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cAMP-dependent protein kinase catalytic subunit alpha (PKA C-alpha) (EC 2.7.11.11)

 KAPCA_HUMAN             Reviewed;         351 AA.
P17612; Q32P54; Q9H2Y0; Q9NRB4; Q9NRH9;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
22-NOV-2017, entry version 207.
RecName: Full=cAMP-dependent protein kinase catalytic subunit alpha;
Short=PKA C-alpha;
EC=2.7.11.11;
Name=PRKACA; Synonyms=PKACA;
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).
PubMed=2843813; DOI=10.1093/nar/16.16.8189;
Maldonado F., Hanks S.K.;
"A cDNA clone encoding human cAMP-dependent protein kinase catalytic
subunit C alpha.";
Nucleic Acids Res. 16:8189-8190(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Thalamus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
SeattleSNPs variation discovery resource;
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Eye, and Testis;
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).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-189 (ISOFORM 2), SUBCELLULAR LOCATION,
AND TISSUE SPECIFICITY.
PubMed=10906071; DOI=10.1095/biolreprod63.2.607;
Reinton N., Orstavik S., Haugen T.B., Jahnsen T., Tasken K.,
Skalhegg B.S.;
"A novel isoform of human cyclic 3',5'-adenosine monophosphate-
dependent protein kinase, c alpha-s, localizes to sperm midpiece.";
Biol. Reprod. 63:607-611(2000).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-152 (ISOFORM 2).
TISSUE=Testis;
PubMed=10982398; DOI=10.1091/mbc.11.9.3031;
San Agustin J.T., Wilkerson C.G., Witman G.B.;
"The unique catalytic subunit of sperm cAMP-dependent protein kinase
is the product of an alternative C-alpha mRNA expressed specifically
in spermatogenic cells.";
Mol. Biol. Cell 11:3031-3044(2000).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-39 (ISOFORM 2).
TISSUE=Testis;
PubMed=10841548; DOI=10.1073/pnas.97.12.6433;
Desseyn J.-L., Burton K.A., McKnight G.S.;
"Expression of a nonmyristylated variant of the catalytic subunit of
protein kinase A during male germ-cell development.";
Proc. Natl. Acad. Sci. U.S.A. 97:6433-6438(2000).
[9]
AUTOPHOSPHORYLATION, PHOSPHORYLATION AT THR-196, PHOSPHORYLATION AT
THR-198 BY PDK1, AND MUTAGENESIS OF ARG-195; GLY-201 AND THR-202.
PubMed=12372837; DOI=10.1074/jbc.M204970200;
Moore M.J., Kanter J.R., Jones K.C., Taylor S.S.;
"Phosphorylation of the catalytic subunit of protein kinase A.
Autophosphorylation versus phosphorylation by phosphoinositide-
dependent kinase-1.";
J. Biol. Chem. 277:47878-47884(2002).
[10]
INTERACTION WITH RAB13.
PubMed=15096524; DOI=10.1083/jcb.200312118;
Koehler K., Louvard D., Zahraoui A.;
"Rab13 regulates PKA signaling during tight junction assembly.";
J. Cell Biol. 165:175-180(2004).
[11]
FUNCTION AS NFKB1 KINASE.
PubMed=15642694; DOI=10.1074/jbc.M412180200;
Guan H., Hou S., Ricciardi R.P.;
"DNA binding of repressor nuclear factor-kappaB p50/p50 depends on
phosphorylation of Ser337 by the protein kinase A catalytic subunit.";
J. Biol. Chem. 280:9957-9962(2005).
[12]
FUNCTION AS CLDN3 KINASE.
PubMed=15905176; DOI=10.1074/jbc.M502003200;
D'Souza T., Agarwal R., Morin P.J.;
"Phosphorylation of claudin-3 at threonine 192 by cAMP-dependent
protein kinase regulates tight junction barrier function in ovarian
cancer cells.";
J. Biol. Chem. 280:26233-26240(2005).
[13]
FUNCTION, AND 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).
[14]
FUNCTION IN PROTEASOME REGULATION, AND FUNCTION AS PSMC5/RPT6 KINASE.
PubMed=17565987; DOI=10.1074/jbc.M702439200;
Zhang F., Hu Y., Huang P., Toleman C.A., Paterson A.J., Kudlow J.E.;
"Proteasome function is regulated by cyclic AMP-dependent protein
kinase through phosphorylation of Rpt6.";
J. Biol. Chem. 282:22460-22471(2007).
[15]
FUNCTION AS RYR2 KINASE.
PubMed=17693412; DOI=10.1074/jbc.M703510200;
Xiao B., Tian X., Xie W., Jones P.P., Cai S., Wang X., Jiang D.,
Kong H., Zhang L., Chen K., Walsh M.P., Cheng H., Chen S.R.W.;
"Functional consequence of protein kinase A-dependent phosphorylation
of the cardiac ryanodine receptor: sensitization of store overload-
induced Ca2+ release.";
J. Biol. Chem. 282:30256-30264(2007).
[16]
PHOSPHORYLATION, AND ENZYME REGULATION.
PubMed=17909264; DOI=10.1677/JME-07-0048;
Ichikawa T., Horie-Inoue K., Ikeda K., Blumberg B., Inoue S.;
"Vitamin K2 induces phosphorylation of protein kinase A and expression
of novel target genes in osteoblastic cells.";
J. Mol. Endocrinol. 39:239-247(2007).
[17]
FUNCTION AS ALPHA-DIFLUOROMETHYLORNITHINE ANTAGONIST.
PubMed=17333334; DOI=10.1007/s10549-007-9536-5;
Xu H., Washington S., Verderame M.F., Manni A.;
"Activation of protein kinase A (PKA) signaling mitigates the
antiproliferative and antiinvasive effects of alpha-
difluoromethylornithine in breast cancer cells.";
Breast Cancer Res. Treat. 107:63-70(2008).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-49 AND SER-339, 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).
[19]
FUNCTION, AND INTERACTION WITH APOBEC3G.
PubMed=18836454; DOI=10.1038/nsmb.1497;
Shirakawa K., Takaori-Kondo A., Yokoyama M., Izumi T., Matsui M.,
Io K., Sato T., Sato H., Uchiyama T.;
"Phosphorylation of APOBEC3G by protein kinase A regulates its
interaction with HIV-1 Vif.";
Nat. Struct. Mol. Biol. 15:1184-1191(2008).
[20]
ENZYME REGULATION, AND MUTAGENESIS OF TYR-205.
PubMed=18178622; DOI=10.1073/pnas.0709214104;
Masterson L.R., Mascioni A., Traaseth N.J., Taylor S.S., Veglia G.;
"Allosteric cooperativity in protein kinase A.";
Proc. Natl. Acad. Sci. U.S.A. 105:506-511(2008).
