Variant position: 62 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 230 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 KHWGRRKAWCRQLGEKGPCQ RVVSTHNLWLLSFLRRWNGST
Mouse KHWGRRKAWCRQLGEEGPCQ RVVSTHGVWLLAFLKKRNGST
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 – 230 Triggering receptor expressed on myeloid cells 2
19 – 174 Extracellular
29 – 112 Ig-like V-type
67 – 67 Phosphatidylserine
68 – 68 Phosphatidylserine; via amide nitrogen
77 – 77 Phosphatidylserine
79 – 79 N-linked (GlcNAc...) asparagine
36 – 110
48 – 48 K -> M. Loss of LDL, CLU and APOE binding.
60 – 60 C -> A. Loss of proteolytic cleavage by ADAM10 and ectodomain shedding. Decreases protein maturation and cell membrane localization.
68 – 68 N -> K. No effect on cell membrane localization.
76 – 76 R -> D. Decreases binding to THP-1 cells.
77 – 77 R -> D. Decreases binding to THP-1 cells.
60 – 66
TREM2 Binds to Apolipoproteins, Including APOE and CLU/APOJ, and Thereby Facilitates Uptake of Amyloid-Beta by Microglia.
Yeh F.L.; Wang Y.; Tom I.; Gonzalez L.C.; Sheng M.;
Cited for: FUNCTION; TISSUE SPECIFICITY; CHARACTERIZATION OF VARIANTS CYS-38; HIS-47; HIS-62; MET-66 AND ASN-87; MUTAGENESIS OF LYS-48;
TREM2 Maintains Microglial Metabolic Fitness in Alzheimer's Disease.
Ulland T.K.; Song W.M.; Huang S.C.; Ulrich J.D.; Sergushichev A.; Beatty W.L.; Loboda A.A.; Zhou Y.; Cairns N.J.; Kambal A.; Loginicheva E.; Gilfillan S.; Cella M.; Virgin H.W.; Unanue E.R.; Wang Y.; Artyomov M.N.; Holtzman D.M.; Colonna M.;
Cited for: TISSUE SPECIFICITY; CHARACTERIZATION OF VARIANTS HIS-47 AND HIS-62;
TREM2 Is a Receptor for beta-Amyloid that Mediates Microglial Function.
Zhao Y.; Wu X.; Li X.; Jiang L.L.; Gui X.; Liu Y.; Sun Y.; Zhu B.; Pina-Crespo J.C.; Zhang M.; Zhang N.; Chen X.; Bu G.; An Z.; Huang T.Y.; Xu H.;
Cited for: FUNCTION; CHARACTERIZATION OF VARIANTS HIS-47 AND HIS-62;
Neurodegenerative disease mutations in TREM2 reveal a functional surface and distinct loss-of-function mechanisms.
Kober D.L.; Alexander-Brett J.M.; Karch C.M.; Cruchaga C.; Colonna M.; Holtzman M.J.; Brett T.J.;
Cited for: X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 19-133; DISULFIDE BONDS; SUBUNIT; SUBCELLULAR LOCATION; MUTAGENESIS OF ASN-68; ARG-76 AND ARG-77; GLYCOSYLATION AT ASN-79; CHARACTERIZATION OF VARIANTS CYS-38; HIS-47; HIS-62; MET-66; ASN-87 AND LYS-96; CHARACTERIZATION OF VARIANT PLOSL2 GLY-126;
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.