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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P10644: Variant p.Ala213Asp

cAMP-dependent protein kinase type I-alpha regulatory subunit
Gene: PRKAR1A
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Variant information Variant position: help 213 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 Alanine (A) to Aspartate (D) at position 213 (A213D, p.Ala213Asp). 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 small size and hydrophobic (A) to medium size and acidic (D) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -2 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 CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit; reduces protein degradation. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 213 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 381 The length of the canonical sequence.
Location on the sequence: help SVGEGGSFGELALIYGTPRA A TVKAKTNVKLWGIDRDSYRR 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                         SVGEGGSFGELALIYGTPRAATVKAKTNVKLWGIDRDSYRR

Mouse                         SVGEGGSFGELALIYGTPRAATVKAKTNVKLWGIDRDSYRR

Rat                           SVGEGGSFGELALIYGTPRAATVKAKTNVKLWGIDRDSYRR

Pig                           SVGEGGSFGELALIYGTPRAATVKAKTNVKLWGNDRDSYRR

Bovine                        SVGEGGSFGELALIYGTPRAATVKAKTNVKLWGIDRDSYRR

Chicken                       SVGEGGSFGELALIYGTPRAATVKAKTNVKLWGIDRDSYRR

Zebrafish                     SIGEGGSFGELALIYGTPRAATVRAKTNVKLWGIDRDSYRR
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 – 381 cAMP-dependent protein kinase type I-alpha regulatory subunit
Binding site 137 – 254
Binding site 202 – 202
Binding site 211 – 211



Literature citations
In vitro functional studies of naturally occurring pathogenic PRKAR1A mutations that are not subject to nonsense mRNA decay.
Greene E.L.; Horvath A.D.; Nesterova M.; Giatzakis C.; Bossis I.; Stratakis C.A.;
Hum. Mutat. 29:633-639(2008)
Cited for: VARIANTS CNC1 ASN-9; SER-146; TYR-183; ASP-213 AND TRP-289; CHARACTERIZATION OF VARIANTS CNC1 ASN-9; CYS-74; SER-146; TYR-183; ASP-213 AND TRP-289; Functional characterization of PRKAR1A mutations reveals a unique molecular mechanism causing acrodysostosis but multiple mechanisms causing carney complex.
Rhayem Y.; Le Stunff C.; Abdel Khalek W.; Auzan C.; Bertherat J.; Linglart A.; Couvineau A.; Silve C.; Clauser E.;
J. Biol. Chem. 290:27816-27828(2015)
Cited for: VARIANT ACRDYS1 CYS-175; CHARACTERIZATION OF VARIANTS ACRDYS1 CYS-175; THR-213; ARG-285; GLU-289; VAL-328 AND LEU-335; CHARACTERIZATION OF VARIANTS CNC1 ASP-213 AND TRP-289; FUNCTION;
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.