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

 KAPCA_MOUSE             Reviewed;         351 AA.
P05132; Q9JID0;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 214.
RecName: Full=cAMP-dependent protein kinase catalytic subunit alpha;
Short=PKA C-alpha;
EC=2.7.11.11;
Name=Prkaca; Synonyms=Pkaca;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
PubMed=2833513;
Chrivia J.C., Uhler M.D., McKnight G.S.;
"Characterization of genomic clones coding for the C alpha and C beta
subunits of mouse cAMP-dependent protein kinase.";
J. Biol. Chem. 263:5739-5744(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=3456589; DOI=10.1073/pnas.83.5.1300;
Uhler M.D., Carmichael D.F., Lee D.C., Chrivia J.C., Krebs E.G.,
McKnight G.S.;
"Isolation of cDNA clones coding for the catalytic subunit of mouse
cAMP-dependent protein kinase.";
Proc. Natl. Acad. Sci. U.S.A. 83:1300-1304(1986).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=FVB/N-3; TISSUE=Mammary tumor;
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).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-153 (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).
[5]
PHOSPHORYLATION AT SER-11; SER-140; THR-198 AND SER-339.
PubMed=8395513;
Yonemoto W., Garrod S.M., Bell S.M., Taylor S.S.;
"Identification of phosphorylation sites in the recombinant catalytic
subunit of cAMP-dependent protein kinase.";
J. Biol. Chem. 268:18626-18632(1993).
[6]
PHOSPHORYLATION AT THR-198 BY PDPK1.
PubMed=9707564; DOI=10.1073/pnas.95.17.9849;
Cheng X., Ma Y., Moore M., Hemmings B.A., Taylor S.S.;
"Phosphorylation and activation of cAMP-dependent protein kinase by
phosphoinositide-dependent protein kinase.";
Proc. Natl. Acad. Sci. U.S.A. 95:9849-9854(1998).
[7]
MYRISTOYLATION AT GLY-2, PHOSPHORYLATION AT SER-11, AND DEAMIDATION AT
ASN-3.
PubMed=11141074; DOI=10.1021/bi0021277;
Tholey A., Pipkorn R., Bossemeyer D., Kinzel V., Reed J.;
"Influence of myristoylation, phosphorylation, and deamidation on the
structural behavior of the N-terminus of the catalytic subunit of
cAMP-dependent protein kinase.";
Biochemistry 40:225-231(2001).
[8]
DISRUPTION PHENOTYPE.
PubMed=11875122; DOI=10.1210/mend.16.3.0793;
Skaalhegg B.S., Huang Y., Su T., Idzerda R.L., McKnight G.S.,
Burton K.A.;
"Mutation of the Calpha subunit of PKA leads to growth retardation and
sperm dysfunction.";
Mol. Endocrinol. 16:630-639(2002).
[9]
FUNCTION IN SPERMATOZOA CAPACITATION (ISOFORM 2), AND TISSUE
SPECIFICITY (ISOFORM 2).
PubMed=15340140; DOI=10.1073/pnas.0405580101;
Nolan M.A., Babcock D.F., Wennemuth G., Brown W., Burton K.A.,
McKnight G.S.;
"Sperm-specific protein kinase A catalytic subunit Calpha2
orchestrates cAMP signaling for male fertility.";
Proc. Natl. Acad. Sci. U.S.A. 101:13483-13488(2004).
[10]
SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
PubMed=18367160; DOI=10.1016/j.ydbio.2008.01.045;
Webb R.J., Tinworth L., Thomas G.M., Zaccolo M., Carroll J.;
"Developmentally acquired PKA localisation in mouse oocytes and
embryos.";
Dev. Biol. 317:36-45(2008).
[11]
FUNCTION IN MEIOSIS RESUMPTION, FUNCTION AS CDC25B KINASE, AND
INTERACTION WITH CDC25B.
PubMed=19223768; DOI=10.4161/cc.8.4.7846;
Pirino G., Wescott M.P., Donovan P.J.;
"Protein kinase A regulates resumption of meiosis by phosphorylation
of Cdc25B in mammalian oocytes.";
Cell Cycle 8:665-670(2009).
[12]
FUNCTION IN SPERMATOZOA CAPACITATION, FUNCTION AS ABL1 KINASE, AND
INTERACTION WITH ABL1.
