VRK2_HUMAN - dbPTM
VRK2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VRK2_HUMAN
UniProt AC Q86Y07
Protein Name Serine/threonine-protein kinase VRK2
Gene Name VRK2
Organism Homo sapiens (Human).
Sequence Length 508
Subcellular Localization Isoform 1: Cytoplasm. Endoplasmic reticulum membrane
Single-pass type IV membrane protein . Mitochondrion membrane
Single-pass type IV membrane protein .
Isoform 2: Cytoplasm. Nucleus.
Protein Description Serine/threonine kinase that regulates several signal transduction pathways. Isoform 1 modulates the stress response to hypoxia and cytokines, such as interleukin-1 beta (IL1B) and this is dependent on its interaction with MAPK8IP1, which assembles mitogen-activated protein kinase (MAPK) complexes. Inhibition of signal transmission mediated by the assembly of MAPK8IP1-MAPK complexes reduces JNK phosphorylation and JUN-dependent transcription. Phosphorylates 'Thr-18' of p53/TP53, histone H3, and may also phosphorylate MAPK8IP1. Phosphorylates BANF1 and disrupts its ability to bind DNA and reduces its binding to LEM domain-containing proteins. Downregulates the transactivation of transcription induced by ERBB2, HRAS, BRAF, and MEK1. Blocks the phosphorylation of ERK in response to ERBB2 and HRAS. Can also phosphorylate the following substrates that are commonly used to establish in vitro kinase activity: casein, MBP and histone H2B, but it is not sure that this is physiologically relevant.; Isoform 2 phosphorylates 'Thr-18' of p53/TP53, as well as histone H3. Reduces p53/TP53 ubiquitination by MDM2, promotes p53/TP53 acetylation by EP300 and thereby increases p53/TP53 stability and activity..
Protein Sequence MPPKRNEKYKLPIPFPEGKVLDDMEGNQWVLGKKIGSGGFGLIYLAFPTNKPEKDARHVVKVEYQENGPLFSELKFYQRVAKKDCIKKWIERKQLDYLGIPLFYGSGLTEFKGRSYRFMVMERLGIDLQKISGQNGTFKKSTVLQLGIRMLDVLEYIHENEYVHGDIKAANLLLGYKNPDQVYLADYGLSYRYCPNGNHKQYQENPRKGHNGTIEFTSLDAHKGVALSRRSDVEILGYCMLRWLCGKLPWEQNLKDPVAVQTAKTNLLDELPQSVLKWAPSGSSCCEIAQFLVCAHSLAYDEKPNYQALKKILNPHGIPLGPLDFSTKGQSINVHTPNSQKVDSQKAATKQVNKAHNRLIEKKVHSERSAESCATWKVQKEEKLIGLMNNEAAQESTRRRQKYQESQEPLNEVNSFPQKISYTQFPNSFYEPHQDFTSPDIFKKSRSPSWYKYTSTVSTGITDLESSTGLWPTISQFTLSEETNADVYYYRIIIPVLLMLVFLALFFL
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
10UbiquitinationPKRNEKYKLPIPFPE
CCCCCCCCCCCCCCC		59.87-
33 (in isoform 1)Ubiquitination-36.7421906983
33 (in isoform 2)Ubiquitination-36.7421906983
33UbiquitinationGNQWVLGKKIGSGGF
CCEEEEEEEECCCCE		36.7421906983
33 (in isoform 5)Ubiquitination-36.7421906983
44PhosphorylationSGGFGLIYLAFPTNK
CCCEEEEEEECCCCC		9.3022817900
52 (in isoform 3)Ubiquitination-56.8121906983
59 (in isoform 4)Ubiquitination-3.5721906983
61AcetylationKDARHVVKVEYQENG
CCCCEEEEEEEECCC		28.4126051181
75 (in isoform 1)Ubiquitination-37.6621906983
75AcetylationGPLFSELKFYQRVAK
