Sequence information
Variant position: 118 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 140 The length of the canonical sequence.
Location on the sequence:
TFNVTVTKTDKTLVLLMGKE
G VHGGLINKKCYEMASHLRRS
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 TFNVTVTKTDKTLVLLMGKEG VH-GGLINKKCYEMASHLRRS
Mouse TFNVTVTMTAKTLVLLMGKEG VH-GGLINKKCYEMASHLRR
Rat TFNVTVTMTAKTLVLLMGKEG VH-GGLINKKCYEMASHLRR
Bovine TFNITVTMTAKTLVLLMGKEG VH-GGMINKKCYEMASHLRR
Caenorhabditis elegans ---FFAVKTKSAVLIAVYEGP NEVAAQVRKAVESMQTYLNN
Slime mold ---CVLVRTGQAIIVGIYDDK VQ-PGSAALIVEKLGDYLRD
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
2 – 140
Profilin-1
Modified residue
105 – 105
N6-acetyllysine
Modified residue
108 – 108
N6-acetyllysine
Modified residue
129 – 129
Phosphotyrosine
Modified residue
138 – 138
Phosphoserine; by ROCK1
Literature citations
Mutations in the profilin 1 gene cause familial amyotrophic lateral sclerosis.
Wu C.H.; Fallini C.; Ticozzi N.; Keagle P.J.; Sapp P.C.; Piotrowska K.; Lowe P.; Koppers M.; McKenna-Yasek D.; Baron D.M.; Kost J.E.; Gonzalez-Perez P.; Fox A.D.; Adams J.; Taroni F.; Tiloca C.; Leclerc A.L.; Chafe S.C.; Mangroo D.; Moore M.J.; Zitzewitz J.A.; Xu Z.S.; van den Berg L.H.; Glass J.D.; Siciliano G.; Cirulli E.T.; Goldstein D.B.; Salachas F.; Meininger V.; Rossoll W.; Ratti A.; Gellera C.; Bosco D.A.; Bassell G.J.; Silani V.; Drory V.E.; Brown R.H. Jr.; Landers J.E.;
Nature 488:499-503(2012)
Cited for: VARIANTS ALS18 GLY-71; THR-114; GLY-117 AND VAL-118; CHARACTERIZATION OF VARIANTS ALS18 GLY-71; THR-114; GLY-117 AND VAL-118;
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.