Variant position: 34 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:
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 DKVNCSFYFKIGACRHGDRC SRLHNKPTFSQTIALLNIYRN
Mouse DKVNCSFYFKIGACRHGDRC SRLHNKPTFSQTIALLNIYRN
Bovine DKVNCSFYFKIGACRHGDRC SRLHNKPTFSQTIALLNIYRN
Drosophila DKVNCSFYFKIGACRHGDRC SRIHNKPTFSQTVLLQNLYVN
Fission yeast DKVNCSFYYKIGACRHGERC SRKHVKPNFSQTILCPNMYKN
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
2 – 240 Splicing factor U2AF 35 kDa subunit
12 – 40 C3H1-type 1
39 – 39 N6-methyllysine
1 – 73 Missing. In isoform 4.
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.;
Cited for: FUNCTION; INVOLVEMENT IN MDS; SUBCELLULAR LOCATION; CHARACTERIZATION OF VARIANTS MDS PHE-34; TYR-34 AND ARG-157;
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