P10644 (KAP0_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
cAMP-dependent protein kinase type I-alpha regulatory subunit

Alternative name(s):
Tissue-specific extinguisher 1
Short name=TSE1

Cleaved into the following chain:

1. cAMP-dependent protein kinase type I-alpha regulatory subunit, N-terminally processed

Gene names

Name:	PRKAR1A
Synonyms:	PKR1, PRKAR1, TSE1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	381 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. Ref.10 Ref.19
Subunit structure	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. Ref.8 Ref.10 Ref.11 Ref.19 Ref.22 Ref.24
Subcellular location	Cell membrane Ref.24.
Tissue specificity	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.
Post-translational modification	The pseudophosphorylation site binds to the substrate-binding region of the catalytic chain, resulting in the inhibition of its activity.
Involvement in 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.25 Ref.26 Intracardiac myxoma (INTMYX) [MIM:255960]: Inheritance is autosomal recessive. Note: The disease is caused by mutations affecting the gene represented in this entry. 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 trunkal 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.27
Sequence similarities	Belongs to the cAMP-dependent kinase regulatory chain family. Contains 2 cyclic nucleotide-binding domains.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Disease	Cushing syndrome Disease mutation
Domain	Repeat
Ligand	Nucleotide-binding cAMP cAMP-binding
PTM	Acetylation Disulfide bond Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	activation of phospholipase C activity Traceable author statement. Source: Reactome activation of protein kinase A activity Traceable author statement. Source: Reactome blood coagulation Traceable author statement. Source: Reactome cellular response to glucagon stimulus Traceable author statement. Source: Reactome energy reserve metabolic process Traceable author statement. Source: Reactome epidermal growth factor receptor signaling pathway Traceable author statement. Source: Reactome fibroblast growth factor receptor signaling pathway Traceable author statement. Source: Reactome intracellular signal transduction Traceable author statement Ref.3. Source: ProtInc nerve growth factor receptor signaling pathway Traceable author statement. Source: Reactome regulation of insulin secretion Traceable author statement. Source: Reactome regulation of transcription from RNA polymerase II promoter Traceable author statement PubMed 1832337. Source: ProtInc small molecule metabolic process Traceable author statement. Source: Reactome transmembrane transport Traceable author statement. Source: Reactome water transport Traceable author statement. Source: Reactome
Cellular_component	cAMP-dependent protein kinase complex Inferred from electronic annotation. Source: InterPro cytosol Traceable author statement. Source: Reactome plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell protein complex Inferred from direct assay. Source: LIFEdb
Molecular_function	cAMP binding Inferred from electronic annotation. Source: UniProtKB-KW cAMP-dependent protein kinase regulator activity Traceable author statement Ref.1. Source: ProtInc ubiquitin protein ligase binding Inferred from direct assay Ref.22. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GABARAPL1	Q9H0R8	2	EBI-476431,EBI-746969
PLEKHF2	Q9H8W4	3	EBI-476431,EBI-742388
PRKACA	P17612	2	EBI-476431,EBI-476586
PRKX	P51817	2	EBI-476431,EBI-4302903
RFC2	P35250	7	EBI-476431,EBI-476409
SET	Q01105	2	EBI-476431,EBI-1053182

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 381	381	cAMP-dependent protein kinase type I-alpha regulatory subunit		PRO_0000205377
	Initiator methionine	1	1	Removed; alternate By similarity
	Chain	2 – 381	380	cAMP-dependent protein kinase type I-alpha regulatory subunit, N-terminally processed		PRO_0000421785
Regions
	Nucleotide binding	137 – 254	118	cAMP 1
	Nucleotide binding	255 – 381	127	cAMP 2
	Region	1 – 136	136	Dimerization and phosphorylation
	Motif	96 – 100	5	Pseudophosphorylation motif
Sites
	Binding site	202	1	cAMP 1
	Binding site	211	1	cAMP 1
	Binding site	326	1	cAMP 2
	Binding site	335	1	cAMP 2
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine Ref.6
	Modified residue	77	1	Phosphoserine By similarity
	Modified residue	83	1	Phosphoserine Ref.9 Ref.12 Ref.14 Ref.16 Ref.17 Ref.18 Ref.20 Ref.23
	Modified residue	101	1	Phosphoserine By similarity
	Disulfide bond	18		Interchain (with C-39) By similarity
	Disulfide bond	39		Interchain (with C-18) By similarity
Natural variations
	Natural variant	9	1	S → N in CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit. Ref.26		VAR_046894
	Natural variant	74	1	R → C in CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit. Ref.25 Ref.26		VAR_046895
	Natural variant	146	1	R → S in CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit. Ref.26		VAR_046896
	Natural variant	183	1	D → Y in CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit. Ref.26		VAR_046897
	Natural variant	213	1	A → D in CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit. Ref.26		VAR_046898
	Natural variant	289	1	G → W in CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit. Ref.26		VAR_046899
	Natural variant	373	1	Y → H in ACRDYS1. Ref.27		VAR_068241

