Variant position: 354 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 846 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 TFEQID--------DYNPDTAM---PAHSRS HSWDDKT-CQKSANVSSIWHRN-----------------------------------
Mouse TFEQID--------DYSPDTM----PAHSRS HSWNEKA-GQ
Xenopus laevis TRKQID--------DYNPDIPQ---LSHHRS QSWDNKQLNR
Zebrafish TMQRID--------DFNPDAPQTQPPKAPRS SSWNDRC-DK
Drosophila SMKRLD--------SWTPE------------ KAWPTPK-NV
Slime mold THEQFDKTQPYPKNTFTPQPKKLLSPISFNT KEFKNQT-NN
Baker's yeast HHLHLK--------IAQGDL-----NPYDFH QPLANREHKL
Fission yeast TKCAFD--------IKDSSM-----QSFTKT TITISKRKGI
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
1 – 846 Exonuclease 1
129 – 387 Interaction with MSH3
Human exonuclease I interacts with the mismatch repair protein hMSH2.
Schmutte C.; Marinescu R.C.; Sadoff M.M.; Guerrette S.; Overhauser J.; Fishel R.;
Cancer Res. 58:4537-4542(1998)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1); INTERACTION WITH MSH2; TISSUE SPECIFICITY; VARIANTS ARG-354; LYS-589; GLY-670; CYS-723 AND LEU-757;
Identification of a human gene encoding a homologue of Saccharomyces cerevisiae EXO1, an exonuclease implicated in mismatch repair and recombination.
Tishkoff D.X.; Amin N.S.; Viars C.S.; Arden K.C.; Kolodner R.D.;
Cancer Res. 58:5027-5031(1998)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]; ALTERNATIVE SPLICING; TISSUE SPECIFICITY; VARIANTS ARG-354; LYS-589; GLY-670 AND CYS-723;
Hex1: a new human Rad2 nuclease family member with homology to yeast exonuclease 1.
Wilson D.M. III; Carney J.P.; Coleman M.A.; Adamson A.W.; Christensen M.; Lamerdin J.E.;
Nucleic Acids Res. 26:3762-3768(1998)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]; ALTERNATIVE SPLICING; FUNCTION; TISSUE SPECIFICITY; VARIANTS ARG-354; LYS-589; GLY-670 AND CYS-723;
Human exonuclease 1 functionally complements its yeast homologues in DNA recombination, RNA primer removal, and mutation avoidance.
Qiu J.; Qian Y.; Chen V.; Guan M.-X.; Shen B.;
J. Biol. Chem. 274:17893-17900(1999)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2); PROTEIN SEQUENCE OF 1-7 (ISOFORMS 1/2); FUNCTION; VARIANTS ARG-354; LYS-589; GLY-670 AND CYS-723;
NIEHS SNPs program;
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]; VARIANTS ILE-76; GLY-93; SER-279; SER-299; ARG-354; ASN-428; MET-439; TYR-456; MET-458; LEU-460; THR-503; LYS-589; GLN-634; GLY-670; CYS-723; LEU-757 AND GLU-759;
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