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cAMP-dependent protein kinase type I-alpha regulatory subunit (Tissue-specific extinguisher 1) (TSE1)

 KAP0_HUMAN              Reviewed;         381 AA.
P10644; K7ER48; Q567S7;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 1.
23-MAY-2018, entry version 212.
RecName: Full=cAMP-dependent protein kinase type I-alpha regulatory subunit;
AltName: Full=Tissue-specific extinguisher 1;
Short=TSE1;
Name=PRKAR1A; Synonyms=PKR1, PRKAR1, TSE1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Testis;
PubMed=3426618; DOI=10.1016/0006-291X(87)90499-2;
Sandberg M., Tasken K., Oeyen O., Hansson V., Jahnsen T.;
"Molecular cloning, cDNA structure and deduced amino acid sequence for
a type I regulatory subunit of cAMP-dependent protein kinase from
human testis.";
Biochem. Biophys. Res. Commun. 149:939-945(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Testis;
PubMed=2310396; DOI=10.1016/0006-291X(90)91768-N;
Sandberg M., Skalhegg B., Jahnsen T.;
"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.";
Biochem. Biophys. Res. Commun. 167:323-330(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1889088; DOI=10.1016/0092-8674(91)90433-Y;
Jones K.W., Shapero M.H., Chevrette M., Fournier R.E.;
"Subtractive hybridization cloning of a tissue-specific extinguisher:
TSE1 encodes a regulatory subunit of protein kinase A.";
Cell 66:861-872(1991).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Testis;
PubMed=8977401; DOI=10.1210/endo.138.1.4864;
Solberg R., Sandberg M., Natarajan V., Torjesen P.A., Hansson V.,
Jahnsen T., Tasken K.;
"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.";
Endocrinology 138:169-181(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
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., 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.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lymph, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 1-13, AND ACETYLATION AT MET-1.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[8]
INVOLVEMENT IN PPNAD1.
PubMed=12213893; DOI=10.1210/jc.2002-020592;
Groussin L., Jullian E., Perlemoine K., Louvel A., Leheup B.,
Luton J.P., Bertagna X., Bertherat J.;
"Mutations of the PRKAR1A gene in Cushing's syndrome due to sporadic
primary pigmented nodular adrenocortical disease.";
J. Clin. Endocrinol. Metab. 87:4324-4329(2002).
[9]
INTERACTION WITH RFC2.
PubMed=15655353;
Gupte R.S., Weng Y., Liu L., Lee M.Y.;
"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.";
Cell Cycle 4:323-329(2005).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[11]
FUNCTION, AND INTERACTION WITH PRKX.
PubMed=16491121; DOI=10.1038/sj.onc.1209436;
Glesne D., Huberman E.;
"Smad6 is a protein kinase X phosphorylation substrate and is required
for HL-60 cell differentiation.";
Oncogene 25:4086-4098(2006).
[12]
INTERACTION WITH AICDA.
PubMed=16387847; DOI=10.1073/pnas.0509969103;
Pasqualucci L., Kitaura Y., Gu H., Dalla-Favera R.;
"PKA-mediated phosphorylation regulates the function of activation-
induced deaminase (AID) in B cells.";
Proc. Natl. Acad. Sci. U.S.A. 103:395-400(2006).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=T-cell;
PubMed=19367720; DOI=10.1021/pr800500r;
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
"Phosphorylation analysis of primary human T lymphocytes using
sequential IMAC and titanium oxide enrichment.";
J. Proteome Res. 7:5167-5176(2008).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18318008; DOI=10.1002/pmic.200700884;
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
Zou H., Gu J.;
"Large-scale phosphoproteome analysis of human liver tissue by
enrichment and fractionation of phosphopeptides with strong anion
exchange chromatography.";
Proteomics 8:1346-1361(2008).
[18]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[21]
INTERACTION WITH RARA, AND FUNCTION.