Sequences

	Sequence		Length	Mass (Da)
	P10644 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: 2D04F08CE8857A6D	FASTA	381	42,982
	10 20 30 40 50 60 MESGSTAASE EARSLRECEL YVQKHNIQAL LKDSIVQLCT ARPERPMAFL REYFERLEKE 70 80 90 100 110 120 EAKQIQNLQK AGTRTDSRED EISPPPPNPV VKGRRRRGAI SAEVYTEEDA ASYVRKVIPK 130 140 150 160 170 180 DYKTMAALAK AIEKNVLFSH LDDNERSDIF DAMFSVSFIA GETVIQQGDE GDNFYVIDQG 190 200 210 220 230 240 ETDVYVNNEW ATSVGEGGSF GELALIYGTP RAATVKAKTN VKLWGIDRDS YRRILMGSTL 250 260 270 280 290 300 RKRKMYEEFL SKVSILESLD KWERLTVADA LEPVQFEDGQ KIVVQGEPGD EFFIILEGSA 310 320 330 340 350 360 AVLQRRSENE EFVEVGRLGP SDYFGEIALL MNRPRAATVV ARGPLKCVKL DRPRFERVLG 370 380 PCSDILKRNI QQYNSFVSLS V

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning, cDNA structure and deduced amino acid sequence for a type I regulatory subunit of cAMP-dependent protein kinase from human testis." Sandberg M., Tasken K., Oeyen O., Hansson V., Jahnsen T. Biochem. Biophys. Res. Commun. 149:939-945(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Testis.
[2]	"The two mRNA forms for the type I alpha regulatory subunit of cAMP-dependent protein kinase from human testis are due to the use of different polyadenylation site signals." Sandberg M., Skalhegg B., Jahnsen T. Biochem. Biophys. Res. Commun. 167:323-330(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Testis.
[3]	"Subtractive hybridization cloning of a tissue-specific extinguisher: TSE1 encodes a regulatory subunit of protein kinase A." Jones K.W., Shapero M.H., Chevrette M., Fournier R.E. Cell 66:861-872(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"The human gene for the regulatory subunit RI alpha of cyclic adenosine 3', 5'-monophosphate-dependent protein kinase: two distinct promoters provide differential regulation of alternately spliced messenger ribonucleic acids." Solberg R., Sandberg M., Natarajan V., Torjesen P.A., Hansson V., Jahnsen T., Tasken K. Endocrinology 138:169-181(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Testis.
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lymph and Uterus.
[6]	"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-13, ACETYLATION AT MET-1. Tissue: Platelet.
[7]	"Mutations of the PRKAR1A gene in Cushing's syndrome due to sporadic primary pigmented nodular adrenocortical disease." Groussin L., Jullian E., Perlemoine K., Louvel A., Leheup B., Luton J.P., Bertagna X., Bertherat J. J. Clin. Endocrinol. Metab. 87:4324-4329(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN PPNAD1.
[8]	"The second subunit of the replication factor C complex (RFC40) and the regulatory subunit (RIalpha) of protein kinase A form a protein complex promoting cell survival." Gupte R.S., Weng Y., Liu L., Lee M.Y. Cell Cycle 4:323-329(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RFC2.
[9]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Smad6 is a protein kinase X phosphorylation substrate and is required for HL-60 cell differentiation." Glesne D., Huberman E. Oncogene 25:4086-4098(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH PRKX.
[11]	"PKA-mediated phosphorylation regulates the function of activation-induced deaminase (AID) in B cells." Pasqualucci L., Kitaura Y., Gu H., Dalla-Favera R. Proc. Natl. Acad. Sci. U.S.A. 103:395-400(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH AICDA.
[12]	"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment." Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J. J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, MASS SPECTROMETRY. Tissue: T-cell.
[13]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Platelet.
[14]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[16]	"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography." Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J. Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, MASS SPECTROMETRY. Tissue: Liver.
[17]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, MASS SPECTROMETRY.
[18]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[19]	"Activity of retinoic acid receptor-alpha is directly regulated at its protein kinase A sites in response to follicle-stimulating hormone signaling." Santos N.C., Kim K.H. Endocrinology 151:2361-2372(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RARA, FUNCTION.
[20]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]	"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.
[23]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, MASS SPECTROMETRY.
[24]	"A small novel A-kinase anchoring protein (AKAP) that localizes specifically protein kinase A-regulatory subunit I (PKA-RI) to the plasma membrane." Burgers P.P., Ma Y., Margarucci L., Mackey M., van der Heyden M.A., Ellisman M., Scholten A., Taylor S.S., Heck A.J. J. Biol. Chem. 287:43789-43797(2012) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH C2ORF88/SMAKAP, SUBCELLULAR LOCATION.
