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UniProtKB/Swiss-Prot P63000: Variant p.Val51Met

Ras-related C3 botulinum toxin substrate 1
Gene: RAC1
Variant information

Variant position:  51
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  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:  From Valine (V) to Methionine (M) at position 51 (V51M, p.Val51Met).
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:  Similar physico-chemical property. Both residues are medium size and hydrophobic.
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  1
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:  In MRD48; decreased substrate adhesion-dependent cell spreading; weak dominant-negative effect.
Any additional useful information about the variant.

Other resources:  
Links to websites of interest for the variant.



Sequence information

Variant position:  51
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  192
The length of the canonical sequence.

Location on the sequence:   EYIPTVFDNYSANVMVDGKP  V NLGLWDTAGQEDYDRLRPLS
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.

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.

TypePositionsDescription
Chain 1 – 189 Ras-related C3 botulinum toxin substrate 1
Binding site 60 – 60 GTP; via amide nitrogen
Modified residue 32 – 32 (Microbial infection) O-AMP-tyrosine; by Haemophilus IbpA; alternate
Modified residue 35 – 35 (Microbial infection) O-AMP-threonine; by Vibrio VopS
Modified residue 39 – 39 ADP-ribosylasparagine; by botulinum toxin
Glycosylation 32 – 32 (Microbial infection) O-linked (GlcNAc) tyrosine; by Photorhabdus PAU_02230; alternate
Glycosylation 35 – 35 (Microbial infection) O-alpha-linked (GlcNAc) threonine; by C.novyi toxin TcdA; alternate
Glycosylation 35 – 35 (Microbial infection) O-linked (Glc) threonine; by C.difficile toxins TcdA and TcdB, and by P.sordellii toxin TcsL; alternate
Mutagenesis 32 – 32 Y -> F. Abolishes AMPylation by Haemophilus IbpA.
Mutagenesis 35 – 35 T -> A. Abolishes AMPylation by Vibrio VopS.
Mutagenesis 35 – 35 T -> S. No interaction with PPP5C; when associated with L-61. Translocates to the plasma membrane; also when associated with L-61.
Mutagenesis 37 – 37 F -> A. Strongly reduced interaction with PLCB2.
Mutagenesis 56 – 56 W -> A. Strongly reduced interaction with PLCB2.
Mutagenesis 61 – 61 Q -> L. Constitutively active. Interacts with PARD6 proteins. Interacts with PPP5C, activates its phosphatase activity and translocates PPP5C to the plasma membrane. No effect on interaction with RAPH1. Interacts with CYRIB. No interaction with PPP5C; when associated with V-30 or S-35. Translocates to the plasma membrane; also when associated with V-30 or S-35.
Mutagenesis 67 – 67 L -> A. Strongly reduced interaction with PLCB2.
Mutagenesis 70 – 70 L -> A. Strongly reduced interaction with PLCB2.
Beta strand 49 – 56


Literature citations

RAC1 Missense Mutations in Developmental Disorders with Diverse Phenotypes.
Reijnders M.R.F.; Ansor N.M.; Kousi M.; Yue W.W.; Tan P.L.; Clarkson K.; Clayton-Smith J.; Corning K.; Jones J.R.; Lam W.W.K.; Mancini G.M.S.; Marcelis C.; Mohammed S.; Pfundt R.; Roifman M.; Cohn R.; Chitayat D.; Millard T.H.; Katsanis N.; Brunner H.G.; Banka S.;
Am. J. Hum. Genet. 101:466-477(2017)
Cited for: FUNCTION; INVOLVEMENT IN MRD48; VARIANTS MRD48 TYR-18; SER-39; LEU-51; MET-51; ASP-64; LEU-73 AND TYR-157; CHARACTERIZATION OF VARIANTS MRD48 TYR-18; SER-39; MET-51; ASP-64; LEU-73 AND TYR-157;

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.