Variant position: 328 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 381 The length of the canonical sequence.
Location on the sequence:
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: The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human ENEEFVEVGRLGPSDYFGEI ALLMNRPRAATVVARGPLKCV
Mouse ENEEFVEVGRLGPSDYFGEI ALLMNRPRAATVVARGPLKCV
Rat ENEEFVEVGRLGPSDYFGEI ALLMNRPRAATVVARGPLKCV
Pig ENEEFVEVGRLGPSDYFGEI ALLMNRPRAATVVARGPLKCV
Bovine ENEEFVEVGRLGPSDYFGEI ALLMNRPRAATVVARGPLKCV
Chicken ENEEFVEVGRLAPSDYFGEI ALLMNRPRAATVVARGLLKCV
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.
Type Positions Description
1 – 381 cAMP-dependent protein kinase type I-alpha regulatory subunit
255 – 381 cAMP 2
326 – 326 cAMP 2
335 – 335 cAMP 2
326 – 337 EIALLMNRPRAA -> HLIISRRSIPLG. In isoform 2.
326 – 330
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;
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.