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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q99986: Variant p.Arg387His

Serine/threonine-protein kinase VRK1
Gene: VRK1
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Variant information Variant position: help 387 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LP/P [Disclaimer] The variants are classified into three categories: LP/P, LB/B and US.
  • LP/P: likely pathogenic or pathogenic.
  • LB/B: likely benign or benign.
  • US: uncertain significance
Residue change: help From Arginine (R) to Histidine (H) at position 387 (R387H, p.Arg387His). Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.
Physico-chemical properties: help Change from large size and basic (R) to medium size and polar (H) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 0 The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:
  • Lowest score: -4 (low probability of substitution).
  • Highest score: 11 (high probability of substitution).
More information can be found on the following page
Variant description: help In HMNR10; likely pathogenic; severely decreased interaction with nucleosome. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 387 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 396 The length of the canonical sequence.
Location on the sequence: help EPGVEDTEWSNTQTEEAIQT R SRTRKRVQK The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation: help The multiple alignment of the region surrounding the variant against various orthologous sequences. 
Human                         EPGVEDTEWSNTQTEEAIQTR--------------------------------------------------SRTRKRVQK----------------------------------------------------------------------------------------------------------------------------------------------------

Mouse                         VCAVEDMECSDTQVQEAAQTRSVESQGAIH

Bovine                        ESSVEDMECSDKQTEEATQTR---------

Zebrafish                     GQSADETDSTPAKKRRAPQKKEVNGAKKTA

Caenorhabditis elegans        AVEVNNDSDDNEEQYENPKSKSSRTQTKSK
Sequence annotation in neighborhood: help The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:
  • Type: the type of sequence feature.
  • Positions: endpoints of the sequence feature.
  • Description: contains additional information about the feature.
TypePositionsDescription
Chain 1 – 396 Serine/threonine-protein kinase VRK1
Region 354 – 396 Disordered
Region 387 – 393 Required for interaction with the nucleosome
Compositional bias 375 – 387 Polar residues
Modified residue 376 – 376 Phosphoserine
Modified residue 378 – 378 Phosphothreonine
Mutagenesis 387 – 393 RSRTRKR -> ASATAKA. Abolishes interaction with nucleosome. Decreased histone H3 phosphorylation.
Mutagenesis 390 – 390 T -> A. Does not abolish autophosphorylation.



Literature citations
Multivalent DNA and nucleosome acidic patch interactions specify VRK1 mitotic localization and activity.
Budziszewski G.R.; Zhao Y.; Spangler C.J.; Kedziora K.M.; Williams M.R.; Azzam D.N.; Skrajna A.; Koyama Y.; Cesmat A.P.; Simmons H.C.; Arteaga E.C.; Strauss J.D.; Kireev D.; McGinty R.K.;
Nucleic Acids Res. 50:4355-4371(2022)
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.00 ANGSTROMS) IN COMPLEX WITH NUCLEOSOME CORE; INTERACTION WITH H2A AND H2B; SUBCELLULAR LOCATION; REGION; MUTAGENESIS OF 387-ARG--ARG-393; CHARACTERIZATION OF VARIANTS HMNR10 375-TRP--LYS-396 DEL AND HIS-387;
Molecular analysis and clinical diversity of distal hereditary motor neuropathy.
Liu X.; Duan X.; Zhang Y.; Sun A.; Fan D.;
Eur. J. Neurol. 27:1319-1326(2020)
Cited for: VARIANTS HMNR10 375-TRP--LYS-396 DEL AND HIS-387;
Identification of a homozygous VRK1 mutation in two patients with adult-onset distal hereditary motor neuropathy.
Greenbaum L.; Barel O.; Nikitin V.; Hersalis-Eldar A.; Kol N.; Reznik-Wolf H.; Dominissini D.; Pras E.; Dori A.;
Muscle Nerve 61:395-400(2020)
Cited for: VARIANT HMNR10 HIS-387; INVOLVEMENT IN HMNR10;
Disclaimer: Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.