CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-016321
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Serine/threonine-protein kinase VRK2 
Protein Synonyms/Alias
 Vaccinia-related kinase 2 
Gene Name
 VRK2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
10PKRNEKYKLPIPFPEubiquitination[1]
33GNQWVLGKKIGSGGFubiquitination[2]
75GPLFSELKFYQRVAKubiquitination[2]
112GSGLTEFKGRSYRFMubiquitination[1, 3]
177ANLLLGYKNPDQVYLubiquitination[2, 3, 4]
200YCPNGNHKQYQENPRubiquitination[3]
223FTSLDAHKGVALSRRubiquitination[2]
255LPWEQNLKDPVAVQTubiquitination[2, 4]
264PVAVQTAKTNLLDELubiquitination[2, 4]
328GPLDFSTKGQSINVHubiquitination[2, 3, 4]
383WKVQKEEKLIGLMNNubiquitination[2]
402ESTRRRQKYQESQEPubiquitination[2]
419EVNSFPQKISYTQFPubiquitination[4]
443FTSPDIFKKSRSPSWubiquitination[2, 3, 4]
Reference
 [1] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [2] 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]
 [3] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [4] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661
Functional 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. 
Sequence Annotation
 DOMAIN 29 319 Protein kinase.
 NP_BIND 35 43 ATP (By similarity).
 REGION 397 508 Interaction with MAP3K7.
 ACT_SITE 166 166 Proton acceptor (By similarity).
 BINDING 61 61 ATP (By similarity).
 MOD_RES 336 336 Phosphothreonine.  
Keyword
 3D-structure; Alternative splicing; ATP-binding; Complete proteome; Cytoplasm; Endoplasmic reticulum; Host-virus interaction; Kinase; Membrane; Mitochondrion; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Serine/threonine-protein kinase; Transferase; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 508 AA 
Protein Sequence
MPPKRNEKYK LPIPFPEGKV LDDMEGNQWV LGKKIGSGGF GLIYLAFPTN KPEKDARHVV 60
KVEYQENGPL FSELKFYQRV AKKDCIKKWI ERKQLDYLGI PLFYGSGLTE FKGRSYRFMV 120
MERLGIDLQK ISGQNGTFKK STVLQLGIRM LDVLEYIHEN EYVHGDIKAA NLLLGYKNPD 180
QVYLADYGLS YRYCPNGNHK QYQENPRKGH NGTIEFTSLD AHKGVALSRR SDVEILGYCM 240
LRWLCGKLPW EQNLKDPVAV QTAKTNLLDE LPQSVLKWAP SGSSCCEIAQ FLVCAHSLAY 300
DEKPNYQALK KILNPHGIPL GPLDFSTKGQ SINVHTPNSQ KVDSQKAATK QVNKAHNRLI 360
EKKVHSERSA ESCATWKVQK EEKLIGLMNN EAAQESTRRR QKYQESQEPL NEVNSFPQKI 420
SYTQFPNSFY EPHQDFTSPD IFKKSRSPSW YKYTSTVSTG ITDLESSTGL WPTISQFTLS 480
EETNADVYYY RIIIPVLLML VFLALFFL 508 
Gene Ontology
 GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0031966; C:mitochondrial membrane; IDA:UniProtKB.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
 GO:0034599; P:cellular response to oxidative stress; IMP:UniProtKB.
 GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
 GO:2000659; P:regulation of interleukin-1-mediated signaling pathway; IMP:UniProtKB.
 GO:0043408; P:regulation of MAPK cascade; IMP:UniProtKB.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 
Interpro
 IPR011009; Kinase-like_dom.
 IPR000719; Prot_kinase_cat_dom.
 IPR008271; Ser/Thr_kinase_AS. 
Pfam
 PF00069; Pkinase 
SMART
  
PROSITE
 PS00107; PROTEIN_KINASE_ATP
 PS50011; PROTEIN_KINASE_DOM
 PS00108; PROTEIN_KINASE_ST 
PRINTS