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P10644 (KAP0_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 171. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
cAMP-dependent protein kinase type I-alpha regulatory subunit
Alternative name(s):
Tissue-specific extinguisher 1
Short name=TSE1
Gene names
Name:PRKAR1A
Synonyms:PKR1, PRKAR1, TSE1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length381 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. Ref.11 Ref.21

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.9 Ref.11 Ref.12 Ref.21 Ref.25 Ref.28

Subcellular location

Cell membrane Ref.28.

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.27 Ref.29 Ref.32 Ref.33

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 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.8

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.24 Ref.34 Ref.35 Ref.36 Ref.37 Ref.38

Sequence similarities

Belongs to the cAMP-dependent kinase regulatory chain family.

Contains 2 cyclic nucleotide-binding domains.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
   DiseaseCushing syndrome
Disease mutation
   DomainRepeat
   LigandcAMP
cAMP-binding
Nucleotide-binding
   PTMAcetylation
Disulfide bond
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactivation 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

cardiac muscle cell proliferation

Inferred from electronic annotation. Source: Ensembl

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

female meiotic division

Inferred from electronic annotation. Source: Ensembl

fibroblast growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

innate immune response

Traceable author statement. Source: Reactome

intracellular signal transduction

Traceable author statement Ref.3. Source: ProtInc

mesoderm formation

Inferred from electronic annotation. Source: Ensembl

negative regulation of cAMP-dependent protein kinase activity

Inferred from direct assay PubMed 21812984. Source: BHF-UCL

negative regulation of meiosis

Inferred from electronic annotation. Source: Ensembl

neurotrophin TRK 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

sarcomere organization

Inferred from electronic annotation. Source: Ensembl

signal transduction

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

transmembrane transport

Traceable author statement. Source: Reactome

water transport

Traceable author statement. Source: Reactome

   Cellular_componentAMP-activated protein kinase complex

Inferred from direct assay PubMed 21812984. Source: BHF-UCL

cAMP-dependent protein kinase complex

Inferred from electronic annotation. Source: Ensembl

cytosol

Traceable author statement. Source: Reactome

neuromuscular junction

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

protein complex

Inferred from direct assay. Source: LIFEdb

   Molecular_functioncAMP binding

Inferred from electronic annotation. Source: UniProtKB-KW

cAMP-dependent protein kinase inhibitor activity

Inferred from direct assay PubMed 21812984. Source: BHF-UCL

cAMP-dependent protein kinase regulator activity

Inferred from direct assay PubMed 21812984. Source: BHF-UCL

protein binding

Inferred from physical interaction PubMed 11414803Ref.9PubMed 16189514Ref.11PubMed 19060904PubMed 20195357PubMed 20562859PubMed 23455922. Source: IntAct

protein kinase A catalytic subunit binding

Inferred from physical interaction PubMed 21812984. Source: BHF-UCL

ubiquitin protein ligase binding

Inferred from direct assay Ref.25. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P10644-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P10644-2)

The sequence of this isoform differs from the canonical sequence as follows:
     326-337: EIALLMNRPRAA → HLIISRRSIPLG
     338-381: Missing.
Note: No experimental confirmation available. Gene prediction based on EST data.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 381381cAMP-dependent protein kinase type I-alpha regulatory subunit
PRO_0000205377
Initiator methionine11Removed; alternate By similarity
Chain2 – 381380cAMP-dependent protein kinase type I-alpha regulatory subunit, N-terminally processed
PRO_0000421785

Regions

Nucleotide binding137 – 254118cAMP 1
Nucleotide binding255 – 381127cAMP 2
Region1 – 136136Dimerization and phosphorylation
Motif96 – 1005Pseudophosphorylation motif

Sites

Binding site2021cAMP 1
Binding site2111cAMP 1
Binding site3261cAMP 2
Binding site3351cAMP 2

Amino acid modifications

Modified residue11N-acetylmethionine Ref.7 Ref.18 Ref.30 Ref.31
Modified residue831Phosphoserine Ref.10 Ref.13 Ref.15 Ref.17 Ref.19 Ref.20 Ref.22 Ref.26
Modified residue1011Phosphoserine By similarity
Disulfide bond18Interchain (with C-39) By similarity
Disulfide bond39Interchain (with C-18) By similarity