CCCCHHHHHHHHHHH		37.6626051181
75 (in isoform 2)Ubiquitination-37.6621906983
75 (in isoform 5)Ubiquitination-37.6621906983
75UbiquitinationGPLFSELKFYQRVAK
CCCCHHHHHHHHHHH		37.6621906983
93AcetylationIKKWIERKQLDYLGI
HHHHHHHHCCCCCCC		42.2819809961
104PhosphorylationYLGIPLFYGSGLTEF
CCCCCEEECCCCCCC		20.3320860994
105 (in isoform 4)Ubiquitination-14.1121906983
106PhosphorylationGIPLFYGSGLTEFKG
CCCEEECCCCCCCCC		21.1720860994
109PhosphorylationLFYGSGLTEFKGRSY
EEECCCCCCCCCCCH		42.7920860994
112UbiquitinationGSGLTEFKGRSYRFM
CCCCCCCCCCCHHHE		47.37-
137 (in isoform 4)Ubiquitination-39.5721906983
139UbiquitinationSGQNGTFKKSTVLQL
CCCCCCCCHHHHHHH		45.73-
141PhosphorylationQNGTFKKSTVLQLGI
CCCCCCHHHHHHHHH		25.0824114839
142PhosphorylationNGTFKKSTVLQLGIR
CCCCCHHHHHHHHHH		33.8324114839
146 (in isoform 4)Ubiquitination-5.5721906983
154 (in isoform 3)Ubiquitination-4.0621906983
177 (in isoform 1)Ubiquitination-61.2721906983
177 (in isoform 2)Ubiquitination-61.2721906983
177UbiquitinationANLLLGYKNPDQVYL
HHHHHCCCCCCCEEE		61.2721906983
177 (in isoform 5)Ubiquitination-61.2721906983
200 (in isoform 3)Ubiquitination-55.4921906983
200UbiquitinationYCPNGNHKQYQENPR
ECCCCCCCCCCCCCC		55.49-
202PhosphorylationPNGNHKQYQENPRKG
CCCCCCCCCCCCCCC		23.6929496907
208UbiquitinationQYQENPRKGHNGTIE
CCCCCCCCCCCCEEE		66.82-
210 (in isoform 4)Ubiquitination-32.3621906983
223UbiquitinationFTSLDAHKGVALSRR
EEECCCCCCEEECCC		57.7221906983
223 (in isoform 1)Ubiquitination-57.7221906983
223 (in isoform 5)Ubiquitination-57.7221906983
223 (in isoform 2)Ubiquitination-57.7221906983
232 (in isoform 3)Ubiquitination-40.0121906983
241 (in isoform 3)Ubiquitination-2.9521906983
255UbiquitinationLPWEQNLKDPVAVQT
CCHHHCCCCCHHHHH		68.4821906983
255 (in isoform 2)Ubiquitination-68.4821906983
255 (in isoform 1)Ubiquitination-68.4821906983
255 (in isoform 5)Ubiquitination-68.4821906983
264UbiquitinationPVAVQTAKTNLLDEL
CHHHHHHCCCHHHHC		41.1421906983
264 (in isoform 1)Ubiquitination-41.1421906983
264 (in isoform 2)Ubiquitination-41.1421906983
264 (in isoform 5)Ubiquitination-41.1421906983
265 (in isoform 4)Ubiquitination-28.7421906983
284 (in isoform 4)Ubiquitination-26.7221906983
305 (in isoform 3)Ubiquitination-53.2521906983
311UbiquitinationPNYQALKKILNPHGI
CCHHHHHHHHCCCCC		53.96-
325 (in isoform 4)Ubiquitination-15.2821906983
328 (in isoform 2)Ubiquitination-54.4721906983
328 (in isoform 1)Ubiquitination-54.4721906983
328 (in isoform 5)Ubiquitination-54.4721906983
328UbiquitinationGPLDFSTKGQSINVH
CCCCCCCCCCEEEEE		54.4721906983
331PhosphorylationDFSTKGQSINVHTPN
CCCCCCCEEEEECCC		25.4630266825
336PhosphorylationGQSINVHTPNSQKVD
CCEEEEECCCCHHCC		21.6330266825
339PhosphorylationINVHTPNSQKVDSQK
EEEECCCCHHCCCHH		32.3630266825
344PhosphorylationPNSQKVDSQKAATKQ
CCCHHCCCHHHHHHH		36.2523403867
360 (in isoform 3)Ubiquitination-7.0521906983