PubMed=20215566; DOI=10.1210/en.2009-1338;
Santos N.C., Kim K.H.;
"Activity of retinoic acid receptor-alpha is directly regulated at its
protein kinase A sites in response to follicle-stimulating hormone
signaling.";
Endocrinology 151:2361-2372(2010).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[24]
INVOLVEMENT IN ACRDYS1, AND MUTAGENESIS OF TYR-373.
PubMed=21651393; DOI=10.1056/NEJMoa1012717;
Linglart A., Menguy C., Couvineau A., Auzan C., Gunes Y., Cancel M.,
Motte E., Pinto G., Chanson P., Bougneres P., Clauser E., Silve C.;
"Recurrent PRKAR1A mutation in acrodysostosis with hormone
resistance.";
N. Engl. J. Med. 364:2218-2226(2011).
[25]
INTERACTION WITH PJA2.
PubMed=21423175; DOI=10.1038/ncb2209;
Lignitto L., Carlucci A., Sepe M., Stefan E., Cuomo O., Nistico R.,
Scorziello A., Savoia C., Garbi C., Annunziato L., Feliciello A.;
"Control of PKA stability and signalling by the RING ligase praja2.";
Nat. Cell Biol. 13:412-422(2011).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[27]
INVOLVEMENT IN CNC1.
PubMed=22785148; DOI=10.1507/endocrj.EJ12-0040;
Tung S.C., Hwang D.Y., Yang J.W., Chen W.J., Lee C.T.;
"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.";
Endocr. J. 59:823-830(2012).
[28]
INTERACTION WITH C2ORF88/SMAKAP, AND SUBCELLULAR LOCATION.
PubMed=23115245; DOI=10.1074/jbc.M112.395970;
Burgers P.P., Ma Y., Margarucci L., Mackey M., van der Heyden M.A.,
Ellisman M., Scholten A., Taylor S.S., Heck A.J.;
"A small novel A-kinase anchoring protein (AKAP) that localizes
specifically protein kinase A-regulatory subunit I (PKA-RI) to the
plasma membrane.";
J. Biol. Chem. 287:43789-43797(2012).
[29]
INVOLVEMENT IN CNC1.
PubMed=23323113; DOI=10.4132/KoreanJPathol.2012.46.6.595;
Park K.U., Kim H.S., Lee S.K., Jung W.W., Park Y.K.;
"Novel Mutation in PRKAR1A in Carney Complex.";
Korean J. Pathol. 46:595-600(2012).
[30]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[31]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
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.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-75; SER-77 AND SER-83,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[34]
VARIANT CNC1 CYS-74.
PubMed=15371594; DOI=10.1073/pnas.0405535101;
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.;
"Comparative PRKAR1A genotype-phenotype analyses in humans with Carney
complex and prkar1a haploinsufficient mice.";
Proc. Natl. Acad. Sci. U.S.A. 101:14222-14227(2004).
[35]
VARIANTS CNC1 ASN-9; SER-146; TYR-183; ASP-213 AND TRP-289, AND
CHARACTERIZATION OF VARIANTS CNC1 ASN-9; CYS-74; SER-146; TYR-183;
ASP-213 AND TRP-289.
PubMed=18241045; DOI=10.1002/humu.20688;
Greene E.L., Horvath A.D., Nesterova M., Giatzakis C., Bossis I.,
Stratakis C.A.;
"In vitro functional studies of naturally occurring pathogenic PRKAR1A
mutations that are not subject to nonsense mRNA decay.";
Hum. Mutat. 29:633-639(2008).
[36]
VARIANT ACRDYS1 HIS-373.
PubMed=22464250; DOI=10.1016/j.ajhg.2012.03.003;
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.;
"Exome sequencing identifies PDE4D mutations as another cause of
acrodysostosis.";
Am. J. Hum. Genet. 90:740-745(2012).
[37]
VARIANTS ACRDYS1 THR-327 AND PRO-335.
