UniProtKB/Swiss-Prot Q9BQ65: Variant p.Arg115Lys

U6 snRNA phosphodiesterase 1
Gene: USB1
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Variant information Variant position:

115 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:

LB/B 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:

From Arginine (R) to Lysine (K) at position 115 (R115K, p.Arg115Lys). 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:

Similar physico-chemical property. Both residues are large size and basic. The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

2 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.

Variant rs35025252 [ dbSNP | Ensembl ]

Sequence information Variant position:

115 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length:

265 The length of the canonical sequence.
Location on the sequence:

FLDLLDVLLPHAQTYVPRLV R MKVFHLSLSQSVVLRHHWIL 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                         FLDLLDVLLP-------------------HAQTYVPRLVRMKVFHLSLSQSVVLRH-------HWIL

Mouse                         FRDLLDALLP-------------------RAQMFVPRLVLM

Rat                           FQDLLDVLLP-------------------RAQMFAPRLVQM

Bovine                        FLDLLDALLC-------------------HAQTYVPRLVRM

Xenopus laevis                FLDLLDELVS-------------------VAAENGVLLTKM

Zebrafish                     FLEVLNKMMA-------------------AAEAHDIPLTVS

Drosophila                    QLEEFQTEAI-------------------ARLEPHLELQPN

Slime mold                    IKELIEQVKE-------------------IGNEINIKQDTE

Baker's yeast                 IHRQLQKIICKYKETFMKQEYTNPYQLVDFDPLFISHLGAP

Fission yeast                 IREFLNSQSR-------------------FQSLLCSEHNVP

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.

Type	Positions	Description
Chain	1 – 265	U6 snRNA phosphodiesterase 1
Active site	120 – 120	Proton acceptor
Mutagenesis	120 – 120	H -> A. Abolishes exoribonuclease activity. Does not restore U6 snRNA processing when expressed in deleted mpn1 yeast cells; when associated with A-208. Increases the accumulation of unspliced pre-mRNAs when expressed in deleted mpn1 yeast cells; when associated with A-208. Slows growth in the cold when expressed in deleted mpn1 yeast cells; when associated with A-208. Abolishes exoribonuclease activity; when associated with A-208. Decreases U6 and U6atac motility.
Mutagenesis	120 – 120	H -> N. Significantly decreases exonuclease activity.
Mutagenesis	122 – 122	S -> C. Significantly decreases exonuclease activity.

Literature citations
No reference for the current variant in UniProtKB/Swiss-Prot.

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.