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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P50461: Variant p.Cys58Gly

Cysteine and glycine-rich protein 3
Gene: CSRP3
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Variant information Variant position: help 58 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 Cysteine (C) to Glycine (G) at position 58 (C58G, p.Cys58Gly). 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 medium size and polar (C) to glycine (G) 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 CMH12; decreases interaction with NRAP and ACTN2, decreases zinc-binding and impairs protein stability, decreases PKC/PRKCA activity. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 58 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 194 The length of the canonical sequence.
Location on the sequence: help MACRKALDSTTVAAHESEIY C KVCYGRRYGPKGIGYGQGAG 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                         MACRKALDSTTVAAHESEIYCKVCYGRRYGPKGIGYGQGAG

Mouse                         MACRKALDSTTVAAHESEIYCKVCYGRRYGPKGIGFGQGAG

Rat                           MACRKALDSTTVAAHESEIYCKVCYGRKYGPKGIGFGQGAG

Bovine                        MACRKALDSTTVAAHESEIYCKVCYGRRYGPKGIGYGQGAG
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 1 – 194 Cysteine and glycine-rich protein 3
Domain 10 – 61 LIM zinc-binding 1
Alternative sequence 38 – 59 MACRKALDSTTVAAHESEIYCK -> TLAQDLFPLCHLWEESGVHKC. In isoform 2.
Mutagenesis 69 – 69 K -> R. Increases PKC/PRKCA activity.



Literature citations
Decreased interactions of mutant muscle LIM protein (MLP) with N-RAP and alpha-actinin and their implication for hypertrophic cardiomyopathy.
Gehmlich K.; Geier C.; Osterziel K.J.; Van der Ven P.F.; Fuerst D.O.;
Cell Tissue Res. 317:129-136(2004)
Cited for: INTERACTION WITH NRAP AND ACTN2; CHARACTERIZATION OF VARIANT CMH12 GLY-58; MLP and CARP are linked to chronic PKCalpha signalling in dilated cardiomyopathy.
Lange S.; Gehmlich K.; Lun A.S.; Blondelle J.; Hooper C.; Dalton N.D.; Alvarez E.A.; Zhang X.; Bang M.L.; Abassi Y.A.; Dos Remedios C.G.; Peterson K.L.; Chen J.; Ehler E.;
Nat. Commun. 7:12120-12120(2016)
Cited for: FUNCTION; PHOSPHORYLATION; CHARACTERIZATION OF VARIANTS CMH12 PRO-44; 54-SER-GLU-55 DELINS ARG-GLY AND GLY-58; CHARACTERIZATION OF VARIANT ARG-72; MUTAGENESIS OF LYS-69; Mutations in the human muscle LIM protein gene in families with hypertrophic cardiomyopathy.
Geier C.; Perrot A.; Ozcelik C.; Binner P.; Counsell D.; Hoffmann K.; Pilz B.; Martiniak Y.; Gehmlich K.; van der Ven P.F.M.; Furst D.O.; Vornwald A.; von Hodenberg E.; Nurnberg P.; Scheffold T.; Dietz R.; Osterziel K.J.;
Circulation 107:1390-1395(2003)
Cited for: VARIANTS CMH12 PRO-44; 54-SER-GLU-55 DELINS ARG-GLY AND GLY-58; Beyond the sarcomere: CSRP3 mutations cause hypertrophic cardiomyopathy.
Geier C.; Gehmlich K.; Ehler E.; Hassfeld S.; Perrot A.; Hayess K.; Cardim N.; Wenzel K.; Erdmann B.; Krackhardt F.; Posch M.G.; Osterziel K.J.; Bublak A.; Nagele H.; Scheffold T.; Dietz R.; Chien K.R.; Spuler S.; Furst D.O.; Nurnberg P.; Ozcelik C.;
Hum. Mol. Genet. 17:2753-2765(2008)
Cited for: CHARACTERIZATION OF VARIANT CMD1M ARG-4; VARIANT CMH12 GLY-58; SUBCELLULAR LOCATION;
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.