PubMed=22464252; DOI=10.1016/j.ajhg.2012.03.004;
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.;
"Exome sequencing identifies PDE4D mutations in acrodysostosis.";
Am. J. Hum. Genet. 90:746-751(2012).
[38]
VARIANTS ACRDYS1 ARG-285; GLU-289; VAL-328 AND LEU-335.
PubMed=23043190; DOI=10.1210/jc.2012-2326;
Linglart A., Fryssira H., Hiort O., Holterhus P.M.,
Perez de Nanclares G., Argente J., Heinrichs C., Kuechler A.,
Mantovani G., Leheup B., Wicart P., Chassot V., Schmidt D.,
Rubio-Cabezas O., Richter-Unruh A., Berrade S., Pereda A., Boros E.,
Munoz-Calvo M.T., Castori M., Gunes Y., Bertrand G., Bougneres P.,
Clauser E., Silve C.;
"PRKAR1A and PDE4D mutations cause acrodysostosis but two distinct
syndromes with or without GPCR-signaling hormone resistance.";
J. Clin. Endocrinol. Metab. 97:E2328-E2338(2012).
[39]
VARIANT ACRDYS1 ALA-239, AND CHARACTERIZATION OF VARIANT ACRDYS1
ALA-239.
PubMed=22723333; DOI=10.1210/jc.2012-1369;
Nagasaki K., Iida T., Sato H., Ogawa Y., Kikuchi T., Saitoh A.,
Ogata T., Fukami M.;
"PRKAR1A mutation affecting cAMP-mediated G protein-coupled receptor
signaling in a patient with acrodysostosis and hormone resistance.";
J. Clin. Endocrinol. Metab. 97:E1808-E1813(2012).
[40]
VARIANTS ACRDYS1 THR-213 AND CYS-373, AND VARIANT ASN-227.
PubMed=23425300; DOI=10.1111/cge.12106;
Muhn F., Klopocki E., Graul-Neumann L., Uhrig S., Colley A.,
Castori M., Lankes E., Henn W., Gruber-Sedlmayr U., Seifert W.,
Horn D.;
"Novel mutations of the PRKAR1A gene in patients with
acrodysostosis.";
Clin. Genet. 84:531-538(2013).
[41]
VARIANT ACRDYS1 CYS-175, CHARACTERIZATION OF VARIANTS ACRDYS1 CYS-175;
THR-213; ARG-285; GLU-289; VAL-328 AND LEU-335, CHARACTERIZATION OF
VARIANTS CNC1 ASP-213 AND TRP-289, AND FUNCTION.
PubMed=26405036; DOI=10.1074/jbc.M115.656553;
Rhayem Y., Le Stunff C., Abdel Khalek W., Auzan C., Bertherat J.,
Linglart A., Couvineau A., Silve C., Clauser E.;
"Functional characterization of PRKAR1A mutations reveals a unique
molecular mechanism causing acrodysostosis but multiple mechanisms
causing carney complex.";
J. Biol. Chem. 290:27816-27828(2015).
-!- FUNCTION: Regulatory subunit of the cAMP-dependent protein kinases
involved in cAMP signaling in cells. {ECO:0000269|PubMed:16491121,
ECO:0000269|PubMed:20215566, ECO:0000269|PubMed:26405036}.
-!- SUBUNIT: 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. {ECO:0000250,
ECO:0000269|PubMed:15655353, ECO:0000269|PubMed:16387847,
ECO:0000269|PubMed:16491121, ECO:0000269|PubMed:20215566,
ECO:0000269|PubMed:21423175, ECO:0000269|PubMed:23115245}.
