UniProtKB/Swiss-Prot O75354: Variant p.Lys202Glu

Ectonucleoside triphosphate diphosphohydrolase 6
Gene: ENTPD6
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Variant information Variant position:

202 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:

LB/B 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 Lysine (K) to Glutamate (E) at position 202 (K202E, p.Lys202Glu). 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 large size and basic (K) to medium size and acidic (E) 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
Other resources:

Links to websites of interest for the variant.

Variant rs6050446 [ dbSNP | Ensembl ]

Sequence information Variant position:

202 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length:

484 The length of the canonical sequence.
Location on the sequence:

TAGLRLLPGEKAQKLLQKVK K VFKASPFLVGDDCVSIMNGT 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                         TAGLRLLPGEKAQKLLQKVKKVFKASPFLVGDDCVSIMNGT

Mouse                         TAGLRLLPGEKAQKLLQKVKEVFKASPFLVGDDCVSIMNGT

Rat                           TAGLRLLPGEKAQKLLQKVKEVFKASPFLVGDDCVSIMNGT

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	1 – 484	Ectonucleoside triphosphate diphosphohydrolase 6
Topological domain	61 – 484	Lumenal
Glycosylation	220 – 220	N-linked (GlcNAc...) asparagine
Mutagenesis	215 – 215	C -> S. Does not affect nucleoside-triphosphatase activity. Does not affeet KM for GDP.

Literature citations
The CD39-like gene family: identification of three new human members (CD39L2, CD39L3, and CD39L4), their murine homologues, and a member of the gene family from Drosophila melanogaster.
Chadwick B.P.; Frischauf A.-M.;
Genomics 50:357-367(1998)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1); VARIANTS VAL-138 AND GLU-202; Bacterial expression, characterization, and disulfide bond determination of soluble human NTPDase6 (CD39L2) nucleotidase: implications for structure and function.
Ivanenkov V.V.; Murphy-Piedmonte D.M.; Kirley T.L.;
Biochemistry 42:11726-11735(2003)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1); GLYCOSYLATION AT ASN-220 AND ASN-284; DISULFIDE BONDS; MUTAGENESIS OF CYS-215; VARIANTS ASN-14 AND GLU-202; BIOPHYSICOCHEMICAL PROPERTIES; CATALYTIC ACTIVITY; FUNCTION; SUBSTRATE SPECIFICITY; COFACTOR; ACTIVITY REGULATION; The full-ORF clone resource of the German cDNA consortium.
Bechtel S.; Rosenfelder H.; Duda A.; Schmidt C.P.; Ernst U.; Wellenreuther R.; Mehrle A.; Schuster C.; Bahr A.; Bloecker H.; Heubner D.; Hoerlein A.; Michel G.; Wedler H.; Koehrer K.; Ottenwaelder B.; Poustka A.; Wiemann S.; Schupp I.;
BMC Genomics 8:399-399(2007)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2); VARIANT GLU-202; Submission
Mural R.J.; Istrail S.; Sutton G.G.; Florea L.; Halpern A.L.; Mobarry C.M.; Lippert R.; Walenz B.; Shatkay H.; Dew I.; Miller J.R.; Flanigan M.J.; Edwards N.J.; Bolanos R.; Fasulo D.; Halldorsson B.V.; Hannenhalli S.; Turner R.; Yooseph S.; Lu F.; Nusskern D.R.; Shue B.C.; Zheng X.H.; Zhong F.; Delcher A.L.; Huson D.H.; Kravitz S.A.; Mouchard L.; Reinert K.; Remington K.A.; Clark A.G.; Waterman M.S.; Eichler E.E.; Adams M.D.; Hunkapiller M.W.; Myers E.W.; Venter J.C.;
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]; VARIANT GLU-202; The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
The MGC Project Team;
Genome Res. 14:2121-2127(2004)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3); VARIANT GLU-202;

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.