Variant position: 55 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 113 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 CSTVSPGVLAGIVMGDLVLT VLIALAVYFLGRLVPRGRGAA
Rhesus macaque CSTVSPGVLAGIVLGDLVLT VLIALAVYFLGRLVPRGRGAA
Chimpanzee CSTVSPGVLAGIVMGDLVLT VLIALAVYFLGRLVHRGRGAA
Mouse CSSVSPGVLAGIVLGDLVLT LLIALAVYSLGRLVSRGQGTA
Rat CSSVSPGVLAGIVLGDLVLT LLIALAVYSLGRLVSRGRGTA
Pig CSAVSPGILAGIVLGDLVLT LLIALAVYSLGRLVPRTRGAV
Bovine CSSVSPGVLAGIVLGDLMLT LLIALAVYYLGRLVPRGRGAT
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
22 – 113 TYRO protein tyrosine kinase-binding protein
41 – 61 Helical
50 – 50 Metal cation; shared with neighboring subunit in homooligomer
54 – 54 Important for interaction with transmembrane receptors
35 – 35 Interchain
41 – 41 G -> L. Does not significantly alter the formation of homotrimers or homotetramers; when associated with L-45 and L-49.
45 – 45 G -> L. Does not significantly alter the formation of homotrimers or homotetramers; when associated with L-41 and L-49.
49 – 49 G -> L. Does not significantly alter the formation of homotrimers or homotetramers; when associated with L-41 and L-45.
50 – 50 D -> A. Reduced cell surface expression of KIR2DS1. Severely impairs formation of homotrimers and homotetramers. Abolishes interaction with TREM2 and stabilization of TREM2-CTF.
50 – 50 D -> EQ. Severely impairs formation of homotrimers and homotetramers.
50 – 50 D -> N. Reduces formation of homotrimers and homotetramers.
54 – 54 T -> A. Reduced interaction with KLRC2 and KIR2DS3. Reduces homotrimer formation and increases homotetramer formation.
40 – 65
TYROBP genetic variants in early-onset Alzheimer's disease.
Pottier C.; Ravenscroft T.A.; Brown P.H.; Finch N.A.; Baker M.; Parsons M.; Asmann Y.W.; Ren Y.; Christopher E.; Levitch D.; van Blitterswijk M.; Cruchaga C.; Campion D.; Nicolas G.; Richard A.C.; Guerreiro R.; Bras J.T.; Zuchner S.; Gonzalez M.A.; Bu G.; Younkin S.; Knopman D.S.; Josephs K.A.; Parisi J.E.; Petersen R.C.; Ertekin-Taner N.; Graff-Radford N.R.; Boeve B.F.; Dickson D.W.; Rademakers R.;
Neurobiol. Aging 48:222.E9-222.E15(2016)
Cited for: VARIANTS GLU-2; CYS-23; ALA-47; PRO-ALA-ASP-GLY-ARG-LEU-VAL-LEU-GLY-ASP-ARG-ASP-GLY-ARG-50 INS; LEU-55; TRP-80; VAL-84 AND LEU-89;
Mutations in TYROBP are not a common cause of dementia in a Turkish cohort.
Darwent L.; Carmona S.; Lohmann E.; Guven G.; Kun-Rodrigues C.; Bilgic B.; Hanagasi H.; Gurvit H.; Erginel-Unaltuna N.; Pak M.; Hardy J.; Singleton A.; Bras J.; Guerreiro R.;
Neurobiol. Aging 58:240.E1-240.E3(2017)
Cited for: VARIANT LEU-55;
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.