-!- INTERACTION:
P03259-2:- (xeno); NbExp=5; IntAct=EBI-476431, EBI-7225021;
Q9GZX7:AICDA; NbExp=5; IntAct=EBI-476431, EBI-3834328;
O43687-2:AKAP7; NbExp=4; IntAct=EBI-476431, EBI-10185182;
Q9BSF0:C2orf88; NbExp=5; IntAct=EBI-476431, EBI-744298;
Q9H0R8:GABARAPL1; NbExp=2; IntAct=EBI-476431, EBI-746969;
Q9H8W4:PLEKHF2; NbExp=3; IntAct=EBI-476431, EBI-742388;
P17612:PRKACA; NbExp=8; IntAct=EBI-476431, EBI-476586;
P51817:PRKX; NbExp=2; IntAct=EBI-476431, EBI-4302903;
P35250:RFC2; NbExp=7; IntAct=EBI-476431, EBI-476409;
Q01105:SET; NbExp=2; IntAct=EBI-476431, EBI-1053182;
P0DO92:T-ENOL; NbExp=4; IntAct=EBI-476431, EBI-13044706;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23115245}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P10644-1; Sequence=Displayed;
Name=2;
IsoId=P10644-2; Sequence=VSP_054833, VSP_054834;
Note=No experimental confirmation available. Gene prediction
based on EST data.;
-!- 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.
-!- PTM: The pseudophosphorylation site binds to the substrate-binding
region of the catalytic chain, resulting in the inhibition of its
activity.
-!- DISEASE: Carney complex 1 (CNC1) [MIM:160980]: CNC is a multiple
neoplasia syndrome characterized by spotty skin pigmentation,
cardiac and other myxomas, endocrine tumors, and psammomatous
melanotic schwannomas. {ECO:0000269|PubMed:15371594,
ECO:0000269|PubMed:18241045, ECO:0000269|PubMed:22785148,
ECO:0000269|PubMed:23323113, ECO:0000269|PubMed:26405036}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Intracardiac myxoma (INTMYX) [MIM:255960]: Inheritance is
autosomal recessive. Note=The disease is caused by mutations
affecting the gene represented in this entry.
-!- DISEASE: Primary pigmented nodular adrenocortical disease 1
(PPNAD1) [MIM:610489]: A rare bilateral adrenal defect causing
ACTH-independent Cushing syndrome. Macroscopic appearance of the
adrenals is characteristic with small pigmented micronodules
observed in the cortex. Clinical manifestations of Cushing
syndrome include facial and truncal obesity, abdominal striae,
muscular weakness, osteoporosis, arterial hypertension, diabetes.
PPNAD1 is most often diagnosed in patients with Carney complex, a
multiple neoplasia syndrome. However it can also be observed in
patients without other manifestations.
{ECO:0000269|PubMed:12213893}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Acrodysostosis 1, with or without hormone resistance
(ACRDYS1) [MIM:101800]: A form of skeletal dysplasia characterized
by short stature, severe brachydactyly, facial dysostosis, and
nasal hypoplasia. Affected individuals often have advanced bone
age and obesity. Laboratory studies show resistance to multiple
hormones, including parathyroid, thyrotropin, calcitonin, growth
hormone-releasing hormone, and gonadotropin. However, not all
patients show endocrine abnormalities.
{ECO:0000269|PubMed:21651393, ECO:0000269|PubMed:22464250,
ECO:0000269|PubMed:22464252, ECO:0000269|PubMed:22723333,
ECO:0000269|PubMed:23043190, ECO:0000269|PubMed:23425300,
ECO:0000269|PubMed:26405036}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the cAMP-dependent kinase regulatory chain
family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/PRKAR1AID387.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M18468; AAB50922.1; -; mRNA.
EMBL; M33336; AAB50921.1; -; mRNA.
EMBL; S54705; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; S54707; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; S54709; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; S54711; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; Y07642; CAA68925.1; -; mRNA.
EMBL; AC079210; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC036285; AAH36285.1; -; mRNA.
EMBL; BC093042; AAH93042.1; -; mRNA.
CCDS; CCDS11678.1; -. [P10644-1]
CCDS; CCDS62307.1; -. [P10644-2]
PIR; A34627; OKHU1R.