[25]	"Comparative PRKAR1A genotype-phenotype analyses in humans with Carney complex and prkar1a haploinsufficient mice." Veugelers M., Wilkes D., Burton K., McDermott D.A., Song Y., Goldstein M.M., La Perle K., Vaughan C.J., O'Hagan A., Bennett K.R., Meyer B.J., Legius E., Karttunen M., Norio R., Kaariainen H., Lavyne M., Neau J.-P., Richter G. , Kirali K., Farnsworth A., Stapleton K., Morelli P., Takanashi Y., Bamforth J.-S., Eitelberger F., Noszian I., Manfroi W., Powers J., Mochizuki Y., Imai T., Ko G.T.C., Driscoll D.A., Goldmuntz E., Edelberg J.M., Collins A., Eccles D., Irvine A.D., McKnight G.S., Basson C.T. Proc. Natl. Acad. Sci. U.S.A. 101:14222-14227(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CNC1 CYS-74.
[26]	"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) [PubMed] [Europe PMC] [Abstract] 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.
[27]	"Exome sequencing identifies PDE4D mutations as another cause of acrodysostosis." Michot C., Le Goff C., Goldenberg A., Abhyankar A., Klein C., Kinning E., Guerrot A.M., Flahaut P., Duncombe A., Baujat G., Lyonnet S., Thalassinos C., Nitschke P., Casanova J.L., Le Merrer M., Munnich A., Cormier-Daire V. Am. J. Hum. Genet. 90:740-745(2012) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ACRDYS1 HIS-373.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	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. BC036285 mRNA. Translation: AAH36285.1. BC093042 mRNA. Translation: AAH93042.1.
IPI	IPI00021831.
PIR	OKHU1R. A34627.
RefSeq	NP_001263218.1. NM_001276289.1. NP_002725.1. NM_002734.4. NP_997636.1. NM_212471.2. NP_997637.1. NM_212472.2.
UniGene	Hs.280342.
3D structure databases
ProteinModelPortal	P10644.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-34368N.
IntAct	P10644. 38 interactions.
MINT	MINT-1194164.
STRING	9606.ENSP00000351410.
PTM databases
PhosphoSite	P10644.
Polymorphism databases
DMDM	125193.
2D gel databases
OGP	P10644.
REPRODUCTION-2DPAGE	IPI00021831.
Proteomic databases
PaxDb	P10644.
PeptideAtlas	P10644.
PRIDE	P10644.
Protocols and materials databases
DNASU	5573.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000358598; ENSP00000351410; ENSG00000108946. ENST00000392711; ENSP00000376475; ENSG00000108946. ENST00000536854; ENSP00000445625; ENSG00000108946. ENST00000586397; ENSP00000466459; ENSG00000108946. ENST00000589228; ENSP00000464977; ENSG00000108946.
GeneID	5573.
KEGG	hsa:5573.
UCSC	uc002jhg.3. human.
Organism-specific databases
CTD	5573.
GeneCards	GC17P066508.
HGNC	HGNC:9388. PRKAR1A.
HPA	CAB019378.
MIM	101800. phenotype. 160980. phenotype. 188830. gene. 255960. phenotype. 610489. phenotype.
neXtProt	NX_P10644.
Orphanet	950. Acrodysostosis. 280651. Acrodysostosis with multiple hormone resistance. 1359. Carney complex. 615. Familial atrial myxoma. 189439. Primary pigmented nodular adrenocortical disease.
PharmGKB	PA33754.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0664.
HOGENOM	HOG000196669.
HOVERGEN	HBG002025.
InParanoid	P10644.
KO	K04739.
OMA	KNILFSH.
OrthoDB	EOG4JQ3XP.
PhylomeDB	P10644.
Enzyme and pathway databases
Reactome	REACT_111102. Signal Transduction. REACT_111217. Metabolism. REACT_116125. Disease. REACT_15518. Transmembrane transport of small molecules. REACT_604. Hemostasis. REACT_6900. Immune System.
Gene expression databases
ArrayExpress	P10644.
Bgee	P10644.
CleanEx	HS_PRKAR1A.
Genevestigator	P10644.
GermOnline	ENSG00000108946. Homo sapiens.
Family and domain databases
Gene3D	2.60.120.10. 2 hits.
InterPro	IPR002373. cAMP/cGMP_kin. 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. [Graphical view]
Pfam	PF00027. cNMP_binding. 2 hits. PF02197. RIIa. 1 hit. [Graphical view]
PIRSF	PIRSF000548. PK_regulatory. 1 hit.
PRINTS	PR00103. CAMPKINASE.
SMART	SM00100. cNMP. 2 hits. SM00394. RIIa. 1 hit. [Graphical view]
SUPFAM	SSF47391. cAMP-dep_prot_kin_reg_I/II_a/b. 1 hit. SSF51206. cNMP_binding. 2 hits.
PROSITE	PS00888. CNMP_BINDING_1. 2 hits. PS00889. CNMP_BINDING_2. 2 hits. PS50042. CNMP_BINDING_3. 2 hits. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P10644.
ChEMBL	CHEMBL4928.
ChiTaRS	PRKAR1A. human.
GenomeRNAi	5573.
NextBio	21602.
SOURCE	Search...

Entry information

Entry name

KAP0_HUMAN

Accession

Primary (citable) accession number: P10644
Secondary accession number(s): Q567S7

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	May 1, 2013
This is version 157 of the entry and version 1 of the sequence. [Complete history]

Entry status

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.