Sequence information
Variant position: 138 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 377 The length of the canonical sequence.
Location on the sequence:
REKMTQIMFETFNVPAMYVA
I QAVLSLYASGRTTGIVLDSG
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 REKMTQIMFETFNVPAMYVAI QAVLSLYASGRTTGIVLDSG
Mouse REKMTQIMFETFNVPAMYVAI QAVLSLYASGRTTGIVLDSG
Rat REKMTQIMFETFNVPAMYVAI QAVLSLYASGRTTGIVLDSG
Pig REKMTQIMFETFNVPAMYVAI QAVLSLYASGRTTGIVLDSG
Bovine REKMTQIMFETFNVPAMYVAI QAVLSLYASGRTTGIVLDSG
Rabbit REKMTQIMFETFNVPAMYVAI QAVLSLYASGRTTGIVLDSG
Chicken REKMTQIMFETFNVPAMYVAI QAVLSLYASGRTTGIVLDSG
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 – 377
Actin, alpha skeletal muscle, intermediate form
Chain
3 – 377
Actin, alpha skeletal muscle
Literature citations
Nemaline myopathy caused by mutations in the muscle alpha-skeletal-actin gene.
Ilkovski B.; Cooper S.T.; Nowak K.; Ryan M.M.; Yang N.; Schnell C.; Durling H.J.; Roddick L.G.; Wilkinson I.; Kornberg A.J.; Collins K.J.; Wallace G.; Gunning P.; Hardeman E.C.; Laing N.G.; North K.N.;
Am. J. Hum. Genet. 68:1333-1343(2001)
Cited for: VARIANTS NEM3 SER-117; MET-138; GLY-185; CYS-270 AND LEU-359;
Evidence for a dominant-negative effect in ACTA1 nemaline myopathy caused by abnormal folding, aggregation and altered polymerization of mutant actin isoforms.
Ilkovski B.; Nowak K.J.; Domazetovska A.; Maxwell A.L.; Clement S.; Davies K.E.; Laing N.G.; North K.N.; Cooper S.T.;
Hum. Mol. Genet. 13:1727-1743(2004)
Cited for: VARIANTS NEM3 ILE-68; LYS-74; SER-117; MET-138; LEU-165; MET-165; GLY-185; CYS-270 AND LEU-359;
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.