RefSeq; NP_001263218.1; NM_001276289.1. [P10644-1]
RefSeq; NP_001263219.1; NM_001276290.1. [P10644-2]
RefSeq; NP_001265362.1; NM_001278433.1. [P10644-1]
RefSeq; NP_002725.1; NM_002734.4. [P10644-1]
RefSeq; NP_997636.1; NM_212471.2. [P10644-1]
RefSeq; NP_997637.1; NM_212472.2. [P10644-1]
RefSeq; XP_011523285.1; XM_011524983.2. [P10644-1]
RefSeq; XP_011523286.1; XM_011524984.2. [P10644-1]
RefSeq; XP_011523287.1; XM_011524985.2. [P10644-1]
UniGene; Hs.280342; -.
UniGene; Hs.745160; -.
PDB; 5KJX; X-ray; 1.90 A; A=234-381.
PDB; 5KJY; X-ray; 2.00 A; A=234-381.
PDB; 5KJZ; X-ray; 1.35 A; A=234-381.
PDBsum; 5KJX; -.
PDBsum; 5KJY; -.
PDBsum; 5KJZ; -.
ProteinModelPortal; P10644; -.
SMR; P10644; -.
BioGrid; 111559; 89.
DIP; DIP-34368N; -.
IntAct; P10644; 87.
MINT; P10644; -.
STRING; 9606.ENSP00000351410; -.
BindingDB; P10644; -.
DrugBank; DB02527; Cyclic Adenosine Monophosphate.
DrugBank; DB02315; Cyclic Guanosine Monophosphate.
DrugBank; DB05798; GEM-231.
GuidetoPHARMACOLOGY; 1472; -.
iPTMnet; P10644; -.
PhosphoSitePlus; P10644; -.
SwissPalm; P10644; -.
DMDM; 125193; -.
OGP; P10644; -.
REPRODUCTION-2DPAGE; IPI00021831; -.
EPD; P10644; -.
MaxQB; P10644; -.
PaxDb; P10644; -.
PeptideAtlas; P10644; -.
PRIDE; P10644; -.
DNASU; 5573; -.
Ensembl; ENST00000358598; ENSP00000351410; ENSG00000108946. [P10644-1]
Ensembl; ENST00000392711; ENSP00000376475; ENSG00000108946. [P10644-1]
Ensembl; ENST00000536854; ENSP00000445625; ENSG00000108946. [P10644-1]
Ensembl; ENST00000586397; ENSP00000466459; ENSG00000108946. [P10644-1]
Ensembl; ENST00000588188; ENSP00000468106; ENSG00000108946. [P10644-2]
Ensembl; ENST00000589228; ENSP00000464977; ENSG00000108946. [P10644-1]
GeneID; 5573; -.
KEGG; hsa:5573; -.
UCSC; uc002jhg.5; human. [P10644-1]
CTD; 5573; -.
DisGeNET; 5573; -.
EuPathDB; HostDB:ENSG00000108946.14; -.
GeneCards; PRKAR1A; -.
GeneReviews; PRKAR1A; -.
HGNC; HGNC:9388; PRKAR1A.
HPA; CAB019378; -.
HPA; HPA049979; -.
MalaCards; PRKAR1A; -.
MIM; 101800; phenotype.
MIM; 160980; phenotype.
MIM; 188830; gene.
MIM; 255960; phenotype.
MIM; 610489; phenotype.
neXtProt; NX_P10644; -.
OpenTargets; ENSG00000108946; -.
Orphanet; 950; Acrodysostosis.
Orphanet; 280651; Acrodysostosis with multiple hormone resistance.
Orphanet; 520; Acute promyelocytic leukemia.
Orphanet; 1359; Carney complex.
Orphanet; 615; Familial atrial myxoma.
Orphanet; 189439; Primary pigmented nodular adrenocortical disease.
PharmGKB; PA33754; -.
eggNOG; KOG1113; Eukaryota.
eggNOG; COG0664; LUCA.
GeneTree; ENSGT00530000062947; -.
