Overview
| Uniprot ID | Q99986 |
|---|
| Protein Name | Serine/threonine-protein kinase VRK1 |
|---|
| Gene Name | VRK1 |
|---|
| Organism | Homo sapiens |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 352 |
ENGGLKAKTITKKRK |
Function
Serine/threonine kinase involved in the regulation of key cellular processes including the cell cycle, nuclear condensation, transcription regulation, and DNA damage response (PubMed:14645249, PubMed:18617507, PubMed:19103756, PubMed:33076429). Controls chromatin organization and remodeling by mediating phosphorylation of histone H3 on 'Thr-4' and histone H2AX (H2aXT4ph) (PubMed:31527692, PubMed:37179361). It also phosphorylates KAT5 in response to DNA damage, promoting KAT5 association with chromatin and histone acetyltransferase activity (PubMed:33076429). Is involved in the regulation of cell cycle progression of neural progenitors, and is required for proper cortical neuronal migration (By similarity). Is involved in neurite elongation and branching in motor neurons, and has an essential role in Cajal bodies assembly, acting through COIL phosphorylation and the control of coilin degradation (PubMed:21920476, PubMed:31090908, PubMed:31527692). Involved in Golgi disassembly during the cell cycle: following phosphorylation by PLK3 during mitosis, it is required to induce Golgi fragmentation (PubMed:19103756). 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 (PubMed:16495336). Phosphorylates TP53BP1 and p53/TP53 on 'Thr-18', preventing the interaction between p53/TP53 and MDM2 (PubMed:10951572, PubMed:31527692). Phosphorylates ATF2 which activates its transcriptional activity (PubMed:15105425). Phosphorylates JUN (PubMed:31527692)
Protein Sequence
10
MPRVKAAQAG
20
RQSSAKRHLA
30
EQFAVGEIIT
40
DMAKKEWKVG
50
LPIGQGGFGC
60
IYLADMNSSE
70
SVGSDAPCVV
80
KVEPSDNGPL
90
FTELKFYQRA
100
AKPEQIQKWI
110
RTRKLKYLGV
120
PKYWGSGLHD
130
KNGKSYRFMI
140
MDRFGSDLQK
150
IYEANAKRFS
160
RKTVLQLSLR
170
ILDILEYIHE
180
HEYVHGDIKA
190
SNLLLNYKNP
200
DQVYLVDYGL
210
AYRYCPEGVH
220
KEYKEDPKRC
230
HDGTIEFTSI
240
DAHNGVAPSR
250
RGDLEILGYC
260
MIQWLTGHLP
270
WEDNLKDPKY
280
VRDSKIRYRE
290
NIASLMDKCF
300
PEKNKPGEIA
310
KYMETVKLLD
320
YTEKPLYENL
330
RDILLQGLKA
340
IGSKDDGKLD
350
LSVVENGGLK
360
AKTITKKRKK
370
EIEESKEPGV
380
EDTEWSNTQT
390
EEAIQTRSRT
RKRVQK
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0015030 |
Cajal body |
| Cellular Component |
GO:0000785 |
chromatin |
| Cellular Component |
GO:0005737 |
cytoplasm |
| Cellular Component |
GO:0005829 |
cytosol |
| Cellular Component |
GO:0005795 |
Golgi stack |
| Cellular Component |
GO:0005654 |
nucleoplasm |
| Cellular Component |
GO:0005634 |
nucleus |
| Molecular Function |
GO:0005524 |
ATP binding |
| Molecular Function |
GO:0042393 |
histone binding |
| Molecular Function |
GO:0141003 |
histone H2AX kinase activity |
| Molecular Function |
GO:0035175 |
histone H3S10 kinase activity |
| Molecular Function |
GO:0072354 |
histone H3T3 kinase activity |
| Molecular Function |
GO:0016301 |
kinase activity |
| Molecular Function |
GO:0031492 |
nucleosomal DNA binding |
| Molecular Function |
GO:0004672 |
protein kinase activity |
| Molecular Function |
GO:0019901 |
protein kinase binding |
| Molecular Function |
GO:0106310 |
protein serine kinase activity |
| Molecular Function |
GO:0004674 |
protein serine/threonine kinase activity |
| Biological Process |
GO:0030576 |
Cajal body organization |
| Biological Process |
GO:0051301 |
cell division |
| Biological Process |
GO:0006338 |
chromatin remodeling |
| Biological Process |
GO:0006974 |
DNA damage response |
| Biological Process |
GO:0090166 |
Golgi disassembly |
| Biological Process |
GO:0007077 |
mitotic nuclear membrane disassembly |
| Biological Process |
GO:0031175 |
neuron projection development |
| Biological Process |
GO:0120187 |
positive regulation of protein localization to chromatin |
| Biological Process |
GO:0046777 |
protein autophosphorylation |
| Biological Process |
GO:0006468 |
protein phosphorylation |
| Biological Process |
GO:2001222 |
regulation of neuron migration |
| Biological Process |
GO:0007165 |
signal transduction |
Reference
[1] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.