PubMed=19560455; DOI=10.1016/j.ydbio.2009.06.022;
Baker M.A., Hetherington L., Curry B., Aitken R.J.;
"Phosphorylation and consequent stimulation of the tyrosine kinase c-
Abl by PKA in mouse spermatozoa; its implications during
capacitation.";
Dev. Biol. 333:57-66(2009).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[14]
PHOSPHORYLATION AT TYR-331.
PubMed=21866565; DOI=10.1002/jcb.23325;
Caldwell G.B., Howe A.K., Nickl C.K., Dostmann W.R., Ballif B.A.,
Deming P.B.;
"Direct modulation of the protein kinase A catalytic subunit alpha by
growth factor receptor tyrosine kinases.";
J. Cell. Biochem. 113:39-48(2012).
[15]
IDENTIFICATION IN A COMPLEX WITH MROH2B AND TCP11, INTERACTION WITH
MROH2B AND TCP11, AND SUBCELLULAR LOCATION.
PubMed=27105888; DOI=10.1096/fj.201500136R;
Stanger S.J., Law E.A., Jamsai D., O'Bryan M.K., Nixon B.,
McLaughlin E.A., Aitken R.J., Roman S.D.;
"A novel germ cell protein, SPIF (sperm PKA interacting factor), is
essential for the formation of a PKA/TCP11 complex that undergoes
conformational and phosphorylation changes upon capacitation.";
FASEB J. 30:2777-2791(2016).
[16]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
PubMed=1862342; DOI=10.1126/science.1862342;
Knighton D.R., Zheng J., ten Eyck L.F., Ashford V.A., Xuong N.-H.,
Taylor S.S., Sowadski J.M.;
"Crystal structure of the catalytic subunit of cyclic adenosine
monophosphate-dependent protein kinase.";
Science 253:407-414(1991).
[17]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF COMPLEX WITH INHIBITOR.
PubMed=8443157; DOI=10.1021/bi00060a005;
Zheng J., Knighton D.R., ten Eyck L.F., Karlsson R., Xuong N.-H.,
Taylor S.S., Sowadski J.M.;
"Crystal structure of the catalytic subunit of cAMP-dependent protein
kinase complexed with MgATP and peptide inhibitor.";
Biochemistry 32:2154-2161(1993).
[18]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF COMPLEX WITH INHIBITOR.
PubMed=9109651; DOI=10.1021/bi961947+;
Narayana N., Cox S., Shaltiel S., Taylor S.S., Xuong N.;
"Crystal structure of a polyhistidine-tagged recombinant catalytic
subunit of cAMP-dependent protein kinase complexed with the peptide
inhibitor PKI(5-24) and adenosine.";
Biochemistry 36:4438-4448(1997).
[19]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
PubMed=9261084; DOI=10.1016/S0969-2126(97)00246-3;
Narayana N., Cox S., Nguyen-Huu X., ten Eyck L.F., Taylor S.S.;
"A binary complex of the catalytic subunit of cAMP-dependent protein
kinase and adenosine further defines conformational flexibility.";
Structure 5:921-935(1997).
[20]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH ATP ANALOG.
PubMed=17889648; DOI=10.1016/j.cell.2007.07.018;
Kim C., Cheng C.Y., Saldanha S.A., Taylor S.S.;
"PKA-I holoenzyme structure reveals a mechanism for cAMP-dependent
activation.";
Cell 130:1032-1043(2007).
[21]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS).
PubMed=17932298; DOI=10.1126/science.1146447;
Wu J., Brown S.H., von Daake S., Taylor S.S.;
"PKA type IIalpha holoenzyme reveals a combinatorial strategy for
isoform diversity.";
Science 318:274-279(2007).
[22]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH ADP, SUBUNIT,
AND MUTAGENESIS OF LYS-286 AND PHE-328.
PubMed=19122195; DOI=10.1074/jbc.M805862200;
Yang J., Kennedy E.J., Wu J., Deal M.S., Pennypacker J., Ghosh G.,
Taylor S.S.;
"Contribution of non-catalytic core residues to activity and
regulation in protein kinase A.";
J. Biol. Chem. 284:6241-6248(2009).
[23]
X-RAY CRYSTALLOGRAPHY (1.62 ANGSTROMS) IN COMPLEX WITH ATP ANALOGS.
PubMed=19748511; DOI=10.1016/j.jmb.2009.09.014;
Brown S.H.J., Wu J., Kim C., Alberto K., Taylor S.S.;
"Novel isoform-specific interfaces revealed by PKA RIIbeta holoenzyme
structures.";
J. Mol. Biol. 393:1070-1082(2009).
[24]
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH ATP ANALOG AND
SUBSTRATE PEPTIDE, AND ENZYME REGULATION.