HOGENOM; HOG000196669; -.
HOVERGEN; HBG002025; -.
InParanoid; P10644; -.
KO; K04739; -.
OMA; VQLCTVR; -.
OrthoDB; EOG091G0F1K; -.
PhylomeDB; P10644; -.
TreeFam; TF314920; -.
Reactome; R-HSA-163615; PKA activation.
Reactome; R-HSA-164378; PKA activation in glucagon signalling.
Reactome; R-HSA-180024; DARPP-32 events.
Reactome; R-HSA-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
Reactome; R-HSA-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
Reactome; R-HSA-5610787; Hedgehog 'off' state.
Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
SignaLink; P10644; -.
SIGNOR; P10644; -.
ChiTaRS; PRKAR1A; human.
GenomeRNAi; 5573; -.
PRO; PR:P10644; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000108946; -.
CleanEx; HS_PRKAR1A; -.
ExpressionAtlas; P10644; baseline and differential.
Genevisible; P10644; HS.
GO; GO:0005952; C:cAMP-dependent protein kinase complex; IEA:Ensembl.
GO; GO:0097546; C:ciliary base; TAS:Reactome.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
GO; GO:0031588; C:nucleotide-activated protein kinase complex; IDA:BHF-UCL.
GO; GO:0044853; C:plasma membrane raft; IDA:UniProtKB.
GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
GO; GO:0030552; F:cAMP binding; IEA:UniProtKB-KW.
GO; GO:0004862; F:cAMP-dependent protein kinase inhibitor activity; IDA:BHF-UCL.
GO; GO:0008603; F:cAMP-dependent protein kinase regulator activity; IDA:BHF-UCL.
GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
GO; GO:0034236; F:protein kinase A catalytic subunit binding; IPI:UniProtKB.
GO; GO:0031625; F:ubiquitin protein ligase binding; IDA:UniProtKB.
GO; GO:0034199; P:activation of protein kinase A activity; TAS:Reactome.
GO; GO:0007596; P:blood coagulation; TAS:Reactome.
GO; GO:0060038; P:cardiac muscle cell proliferation; IEA:Ensembl.
GO; GO:0071377; P:cellular response to glucagon stimulus; TAS:Reactome.
GO; GO:0007143; P:female meiotic nuclear division; IEA:Ensembl.
GO; GO:0035556; P:intracellular signal transduction; TAS:ProtInc.
GO; GO:0001707; P:mesoderm formation; IEA:Ensembl.
GO; GO:0046007; P:negative regulation of activated T cell proliferation; IMP:UniProtKB.
GO; GO:2000480; P:negative regulation of cAMP-dependent protein kinase activity; IDA:BHF-UCL.
GO; GO:0045835; P:negative regulation of meiotic nuclear division; IEA:Ensembl.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; TAS:ProtInc.
GO; GO:0003091; P:renal water homeostasis; TAS:Reactome.
GO; GO:0045214; P:sarcomere organization; IEA:Ensembl.
CDD; cd00038; CAP_ED; 2.
Gene3D; 2.60.120.10; -; 2.
InterPro; IPR012198; cAMP_dep_PK_reg_su.
InterPro; IPR003117; cAMP_dep_PK_reg_su_I/II_a/b.
InterPro; IPR018490; cNMP-bd-like.
InterPro; IPR018488; cNMP-bd_CS.
InterPro; IPR000595; cNMP-bd_dom.
InterPro; IPR014710; RmlC-like_jellyroll.
Pfam; PF00027; cNMP_binding; 2.
Pfam; PF02197; RIIa; 1.
PIRSF; PIRSF000548; PK_regulatory; 1.
SMART; SM00100; cNMP; 2.
SMART; SM00394; RIIa; 1.
SUPFAM; SSF51206; SSF51206; 2.
PROSITE; PS00888; CNMP_BINDING_1; 2.
PROSITE; PS00889; CNMP_BINDING_2; 2.