[21]
SUBCELLULAR LOCATION.
PubMed=19210988; DOI=10.1016/j.yexcr.2008.12.026;
Yan X., Walkiewicz M., Carlson J., Leiphon L., Grove B.;
"Gravin dynamics regulates the subcellular distribution of PKA.";
Exp. Cell Res. 315:1247-1259(2009).
[22]
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).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339, 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).
[24]
FUNCTION IN PLATELETS, FUNCTION AS VASP KINASE, AND INTERACTION WITH
NFKB1; NFKB2 AND NFKBIA.
PubMed=20356841; DOI=10.1074/jbc.M109.077602;
Gambaryan S., Kobsar A., Rukoyatkina N., Herterich S., Geiger J.,
Smolenski A., Lohmann S.M., Walter U.;
"Thrombin and collagen induce a feedback inhibitory signaling pathway
in platelets involving dissociation of the catalytic subunit of
protein kinase A from an NFkappaB-IkappaB complex.";
J. Biol. Chem. 285:18352-18363(2010).
[25]
FUNCTION IN OSTEOBLAST DIFFERENTIATION, AND ENZYME REGULATION.
PubMed=19949837; DOI=10.1007/s11010-009-0344-6;
Wang W., Zhang X., Zheng J., Yang J.;
"High glucose stimulates adipogenic and inhibits osteogenic
differentiation in MG-63 cells through cAMP/protein kinase
A/extracellular signal-regulated kinase pathway.";
Mol. Cell. Biochem. 338:115-122(2010).
[26]
FUNCTION IN PHOSPHORYLATION OF HSF1, INTERACTION WITH HSF1, AND
SUBCELLULAR LOCATION.
PubMed=21085490; DOI=10.1371/journal.pone.0013830;
Murshid A., Chou S.D., Prince T., Zhang Y., Bharti A.,
Calderwood S.K.;
"Protein kinase A binds and activates heat shock factor 1.";
PLoS ONE 5:E13830-E13830(2010).
[27]
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).
[28]
FUNCTION AS RORA KINASE.
PubMed=21514275; DOI=10.1016/j.bbrc.2011.04.046;
Ermisch M., Firla B., Steinhilber D.;
"Protein kinase A activates and phosphorylates ROR?4 in vitro and
takes part in ROR? activation by CaMK-IV.";
Biochem. Biophys. Res. Commun. 408:442-446(2011).
[29]
FUNCTION AS KINASE, TISSUE SPECIFICITY, AND INTERACTION WITH
PRKAR1A/PKR1 AND PRKAR2A/PKR2.
PubMed=21812984; DOI=10.1186/1471-2091-12-40;
Vetter M.M., Zenn H.-M., Mendez E., van den Boom H., Herberg F.W.,
Skaalhegg B.S.;
"The testis-specific C?2 subunit of PKA is kinetically
indistinguishable from the common C?1 subunit of PKA.";
BMC Biochem. 12:40-40(2011).
[30]
FUNCTION, AND SUBCELLULAR LOCATION.
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).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339, 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).
[32]
MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=25255805; DOI=10.1038/ncomms5919;
Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U.,
Wright M.H., Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.;
"Global profiling of co- and post-translationally N-myristoylated
proteomes in human cells.";
Nat. Commun. 5:4919-4919(2014).
[33]
INVOLVEMENT IN PPNAD4, VARIANT PPNAD4 ARG-206, AND CHARACTERIZATION OF
VARIANT PPNAD4 ARG-206.
PubMed=24747643; DOI=10.1038/ng.2956;
Goh G., Scholl U.I., Healy J.M., Choi M., Prasad M.L.,
Nelson-Williams C., Kunstman J.W., Kuntsman J.W., Korah R.,
Suttorp A.C., Dietrich D., Haase M., Willenberg H.S., Staalberg P.,
Hellman P., Akerstroem G., Bjoerklund P., Carling T., Lifton R.P.;
"Recurrent activating mutation in PRKACA in cortisol-producing adrenal
tumors.";
Nat. Genet. 46:613-617(2014).
[34]
MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=25807930; DOI=10.1002/anie.201500342;
Broncel M., Serwa R.A., Ciepla P., Krause E., Dallman M.J.,
Magee A.I., Tate E.W.;
"Multifunctional reagents for quantitative proteome-wide analysis of
protein modification in human cells and dynamic profiling of protein
lipidation during vertebrate development.";
Angew. Chem. Int. Ed. 54:5948-5951(2015).
[35]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[36]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 15-351, AND PHOSPHORYLATION
AT THR-198 AND SER-339.
PubMed=16765046; DOI=10.1016/j.bmcl.2006.05.092;
Lin X., Murray J.M., Rico A.C., Wang M.X., Chu D.T., Zhou Y.,
Del Rosario M., Kaufman S., Ma S., Fang E., Crawford K.,
Jefferson A.B.;
"Discovery of 2-pyrimidyl-5-amidothiophenes as potent inhibitors for
AKT: synthesis and SAR studies.";
Bioorg. Med. Chem. Lett. 16:4163-4168(2006).
[37]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS), PHOSPHORYLATION AT THR-198 AND
SER-339, AND ENZYME REGULATION.
PubMed=20137943; DOI=10.1016/j.bmcl.2010.01.067;
Zeng Q., Allen J.G., Bourbeau M.P., Wang X., Yao G., Tadesse S.,
Rider J.T., Yuan C.C., Hong F.-T., Lee M.R., Zhang S., Lofgren J.A.,
Freeman D.J., Yang S., Li C., Tominey E., Huang X., Hoffman D.,
Yamane H.K., Fotsch C., Dominguez C., Hungate R., Zhang X.;
"Azole-based inhibitors of AKT/PKB for the treatment of cancer.";
Bioorg. Med. Chem. Lett. 20:1559-1564(2010).
[38]
X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS), PHOSPHORYLATION AT THR-198 AND
SER-339, AND ENZYME REGULATION.
PubMed=20481595; DOI=10.1021/jm1003842;
Freeman-Cook K.D., Autry C., Borzillo G., Gordon D.,
Barbacci-Tobin E., Bernardo V., Briere D., Clark T., Corbett M.,
Jakubczak J., Kakar S., Knauth E., Lippa B., Luzzio M.J., Mansour M.,
Martinelli G., Marx M., Nelson K., Pandit J., Rajamohan F.,
Robinson S., Subramanyam C., Wei L., Wythes M., Morris J.;
"Design of selective, ATP-competitive inhibitors of Akt.";
J. Med. Chem. 53:4615-4622(2010).
[39]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH ADENOSINE
ANALOG, PHOSPHORYLATION AT SER-11; THR-198 AND SER-339, AND ENZYME
REGULATION.
