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UniProtKB/Swiss-Prot Q9UQ84: Variant p.His354Arg

Exonuclease 1
Gene: EXO1
Variant information

Variant position:  354
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  Polymorphism
The variants are classified into three categories: Disease, Polymorphism and Unclassified.
  • Disease: Variants implicated in disease according to literature reports.
  • Polymorphism: Variants not reported to be implicated in disease.
  • Unclassified: Variants with uncertain implication in disease according to literature reports. Evidence against or in favor of a pathogenic role is limited and/or conflicting.

Residue change:  From Histidine (H) to Arginine (R) at position 354 (H354R, p.His354Arg).
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 (H) to large size and basic (R)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  0
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

Polymorphism:  Most naturally occurring variants in this protein are not associated with familial disposition to hereditary non-polyposis colorectal cancer (HNPCC) (PubMed:12517792). Furthermore, germline deletions involving this locus are not associated with clinically manifested colorectal tumors (PubMed:14623461).
Additional information on the polymorphism described.

Other resources:  
Links to websites of interest for the variant.



Sequence information

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:   TFEQIDDYNPDTAMPAHSRS  H SWDDKTCQKSANVSSIWHRN
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---PAHSRSHSWDDKT-CQKSANVSSIWHRN-----------------------------------

Mouse                         TFEQID--------DYSPDTM----PAHSRSHSWNEKA-GQ

Xenopus laevis                TRKQID--------DYNPDIPQ---LSHHRSQSWDNKQLNR

Zebrafish                     TMQRID--------DFNPDAPQTQPPKAPRSSSWNDRC-DK

Drosophila                    SMKRLD--------SWTPE------------KAWPTPK-NV

Slime mold                    THEQFDKTQPYPKNTFTPQPKKLLSPISFNTKEFKNQT-NN

Baker's yeast                 HHLHLK--------IAQGDL-----NPYDFHQPLANREHKL

Fission yeast                 TKCAFD--------IKDSSM-----QSFTKTTITISKRKGI

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.

TypePositionsDescription
Chain 1 – 846 Exonuclease 1
Region 129 – 387 Interaction with MSH3


Literature citations

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;

Submission
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;

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.