		33.4822167270
386PhosphorylationQTEEAIQTRSRTRKR
HHHHHHHHHHHHHHH		25.2123403867
390PhosphorylationAIQTRSRTRKRVQK-
HHHHHHHHHHHHCC-		41.6111883897
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
342SPhosphorylationKinasePLK3Q9H4B4
Uniprot
355TPhosphorylationKinaseVRK1Q99986
PSP
376SPhosphorylationKinaseVRK1Q99986
PSP
386TPhosphorylationKinaseVRK1Q99986
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VRK1_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 VRK1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VRK1_HUMANVRK1physical
10951572
P53_HUMANTP53physical
10951572
H32_HUMANHIST2H3Cphysical
17938195
H2B2E_HUMANHIST2H2BEphysical
17938195
P53_HUMANTP53physical
15542844
VRK1_HUMANVRK1physical
11883897
P53_HUMANTP53physical
11883897
PYM1_HUMANWIBGphysical
22939629
RGAP1_HUMANRACGAP1physical
26344197
COIL_HUMANCOILphysical
26068304
H31T_HUMANHIST3H3physical
26068304
VRK1_HUMANVRK1physical
26068304
NBN_HUMANNBNphysical
26869104
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
607596Pontocerebellar hypoplasia 1A (PCH1A)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of VRK1_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Plk3 interacts with and specifically phosphorylates VRK1 in Ser342, adownstream target in a pathway that induces Golgi fragmentation.";
Lopez-Sanchez I., Sanz-Garcia M., Lazo P.A.;
Mol. Cell. Biol. 29:1189-1201(2009).
Cited for: FUNCTION, PHOSPHORYLATION AT SER-342, AND MUTAGENESIS OF LYS-179 ANDSER-342.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory