PRKAR1A

Functionⁱ

Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells.

3 Publications

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	202	3',5'-cAMP 1	1
Binding siteⁱ	211	3',5'-cAMP 1	1
Binding siteⁱ	326	3',5'-cAMP 2	1
Binding siteⁱ	335	3',5'-cAMP 2	1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Nucleotide bindingⁱ	137 – 254	3',5'-cAMP 1Add BLAST		118
Nucleotide bindingⁱ	255 – 381	3',5'-cAMP 2Add BLAST		127

GO - Molecular functionⁱ

cAMP binding Source: UniProtKB-KW
cAMP-dependent protein kinase inhibitor activity
Source: BHF-UCL
Inferred from direct assayⁱ
- "The testis-specific C?2 subunit of PKA is kinetically indistinguishable from the common C?1 subunit of PKA."
  Vetter M.M., Zenn H.-M., Mendez E., van den Boom H., Herberg F.W., Skaalhegg B.S.
  BMC Biochem. 12:40-40(2011) [PubMed] [Europe PMC] [Abstract]
cAMP-dependent protein kinase regulator activity
Source: BHF-UCL
Inferred from direct assayⁱ
- "The testis-specific C?2 subunit of PKA is kinetically indistinguishable from the common C?1 subunit of PKA."
  Vetter M.M., Zenn H.-M., Mendez E., van den Boom H., Herberg F.W., Skaalhegg B.S.
  BMC Biochem. 12:40-40(2011) [PubMed] [Europe PMC] [Abstract]
protein domain specific binding
Source: UniProtKB
Inferred from physical interactionⁱ
- "A systematic evaluation of protein kinase A-A-Kinase anchoring protein interaction motifs."
  Burgers P.P., van der Heyden M.A., Kok B., Heck A.J., Scholten A.
  Biochemistry 54:11-21(2015) [PubMed] [Europe PMC] [Abstract]
protein kinase A catalytic subunit binding
Source: UniProtKB
Inferred from physical interactionⁱ
- "Inhibition of T cell activation by cyclic adenosine 5'-monophosphate requires lipid raft targeting of protein kinase A type I by the A-kinase anchoring protein ezrin."
  Ruppelt A., Mosenden R., Gronholm M., Aandahl E.M., Tobin D., Carlson C.R., Abrahamsen H., Herberg F.W., Carpen O., Tasken K.
  J Immunol 179:5159-5168(2007) [PubMed] [Europe PMC] [Abstract]
ubiquitin protein ligase binding
Source: UniProtKB
Inferred from direct assayⁱ
- Ref.26
  "Control of PKA stability and signalling by the RING ligase praja2."
  Lignitto L., Carlucci A., Sepe M., Stefan E., Cuomo O., Nistico R., Scorziello A., Savoia C., Garbi C., Annunziato L., Feliciello A.
  Nat. Cell Biol. 13:412-422(2011) [PubMed] [Europe PMC] [Abstract]
  Cited for: INTERACTION WITH PJA2.

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Ligand	cAMP, cAMP-binding, Nucleotide-binding

Ligand

cAMP, cAMP-binding, Nucleotide-binding

Enzyme and pathway databases

PathwayCommonsⁱ	P10644
Reactomeⁱ	R-HSA-163615, PKA activation R-HSA-164378, PKA activation in glucagon signalling R-HSA-180024, DARPP-32 events R-HSA-381676, Glucagon-like Peptide-1 (GLP1) regulates insulin secretion R-HSA-432040, Vasopressin regulates renal water homeostasis via Aquaporins R-HSA-442720, CREB1 phosphorylation through the activation of Adenylate Cyclase R-HSA-5610787, Hedgehog 'off' state R-HSA-9660821, ADORA2B mediated anti-inflammatory cytokines production R-HSA-9664323, FCGR3A-mediated IL10 synthesis R-HSA-983231, Factors involved in megakaryocyte development and platelet production
SignaLinkⁱ	P10644
SIGNORⁱ	P10644

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: cAMP-dependent protein kinase type I-alpha regulatory subunit Alternative name(s): Tissue-specific extinguisher 1 Short name: TSE1
Gene namesⁱ	Name:PRKAR1A Synonyms:PKR1, PRKAR1, TSE1
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 17

Organism-specific databases

Human Gene Nomenclature Database More...HGNCⁱ	HGNC:9388, PRKAR1A
MIMⁱ	188830, gene
neXtProtⁱ	NX_P10644
VEuPathDBⁱ	HostDB:ENSG00000108946.14

Keywords - Cellular componentⁱ

Cell membrane, Membrane

Pathology & Biotechⁱ

Involvement in diseaseⁱ

Carney complex 1 (CNC1)5 Publications

The disease is caused by variants affecting the gene represented in this entry.

Disease descriptionCNC is a multiple neoplasia syndrome characterized by spotty skin pigmentation, cardiac and other myxomas, endocrine tumors, and psammomatous melanotic schwannomas.

Related information in OMIM

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_046894	9	S → N in CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit. 1 Publication	1
Natural variantⁱVAR_046895	74	R → C in CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit. 2 PublicationsCorresponds to variant dbSNP:rs137853303EnsemblClinVar.	1
Natural variantⁱVAR_046896	146	R → S in CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit. 1 Publication	1
Natural variantⁱVAR_046897	183	D → Y in CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit. 1 Publication	1
Natural variantⁱVAR_046898	213	A → D in CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit; reduces protein degradation. 2 PublicationsCorresponds to variant dbSNP:rs281864786EnsemblClinVar.	1
Natural variantⁱVAR_046899	289	G → W in CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit; accelerates protein degradation. 2 Publications	1

Intracardiac myxoma (INTMYX)

The disease is caused by variants affecting the gene represented in this entry.

Disease descriptionInheritance is autosomal recessive.

Related information in OMIM

Primary pigmented nodular adrenocortical disease 1 (PPNAD1)1 Publication

The disease is caused by variants affecting the gene represented in this entry.

Disease descriptionA 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.

Related information in OMIM

Acrodysostosis 1, with or without hormone resistance (ACRDYS1)7 Publications

The disease is caused by variants affecting the gene represented in this entry.

Disease descriptionA 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.

Related information in OMIM

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_075533	175	Y → C in ACRDYS1; reduces PKA activity; decreases cAMP binding. 1 Publication	1
Natural variantⁱVAR_069456	213	A → T in ACRDYS1; reduces PKA activity; decreases cAMP binding; reduces protein degradation. 2 Publications	1
Natural variantⁱVAR_069458	239	T → A in ACRDYS1; impairs response of PKA to c-AMP. 1 Publication	1
Natural variantⁱVAR_069459	285	Q → R in ACRDYS1; reduces PKA activity; decreases cAMP binding. 2 PublicationsCorresponds to variant dbSNP:rs1555814719EnsemblClinVar.	1
Natural variantⁱVAR_069460	289	G → E in ACRDYS1; reduces PKA activity; decreases cAMP binding; reduces protein degradation. 2 Publications	1
Natural variantⁱVAR_069461	327	I → T in ACRDYS1. 1 PublicationCorresponds to variant dbSNP:rs387906695EnsemblClinVar.	1
Natural variantⁱVAR_069462	328	A → V in ACRDYS1; disrupts cAMP binding. 2 Publications	1
Natural variantⁱVAR_069464	335	R → L in ACRDYS1; disrupts cAMP binding. 2 Publications	1
Natural variantⁱVAR_069463	335	R → P in ACRDYS1. 1 PublicationCorresponds to variant dbSNP:rs387906694EnsemblClinVar.	1
Natural variantⁱVAR_069465	373	Y → C in ACRDYS1. 1 Publication	1
Natural variantⁱVAR_068241	373	Y → H in ACRDYS1. 1 PublicationCorresponds to variant dbSNP:rs387906693EnsemblClinVar.	1

Mutagenesis

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Mutagenesisⁱ	373	Y → A: Impairs response of PKA to c-AMP. 1 Publication		1

Keywords - Diseaseⁱ

Cushing syndrome, Disease variant

Organism-specific databases

DisGeNET More...DisGeNETⁱ	5573
GeneReviewsⁱ	PRKAR1A
MalaCards human disease database More...MalaCardsⁱ	PRKAR1A
MIMⁱ	101800, phenotype 160980, phenotype 255960, phenotype 610489, phenotype
Open Targets More...OpenTargetsⁱ	ENSG00000108946
Orphanetⁱ	950, Acrodysostosis 280651, Acrodysostosis with multiple hormone resistance 520, Acute promyelocytic leukemia 1359, Carney complex 615, Familial atrial myxoma 189439, Primary pigmented nodular adrenocortical disease
PharmGKBⁱ	PA33754

Miscellaneous databases

Pharosⁱ	P10644, Tbio

Pharosⁱ

P10644, Tbio

Chemistry databases

ChEMBLⁱ	CHEMBL4928
Drug and drug target database More...DrugBankⁱ	DB01790, (Rp)-cAMPS DB02527, Cyclic adenosine monophosphate DB02315, Cyclic GMP DB05798, GEM-231
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYⁱ	1472

Genetic variation databases

BioMutaⁱ	PRKAR1A
DMDMⁱ	125193

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000205377	1 – 381	cAMP-dependent protein kinase type I-alpha regulatory subunitAdd BLAST		381

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	1	N-acetylmethionineCombined sources1 Publication	1
Modified residueⁱ	3	PhosphoserineBy similarity	1
Disulfide bondⁱ	18	Interchain (with C-39)By similarity
Disulfide bondⁱ	39	Interchain (with C-18)By similarity
Modified residueⁱ	75	PhosphothreonineCombined sources	1
Modified residueⁱ	77	PhosphoserineCombined sources	1
Modified residueⁱ	83	PhosphoserineCombined sources	1
Modified residueⁱ	101	PhosphoserineBy similarity	1
Modified residueⁱ	258	PhosphoserineBy similarity	1

Post-translational modificationⁱ

The pseudophosphorylation site binds to the substrate-binding region of the catalytic chain, resulting in the inhibition of its activity.

Keywords - PTMⁱ

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

EPDⁱ	P10644
jPOSTⁱ	P10644
MassIVEⁱ	P10644
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P10644
PaxDbⁱ	P10644
PeptideAtlas More...PeptideAtlasⁱ	P10644
PRIDEⁱ	P10644
ProteomicsDBⁱ	52634 [P10644-1]

2D gel databases

USC-OGP 2-DE database More...OGPⁱ	P10644
REPRODUCTION-2DPAGE More...REPRODUCTION-2DPAGEⁱ	IPI00021831

PTM databases

iPTMnetⁱ	P10644
MetOSiteⁱ	P10644
PhosphoSitePlusⁱ	P10644
SwissPalmⁱ	P10644

Expressionⁱ

Tissue specificityⁱ

Four types of regulatory chains are found: I-alpha, I-beta, II-alpha, and II-beta. Their expression varies among tissues and is in some cases constitutive and in others inducible.

Gene expression databases

Bgeeⁱ	ENSG00000108946, Expressed in substantia nigra and 251 other tissues
ExpressionAtlasⁱ	P10644, baseline and differential
Genevisibleⁱ	P10644, HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	ENSG00000108946, Low tissue specificity

HPAⁱ

ENSG00000108946, Low tissue specificity

Interactionⁱ

Subunit structureⁱ

The inactive holoenzyme is composed of two regulatory chains and two catalytic chains. Activation by cAMP releases the two active catalytic monomers and the regulatory dimer. PRKAR1A also interacts with RFC2; the complex may be involved in cell survival.

Interacts with AKAP4.

Interacts with RARA; the interaction occurs in the presence of cAMP or FSH and regulates RARA transcriptional activity.

Interacts with the phosphorylated form of PJA2.

Interacts with CBFA2T3 (By similarity).

Interacts with PRKX; regulates this cAMP-dependent protein kinase.

Interacts with C2orf88/smAKAP; this interaction may target PRKAR1A to the plasma membrane.

Interacts with AICDA.

By similarity6 Publications

Binary interactionsⁱ

Hide details

P10644

With	#Exp.	IntAct
AICDA [Q9GZX7]	5	EBI-476431,EBI-3834328
AKAP5 [P24588]	3	EBI-476431,EBI-703640
AKAP7 - isoform Alpha [O43687-2]	3	EBI-476431,EBI-10185182
C11orf49 - isoform 2 [Q9H6J7-2]	3	EBI-476431,EBI-13328871
C2orf88 [Q9BSF0]	9	EBI-476431,EBI-744298
DTX1 [Q86Y01]	3	EBI-476431,EBI-1755174
FAM153B - isoform 2 [P0C7A2-2]	3	EBI-476431,EBI-12940382
GABARAPL1 [Q9H0R8]	2	EBI-476431,EBI-746969
PLEKHF2 [Q9H8W4]	3	EBI-476431,EBI-742388
PRKACA [P17612]	12	EBI-476431,EBI-476586
PRKAR1B [P31321]	6	EBI-476431,EBI-2805516
PRKX [P51817]	2	EBI-476431,EBI-4302903
RFC2 [P35250]	7	EBI-476431,EBI-476409
RSPH3 [Q86UC2]	3	EBI-476431,EBI-6873025
SET [Q01105]	2	EBI-476431,EBI-1053182
SPART [Q8N0X7]	3	EBI-476431,EBI-2643803
Isoform Early E1A 26 kDa protein [P03259-2] from Human adenovirus A serotype 12.	5	EBI-476431,EBI-7225021

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGRIDⁱ	111559, 199 interactors
Database of interacting proteins More...DIPⁱ	DIP-34368N
IntActⁱ	P10644, 186 interactors
Molecular INTeraction database More...MINTⁱ	P10644
STRINGⁱ	9606.ENSP00000376475

Chemistry databases

BindingDBⁱ

P10644

Miscellaneous databases

RNActⁱ	P10644, protein

RNActⁱ

P10644, protein

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	237 – 250	Combined sources	14
Helixⁱ	254 – 256	Combined sources	3
Helixⁱ	261 – 270	Combined sources	10
Beta strandⁱ	272 – 276	Combined sources	5
Beta strandⁱ	281 – 283	Combined sources	3
Beta strandⁱ	291 – 304	Combined sources	14
Beta strandⁱ	313 – 318	Combined sources	6
Helixⁱ	326 – 330	Combined sources	5
Beta strandⁱ	336 – 351	Combined sources	16
Helixⁱ	352 – 358	Combined sources	7
Helixⁱ	360 – 362	Combined sources	3
Helixⁱ	363 – 370	Combined sources	8
Turnⁱ	371 – 376	Combined sources	6

Show more details

3D structure databases

SMRⁱ	P10644
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	1 – 136	Dimerization and phosphorylationAdd BLAST		136
Regionⁱ	64 – 96	DisorderedSequence analysisAdd BLAST		33

Motif

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Motifⁱ	96 – 100	Pseudophosphorylation motif		5

Sequence similaritiesⁱ

Belongs to the cAMP-dependent kinase regulatory chain family.Curated

Keywords - Domainⁱ

Repeat

Phylogenomic databases

eggNOGⁱ	KOG1113, Eukaryota
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00940000155148
HOGENOMⁱ	CLU_018310_1_0_1
InParanoidⁱ	P10644
OMAⁱ	RPMGFLR
PhylomeDBⁱ	P10644
TreeFamⁱ	TF314920

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd00038, CAP_ED, 2 hits
Gene3Dⁱ	2.60.120.10, 2 hits
InterProⁱ	View protein in InterPro IPR012198, cAMP_dep_PK_reg_su IPR003117, cAMP_dep_PK_reg_su_I/II_a/b IPR018490, cNMP-bd-like IPR018488, cNMP-bd_CS IPR000595, cNMP-bd_dom IPR014710, RmlC-like_jellyroll
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00027, cNMP_binding, 2 hits PF02197, RIIa, 1 hit
PIRSFⁱ	PIRSF000548, PK_regulatory, 1 hit
SMARTⁱ	View protein in SMART SM00100, cNMP, 2 hits SM00394, RIIa, 1 hit
SUPFAMⁱ	SSF51206, SSF51206, 2 hits
PROSITEⁱ	View protein in PROSITE PS00888, CNMP_BINDING_1, 2 hits PS00889, CNMP_BINDING_2, 2 hits PS50042, CNMP_BINDING_3, 2 hits

Sequences (2+)ⁱ

Sequence statusⁱ: Complete.

This entry describes 2 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 2 described isoforms and 12 potential isoforms that are computationally mapped.Show all Align All

Isoform 1 (identifier: P10644-1) [UniParc]FASTA Add to basket

This isoform has been chosen as the canonicalⁱ sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MESGSTAASE EARSLRECEL YVQKHNIQAL LKDSIVQLCT ARPERPMAFL 
        60         70         80         90        100
REYFERLEKE EAKQIQNLQK AGTRTDSRED EISPPPPNPV VKGRRRRGAI 
       110        120        130        140        150
SAEVYTEEDA ASYVRKVIPK DYKTMAALAK AIEKNVLFSH LDDNERSDIF 
       160        170        180        190        200
DAMFSVSFIA GETVIQQGDE GDNFYVIDQG ETDVYVNNEW ATSVGEGGSF 
       210        220        230        240        250
GELALIYGTP RAATVKAKTN VKLWGIDRDS YRRILMGSTL RKRKMYEEFL 
       260        270        280        290        300
SKVSILESLD KWERLTVADA LEPVQFEDGQ KIVVQGEPGD EFFIILEGSA 
       310        320        330        340        350
AVLQRRSENE EFVEVGRLGP SDYFGEIALL MNRPRAATVV ARGPLKCVKL 
       360        370        380 
DRPRFERVLG PCSDILKRNI QQYNSFVSLS V

Length:381

Mass (Da):42,982

Last modified:July 1, 1989 - v1

Checksum:ⁱ2D04F08CE8857A6D

GO

Isoform 2 (identifier: P10644-2) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
326-337: EIALLMNRPRAA → HLIISRRSIPLG
338-381: Missing.

« Hide

        10         20         30         40         50
MESGSTAASE EARSLRECEL YVQKHNIQAL LKDSIVQLCT ARPERPMAFL 
        60         70         80         90        100
REYFERLEKE EAKQIQNLQK AGTRTDSRED EISPPPPNPV VKGRRRRGAI 
       110        120        130        140        150
SAEVYTEEDA ASYVRKVIPK DYKTMAALAK AIEKNVLFSH LDDNERSDIF 
       160        170        180        190        200
DAMFSVSFIA GETVIQQGDE GDNFYVIDQG ETDVYVNNEW ATSVGEGGSF 
       210        220        230        240        250
GELALIYGTP RAATVKAKTN VKLWGIDRDS YRRILMGSTL RKRKMYEEFL 
       260        270        280        290        300
SKVSILESLD KWERLTVADA LEPVQFEDGQ KIVVQGEPGD EFFIILEGSA 
       310        320        330 
AVLQRRSENE EFVEVGRLGP SDYFGHLIIS RRSIPLG

Show »

Length:337

Mass (Da):38,003

Checksum:ⁱ8C14AF540F3150CF

GO

Computationally mapped potential isoform sequencesⁱ

There are 12 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

	Entry	Entry name	Protein names	Gene names	Length	Annotation

	K7EJ40	K7EJ40_HUMAN	cAMP-dependent protein kinase type ... cAMP-dependent protein kinase type I-alpha regulatory subunit	PRKAR1A	182	Annotation score:
	K7EPB2	K7EPB2_HUMAN	cAMP-dependent protein kinase type ... cAMP-dependent protein kinase type I-alpha regulatory subunit	PRKAR1A	297	Annotation score:
	K7EK41	K7EK41_HUMAN	cAMP-dependent protein kinase type ... cAMP-dependent protein kinase type I-alpha regulatory subunit	PRKAR1A	204	Annotation score:
	K7EID3	K7EID3_HUMAN	cAMP-dependent protein kinase type ... cAMP-dependent protein kinase type I-alpha regulatory subunit	PRKAR1A	167	Annotation score:
	K7EIE5	K7EIE5_HUMAN	cAMP-dependent protein kinase type ... cAMP-dependent protein kinase type I-alpha regulatory subunit	PRKAR1A	157	Annotation score:
	K7EMU2	K7EMU2_HUMAN	cAMP-dependent protein kinase type ... cAMP-dependent protein kinase type I-alpha regulatory subunit	PRKAR1A	113	Annotation score:
	K7EMZ6	K7EMZ6_HUMAN	cAMP-dependent protein kinase type ... cAMP-dependent protein kinase type I-alpha regulatory subunit	PRKAR1A	131	Annotation score:
	K7EM13	K7EM13_HUMAN	cAMP-dependent protein kinase type ... cAMP-dependent protein kinase type I-alpha regulatory subunit	PRKAR1A	153	Annotation score:
	K7EQK3	K7EQK3_HUMAN	cAMP-dependent protein kinase type ... cAMP-dependent protein kinase type I-alpha regulatory subunit	PRKAR1A	65	Annotation score:
	K7EKR1	K7EKR1_HUMAN	cAMP-dependent protein kinase type ... cAMP-dependent protein kinase type I-alpha regulatory subunit	PRKAR1A	35	Annotation score:
There are more potential isoformsShow all

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_046894	9	S → N in CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit. 1 Publication	1
Natural variantⁱVAR_046895	74	R → C in CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit. 2 PublicationsCorresponds to variant dbSNP:rs137853303EnsemblClinVar.	1
Natural variantⁱVAR_046896	146	R → S in CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit. 1 Publication	1
Natural variantⁱVAR_075533	175	Y → C in ACRDYS1; reduces PKA activity; decreases cAMP binding. 1 Publication	1
Natural variantⁱVAR_046897	183	D → Y in CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit. 1 Publication	1
Natural variantⁱVAR_046898	213	A → D in CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit; reduces protein degradation. 2 PublicationsCorresponds to variant dbSNP:rs281864786EnsemblClinVar.	1
Natural variantⁱVAR_069456	213	A → T in ACRDYS1; reduces PKA activity; decreases cAMP binding; reduces protein degradation. 2 Publications	1
Natural variantⁱVAR_069457	227	D → N1 Publication	1
Natural variantⁱVAR_069458	239	T → A in ACRDYS1; impairs response of PKA to c-AMP. 1 Publication	1
Natural variantⁱVAR_069459	285	Q → R in ACRDYS1; reduces PKA activity; decreases cAMP binding. 2 PublicationsCorresponds to variant dbSNP:rs1555814719EnsemblClinVar.	1
Natural variantⁱVAR_069460	289	G → E in ACRDYS1; reduces PKA activity; decreases cAMP binding; reduces protein degradation. 2 Publications	1
Natural variantⁱVAR_046899	289	G → W in CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit; accelerates protein degradation. 2 Publications	1
Natural variantⁱVAR_069461	327	I → T in ACRDYS1. 1 PublicationCorresponds to variant dbSNP:rs387906695EnsemblClinVar.	1
Natural variantⁱVAR_069462	328	A → V in ACRDYS1; disrupts cAMP binding. 2 Publications	1
Natural variantⁱVAR_069464	335	R → L in ACRDYS1; disrupts cAMP binding. 2 Publications	1
Natural variantⁱVAR_069463	335	R → P in ACRDYS1. 1 PublicationCorresponds to variant dbSNP:rs387906694EnsemblClinVar.	1
Natural variantⁱVAR_069465	373	Y → C in ACRDYS1. 1 Publication	1
Natural variantⁱVAR_068241	373	Y → H in ACRDYS1. 1 PublicationCorresponds to variant dbSNP:rs387906693EnsemblClinVar.	1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_054833	326 – 337	EIALL…RPRAA → HLIISRRSIPLG in isoform 2. CuratedAdd BLAST		12
Alternative sequenceⁱVSP_054834	338 – 381	Missing in isoform 2. CuratedAdd BLAST		44

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M18468 mRNA Translation: AAB50922.1 M33336 mRNA Translation: AAB50921.1 S54705 mRNA No translation available. S54707 mRNA No translation available. S54709 mRNA No translation available. S54711 mRNA No translation available. Y07642 mRNA Translation: CAA68925.1 AC079210 Genomic DNA No translation available. BC036285 mRNA Translation: AAH36285.1 BC093042 mRNA Translation: AAH93042.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS11678.1 [P10644-1] CCDS62307.1 [P10644-2]
PIRⁱ	A34627, OKHU1R
NCBI Reference Sequences More...RefSeqⁱ	NP_001263218.1, NM_001276289.1 [P10644-1] NP_001263219.1, NM_001276290.1 [P10644-2] NP_001265362.1, NM_001278433.1 [P10644-1] NP_002725.1, NM_002734.4 [P10644-1] NP_997636.1, NM_212471.2 [P10644-1] NP_997637.1, NM_212472.2 [P10644-1] XP_011523285.1, XM_011524983.2 XP_011523286.1, XM_011524984.2 [P10644-1] XP_011523287.1, XM_011524985.2

Genome annotation databases

Ensemblⁱ	ENST00000358598; ENSP00000351410; ENSG00000108946 [P10644-1] ENST00000392711; ENSP00000376475; ENSG00000108946 [P10644-1] ENST00000536854; ENSP00000445625; ENSG00000108946 [P10644-1] ENST00000586397; ENSP00000466459; ENSG00000108946 [P10644-1] ENST00000588188; ENSP00000468106; ENSG00000108946 [P10644-2] ENST00000589228; ENSP00000464977; ENSG00000108946 [P10644-1]
GeneIDⁱ	5573
KEGGⁱ	hsa:5573
UCSC genome browser More...UCSCⁱ	uc002jhg.5, human [P10644-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P10644	cAMP-dependent protein kinase type I-alpha regulatory subunit		PONAB		381	UniRef100_P10644
Epididymis secretory sperm binding protein		HUMAN		381
PRKAR1A isoform 12		PANTR		381
Protein kinase cAMP-dependent type I regulatory subunit alpha		PANPA		381
Uncharacterized protein		NOMLE		381
+5
P10644-2	Protein kinase cAMP-dependent type I regulatory subunit alpha		PANTR		337	UniRef100_A0A2I3RGR9
Protein kinase cAMP-dependent type I regulatory subunit alpha		PANPA		337
PRKAR1A isoform 18		PANTR		337

Protein	Similar proteins		Species	Score	Length	Source
P10644	cAMP-dependent protein kinase type I-alpha regulatory subunit		PONAB		381	UniRef90_P10644
cAMP-dependent protein kinase type I-alpha regulatory subunit		PIG		380
cAMP-dependent protein kinase type I-alpha regulatory subunit	)	BOVIN		380
Epididymis secretory sperm binding protein		HUMAN		381
PRKAR1A isoform 12		PANTR		381
+91
P10644-2	Protein kinase cAMP-dependent type I regulatory subunit alpha		GORGO		337	UniRef90_A0A2I2Y425
Protein kinase cAMP-dependent type I regulatory subunit alpha		CALJA		337
Protein kinase cAMP-dependent type I regulatory subunit alpha		PANTR		337
Protein kinase cAMP-dependent type I regulatory subunit alpha		PANPA		337
PRKAR1A isoform 18		PONAB		337
+5

Protein	Similar proteins		Species	Score	Length	Source
P10644	cAMP-dependent protein kinase type I-alpha regulatory subunit		PONAB		381	UniRef50_P10644
cAMP-dependent protein kinase type I-alpha regulatory subunit		PIG		380
cAMP-dependent protein kinase type I-alpha regulatory subunit	)	BOVIN		380
cAMP-dependent protein kinase type I-alpha regulatory subunit		CHICK		382
Epididymis secretory sperm binding protein		HUMAN		381
+491
P10644-2	Protein kinase cAMP-dependent type I regulatory subunit beta		Agassiz's desert tortoise		302	UniRef50_A0A452GRS9
Uncharacterized protein		Ephemera danica		319
Uncharacterized protein		CIMLE		280
Uncharacterized protein		LOTGI		318
Protein kinase, cAMP-dependent, regulatory, type I, alpha (tissue specific extinguisher 1) a		MOLML		257
+60

Cross-referencesⁱ

Web resourcesⁱ

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M18468 mRNA Translation: AAB50922.1 M33336 mRNA Translation: AAB50921.1 S54705 mRNA No translation available. S54707 mRNA No translation available. S54709 mRNA No translation available. S54711 mRNA No translation available. Y07642 mRNA Translation: CAA68925.1 AC079210 Genomic DNA No translation available. BC036285 mRNA Translation: AAH36285.1 BC093042 mRNA Translation: AAH93042.1
CCDSⁱ	CCDS11678.1 [P10644-1] CCDS62307.1 [P10644-2]
PIRⁱ	A34627, OKHU1R
RefSeqⁱ	NP_001263218.1, NM_001276289.1 [P10644-1] NP_001263219.1, NM_001276290.1 [P10644-2] NP_001265362.1, NM_001278433.1 [P10644-1] NP_002725.1, NM_002734.4 [P10644-1] NP_997636.1, NM_212471.2 [P10644-1] NP_997637.1, NM_212472.2 [P10644-1] XP_011523285.1, XM_011524983.2 XP_011523286.1, XM_011524984.2 [P10644-1] XP_011523287.1, XM_011524985.2

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	5KJX	X-ray	1.90	A	234-381	[»]
	5KJY	X-ray	2.00	A	234-381	[»]
	5KJZ	X-ray	1.35	A	234-381	[»]
SMRⁱ	P10644
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Protein-protein interaction databases

BioGRIDⁱ	111559, 199 interactors
DIPⁱ	DIP-34368N
IntActⁱ	P10644, 186 interactors
MINTⁱ	P10644
STRINGⁱ	9606.ENSP00000376475

Chemistry databases

BindingDBⁱ	P10644
ChEMBLⁱ	CHEMBL4928
DrugBankⁱ	DB01790, (Rp)-cAMPS DB02527, Cyclic adenosine monophosphate DB02315, Cyclic GMP DB05798, GEM-231
GuidetoPHARMACOLOGYⁱ	1472

PTM databases

iPTMnetⁱ	P10644
MetOSiteⁱ	P10644
PhosphoSitePlusⁱ	P10644
SwissPalmⁱ	P10644

Genetic variation databases

BioMutaⁱ	PRKAR1A
DMDMⁱ	125193

2D gel databases

OGPⁱ	P10644
REPRODUCTION-2DPAGEⁱ	IPI00021831

Proteomic databases

EPDⁱ	P10644
jPOSTⁱ	P10644
MassIVEⁱ	P10644
MaxQBⁱ	P10644
PaxDbⁱ	P10644
PeptideAtlasⁱ	P10644
PRIDEⁱ	P10644
ProteomicsDBⁱ	52634 [P10644-1]

Protocols and materials databases

Antibodypediaⁱ	31783, 363 antibodies
The DNASU plasmid repository More...DNASUⁱ	5573

Genome annotation databases

Ensemblⁱ	ENST00000358598; ENSP00000351410; ENSG00000108946 [P10644-1] ENST00000392711; ENSP00000376475; ENSG00000108946 [P10644-1] ENST00000536854; ENSP00000445625; ENSG00000108946 [P10644-1] ENST00000586397; ENSP00000466459; ENSG00000108946 [P10644-1] ENST00000588188; ENSP00000468106; ENSG00000108946 [P10644-2] ENST00000589228; ENSP00000464977; ENSG00000108946 [P10644-1]
GeneIDⁱ	5573
KEGGⁱ	hsa:5573
UCSCⁱ	uc002jhg.5, human [P10644-1]

Organism-specific databases

CTDⁱ	5573
DisGeNETⁱ	5573
GeneCardsⁱ	PRKAR1A
GeneReviewsⁱ	PRKAR1A
HGNCⁱ	HGNC:9388, PRKAR1A
HPAⁱ	ENSG00000108946, Low tissue specificity
MalaCardsⁱ	PRKAR1A
MIMⁱ	101800, phenotype 160980, phenotype 188830, gene 255960, phenotype 610489, phenotype
neXtProtⁱ	NX_P10644
OpenTargetsⁱ	ENSG00000108946
Orphanetⁱ	950, Acrodysostosis 280651, Acrodysostosis with multiple hormone resistance 520, Acute promyelocytic leukemia 1359, Carney complex 615, Familial atrial myxoma 189439, Primary pigmented nodular adrenocortical disease
PharmGKBⁱ	PA33754
VEuPathDBⁱ	HostDB:ENSG00000108946.14
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG1113, Eukaryota
GeneTreeⁱ	ENSGT00940000155148
HOGENOMⁱ	CLU_018310_1_0_1
InParanoidⁱ	P10644
OMAⁱ	RPMGFLR
PhylomeDBⁱ	P10644
TreeFamⁱ	TF314920

Enzyme and pathway databases

PathwayCommonsⁱ	P10644
Reactomeⁱ	R-HSA-163615, PKA activation R-HSA-164378, PKA activation in glucagon signalling R-HSA-180024, DARPP-32 events R-HSA-381676, Glucagon-like Peptide-1 (GLP1) regulates insulin secretion R-HSA-432040, Vasopressin regulates renal water homeostasis via Aquaporins R-HSA-442720, CREB1 phosphorylation through the activation of Adenylate Cyclase R-HSA-5610787, Hedgehog 'off' state R-HSA-9660821, ADORA2B mediated anti-inflammatory cytokines production R-HSA-9664323, FCGR3A-mediated IL10 synthesis R-HSA-983231, Factors involved in megakaryocyte development and platelet production
SignaLinkⁱ	P10644
SIGNORⁱ	P10644

Miscellaneous databases

BioGRID-ORCSⁱ	5573, 91 hits in 999 CRISPR screens
ChiTaRSⁱ	PRKAR1A, human
GenomeRNAiⁱ	5573
Pharosⁱ	P10644, Tbio
Protein Ontology More...PROⁱ	PR:P10644
RNActⁱ	P10644, protein
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000108946, Expressed in substantia nigra and 251 other tissues
ExpressionAtlasⁱ	P10644, baseline and differential
Genevisibleⁱ	P10644, HS

Family and domain databases

CDDⁱ	cd00038, CAP_ED, 2 hits
Gene3Dⁱ	2.60.120.10, 2 hits
InterProⁱ	View protein in InterPro IPR012198, cAMP_dep_PK_reg_su IPR003117, cAMP_dep_PK_reg_su_I/II_a/b IPR018490, cNMP-bd-like IPR018488, cNMP-bd_CS IPR000595, cNMP-bd_dom IPR014710, RmlC-like_jellyroll
Pfamⁱ	View protein in Pfam PF00027, cNMP_binding, 2 hits PF02197, RIIa, 1 hit
PIRSFⁱ	PIRSF000548, PK_regulatory, 1 hit
SMARTⁱ	View protein in SMART SM00100, cNMP, 2 hits SM00394, RIIa, 1 hit
SUPFAMⁱ	SSF51206, SSF51206, 2 hits
PROSITEⁱ	View protein in PROSITE PS00888, CNMP_BINDING_1, 2 hits PS00889, CNMP_BINDING_2, 2 hits PS50042, CNMP_BINDING_3, 2 hits
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	KAP0_HUMAN
Accessionⁱ	P10644Primary (citable) accession number: P10644 Secondary accession number(s): K7ER48, Q567S7
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
	Last sequence update:	July 1, 1989
	Last modified:	June 2, 2021
	This is version 237 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Direct protein sequencing, Reference proteome

Documents

Human chromosome 17
Human chromosome 17: entries, gene names and cross-references to MIM
Human entries with genetic variants
List of human entries with genetic variants
Human variants curated from literature reports
Index of human variants curated from literature reports
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
SIMILARITY comments
Index of protein domains and families

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UniProtKB - P10644 (KAP0_HUMAN)

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cAMP-dependent protein kinase type I-alpha regulatory subunit

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Plasma membrane

Cytoskeleton

Cytosol

Endosome

Plasma Membrane

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Intracardiac myxoma (INTMYX)

Mutagenesis

Keywords - Diseasei

Organism-specific databases

Miscellaneous databases

Chemistry databases

Genetic variation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

2D gel databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

P10644

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

Miscellaneous databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Motif

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Sequence databases

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Protein-protein interaction databases

Chemistry databases

PTM databases

Genetic variation databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

Keywords - Diseaseⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