Natural variations

Alternative sequence326 – 33712EIALL…RPRAA → HLIISRRSIPLG in isoform 2.
VSP_054833
Alternative sequence338 – 38144Missing in isoform 2.
VSP_054834
Natural variant91S → N in CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit. Ref.33
VAR_046894
Natural variant741R → C in CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit. Ref.32 Ref.33
VAR_046895
Natural variant1461R → S in CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit. Ref.33
VAR_046896
Natural variant1831D → Y in CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit. Ref.33
VAR_046897
Natural variant2131A → D in CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit. Ref.33
VAR_046898
Natural variant2131A → T in ACRDYS1. Ref.38
VAR_069456
Natural variant2271D → N. Ref.38
VAR_069457
Natural variant2391T → A in ACRDYS1; impairs response of PKA to c-AMP. Ref.37
VAR_069458
Natural variant2851Q → R in ACRDYS1. Ref.36
VAR_069459
Natural variant2891G → E in ACRDYS1. Ref.36
VAR_069460
Natural variant2891G → W in CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit. Ref.33
VAR_046899
Natural variant3271I → T in ACRDYS1. Ref.35
VAR_069461
Natural variant3281A → V in ACRDYS1. Ref.36
VAR_069462
Natural variant3351R → L in ACRDYS1. Ref.36
VAR_069464
Natural variant3351R → P in ACRDYS1. Ref.35
VAR_069463
Natural variant3731Y → C in ACRDYS1. Ref.38
VAR_069465
Natural variant3731Y → H in ACRDYS1. Ref.34
VAR_068241

Experimental info

Mutagenesis3731Y → A: Impairs response of PKA to c-AMP. Ref.24

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 2D04F08CE8857A6D

FASTA38142,982
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 8C14AF540F3150CF
Show »

FASTA33738,003

References

« Hide '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] (ISOFORM 1).
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] (ISOFORM 1).
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] (ISOFORM 1).
[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] (ISOFORM 1).
Tissue: Testis.
[5]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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] (ISOFORM 1).
Tissue: Lymph and Uterus.
[7]"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.
[8]"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.
[9]"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.
[10]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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.
[12]"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.
[13]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: T-cell.
[14]"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.
[15]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"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.
[17]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[18]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[21]"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.
[22]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[23]"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].
[24]"Recurrent PRKAR1A mutation in acrodysostosis with hormone resistance."
Linglart A., Menguy C., Couvineau A., Auzan C., Gunes Y., Cancel M., Motte E., Pinto G., Chanson P., Bougneres P., Clauser E., Silve C.
N. Engl. J. Med. 364:2218-2226(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN ACRDYS1, MUTAGENESIS OF TYR-373.
[25]"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.
[26]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"An unusual presentation of Carney complex with diffuse primary pigmented nodular adrenocortical disease on one adrenal gland and a nonpigmented adrenocortical adenoma and focal primary pigmented nodular adrenocortical disease on the other."
Tung S.C., Hwang D.Y., Yang J.W., Chen W.J., Lee C.T.
Endocr. J. 59:823-830(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN CNC1.
[28]"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.
[29]"Novel Mutation in PRKAR1A in Carney Complex."
Park K.U., Kim H.S., Lee S.K., Jung W.W., Park Y.K.
Korean J. Pathol. 46:595-600(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN CNC1.
[30]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[31]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[32]"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. expand/collapse author list , 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.
[33]"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.
[34]"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.
[35]"Exome sequencing identifies PDE4D mutations in acrodysostosis."
Lee H., Graham J.M. Jr., Rimoin D.L., Lachman R.S., Krejci P., Tompson S.W., Nelson S.F., Krakow D., Cohn D.H.
Am. J. Hum. Genet. 90:746-751(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ACRDYS1 THR-327 AND PRO-335.
[36]"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. expand/collapse author list , Munoz-Calvo M.T., Castori M., Gunes Y., Bertrand G., Bougneres P., Clauser E., Silve C.
J. Clin. Endocrinol. Metab. 97:E2328-E2338(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ACRDYS1 ARG-285; GLU-289; VAL-328 AND LEU-335.
[37]"PRKAR1A mutation affecting cAMP-mediated G protein-coupled receptor signaling in a patient with acrodysostosis and hormone resistance."
Nagasaki K., Iida T., Sato H., Ogawa Y., Kikuchi T., Saitoh A., Ogata T., Fukami M.
J. Clin. Endocrinol. Metab. 97:E1808-E1813(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ACRDYS1 ALA-239, CHARACTERIZATION OF VARIANT ACRDYS1 ALA-239.
[38]"Novel mutations of the PRKAR1A gene in patients with acrodysostosis."
Muhn F., Klopocki E., Graul-Neumann L., Uhrig S., Colley A., Castori M., Lankes E., Henn W., Gruber-Sedlmayr U., Seifert W., Horn D.
Clin. Genet. 84:531-538(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ACRDYS1 THR-213 AND CYS-373, VARIANT ASN-227.
+Additional computationally mapped references.

