UniProtKB/SwissProt variant VAR

Variant information

Variant position:

157

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

Type of variant:

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:

From Glutamine (Q) to Arginine (R) at position 157 (Q157R, p.Gln157Arg).

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 (Q) to large size and basic (R)

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

Variant description:

In MDS; somatic mutation; affects alternative splicing of target sequences.

Any additional useful information about the variant.

Other resources:

Links to websites of interest for the variant.

Variant rs371246226 [ dbSNP | Ensembl ]

Sequence information

Variant position:

157

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

Protein sequence length:

240

The length of the canonical sequence.

Location on the sequence:

GQPIHAELSPVTDFREACCR Q YEMGECTRGGFCNFMHLKPI

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                         GQPIHAELSPVTDFREACCRQYEMGECTRGGFCNFMHLKPI

Mouse                         GQPIHAELSPVTDFREACCRQYEMGECTRGGFCNFMHLKPI

Bovine                        GQPIHAELSPVTDFREACCRQYEMGECTRGGFCNFMHLKPI

Drosophila                    GRPVYSELSPVTDFREACCRQYEMGECTRSGFCNFMHLKPI

Fission yeast                 QRPVYAELSPVTDFREACCRQHETSECQRGGLCNFMHAKKP

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	2 – 240	Splicing factor U2AF 35 kDa subunit
Zinc finger	149 – 176	C3H1-type 2
Modified residue	145 – 145	Phosphoserine
Modified residue	165 – 165	Omega-N-methylarginine
Alternative sequence	76 – 240	Missing. In isoform 3.

Literature citations

Recurrent mutations in the U2AF1 splicing factor in myelodysplastic syndromes.
Graubert T.A.; Shen D.; Ding L.; Okeyo-Owuor T.; Lunn C.L.; Shao J.; Krysiak K.; Harris C.C.; Koboldt D.C.; Larson D.E.; McLellan M.D.; Dooling D.J.; Abbott R.M.; Fulton R.S.; Schmidt H.; Kalicki-Veizer J.; O'Laughlin M.; Grillot M.; Baty J.; Heath S.; Frater J.L.; Nasim T.; Link D.C.; Tomasson M.H.; Westervelt P.; DiPersio J.F.; Mardis E.R.; Ley T.J.; Wilson R.K.; Walter M.J.;
Nat. Genet. 44:53-57(2011)
Cited for: FUNCTION; INVOLVEMENT IN MDS; VARIANTS MDS PHE-34; TYR-34 AND ARG-157; CHARACTERIZATION OF VARIANT MDS PHE-34;

U2AF1 mutations alter sequence specificity of pre-mRNA binding and splicing.
Okeyo-Owuor T.; White B.S.; Chatrikhi R.; Mohan D.R.; Kim S.; Griffith M.; Ding L.; Ketkar-Kulkarni S.; Hundal J.; Laird K.M.; Kielkopf C.L.; Ley T.J.; Walter M.J.; Graubert T.A.;
Leukemia 29:909-917(2015)
Cited for: FUNCTION; INVOLVEMENT IN MDS; SUBCELLULAR LOCATION; CHARACTERIZATION OF VARIANTS MDS PHE-34; TYR-34 AND ARG-157;

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q01081: Variant p.Gln157Arg