Variant position: 307 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 336 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 FTESWDTQ-KAPNNYRSPIST SQPTNQSMDDTREDIYVNYPT
Rhesus macaque YTESWDTQ-KAPKNYRSPISA SQPTNQSMDDTREDIYVNYP
Mouse LKEPRDKQSKVATNCRSPTSP IQST----DDEKEDIYVNYP
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
19 – 336 CD226 antigen
276 – 336 Cytoplasmic
322 – 322 Phosphotyrosine
DNAM-1, a novel adhesion molecule involved in the cytolytic function of T lymphocytes.
Shibuya A.; Campbell D.; Hannum C.; Yssel H.; Franz-Bacon K.; McClanahan T.; Kitamura T.; Nicholl J.; Sutherland G.R.; Lanier L.L.; Phillips J.H.;
Cited for: NUCLEOTIDE SEQUENCE [MRNA]; PROTEIN SEQUENCE OF 19-39; 54-72; 204-221 AND 285-294; FUNCTION; PHOSPHORYLATION; GLYCOSYLATION; TISSUE SPECIFICITY; VARIANT GLY-307;
Receptor involved in the NK cell triggering.
Cited for: NUCLEOTIDE SEQUENCE [MRNA]; VARIANT GLY-307;
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]; VARIANT GLY-307;
Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.
Mayya V.; Lundgren D.H.; Hwang S.-I.; Rezaul K.; Wu L.; Eng J.K.; Rodionov V.; Han D.K.;
Sci. Signal. 2:RA46-RA46(2009)
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-322; VARIANT [LARGE SCALE ANALYSIS] GLY-307; IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS];
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