PROSITE; PS50042; CNMP_BINDING_3; 2.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; cAMP; cAMP-binding;
Cell membrane; Complete proteome; Cushing syndrome;
Direct protein sequencing; Disease mutation; Disulfide bond; Membrane;
Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat.
CHAIN 1 381 cAMP-dependent protein kinase type I-
alpha regulatory subunit.
/FTId=PRO_0000205377.
NP_BIND 137 254 cAMP 1.
NP_BIND 255 381 cAMP 2.
REGION 1 136 Dimerization and phosphorylation.
MOTIF 96 100 Pseudophosphorylation motif.
BINDING 202 202 cAMP 1.
BINDING 211 211 cAMP 1.
BINDING 326 326 cAMP 2.
BINDING 335 335 cAMP 2.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|PubMed:12665801}.
MOD_RES 3 3 Phosphoserine.
{ECO:0000250|UniProtKB:P09456}.
MOD_RES 75 75 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 77 77 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 83 83 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18318008,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19367720,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 101 101 Phosphoserine.
{ECO:0000250|UniProtKB:Q9DBC7}.
MOD_RES 258 258 Phosphoserine.
{ECO:0000250|UniProtKB:P09456}.
DISULFID 18 18 Interchain (with C-39). {ECO:0000250}.
DISULFID 39 39 Interchain (with C-18). {ECO:0000250}.
VAR_SEQ 326 337 EIALLMNRPRAA -> HLIISRRSIPLG (in isoform
2). {ECO:0000305}.
/FTId=VSP_054833.
VAR_SEQ 338 381 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_054834.
VARIANT 9 9 S -> N (in CNC1; exhibits increased PKA
activity which is attributed to decreased
binding to cAMP and/or the catalytic
subunit). {ECO:0000269|PubMed:18241045}.
/FTId=VAR_046894.
VARIANT 74 74 R -> C (in CNC1; exhibits increased PKA
activity which is attributed to decreased
binding to cAMP and/or the catalytic
subunit; dbSNP:rs137853303).
{ECO:0000269|PubMed:15371594,
ECO:0000269|PubMed:18241045}.
/FTId=VAR_046895.
VARIANT 146 146 R -> S (in CNC1; exhibits increased PKA
activity which is attributed to decreased
binding to cAMP and/or the catalytic
subunit). {ECO:0000269|PubMed:18241045}.
/FTId=VAR_046896.
VARIANT 175 175 Y -> C (in ACRDYS1; reduces PKA activity;
decreases cAMP binding).
{ECO:0000269|PubMed:26405036}.
/FTId=VAR_075533.
VARIANT 183 183 D -> Y (in CNC1; exhibits increased PKA
activity which is attributed to decreased
binding to cAMP and/or the catalytic
subunit). {ECO:0000269|PubMed:18241045}.
/FTId=VAR_046897.
VARIANT 213 213 A -> D (in CNC1; exhibits increased PKA
activity which is attributed to decreased
binding to cAMP and/or the catalytic
subunit; reduces protein degradation;
dbSNP:rs281864786).
{ECO:0000269|PubMed:18241045,
ECO:0000269|PubMed:26405036}.
/FTId=VAR_046898.
VARIANT 213 213 A -> T (in ACRDYS1; reduces PKA activity;
decreases cAMP binding; reduces protein
degradation).
{ECO:0000269|PubMed:23425300,
ECO:0000269|PubMed:26405036}.
/FTId=VAR_069456.
VARIANT 227 227 D -> N. {ECO:0000269|PubMed:23425300}.
/FTId=VAR_069457.
VARIANT 239 239 T -> A (in ACRDYS1; impairs response of
PKA to c-AMP).
{ECO:0000269|PubMed:22723333}.
/FTId=VAR_069458.
VARIANT 285 285 Q -> R (in ACRDYS1; reduces PKA activity;
decreases cAMP binding).
