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 GQPIHAELSPVTDFREACCRQ YEMGECTRGGFCNFMHLKPI
Mouse GQPIHAELSPVTDFREACCRQ YEMGECTRGGFCNFMHLKPI
Bovine GQPIHAELSPVTDFREACCRQ YEMGECTRGGFCNFMHLKPI
Drosophila GRPVYSELSPVTDFREACCRQ YEMGECTRSGFCNFMHLKPI
Fission yeast QRPVYAELSPVTDFREACCRQ HETSECQRGGLCNFMHAKKP
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;
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.