VRK2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: VRK2_MOUSE
• UniProt AC: Q8BN21
• Protein Name: Serine/threonine-protein kinase VRK2
• Gene Name: Vrk2
• Organism: Mus musculus (Mouse).
• Sequence Length: 503
• Subcellular Localization: Cytoplasm . Endoplasmic reticulum membrane ; Single-pass type IV membrane protein . Mitochondrion membrane ; Single-pass type IV membrane protein .
• 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 histone H3. Phosphorylates 'Thr-18' of p53/TP53, and thereby increases its stability and activity. 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. May also phosphorylate MAPK8IP1. 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 (By similarity)..
• Protein Sequence: MAPRRKEKYKLPVPLPEGKILDDMEGNRWALGKMIGSGGFGLIYLAFPTNKPNKDARHVIKLEYQENGPLFSELKFYQRAAKRECIQKWIQQRKLDYLGIPVFYGFGLTDFKGRSYRFMVMERLGIDLQKLLDQNGGFKKLTVLQLGIRMLDVLEYIHENEYVHGDIKAANLLLDFTNPDRVYLADYGLSYRYCPNGNHKQYQEDPRKGHNGTIEFTSLDAHKGVAPSRRSDVEILGYCMLHWLFGKLPWEAKLDDPVAVQTAKTNLLDELPESVLKWAPSGSSCSELVKYLMYVHNLAYDDKPDYQKLKKILNPDGVPLGPLEFSTKVQSVHVRTPAQQKVDSPKATRKPANEFPAKFPKKVHRETRARQREEQEDSQPTMLQSRPAAPENSRTRKIHEYSDIFSEMQSLQQTPSYMSFQGSYCKPYLDCTRRDPIRKPRSLPRYRHTPTGNLGVTDLESSPRFWPAIFQLTLSEETKADVYYYGITIFCLLIFVFLALYFL

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
264	Ubiquitination	PVAVQTAKTNLLDEL CCHHHCCCCCHHHHC	41.14	-
336	Phosphorylation	VQSVHVRTPAQQKVD EEEEEECCHHHHCCC	23.14	-
344	Phosphorylation	PAQQKVDSPKATRKP HHHHCCCCCCCCCCC	31.15	22942356
393	Phosphorylation	RPAAPENSRTRKIHE CCCCCCCCCCCCHHH	33.11	25338131
446	Phosphorylation	KPRSLPRYRHTPTGN CCCCCCCCCCCCCCC	12.57	22345495
449	Phosphorylation	SLPRYRHTPTGNLGV CCCCCCCCCCCCCCC	17.34	25159016
451	Phosphorylation	PRYRHTPTGNLGVTD CCCCCCCCCCCCCCC	39.60	25159016
461	Phosphorylation	LGVTDLESSPRFWPA CCCCCCCCCCCHHHE	53.60	25159016
462	Phosphorylation	GVTDLESSPRFWPAI CCCCCCCCCCHHHEE	15.66	25338131

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of VRK2_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of VRK2_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of VRK2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
M3K7_MOUSE	Map3k7	physical	17709393

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.