PRKAR1A
entrez
5573
canonical
uniprot
P10644
canonical
ensembl
ENSG00000108946
resolver
ensp
ENSP00000351410
resolver
ensp
ENSP00000376475
resolver
ensp
ENSP00000445625
resolver
ensp
ENSP00000464977
resolver
ensp
ENSP00000465013
resolver
ensp
ENSP00000465445
resolver
ensp
ENSP00000466649
resolver
ensp
ENSP00000653516
resolver
ensp
ENSP00000653520
resolver
ensp
ENSP00000745037
resolver
genesymbol
PRKAR1A
resolver
genesymbol_syn
PKR1
resolver
genesymbol_syn
PRKAR1
resolver
genesymbol_syn
TSE1
resolver
hgnc
HGNC:9388
resolver
uniprot
B2R5T5
resolver
uniprot
K7ER48
resolver
uniprot
Q567S7
resolver
uniprot_entry
B2R5T5_HUMAN
resolver
uniprot_entry
KAP0_HUMAN
resolver
uniprot_sec
K7ER48
resolver
uniprot_sec
Q567S7
resolver
amino_acid_sequence
MESGSTAASEEARSLRECELYVQKHNIQALLKDSIVQLCTARPERPMAFLREYFERLEKEEAKQIQNLQKAGTRTDSREDEISPPPPNPVVKGRRRRGAISAEVYTEEDAASYVRKVIPKDYKTMAALAKAIEKNVLFSHLDDNERSDIFDAMFSVSFIAGETVIQQGDEGDNFYVIDQGETDVYVNNEWATSVGEGGSFGELALIYGTPRAATVKAKTNVKLWGIDRDSYRRILMGSTLRKRKMYEEFLSKVSILESLDKWERLTVADALEPVQFEDGQKIVVQGEPGDEFFIILEGSAAVLQRRSENEEFVEVGRLGPSDYFGEIALLMNRPRAATVVARGPLKCVKLDRPRFERVLGPCSDILKRNIQQYNSFVSLSV
uniprot
proteins
disease_involvement
DISEASE: Carney complex 1 (CNC1) [MIM:160980]: CNC is a multiple neoplasia syndrome characterized by spotty skin pigmentation, cardiac and other myxomas, endocrine tumors, and psammomatous melanotic schwannomas. {ECO:0000269|PubMed:15371594, ECO:0000269|PubMed:18241045, ECO:0000269|PubMed:22785148, ECO:0000269|PubMed:23323113, ECO:0000269|PubMed:26405036}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Intracardiac myxoma (INTMYX) [MIM:255960]: Inheritance is autosomal recessive. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Primary pigmented nodular adrenocortical disease 1 (PPNAD1) [MIM:610489]: A rare bilateral adrenal defect causing ACTH-independent Cushing syndrome. Macroscopic appearance of the adrenals is characteristic with small pigmented micronodules observed in the cortex. Clinical manifestations of Cushing syndrome include facial and truncal obesity, abdominal striae, muscular weakness, osteoporosis, arterial hypertension, diabetes. PPNAD1 is most often diagnosed in patients with Carney complex, a multiple neoplasia syndrome. However it can also be observed in patients without other manifestations. {ECO:0000269|PubMed:12213893}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Acrodysostosis 1, with or without hormone resistance (ACRDYS1) [MIM:101800]: A form of skeletal dysplasia characterized by short stature, severe brachydactyly, facial dysostosis, and nasal hypoplasia. Affected individuals often have advanced bone age and obesity. Laboratory studies show resistance to multiple hormones, including parathyroid, thyrotropin, calcitonin, growth hormone-releasing hormone, and gonadotropin. However, not all patients show endocrine abnormalities. {ECO:0000269|PubMed:21651393, ECO:0000269|PubMed:22464250, ECO:0000269|PubMed:22464252, ECO:0000269|PubMed:22723333, ECO:0000269|PubMed:23043190, ECO:0000269|PubMed:23425300, ECO:0000269|PubMed:26405036}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. {ECO:0000269|PubMed:16491121, ECO:0000269|PubMed:20215566, ECO:0000269|PubMed:26405036, ECO:0000269|PubMed:35977512}.
uniprot
proteins
mass_dalton
42982
uniprot
proteins
mutagenesis
MUTAGEN 77; /note="S->E: Stronger inhibition of cellular metabolic activity in response to forskolin and in normal growth conditions; when associated with E-83."; /evidence="ECO:0000269|PubMed:35977512"; MUTAGEN 83; /note="S->E: Stronger inhibition of cellular metabolic activity in response to forskolin and in normal growth conditions; when associated with E-77."; /evidence="ECO:0000269|PubMed:35977512"; MUTAGEN 192; /note="T->R: Reduced affinity for cAMP and moderately increased affinity for cGMP."; /evidence="ECO:0000269|PubMed:28583991"; MUTAGEN 212; /note="A->T: Reduced affinity for cAMP and approximately 50-fold increased affinity for cGMP."; /evidence="ECO:0000269|PubMed:28583991"; MUTAGEN 315; /note="V->L: Negligible effect on affinity for cAMP and moderately increased affinity for cGMP."; /evidence="ECO:0000269|PubMed:28583991"; MUTAGEN 316; /note="G->R: Reduced affinity for cAMP and approximately 4-fold increased affinity for cGMP."; /evidence="ECO:0000269|PubMed:28583991"; MUTAGEN 336; /note="A->T: Negligible effect on affinity for cAMP and approximately 200-fold increased affinity for cGMP."; /evidence="ECO:0000269|PubMed:28583991"; MUTAGEN 373; /note="Y->A: Impairs response of PKA to c-AMP."; /evidence="ECO:0000269|PubMed:21651393
uniprot
proteins
post_translational_modification
PTM: The pseudophosphorylation site binds to the substrate-binding region of the catalytic chain, resulting in the inhibition of its activity.
uniprot
proteins
protein_family
CAMP-dependent kinase regulatory chain family
uniprot
proteins
pubmed
12213893
uniprot
proteins
pubmed
12665801
uniprot
proteins
pubmed
14654843
uniprot
proteins
pubmed
15371594
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15655353
uniprot
proteins
pubmed
16387847
uniprot
proteins
pubmed
16491121
uniprot
proteins
pubmed
16625196
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
18088087
uniprot
proteins
pubmed
18241045
uniprot
proteins
pubmed
18318008
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
1889088
uniprot
proteins
pubmed
19367720
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20018846
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20215566
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21423175
uniprot
proteins
pubmed
21651393
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
22464250
uniprot
proteins
pubmed
22464252
uniprot
proteins
pubmed
22723333
uniprot
proteins
pubmed
22785148
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23043190
uniprot
proteins
pubmed
2310396
uniprot
proteins
pubmed
23115245
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23323113
uniprot
proteins
pubmed
23425300
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
26405036
uniprot
proteins
pubmed
27028580
uniprot
proteins
pubmed
28583991
uniprot
proteins
pubmed
33058759
uniprot
proteins
pubmed
3426618
uniprot
proteins
pubmed
35977512
uniprot
proteins
pubmed
38326651
uniprot
proteins
pubmed
8977401
uniprot
proteins
sequence_length
381
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23115245, ECO:0000269|PubMed:27028580}.
uniprot
proteins