PubMed=20732331; DOI=10.1016/j.jmb.2010.08.028;
Pflug A., Rogozina J., Lavogina D., Enkvist E., Uri A., Engh R.A.,
Bossemeyer D.;
"Diversity of bisubstrate binding modes of adenosine analogue-
oligoarginine conjugates in protein kinase a and implications for
protein substrate interactions.";
J. Mol. Biol. 403:66-77(2010).
[40]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH AURORA KINASE
INHIBITORS, PHOSPHORYLATION AT SER-11; THR-198 AND SER-339, AND
MUTAGENESIS OF LYS-48; LEU-96; MET-121; VAL-124; GLN-182 AND THR-184.
PubMed=21774789; DOI=10.1042/BJ20110592;
Pflug A., de Oliveira T.M., Bossemeyer D., Engh R.A.;
"Mutants of protein kinase A that mimic the ATP-binding site of Aurora
kinase.";
Biochem. J. 440:85-93(2011).
[41]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS), AND PHOSPHORYLATION AT THR-198
AND SER-339.
Behnen J., Koester H., Ritschel T., Neudert G., Heine A., Klebe G.;
"Experimental active site mapping as a starting point to fragment-
based lead discovery.";
Submitted (JUL-2010) to the PDB data bank.
[42]
X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS).
Koester H., Craan T., Brass S., Heine A., Klebe G.;
"Fragment based drug design on PKA.";
Submitted (SEP-2010) to the PDB data bank.
[43]
VARIANTS [LARGE SCALE ANALYSIS] VAL-41; GLN-46 AND CYS-264.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
[44]
VARIANT PPNAD4 ARG-206, AND CHARACTERIZATION OF VARIANT PPNAD4
ARG-206.
PubMed=24571724; DOI=10.1056/NEJMoa1310359;
Beuschlein F., Fassnacht M., Assie G., Calebiro D., Stratakis C.A.,
Osswald A., Ronchi C.L., Wieland T., Sbiera S., Faucz F.R., Schaak K.,
Schmittfull A., Schwarzmayr T., Barreau O., Vezzosi D., Rizk-Rabin M.,
Zabel U., Szarek E., Salpea P., Forlino A., Vetro A., Zuffardi O.,
Kisker C., Diener S., Meitinger T., Lohse M.J., Reincke M.,
Bertherat J., Strom T.M., Allolio B.;
"Constitutive activation of PKA catalytic subunit in adrenal Cushing's
syndrome.";
N. Engl. J. Med. 370:1019-1028(2014).
[45]
VARIANT PPNAD4 ARG-206, AND CHARACTERIZATION OF VARIANT PPNAD4
ARG-206.
PubMed=24700472; DOI=10.1126/science.1249480;
Cao Y., He M., Gao Z., Peng Y., Li Y., Li L., Zhou W., Li X.,
Zhong X., Lei Y., Su T., Wang H., Jiang Y., Yang L., Wei W., Yang X.,
Jiang X., Liu L., He J., Ye J., Wei Q., Li Y., Wang W., Wang J.,
Ning G.;
"Activating hotspot L205R mutation in PRKACA and adrenal Cushing's
syndrome.";
Science 344:913-917(2014).
[46]
VARIANT PPNAD4 ARG-206, AND CHARACTERIZATION OF VARIANT PPNAD4
ARG-206.
PubMed=24855271; DOI=10.1126/science.1252328;
Sato Y., Maekawa S., Ishii R., Sanada M., Morikawa T., Shiraishi Y.,
Yoshida K., Nagata Y., Sato-Otsubo A., Yoshizato T., Suzuki H.,
Shiozawa Y., Kataoka K., Kon A., Aoki K., Chiba K., Tanaka H.,
Kume H., Miyano S., Fukayama M., Nureki O., Homma Y., Ogawa S.;
"Recurrent somatic mutations underlie corticotropin-independent
Cushing's syndrome.";
Science 344:917-920(2014).
-!- FUNCTION: Phosphorylates a large number of substrates in the
cytoplasm and the nucleus. Regulates the abundance of
compartmentalized pools of its regulatory subunits through
phosphorylation of PJA2 which binds and ubiquitinates these
subunits, leading to their subsequent proteolysis. Phosphorylates
CDC25B, ABL1, NFKB1, CLDN3, PSMC5/RPT6, PJA2, RYR2, RORA and VASP.
RORA is activated by phosphorylation. Required for glucose-
mediated adipogenic differentiation increase and osteogenic
differentiation inhibition from osteoblasts. Involved in the
regulation of platelets in response to thrombin and collagen;
maintains circulating platelets in a resting state by
phosphorylating proteins in numerous platelet inhibitory pathways
when in complex with NF-kappa-B (NFKB1 and NFKB2) and I-kappa-B-
alpha (NFKBIA), but thrombin and collagen disrupt these complexes
and free active PRKACA stimulates platelets and leads to platelet
aggregation by phosphorylating VASP. Prevents the
antiproliferative and anti-invasive effects of alpha-
difluoromethylornithine in breast cancer cells when activated.
RYR2 channel activity is potentiated by phosphorylation in
presence of luminal Ca(2+), leading to reduced amplitude and
increased frequency of store overload-induced Ca(2+) release
(SOICR) characterized by an increased rate of Ca(2+) release and
propagation velocity of spontaneous Ca(2+) waves, despite reduced
wave amplitude and resting cytosolic Ca(2+). PSMC5/RPT6 activation
by phosphorylation stimulates proteasome. Negatively regulates
tight junctions (TJs) in ovarian cancer cells via CLDN3
phosphorylation. NFKB1 phosphorylation promotes NF-kappa-B p50-p50
DNA binding. Involved in embryonic development by down-regulating
the Hedgehog (Hh) signaling pathway that determines embryo pattern
formation and morphogenesis. Prevents meiosis resumption in
prophase-arrested oocytes via CDC25B inactivation by
phosphorylation. May also regulate rapid eye movement (REM) sleep
in the pedunculopontine tegmental (PPT). Phosphorylates APOBEC3G
and AICDA. Isoform 2 phosphorylates and activates ABL1 in sperm
flagellum to promote spermatozoa capacitation. Phosphorylates
HSF1; this phosphorylation promotes HSF1 nuclear localization and
transcriptional activity upon heat shock (PubMed:21085490).
