CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019828
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Serine/threonine-protein kinase VRK1 
Protein Synonyms/Alias
 Vaccinia-related kinase 1 
Gene Name
 VRK1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
16AGRQSSAKRHLAEQFubiquitination[1]
35IITDMAKKEWKVGLPubiquitination[2]
85GPLFTELKFYQRAAKubiquitination[2, 3]
92KFYQRAAKPEQIQKWubiquitination[2]
98AKPEQIQKWIRTRKLacetylation[3, 4]
98AKPEQIQKWIRTRKLubiquitination[2, 3, 5]
106WIRTRKLKYLGVPKYubiquitination[2]
112LKYLGVPKYWGSGLHubiquitination[2, 3, 6, 7]
124GLHDKNGKSYRFMIMubiquitination[2]
140RFGSDLQKIYEANAKubiquitination[2, 3]
147KIYEANAKRFSRKTVubiquitination[2]
152NAKRFSRKTVLQLSLubiquitination[2]
188SNLLLNYKNPDQVYLubiquitination[1, 2, 5]
288NIASLMDKCFPEKNKubiquitination[2]
293MDKCFPEKNKPGEIAubiquitination[2]
295KCFPEKNKPGEIAKYubiquitination[2]
301NKPGEIAKYMETVKLubiquitination[1, 2, 5, 6, 7]
307AKYMETVKLLDYTEKubiquitination[2]
314KLLDYTEKPLYENLRubiquitination[2]
329DILLQGLKAIGSKDDubiquitination[1, 2, 6, 7]
338IGSKDDGKLDLSVVEubiquitination[2]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [4] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [5] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [6] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [7] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789
Functional 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. 
Sequence Annotation
 DOMAIN 37 317 Protein kinase.
 NP_BIND 43 51 ATP (By similarity).
 ACT_SITE 177 177 Proton acceptor (By similarity).
 BINDING 71 71 ATP (By similarity).
 MOD_RES 342 342 Phosphoserine; by PLK3.
 MOD_RES 355 355 Phosphothreonine; by autocatalysis.  
Keyword
 3D-structure; ATP-binding; Cell cycle; Cell division; Complete proteome; Cytoplasm; Cytoskeleton; Kinase; Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Serine/threonine-protein kinase; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 396 AA 
Protein Sequence
MPRVKAAQAG RQSSAKRHLA EQFAVGEIIT DMAKKEWKVG LPIGQGGFGC IYLADMNSSE 60
SVGSDAPCVV KVEPSDNGPL FTELKFYQRA AKPEQIQKWI RTRKLKYLGV PKYWGSGLHD 120
KNGKSYRFMI MDRFGSDLQK IYEANAKRFS RKTVLQLSLR ILDILEYIHE HEYVHGDIKA 180
SNLLLNYKNP DQVYLVDYGL AYRYCPEGVH KEYKEDPKRC HDGTIEFTSI DAHNGVAPSR 240
RGDLEILGYC MIQWLTGHLP WEDNLKDPKY VRDSKIRYRE NIASLMDKCF PEKNKPGEIA 300
KYMETVKLLD YTEKPLYENL RDILLQGLKA IGSKDDGKLD LSVVENGGLK AKTITKKRKK 360
EIEESKEPGV EDTEWSNTQT EEAIQTRSRT RKRVQK 396 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005795; C:Golgi stack; IDA:UniProtKB.
 GO:0005730; C:nucleolus; IDA:HPA.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0090166; P:Golgi disassembly; IDA:UniProtKB.
 GO:0007067; P:mitosis; IEA:UniProtKB-KW.
 GO:0007077; P:mitotic nuclear envelope disassembly; TAS:Reactome.
 GO:0007084; P:mitotic nuclear envelope reassembly; TAS:Reactome.
 GO:0046777; P:protein autophosphorylation; IDA:UniProtKB. 
Interpro
 IPR011009; Kinase-like_dom.
 IPR000719; Prot_kinase_cat_dom.
 IPR017441; Protein_kinase_ATP_BS.
 IPR008271; Ser/Thr_kinase_AS. 
Pfam
 PF00069; Pkinase 
SMART
  
PROSITE
 PS00107; PROTEIN_KINASE_ATP
 PS50011; PROTEIN_KINASE_DOM
 PS00108; PROTEIN_KINASE_ST 
PRINTS