366PhosphorylationLIEKKVHSERSAESC
HHHHHHHCCCCHHHH		37.3823312004
369PhosphorylationKKVHSERSAESCATW
HHHHCCCCHHHHCHH		32.1325159151
372PhosphorylationHSERSAESCATWKVQ
HCCCCHHHHCHHHHH		14.5823312004
377UbiquitinationAESCATWKVQKEEKL
HHHHCHHHHHHHHHH		30.36-
379 (in isoform 3)Ubiquitination-43.6521906983
383 (in isoform 1)Ubiquitination-46.6321906983
383UbiquitinationWKVQKEEKLIGLMNN
HHHHHHHHHHHHCCH		46.6321906983
396PhosphorylationNNEAAQESTRRRQKY
CHHHHHHHHHHHHHH		18.3525159151
396 (in isoform 3)Ubiquitination-18.35-
397PhosphorylationNEAAQESTRRRQKYQ
HHHHHHHHHHHHHHH		27.6921815630
402 (in isoform 1)Ubiquitination-47.2721906983
402UbiquitinationESTRRRQKYQESQEP
HHHHHHHHHHHCCCC		47.2721906983
406PhosphorylationRRQKYQESQEPLNEV
HHHHHHHCCCCHHHH		25.079344656
419UbiquitinationEVNSFPQKISYTQFP
HHCCCCCCCCCCCCC		33.58-
420 (in isoform 3)Ubiquitination-2.9921906983
421PhosphorylationNSFPQKISYTQFPNS
CCCCCCCCCCCCCCC		29.2127251275
423PhosphorylationFPQKISYTQFPNSFY
CCCCCCCCCCCCCCC		19.5522199227
428PhosphorylationSYTQFPNSFYEPHQD
CCCCCCCCCCCCCCC		29.4622199227
430PhosphorylationTQFPNSFYEPHQDFT
CCCCCCCCCCCCCCC		28.5030576142
437PhosphorylationYEPHQDFTSPDIFKK
CCCCCCCCCHHHHHC		47.8718691976
438PhosphorylationEPHQDFTSPDIFKKS
CCCCCCCCHHHHHCC		22.1430576142
443 (in isoform 1)Ubiquitination-50.6121906983
443MethylationFTSPDIFKKSRSPSW
CCCHHHHHCCCCCCH		50.6142376669
443UbiquitinationFTSPDIFKKSRSPSW
CCCHHHHHCCCCCCH		50.612190698
445PhosphorylationSPDIFKKSRSPSWYK
CHHHHHCCCCCCHHE		38.2823403867
447PhosphorylationDIFKKSRSPSWYKYT
HHHHCCCCCCHHEEE		30.3125159151
449PhosphorylationFKKSRSPSWYKYTST
HHCCCCCCHHEEEEE		44.2623403867
451PhosphorylationKSRSPSWYKYTSTVS
CCCCCCHHEEEEEEE		9.8423186163
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

Oops, there are no upstream regulatory protein records of VRK2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VRK2_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
59Ubiquitination49 (10)I ⇒ Vrs1051061
  • Schizophrenia
27922604
154Ubiquitination144 (10)I ⇒ Vrs1051061
  • Schizophrenia
27922604
177Ubiquitination167 (10)I ⇒ Vrs1051061
  • Schizophrenia
27922604
177Ubiquitination167 (10)I ⇒ Vrs1051061
  • Schizophrenia
27922604
177Ubiquitination167 (10)I ⇒ Vrs1051061
  • Schizophrenia
27922604
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
P53_HUMANTP53physical
16704422
JIP1_HUMANMAPK8IP1physical
18286207
M3K7_HUMANMAP3K7physical
18286207
MP2K7_HUMANMAP2K7physical
18286207
MK08_HUMANMAPK8physical
18286207
TCPD_HUMANCCT4physical
24298020
TCPA_HUMANTCP1physical
24298020
TCPB_HUMANCCT2physical
24298020
NFAC2_MOUSENfatc2physical
23105117
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 VRK2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 THR-336, AND MASSSPECTROMETRY.

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