{ECO:0000269|PubMed:15642694, ECO:0000269|PubMed:15905176,
ECO:0000269|PubMed:16387847, ECO:0000269|PubMed:17333334,
ECO:0000269|PubMed:17565987, ECO:0000269|PubMed:17693412,
ECO:0000269|PubMed:18836454, ECO:0000269|PubMed:19949837,
ECO:0000269|PubMed:20356841, ECO:0000269|PubMed:21085490,
ECO:0000269|PubMed:21423175, ECO:0000269|PubMed:21514275,
ECO:0000269|PubMed:21812984}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ENZYME REGULATION: Allosterically activated by various compounds,
including ATP. Activated by cAMP; the nucleotide acts as a dynamic
and allosteric activator by coupling the two lobes of apo PKA,
enhancing the enzyme dynamics synchronously and priming it for
catalysis. Inhibited by H89 (N-[2-[[3-(4-Bromophenyl)-2-
propenyl]amino]ethyl]-5-isoquinolinesulfonamide), spiroindoline,
azole-based inhibitors, (3s)-amino-aminomethylbenzamide analogs,
ARC-1032 (6-{[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-
dihydroxyoxolan-2-yl]formamido}-N-[(1R)-4-carbamimidamido-1-
carbamoylbutyl]hexanamide), ARC-1034 (6-{[(2S,3S,4R,5R)-5-(6-
amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]formamido}-N-[(1R)-
4-carbamimidamido-1-{[(1R)-4-carbamimidamido-1-
carbamoylbutyl]carbamoyl}butyl]hexanamide), ARC-582, ARC-902 (Adc-
6-aminohexanoic acid-(D-Arg)(6)-NH(2)), ARC-1012 ((2R)-6-amino-2-
(6-{[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-
2-yl]formamido}hexanamido)-N-(5-{[(1R)-4-carbamimidamido-1-{[(1R)-
4-carbamimidamido-1-
carbamoylbutyl]carbamoyl}butyl]carbamoyl}pentyl)hexanamide) and
ARC-1039 (6-{[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-
dihydroxyoxolan-2-yl]formamido}-N-[(1R)-1-[(5-{[(1R)-4-
carbamimidamido-1-{[(1R)-4-carbamimidamido-1-
carbamoylbutyl]carbamoyl}butyl]carbamoyl}pentyl)carbamoyl]ethyl]he
xanamide). {ECO:0000269|PubMed:17909264,
ECO:0000269|PubMed:18178622, ECO:0000269|PubMed:19949837,
ECO:0000269|PubMed:20137943, ECO:0000269|PubMed:20481595,
ECO:0000269|PubMed:20732331}.
-!- SUBUNIT: A number of inactive tetrameric holoenzymes are produced
by the combination of homo- or heterodimers of the different
regulatory subunits associated with two catalytic subunits. cAMP
causes the dissociation of the inactive holoenzyme into a dimer of
regulatory subunits bound to four cAMP and two free monomeric
catalytic subunits. The cAMP-dependent protein kinase catalytic
subunit binds PJA2. Both isoforms 1 and 2 forms activate cAMP-
sensitive PKAI and PKAII holoenzymes by interacting with
regulatory subunit (R) of PKA, PRKAR1A/PKR1 and PRKAR2A/PKR2,
respectively. Interacts with NFKB1, NFKB2 and NFKBIA in platelets;
these interactions are disrupted by thrombin and collagen. Binds
to ABL1 in spermatozoa and with CDC25B in oocytes. Interacts with
APOBEC3G and AICDA. Interacts with RAB13; downstream effector of
RAB13 involved in tight junction assembly. Found in a complex at
least composed of MROH2B, PRKACA isoform 2 and TCP11 (By
similarity). Interacts with MROH2B (By similarity). Isoform 2
interacts with TCP11 (By similarity). Interacts with HSF1
(PubMed:21085490). {ECO:0000250|UniProtKB:P05132,
ECO:0000269|PubMed:15096524, ECO:0000269|PubMed:16387847,
ECO:0000269|PubMed:18836454, ECO:0000269|PubMed:20356841,
ECO:0000269|PubMed:20732331, ECO:0000269|PubMed:21085490,
ECO:0000269|PubMed:21774789, ECO:0000269|PubMed:21812984}.
-!- INTERACTION:
Q9GZX7:AICDA; NbExp=3; IntAct=EBI-476586, EBI-3834328;
Q9NQ31:AKIP1; NbExp=4; IntAct=EBI-476586, EBI-517035;
P09917:ALOX5; NbExp=2; IntAct=EBI-476586, EBI-79934;
Q9HC16:APOBEC3G; NbExp=6; IntAct=EBI-476586, EBI-717839;
P59215:Gnao1 (xeno); NbExp=4; IntAct=EBI-476586, EBI-8071125;
P49841:GSK3B; NbExp=5; IntAct=EBI-476586, EBI-373586;
Q5S007:LRRK2; NbExp=6; IntAct=EBI-476586, EBI-5323863;
P10644:PRKAR1A; NbExp=8; IntAct=EBI-476586, EBI-476431;
P31321:PRKAR1B; NbExp=4; IntAct=EBI-476586, EBI-2805516;
P31323:PRKAR2B; NbExp=10; IntAct=EBI-476586, EBI-2930670;
P12369:Prkar2b (xeno); NbExp=2; IntAct=EBI-476586, EBI-6096160;
-!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Nucleus
{ECO:0000250}. Mitochondrion {ECO:0000250}. Membrane
{ECO:0000305}; Lipid-anchor {ECO:0000305}. Note=Translocates into
the nucleus (monomeric catalytic subunit). The inactive holoenzyme
is found in the cytoplasm. Distributed throughout the cytoplasm in
meiotically incompetent oocytes. Associated to mitochondrion as
meiotic competence is acquired. Aggregates around the germinal
vesicles (GV) at the immature GV stage oocytes (By similarity).
Colocalizes with HSF1 in nuclear stress bodies (nSBs) upon heat
shock (PubMed:21085490). {ECO:0000250,
ECO:0000269|PubMed:21085490}.
-!- SUBCELLULAR LOCATION: Isoform 2: Cell projection, cilium,
flagellum {ECO:0000269|PubMed:10906071}. Cytoplasmic vesicle,
secretory vesicle, acrosome {ECO:0000250|UniProtKB:P05132}.
Note=Expressed in the midpiece region of the sperm flagellum
(PubMed:10906071). Colocalizes with MROH2B and TCP11 on the
acrosome and tail regions in round spermatids and spermatozoa
regardless of the capacitation status of the sperm (By
similarity). {ECO:0000250|UniProtKB:P05132,
ECO:0000269|PubMed:10906071}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=C-alpha-1;
IsoId=P17612-1; Sequence=Displayed;
Name=2; Synonyms=C-alpha-2, C-alpha-S, C(s);
IsoId=P17612-2; Sequence=VSP_004759;
-!- TISSUE SPECIFICITY: Isoform 1 is ubiquitous. Isoform 2 is sperm-
specific and is enriched in pachytene spermatocytes but is not
detected in round spermatids. {ECO:0000269|PubMed:10906071,
ECO:0000269|PubMed:21812984}.