{ECO:0000269|PubMed:23043190,
ECO:0000269|PubMed:26405036}.
/FTId=VAR_069459.
VARIANT 289 289 G -> E (in ACRDYS1; reduces PKA activity;
decreases cAMP binding; reduces protein
degradation).
{ECO:0000269|PubMed:23043190,
ECO:0000269|PubMed:26405036}.
/FTId=VAR_069460.
VARIANT 289 289 G -> W (in CNC1; exhibits increased PKA
activity which is attributed to decreased
binding to cAMP and/or the catalytic
subunit; accelerates protein
degradation).
{ECO:0000269|PubMed:18241045,
ECO:0000269|PubMed:26405036}.
/FTId=VAR_046899.
VARIANT 327 327 I -> T (in ACRDYS1; dbSNP:rs387906695).
{ECO:0000269|PubMed:22464252}.
/FTId=VAR_069461.
VARIANT 328 328 A -> V (in ACRDYS1; disrupts cAMP
binding). {ECO:0000269|PubMed:23043190,
ECO:0000269|PubMed:26405036}.
/FTId=VAR_069462.
VARIANT 335 335 R -> L (in ACRDYS1; disrupts cAMP
binding). {ECO:0000269|PubMed:23043190,
ECO:0000269|PubMed:26405036}.
/FTId=VAR_069464.
VARIANT 335 335 R -> P (in ACRDYS1; dbSNP:rs387906694).
{ECO:0000269|PubMed:22464252}.
/FTId=VAR_069463.
VARIANT 373 373 Y -> C (in ACRDYS1).
{ECO:0000269|PubMed:23425300}.
/FTId=VAR_069465.
VARIANT 373 373 Y -> H (in ACRDYS1; dbSNP:rs387906693).
{ECO:0000269|PubMed:22464250}.
/FTId=VAR_068241.
MUTAGEN 373 373 Y->A: Impairs response of PKA to c-AMP.
{ECO:0000269|PubMed:21651393}.
HELIX 237 250 {ECO:0000244|PDB:5KJZ}.
HELIX 254 256 {ECO:0000244|PDB:5KJZ}.
HELIX 261 270 {ECO:0000244|PDB:5KJZ}.
STRAND 272 276 {ECO:0000244|PDB:5KJZ}.
STRAND 281 283 {ECO:0000244|PDB:5KJZ}.
STRAND 291 304 {ECO:0000244|PDB:5KJZ}.
STRAND 313 318 {ECO:0000244|PDB:5KJZ}.
HELIX 326 330 {ECO:0000244|PDB:5KJZ}.
STRAND 336 351 {ECO:0000244|PDB:5KJZ}.
HELIX 352 358 {ECO:0000244|PDB:5KJZ}.
HELIX 360 362 {ECO:0000244|PDB:5KJZ}.
HELIX 363 370 {ECO:0000244|PDB:5KJZ}.
TURN 371 376 {ECO:0000244|PDB:5KJZ}.
SEQUENCE 381 AA; 42982 MW; 2D04F08CE8857A6D CRC64;
MESGSTAASE EARSLRECEL YVQKHNIQAL LKDSIVQLCT ARPERPMAFL REYFERLEKE
EAKQIQNLQK AGTRTDSRED EISPPPPNPV VKGRRRRGAI SAEVYTEEDA ASYVRKVIPK
DYKTMAALAK AIEKNVLFSH LDDNERSDIF DAMFSVSFIA GETVIQQGDE GDNFYVIDQG
ETDVYVNNEW ATSVGEGGSF GELALIYGTP RAATVKAKTN VKLWGIDRDS YRRILMGSTL
RKRKMYEEFL SKVSILESLD KWERLTVADA LEPVQFEDGQ KIVVQGEPGD EFFIILEGSA
AVLQRRSENE EFVEVGRLGP SDYFGEIALL MNRPRAATVV ARGPLKCVKL DRPRFERVLG
PCSDILKRNI QQYNSFVSLS V


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