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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P10644: Variant p.Ala328Val

cAMP-dependent protein kinase type I-alpha regulatory subunit
Gene: PRKAR1A
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Variant information Variant position: help 328 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 Valine (V) at position 328 (A328V, p.Ala328Val). 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 hydrophobic (V) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 0 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 ACRDYS1; disrupts cAMP binding. Any additional useful information about the variant.


Sequence information Variant position: help 328 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 ENEEFVEVGRLGPSDYFGEI A LLMNRPRAATVVARGPLKCV 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                         ENEEFVEVGRLGPSDYFGEIALLMNRPRAATVVARGPLKCV

Mouse                         ENEEFVEVGRLGPSDYFGEIALLMNRPRAATVVARGPLKCV

Rat                           ENEEFVEVGRLGPSDYFGEIALLMNRPRAATVVARGPLKCV

Pig                           ENEEFVEVGRLGPSDYFGEIALLMNRPRAATVVARGPLKCV

Bovine                        ENEEFVEVGRLGPSDYFGEIALLMNRPRAATVVARGPLKCV

Chicken                       ENEEFVEVGRLAPSDYFGEIALLMNRPRAATVVARGLLKCV

Zebrafish                     ENEEFVEVGRLAPSDYFGEIALLMNRPRAATVVARGPLKCV
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 255 – 381
Binding site 326 – 326
Binding site 335 – 335
Alternative sequence 326 – 337 EIALLMNRPRAA -> HLIISRRSIPLG. In isoform 2.
Helix 326 – 330



Literature citations
PRKAR1A and PDE4D mutations cause acrodysostosis but two distinct syndromes with or without GPCR-signaling hormone resistance.
Linglart A.; Fryssira H.; Hiort O.; Holterhus P.M.; Perez de Nanclares G.; Argente J.; Heinrichs C.; Kuechler A.; Mantovani G.; Leheup B.; Wicart P.; Chassot V.; Schmidt D.; Rubio-Cabezas O.; Richter-Unruh A.; Berrade S.; Pereda A.; Boros E.; Munoz-Calvo M.T.; Castori M.; Gunes Y.; Bertrand G.; Bougneres P.; Clauser E.; Silve C.;
J. Clin. Endocrinol. Metab. 97:E2328-E2338(2012)
Cited for: VARIANTS ACRDYS1 ARG-285; GLU-289; VAL-328 AND LEU-335; 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.