-!- PTM: Asn-3 is partially deaminated to Asp giving rise to 2 major
isoelectric variants, called CB and CA respectively.
{ECO:0000250}.
-!- PTM: Autophosphorylated. Phosphorylation is enhanced by vitamin
K(2). Phosphorylated on threonine and serine residues.
Phosphorylation on Thr-198 is required for full activity.
{ECO:0000269|PubMed:12372837, ECO:0000269|PubMed:16765046,
ECO:0000269|PubMed:17909264, ECO:0000269|PubMed:20137943,
ECO:0000269|PubMed:20481595, ECO:0000269|PubMed:20732331,
ECO:0000269|PubMed:21774789, ECO:0000269|Ref.41}.
-!- PTM: Phosphorylated at Tyr-331 by activated receptor tyrosine
kinases EGFR and PDGFR; this increases catalytic efficienncy.
{ECO:0000250}.
-!- DISEASE: Primary pigmented nodular adrenocortical disease 4
(PPNAD4) [MIM:615830]: 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. Adrenal glands show overall normal size
and weight, and multiple small yellow-to-dark brown nodules
surrounded by a cortex with a uniform appearance. Microscopically,
there are moderate diffuse cortical hyperplasia with mostly
nonpigmented nodules, multiple capsular deficits and massive
circumscribed and infiltrating extra-adrenal cortical excrescences
with micronodules. Clinical manifestations of Cushing syndrome
include facial and truncal obesity, abdominal striae, muscular
weakness, osteoporosis, arterial hypertension, diabetes.
{ECO:0000269|PubMed:24571724, ECO:0000269|PubMed:24700472,
ECO:0000269|PubMed:24747643, ECO:0000269|PubMed:24855271}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. cAMP subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/prkaca/";
-----------------------------------------------------------------------
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EMBL; X07767; CAA30597.1; -; mRNA.
EMBL; AK290147; BAF82836.1; -; mRNA.
EMBL; DQ667173; ABG25918.1; -; Genomic_DNA.
EMBL; CH471106; EAW84399.1; -; Genomic_DNA.
EMBL; BC039846; AAH39846.1; -; mRNA.
EMBL; BC108259; AAI08260.1; -; mRNA.
EMBL; AF208004; AAG35720.1; -; mRNA.
EMBL; AF239744; AAF76426.1; -; mRNA.
EMBL; AF224718; AAF75622.1; -; mRNA.
CCDS; CCDS12304.1; -. [P17612-1]
CCDS; CCDS12305.1; -. [P17612-2]
PIR; S01404; OKHU2C.
RefSeq; NP_001291278.1; NM_001304349.1.
RefSeq; NP_002721.1; NM_002730.3. [P17612-1]
RefSeq; NP_997401.1; NM_207518.2. [P17612-2]
UniGene; Hs.631630; -.
PDB; 2GU8; X-ray; 2.20 A; A=15-351.
PDB; 3AGL; X-ray; 2.10 A; A/B=1-351.
PDB; 3AGM; X-ray; 2.00 A; A=1-351.
PDB; 3AMA; X-ray; 1.75 A; A=1-351.
PDB; 3AMB; X-ray; 2.25 A; A=1-351.
PDB; 3L9L; X-ray; 2.00 A; A/B=1-351.
PDB; 3L9M; X-ray; 1.90 A; A/B=1-351.
PDB; 3L9N; X-ray; 2.00 A; A=1-351.
PDB; 3MVJ; X-ray; 2.49 A; A/B/E=1-351.
PDB; 3NX8; X-ray; 2.00 A; A=1-351.
PDB; 3OOG; X-ray; 2.00 A; A=1-351.
PDB; 3OVV; X-ray; 1.58 A; A=1-351.
PDB; 3OWP; X-ray; 1.88 A; A=1-351.
PDB; 3OXT; X-ray; 2.20 A; A=1-351.
PDB; 3P0M; X-ray; 2.03 A; A=1-351.
PDB; 3POO; X-ray; 1.60 A; A=1-351.
PDB; 3VQH; X-ray; 1.95 A; A=1-351.
PDB; 4AE6; X-ray; 2.10 A; A/B=16-351.
PDB; 4AE9; X-ray; 2.30 A; A/B=16-351.
PDB; 4UJ1; X-ray; 1.77 A; A=1-351.
PDB; 4UJ2; X-ray; 2.02 A; A=1-351.
PDB; 4UJ9; X-ray; 1.87 A; A=1-351.
PDB; 4UJA; X-ray; 1.93 A; A=1-351.
PDB; 4UJB; X-ray; 1.95 A; A=1-351.
PDB; 4WB5; X-ray; 1.64 A; A=2-351.
PDB; 4WB6; X-ray; 2.10 A; A/B=2-351.
PDB; 4WB7; X-ray; 1.90 A; A/B=16-351.
PDB; 4WB8; X-ray; 1.55 A; A=16-351.
PDB; 5BX6; X-ray; 1.89 A; A=1-351.
PDB; 5BX7; X-ray; 1.89 A; A=1-350.
PDB; 5IZF; X-ray; 2.10 A; A=1-351.
PDB; 5IZJ; X-ray; 1.85 A; A/B=1-351.
PDB; 5J5X; X-ray; 2.60 A; A=1-351.
PDBsum; 2GU8; -.
PDBsum; 3AGL; -.
PDBsum; 3AGM; -.
PDBsum; 3AMA; -.
PDBsum; 3AMB; -.
PDBsum; 3L9L; -.
PDBsum; 3L9M; -.
PDBsum; 3L9N; -.
PDBsum; 3MVJ; -.
PDBsum; 3NX8; -.
PDBsum; 3OOG; -.
PDBsum; 3OVV; -.
PDBsum; 3OWP; -.
PDBsum; 3OXT; -.
PDBsum; 3P0M; -.
PDBsum; 3POO; -.
PDBsum; 3VQH; -.
PDBsum; 4AE6; -.
PDBsum; 4AE9; -.
PDBsum; 4UJ1; -.
PDBsum; 4UJ2; -.
PDBsum; 4UJ9; -.
PDBsum; 4UJA; -.
PDBsum; 4UJB; -.
PDBsum; 4WB5; -.
PDBsum; 4WB6; -.
PDBsum; 4WB7; -.
PDBsum; 4WB8; -.
PDBsum; 5BX6; -.
PDBsum; 5BX7; -.
PDBsum; 5IZF; -.