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.
AC079210 Genomic DNA. No translation available.
BC036285 mRNA. Translation: AAH36285.1.
BC093042 mRNA. Translation: AAH93042.1.
CCDSCCDS11678.1.
PIROKHU1R. A34627.
RefSeqNP_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]
UniGeneHs.280342.
Hs.745160.

3D structure databases

ProteinModelPortalP10644.
SMRP10644. Positions 14-380.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111559. 70 interactions.
DIPDIP-34368N.
IntActP10644. 55 interactions.
MINTMINT-1194164.
STRING9606.ENSP00000351410.

Chemistry

BindingDBP10644.

PTM databases

PhosphoSiteP10644.

Polymorphism databases

DMDM125193.

2D gel databases

OGPP10644.
REPRODUCTION-2DPAGEIPI00021831.

Proteomic databases

MaxQBP10644.
PaxDbP10644.
PeptideAtlasP10644.
PRIDEP10644.

Protocols and materials databases

DNASU5573.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000358598; ENSP00000351410; ENSG00000108946.
ENST00000392711; ENSP00000376475; ENSG00000108946.
ENST00000536854; ENSP00000445625; ENSG00000108946.
ENST00000586397; ENSP00000466459; ENSG00000108946.
ENST00000588188; ENSP00000468106; ENSG00000108946.
ENST00000589228; ENSP00000464977; ENSG00000108946.
GeneID5573.
KEGGhsa:5573.
UCSCuc002jhg.4. human. [P10644-1]

Organism-specific databases

CTD5573.
GeneCardsGC17P066508.
GeneReviewsPRKAR1A.
HGNCHGNC:9388. PRKAR1A.
HPACAB019378.
HPA049847.
HPA049979.
MIM101800. phenotype.
160980. phenotype.
188830. gene.
255960. phenotype.
610489. phenotype.
neXtProtNX_P10644.
Orphanet950. Acrodysostosis.
280651. Acrodysostosis with multiple hormone resistance.
1359. Carney complex.
615. Familial atrial myxoma.
189439. Primary pigmented nodular adrenocortical disease.
PharmGKBPA33754.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0664.
HOGENOMHOG000196669.
HOVERGENHBG002025.
InParanoidP10644.
KOK04739.
OMAFSAEVYT.
PhylomeDBP10644.
TreeFamTF314920.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_116125. Disease.
REACT_15518. Transmembrane transport of small molecules.
REACT_604. Hemostasis.
REACT_6900. Immune System.
SignaLinkP10644.

Gene expression databases

ArrayExpressP10644.
BgeeP10644.
CleanExHS_PRKAR1A.
GenevestigatorP10644.

Family and domain databases

Gene3D2.60.120.10. 2 hits.
InterProIPR002373. 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]
PfamPF00027. cNMP_binding. 2 hits.
PF02197. RIIa. 1 hit.
[Graphical view]
PIRSFPIRSF000548. PK_regulatory. 1 hit.
PRINTSPR00103. CAMPKINASE.
SMARTSM00100. cNMP. 2 hits.
SM00394. RIIa. 1 hit.
[Graphical view]
SUPFAMSSF47391. SSF47391. 1 hit.
SSF51206. SSF51206. 2 hits.
PROSITEPS00888. CNMP_BINDING_1. 2 hits.
PS00889. CNMP_BINDING_2. 2 hits.
PS50042. CNMP_BINDING_3. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPRKAR1A. human.
GenomeRNAi5573.
NextBio21602.
PROP10644.
SOURCESearch...

Entry information

Entry nameKAP0_HUMAN
AccessionPrimary (citable) accession number: P10644
Secondary accession number(s): K7ER48, Q567S7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: July 9, 2014
This is version 171 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM