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UniProtKB/Swiss-Prot Q9BVS4: Variant p.Asn397Ser

Serine/threonine-protein kinase RIO2
Gene: RIOK2
Variant information

Variant position:  397
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  Polymorphism
The variants are classified into three categories: Disease, Polymorphism and Unclassified.
  • Disease: Variants implicated in disease according to literature reports.
  • Polymorphism: Variants not reported to be implicated in disease.
  • Unclassified: Variants with uncertain implication in disease according to literature reports. Evidence against or in favor of a pathogenic role is limited and/or conflicting.

Residue change:  From Asparagine (N) to Serine (S) at position 397 (N397S, p.Asn397Ser).
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:  Change from medium size and polar (N) to small size and polar (S)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  1
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

Other resources:  
Links to websites of interest for the variant.



Sequence information

Variant position:  397
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  552
The length of the canonical sequence.

Location on the sequence:   KEDSLSEESADARSFEMTEF  N QALEEIKGQVVENNSVTEFS
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: 
The multiple alignment of the region surrounding the variant against various orthologous sequences.

Human                         KEDSLSEESADARSFEMTEFNQALEEIKGQVVENNSVTEFS

Mouse                         KDGGLPEESAHVSSFEVTALSQAVEEMERQVLPHRSVTEFS

Caenorhabditis elegans        QAQENTVKQQKIVLSQTTRFTDWLSDATNQLEAVDLDALKS

Sequence annotation in neighborhood:  
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 – 552 Serine/threonine-protein kinase RIO2
Modified residue 380 – 380 Phosphoserine
Modified residue 382 – 382 Phosphoserine
Modified residue 385 – 385 Phosphoserine
Modified residue 390 – 390 Phosphoserine
Modified residue 412 – 412 Phosphoserine
Modified residue 417 – 417 Phosphoserine
Mutagenesis 380 – 380 S -> A. Does not affect autophosphorylation activity; when associated with A-335 and A-548. Does not affect the timing of metaphase-anaphase transition; when associated with A-335 and A-548.
Mutagenesis 380 – 380 S -> D. Increases time spent in metaphase; when associated with D-335 and D-548.
Mutagenesis 400 – 400 L -> A. Nuclear relocalization; when associated with A-403.
Mutagenesis 403 – 403 I -> A. Nuclear relocalization; when associated with A-400.
Helix 394 – 400


Literature citations

Patterns of somatic mutation in human cancer genomes.
Greenman C.; Stephens P.; Smith R.; Dalgliesh G.L.; Hunter C.; Bignell G.; Davies H.; Teague J.; Butler A.; Stevens C.; Edkins S.; O'Meara S.; Vastrik I.; Schmidt E.E.; Avis T.; Barthorpe S.; Bhamra G.; Buck G.; Choudhury B.; Clements J.; Cole J.; Dicks E.; Forbes S.; Gray K.; Halliday K.; Harrison R.; Hills K.; Hinton J.; Jenkinson A.; Jones D.; Menzies A.; Mironenko T.; Perry J.; Raine K.; Richardson D.; Shepherd R.; Small A.; Tofts C.; Varian J.; Webb T.; West S.; Widaa S.; Yates A.; Cahill D.P.; Louis D.N.; Goldstraw P.; Nicholson A.G.; Brasseur F.; Looijenga L.; Weber B.L.; Chiew Y.-E.; DeFazio A.; Greaves M.F.; Green A.R.; Campbell P.; Birney E.; Easton D.F.; Chenevix-Trench G.; Tan M.-H.; Khoo S.K.; Teh B.T.; Yuen S.T.; Leung S.Y.; Wooster R.; Futreal P.A.; Stratton M.R.;
Nature 446:153-158(2007)
Cited for: VARIANTS [LARGE SCALE ANALYSIS] CYS-96; ARG-144; HIS-155; ILE-175; THR-216; VAL-244; ARG-349; SER-397; ASP-409 AND HIS-507;

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.