PDBsum; 5IZJ; -.
PDBsum; 5J5X; -.
ProteinModelPortal; P17612; -.
SMR; P17612; -.
BioGrid; 111553; 148.
CORUM; P17612; -.
DIP; DIP-33878N; -.
ELM; P17612; -.
IntAct; P17612; 88.
MINT; MINT-95365; -.
STRING; 9606.ENSP00000309591; -.
BindingDB; P17612; -.
ChEMBL; CHEMBL4101; -.
DrugBank; DB07107; (1S)-2-(1H-INDOL-3-YL)-1-[({5-[(E)-2-PYRIDIN-4-YLVINYL]PYRIDIN-3-YL}OXY)METHYL]ETHYLAMINE.
DrugBank; DB06959; (1S)-2-(1H-INDOL-3-YL)-1-{[(5-ISOQUINOLIN-6-YLPYRIDIN-3-YL)OXY]METHYL}ETHYLAMINE.
DrugBank; DB07857; (2R)-2-(4-CHLOROPHENYL)-2-[4-(1H-PYRAZOL-4-YL)PHENYL]ETHANAMINE.
DrugBank; DB07860; (2R)-2-(4-CHLOROPHENYL)-2-PHENYLETHANAMINE.
DrugBank; DB08073; (2S)-1-(1H-INDOL-3-YL)-3-{[5-(3-METHYL-1H-INDAZOL-5-YL)PYRIDIN-3-YL]OXY}PROPAN-2-AMINE.
DrugBank; DB06977; (2S)-1-{[5-(1H-INDAZOL-5-YL)PYRIDIN-3-YL]OXY}-3-[(7AS)-7AH-INDOL-3-YL]PROPAN-2-AMINE.
DrugBank; DB08568; (2S)-1-{[5-(3-METHYL-1H-INDAZOL-5-YL)PYRIDIN-3-YL]OXY}-3-PHENYLPROPAN-2-AMINE.
DrugBank; DB07858; (2S)-2-(4-CHLOROPHENYL)-2-[4-(1H-PYRAZOL-4-YL)PHENYL]ETHANAMINE.
DrugBank; DB08756; (R)-TRANS-4-(1-AMINOETHYL)-N-(4-PYRIDYL) CYCLOHEXANECARBOXAMIDE.
DrugBank; DB07855; (S)-1-PHENYL-1-[4-(9H-PURIN-6-YL)PHENYL]METHANAMINE.
DrugBank; DB07876; (S)-2-METHYL-1-[(4-METHYL-5-ISOQUINOLINE)SULFONYL]-HOMOPIPERAZINE.
DrugBank; DB08070; 2-[4-(3-METHYL-1H-PYRAZOL-4-YL)PHENYL]ETHANAMINE.
DrugBank; DB08113; 3-pyridin-4-yl-1H-indazole.
DrugBank; DB07859; 4-(4-CHLOROPHENYL)-4-[4-(1H-PYRAZOL-4-YL)PHENYL]PIPERIDINE.
DrugBank; DB07996; 5-(2-methylpiperazine-1-sulfonyl)isoquinoline.
DrugBank; DB07856; 6-{4-[4-(4-CHLOROPHENYL)PIPERIDIN-4-YL]PHENYL}-9H-PURINE.
DrugBank; DB04098; Balanol.
DrugBank; DB02611; Balanol Analog 1.
DrugBank; DB01940; Balanol Analog 2.
DrugBank; DB02155; Balanol Analog 8.
DrugBank; DB08846; Ellagic Acid.
DrugBank; DB04707; HYDROXYFASUDIL.
DrugBank; DB07947; ISOQUINOLINE-5-SULFONIC ACID (2-(2-(4-CHLOROBENZYLOXY)ETHYLAMINO)ETHYL)AMIDE.
DrugBank; DB08231; MYRISTIC ACID.
DrugBank; DB07995; N-[2-(4-BROMOCINNAMYLAMINO)ETHYL]-5-ISOQUINOLINE SULFONAMIDE.
DrugBank; DB07997; N-[2-(METHYLAMINO)ETHYL]-5-ISOQUINOLINESULFONAMIDE.
DrugBank; DB07854; N-METHYL-1-[4-(9H-PURIN-6-YL)PHENYL]METHANAMINE.
DrugBank; DB01919; Pentanal.
DrugBank; DB04522; Phosphonoserine.
DrugBank; DB02482; Phosphonothreonine.
GuidetoPHARMACOLOGY; 1476; -.
iPTMnet; P17612; -.
PhosphoSitePlus; P17612; -.
SwissPalm; P17612; -.
BioMuta; PRKACA; -.
DMDM; 125205; -.
EPD; P17612; -.
MaxQB; P17612; -.
PaxDb; P17612; -.
PeptideAtlas; P17612; -.
PRIDE; P17612; -.
DNASU; 5566; -.
Ensembl; ENST00000308677; ENSP00000309591; ENSG00000072062. [P17612-1]
Ensembl; ENST00000589994; ENSP00000466651; ENSG00000072062. [P17612-2]
GeneID; 5566; -.
KEGG; hsa:5566; -.
UCSC; uc002myb.4; human. [P17612-1]
CTD; 5566; -.
DisGeNET; 5566; -.
EuPathDB; HostDB:ENSG00000072062.13; -.
GeneCards; PRKACA; -.
HGNC; HGNC:9380; PRKACA.
HPA; CAB010361; -.
HPA; HPA071185; -.
MalaCards; PRKACA; -.
MIM; 601639; gene.
MIM; 615830; phenotype.
neXtProt; NX_P17612; -.
OpenTargets; ENSG00000072062; -.
Orphanet; 401920; Fibrolamellar hepatocellular carcinoma.
PharmGKB; PA33748; -.
eggNOG; KOG0616; Eukaryota.
eggNOG; ENOG410XPQQ; LUCA.
GeneTree; ENSGT00810000125385; -.
HOGENOM; HOG000233033; -.
HOVERGEN; HBG108317; -.
InParanoid; P17612; -.
KO; K04345; -.
OMA; GQHFAMK; -.
OrthoDB; EOG091G10O8; -.
PhylomeDB; P17612; -.
TreeFam; TF313399; -.
BRENDA; 2.7.11.11; 2681.
Reactome; R-HSA-111931; PKA-mediated phosphorylation of CREB.
Reactome; R-HSA-163358; PKA-mediated phosphorylation of key metabolic factors.
Reactome; R-HSA-163560; Triglyceride catabolism.
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-2565942; Regulation of PLK1 Activity at G2/M Transition.
Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
Reactome; R-HSA-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
Reactome; R-HSA-392517; Rap1 signalling.
Reactome; R-HSA-422356; Regulation of insulin secretion.
