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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P63267: Variant p.Arg40Cys

Actin, gamma-enteric smooth muscle
Gene: ACTG2
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Variant information Variant position: help 40 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LP/P [Disclaimer] The variants are classified into three categories: LP/P, LB/B and US.
  • LP/P: likely pathogenic or pathogenic.
  • LB/B: likely benign or benign.
  • US: uncertain significance
Residue change: help From Arginine (R) to Cysteine (C) at position 40 (R40C, p.Arg40Cys). Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.
Physico-chemical properties: help Change from large size and basic (R) to medium size and polar (C) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -3 The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:
  • Lowest score: -4 (low probability of substitution).
  • Highest score: 11 (high probability of substitution).
More information can be found on the following page
Variant description: help In MMIHS5; interferes with proper polymerization into thin filaments. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 40 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 376 The length of the canonical sequence.
Location on the sequence: help AGFAGDDAPRAVFPSIVGRP R HQGVMVGMGQKDSYVGDEAQ 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences. 
Human                         AGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQ

Mouse                         AGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQ

Rat                           AGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQ

Bovine                        AGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQ

Chicken                       AGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQ
Sequence annotation in neighborhood: help 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.
TypePositionsDescription
Chain 2 – 376 Actin, gamma-enteric smooth muscle, intermediate form
Chain 3 – 376 Actin, gamma-enteric smooth muscle
Modified residue 45 – 45 Methionine (R)-sulfoxide
Modified residue 48 – 48 Methionine (R)-sulfoxide
Cross 51 – 51 Isoglutamyl lysine isopeptide (Lys-Glu) (interchain with E-271); by Vibrio toxins RtxA and VgrG1



Literature citations
Heterozygous de novo and inherited mutations in the smooth muscle actin (ACTG2) gene underlie megacystis-microcolon-intestinal hypoperistalsis syndrome.
Wangler M.F.; Gonzaga-Jauregui C.; Gambin T.; Penney S.; Moss T.; Chopra A.; Probst F.J.; Xia F.; Yang Y.; Werlin S.; Eglite I.; Kornejeva L.; Bacino C.A.; Baldridge D.; Neul J.; Lehman E.L.; Larson A.; Beuten J.; Muzny D.M.; Jhangiani S.; Gibbs R.A.; Lupski J.R.; Beaudet A.;
PLoS Genet. 10:E1004258-E1004258(2014)
Cited for: VARIANTS MMIHS5 CYS-40; HIS-40; ASN-134; CYS-178; HIS-178 AND CYS-257; VARIANTS VSCM1 HIS-40; THR-45; GLY-63; LEU-110 AND ASP-198; INVOLVEMENT IN MMIHS5; INVOLVEMENT IN VSCM1; ACTG2 variants impair actin polymerization in sporadic Megacystis Microcolon Intestinal Hypoperistalsis Syndrome.
Halim D.; Hofstra R.M.; Signorile L.; Verdijk R.M.; van der Werf C.S.; Sribudiani Y.; Brouwer R.W.; van Ijcken W.F.; Dahl N.; Verheij J.B.; Baumann C.; Kerner J.; van Bever Y.; Galjart N.; Wijnen R.M.; Tibboel D.; Burns A.J.; Muller F.; Brooks A.S.; Alves M.M.;
Hum. Mol. Genet. 25:571-583(2016)
Cited for: VARIANTS MMIHS5 CYS-40; GLN-63; CYS-178; HIS-178 AND LEU-178; INVOLVEMENT IN MMIHS5; TISSUE SPECIFICITY; CHARACTERIZATION OF VARIANTS MMIHS5 CYS-40; GLN-63; CYS-178; HIS-178 AND LEU-178; CHARACTERIZATION OF VARIANT VSCM1 SER-148; Variants in ACTG2 underlie a substantial number of Australasian patients with primary chronic intestinal pseudo-obstruction.
Ravenscroft G.; Pannell S.; O'Grady G.; Ong R.; Ee H.C.; Faiz F.; Marns L.; Goel H.; Kumarasinghe P.; Sollis E.; Sivadorai P.; Wilson M.; Magoffin A.; Nightingale S.; Freckmann M.L.; Kirk E.P.; Sachdev R.; Lemberg D.A.; Delatycki M.B.; Kamm M.A.; Basnayake C.; Lamont P.J.; Amor D.J.; Jones K.; Schilperoort J.; Davis M.R.; Laing N.G.;
Neurogastroenterol. Motil. 30:e13371-e13371(2018)
Cited for: VARIANTS VSCM1 HIS-40; LEU-148 AND CYS-257; VARIANT MMIHS5 CYS-40;
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.