Reactome; R-HSA-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-HSA-442720; CREB phosphorylation through the activation of Adenylate Cyclase.
Reactome; R-HSA-512988; Interleukin-3, 5 and GM-CSF signaling.
Reactome; R-HSA-5578775; Ion homeostasis.
Reactome; R-HSA-5610780; Degradation of GLI1 by the proteasome.
Reactome; R-HSA-5610783; Degradation of GLI2 by the proteasome.
Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome.
Reactome; R-HSA-5610787; Hedgehog 'off' state.
Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
Reactome; R-HSA-5621575; CD209 (DC-SIGN) signaling.
Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
Reactome; R-HSA-70171; Glycolysis.
Reactome; R-HSA-8853659; RET signaling.
Reactome; R-HSA-8854518; AURKA Activation by TPX2.
Reactome; R-HSA-8963896; HDL assembly.
Reactome; R-HSA-9010642; ROBO receptors bind AKAP5.
Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
SABIO-RK; P17612; -.
SignaLink; P17612; -.
SIGNOR; P17612; -.
ChiTaRS; PRKACA; human.
EvolutionaryTrace; P17612; -.
GeneWiki; PRKACA; -.
GenomeRNAi; 5566; -.
PRO; PR:P17612; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000072062; -.
CleanEx; HS_PRKACA; -.
ExpressionAtlas; P17612; baseline and differential.
Genevisible; P17612; HS.
GO; GO:0001669; C:acrosomal vesicle; ISS:UniProtKB.
GO; GO:0034704; C:calcium channel complex; TAS:BHF-UCL.
GO; GO:0005952; C:cAMP-dependent protein kinase complex; IDA:UniProtKB.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0097546; C:ciliary base; TAS:Reactome.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0045171; C:intercellular bridge; IDA:HPA.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0031588; C:nucleotide-activated protein kinase complex; IDA:BHF-UCL.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0044853; C:plasma membrane raft; IDA:UniProtKB.
GO; GO:0036126; C:sperm flagellum; IEA:Ensembl.
GO; GO:0097225; C:sperm midpiece; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004691; F:cAMP-dependent protein kinase activity; IDA:BHF-UCL.
GO; GO:0000287; F:magnesium ion binding; IEA:Ensembl.
GO; GO:0030145; F:manganese ion binding; IEA:Ensembl.
GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
GO; GO:0034237; F:protein kinase A regulatory subunit binding; IPI:BHF-UCL.
GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IDA:MGI.
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:0035584; P:calcium-mediated signaling using intracellular calcium source; TAS:BHF-UCL.
GO; GO:0086064; P:cell communication by electrical coupling involved in cardiac conduction; TAS:BHF-UCL.
GO; GO:0071872; P:cellular response to epinephrine stimulus; TAS:BHF-UCL.
GO; GO:0071377; P:cellular response to glucagon stimulus; TAS:Reactome.
GO; GO:0071333; P:cellular response to glucose stimulus; IDA:UniProtKB.
GO; GO:0034605; P:cellular response to heat; IDA:UniProtKB.
GO; GO:0071374; P:cellular response to parathyroid hormone stimulus; IEA:Ensembl.
GO; GO:0097711; P:ciliary basal body-plasma membrane docking; TAS:Reactome.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0034380; P:high-density lipoprotein particle assembly; TAS:Reactome.
GO; GO:0001707; P:mesoderm formation; IEA:Ensembl.
GO; GO:0050804; P:modulation of chemical synaptic transmission; IEA:Ensembl.
GO; GO:0006397; P:mRNA processing; IDA:UniProtKB.
GO; GO:1901621; P:negative regulation of smoothened signaling pathway involved in dorsal/ventral neural tube patterning; IEA:Ensembl.
GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:BHF-UCL.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; IEA:Ensembl.
GO; GO:0071158; P:positive regulation of cell cycle arrest; ISS:UniProtKB.
GO; GO:0046827; P:positive regulation of protein export from nucleus; IEA:Ensembl.
GO; GO:0046777; P:protein autophosphorylation; IEA:Ensembl.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:2000810; P:regulation of bicellular tight junction assembly; IDA:UniProtKB.
GO; GO:1903779; P:regulation of cardiac conduction; TAS:Reactome.
GO; GO:0055117; P:regulation of cardiac muscle contraction; TAS:BHF-UCL.
GO; GO:0010881; P:regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion; TAS:BHF-UCL.
GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; TAS:BHF-UCL.
GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0002027; P:regulation of heart rate; TAS:BHF-UCL.
GO; GO:0016241; P:regulation of macroautophagy; TAS:ParkinsonsUK-UCL.
GO; GO:0045667; P:regulation of osteoblast differentiation; IDA:UniProtKB.
GO; GO:0061136; P:regulation of proteasomal protein catabolic process; IDA:UniProtKB.
GO; GO:0043393; P:regulation of protein binding; TAS:BHF-UCL.
GO; GO:0070613; P:regulation of protein processing; IEA:Ensembl.
GO; GO:0060314; P:regulation of ryanodine-sensitive calcium-release channel activity; TAS:BHF-UCL.
GO; GO:0003091; P:renal water homeostasis; TAS:Reactome.
GO; GO:0048240; P:sperm capacitation; ISS:UniProtKB.
GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
InterPro; IPR000961; AGC-kinase_C.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00133; S_TK_X; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51285; AGC_KINASE_CTER; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; cAMP; Cell membrane;
Cell projection; Cilium; Complete proteome; Cushing syndrome;
Cytoplasm; Cytoplasmic vesicle; Disease mutation; Flagellum; Kinase;
Lipoprotein; Membrane; Mitochondrion; Myristate; Nucleotide-binding;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
Serine/threonine-protein kinase; Transferase.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:25255805,
ECO:0000269|PubMed:25807930}.
CHAIN 2 351 cAMP-dependent protein kinase catalytic
subunit alpha.
/FTId=PRO_0000086052.
DOMAIN 44 298 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 299 351 AGC-kinase C-terminal.
NP_BIND 50 58 ATP.
NP_BIND 122 128 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 169 172 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 167 167 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 73 73 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 3 3 Deamidated asparagine. {ECO:0000250}.
MOD_RES 11 11 Phosphoserine; by autocatalysis.
{ECO:0000250|UniProtKB:P05132}.
MOD_RES 49 49 Phosphothreonine.
{ECO:0000244|PubMed:18691976}.
MOD_RES 140 140 Phosphoserine.
{ECO:0000250|UniProtKB:P05132}.
MOD_RES 196 196 Phosphothreonine.
{ECO:0000269|PubMed:12372837}.
MOD_RES 198 198 Phosphothreonine; by PDPK1.
{ECO:0000269|PubMed:12372837,
ECO:0000269|PubMed:16765046,
ECO:0000269|PubMed:20137943,
ECO:0000269|PubMed:20481595,
ECO:0000269|PubMed:20732331,
ECO:0000269|PubMed:21774789,
ECO:0000269|Ref.41}.
MOD_RES 202 202 Phosphothreonine.
{ECO:0000269|PubMed:17909264}.
MOD_RES 331 331 Phosphotyrosine.
{ECO:0000250|UniProtKB:P05132}.
MOD_RES 339 339 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:16765046,
ECO:0000269|PubMed:20137943,
ECO:0000269|PubMed:20481595,
ECO:0000269|PubMed:20732331,
ECO:0000269|PubMed:21774789,
ECO:0000269|Ref.41}.
LIPID 2 2 N-myristoyl glycine.
{ECO:0000269|PubMed:25255805,
ECO:0000269|PubMed:25807930}.
VAR_SEQ 1 15 MGNAAAAKKGSEQES -> MASNSSD (in isoform
2). {ECO:0000303|PubMed:10841548,
ECO:0000303|PubMed:10906071,
ECO:0000303|PubMed:10982398}.
/FTId=VSP_004759.
VARIANT 41 41 L -> V (in dbSNP:rs56029020).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040591.
VARIANT 46 46 R -> Q (in dbSNP:rs56085217).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040592.
VARIANT 206 206 L -> R (in PPNAD4; somatic mutation; the
mutation results in cAMP-independent
basal protein kinase activity and
constitutive activation of protein kinase
A; dbSNP:rs386352352).
{ECO:0000269|PubMed:24571724,
ECO:0000269|PubMed:24700472,
ECO:0000269|PubMed:24747643,
ECO:0000269|PubMed:24855271}.
/FTId=VAR_071707.
VARIANT 264 264 S -> C (in dbSNP:rs35635531).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040593.
MUTAGEN 48 48 K->R: Enhanced basal kinase activity;
when associated with Q-96, L-121, A-124,
K-182 and A-184.
{ECO:0000269|PubMed:21774789}.
MUTAGEN 96 96 L->Q: Enhanced basal kinase activity;
when associated with R-48, L-121, A-124,
K-182 and A-184.
{ECO:0000269|PubMed:21774789}.
MUTAGEN 121 121 M->L: Enhanced basal kinase activity;
when associated with R-48, Q-96, A-124,
K-182 and A-184.
{ECO:0000269|PubMed:21774789}.
MUTAGEN 124 124 V->A: Enhanced basal kinase activity;
when associated with R-48, Q-96, L-121,
K-182 and A-184.
{ECO:0000269|PubMed:21774789}.
MUTAGEN 182 182 Q->K: Enhanced basal kinase activity;
when associated with R-48, Q-96, L-121,
A-124 and A-184.
{ECO:0000269|PubMed:21774789}.
MUTAGEN 184 184 T->A: Enhanced basal kinase activity;
when associated with R-48, Q-96, L-121,
A-124 and K-182.
{ECO:0000269|PubMed:21774789}.
MUTAGEN 195 195 R->A: No phosphorylation.
{ECO:0000269|PubMed:12372837}.
MUTAGEN 201 201 G->A: No phosphorylation.
{ECO:0000269|PubMed:12372837}.
MUTAGEN 202 202 T->A: No phosphorylation.
{ECO:0000269|PubMed:12372837}.
MUTAGEN 205 205 Y->A: Loss of allosteric regulation.
{ECO:0000269|PubMed:18178622}.
HELIX 3 6 {ECO:0000244|PDB:3AMA}.
HELIX 16 32 {ECO:0000244|PDB:4WB8}.
HELIX 41 43 {ECO:0000244|PDB:4WB8}.
STRAND 44 52 {ECO:0000244|PDB:4WB8}.
STRAND 57 63 {ECO:0000244|PDB:4WB8}.
TURN 64 66 {ECO:0000244|PDB:4WB8}.
STRAND 69 76 {ECO:0000244|PDB:4WB8}.
HELIX 77 82 {ECO:0000244|PDB:4WB8}.
HELIX 86 98 {ECO:0000244|PDB:4WB8}.
STRAND 107 112 {ECO:0000244|PDB:4WB8}.
STRAND 114 122 {ECO:0000244|PDB:4WB8}.
HELIX 129 136 {ECO:0000244|PDB:4WB8}.
HELIX 141 160 {ECO:0000244|PDB:4WB8}.
HELIX 170 172 {ECO:0000244|PDB:4WB8}.
STRAND 173 175 {ECO:0000244|PDB:4WB8}.
STRAND 181 183 {ECO:0000244|PDB:4WB8}.
HELIX 186 188 {ECO:0000244|PDB:4UJ2}.
HELIX 203 205 {ECO:0000244|PDB:4WB8}.
HELIX 208 211 {ECO:0000244|PDB:4WB8}.
STRAND 212 214 {ECO:0000244|PDB:5IZJ}.
HELIX 219 234 {ECO:0000244|PDB:4WB8}.
HELIX 244 253 {ECO:0000244|PDB:4WB8}.
HELIX 264 273 {ECO:0000244|PDB:4WB8}.
TURN 278 280 {ECO:0000244|PDB:4WB8}.
TURN 282 284 {ECO:0000244|PDB:5IZF}.
TURN 286 289 {ECO:0000244|PDB:4WB8}.
HELIX 290 293 {ECO:0000244|PDB:4WB8}.
HELIX 296 298 {ECO:0000244|PDB:4WB8}.
HELIX 303 307 {ECO:0000244|PDB:4WB8}.
TURN 345 350 {ECO:0000244|PDB:4WB8}.
SEQUENCE 351 AA; 40590 MW; BF6D3ECD2614E5AB CRC64;
MGNAAAAKKG SEQESVKEFL AKAKEDFLKK WESPAQNTAH LDQFERIKTL GTGSFGRVML
VKHKETGNHY AMKILDKQKV VKLKQIEHTL NEKRILQAVN FPFLVKLEFS FKDNSNLYMV
MEYVPGGEMF SHLRRIGRFS EPHARFYAAQ IVLTFEYLHS LDLIYRDLKP ENLLIDQQGY
IQVTDFGFAK RVKGRTWTLC GTPEYLAPEI ILSKGYNKAV DWWALGVLIY EMAAGYPPFF
ADQPIQIYEK IVSGKVRFPS HFSSDLKDLL RNLLQVDLTK RFGNLKNGVN DIKNHKWFAT
TDWIAIYQRK VEAPFIPKFK GPGDTSNFDD YEEEEIRVSI NEKCGKEFSE F


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