PubMed=20890288; DOI=10.1038/nchembio.452;
Masterson L.R., Cheng C., Yu T., Tonelli M., Kornev A., Taylor S.S.,
Veglia G.;
"Dynamics connect substrate recognition to catalysis in protein kinase
A.";
Nat. Chem. Biol. 6:821-828(2010).
[25]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 2-351 IN COMPLEX WITH
PRKAR2B, SUBUNIT, AND PHOSPHORYLATION AT SER-140 AND THR-198.
PubMed=22323819; DOI=10.1126/science.1213979;
Zhang P., Smith-Nguyen E.V., Keshwani M.M., Deal M.S., Kornev A.P.,
Taylor S.S.;
"Structure and allostery of the PKA RIIbeta tetrameric holoenzyme.";
Science 335:712-716(2012).
-!- 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. Phosphorylates HSF1; this phosphorylation promotes HSF1
nuclear localization and transcriptional activity upon heat shock
(By similarity). Isoform 2 phosphorylates and activates ABL1 in
sperm flagellum to promote spermatozoa capacitation (By
similarity). {ECO:0000250, ECO:0000250|UniProtKB:P17612,
ECO:0000269|PubMed:19223768, ECO:0000269|PubMed:19560455}.
-!- 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. {ECO:0000269|PubMed:20890288}.
-!- 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.
Protein kinase A holoenzyme is comprised of two catalytic (C) and
two regulatory (R) subunits which keep the enzyme in an inhibited
state before activation by cyclic-AMP. 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 (By
similarity). Interacts with RAB13; downstream effector of RAB13
involved in tight junction assembly (By similarity). Found in a
complex at least composed of MROH2B isoform 2, PRKACA isoform 2
and TCP11 (PubMed:27105888). Interacts with MROH2B isoform 2
(PubMed:27105888). Interacts with HSF1 (By similarity). Isoform 2
interacts with TCP11 (PubMed:27105888). {ECO:0000250,
ECO:0000250|UniProtKB:P17612, ECO:0000269|PubMed:22323819}.
-!- INTERACTION:
P39717:GPB2 (xeno); NbExp=2; IntAct=EBI-400564, EBI-20711;
P63248:Pkia; NbExp=2; IntAct=EBI-400564, EBI-2931786;
P00514:PRKAR1A (xeno); NbExp=6; IntAct=EBI-400564, EBI-1041635;
P31324:Prkar2b; NbExp=15; IntAct=EBI-400564, EBI-455340;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18367160}.
Cell membrane {ECO:0000250}. Nucleus {ECO:0000250}. Mitochondrion
{ECO:0000269|PubMed:18367160}. Membrane
{ECO:0000250|UniProtKB:P17612}; Lipid-anchor
{ECO:0000250|UniProtKB:P17612}. Note=Translocates into the nucleus
(monomeric catalytic subunit) (By similarity). 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.
Colocalizes with HSF1 in nuclear stress bodies (nSBs) upon heat
shock (By similarity). {ECO:0000250,
ECO:0000250|UniProtKB:P17612}.
-!- SUBCELLULAR LOCATION: Isoform 2: Cell projection, cilium,
flagellum {ECO:0000269|PubMed:27105888}. Cytoplasmic vesicle,
secretory vesicle, acrosome {ECO:0000269|PubMed:27105888}.
Note=Expressed in the midpiece region of the sperm flagellum (By
similarity). Colocalizes with MROH2B and TCP11 on the acrosome and
tail regions in round spermatids and spermatozoa regardless of the
capacitation status of the sperm (PubMed:27105888). {ECO:0000250,
ECO:0000269|PubMed:27105888}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=C-alpha-1;
IsoId=P05132-1; Sequence=Displayed;
Name=2; Synonyms=C-alpha-2, C-alpha-S, C(s);
IsoId=P05132-2; Sequence=VSP_004760;
-!- TISSUE SPECIFICITY: Isoform 2 is sperm specific.
-!- DEVELOPMENTAL STAGE: Accumulates in oocytes before fertilization
but fades out after fertilization. {ECO:0000269|PubMed:18367160}.
-!- PTM: Autophosphorylated. Phosphorylation is enhanced by vitamin
K(2) (By similarity). Phosphorylated on threonine and serine
residues. Phosphorylation on Thr-198 is required for full
activity. {ECO:0000250, ECO:0000269|PubMed:8395513,
ECO:0000269|PubMed:9707564}.
-!- PTM: Asn-3 is partially deaminated to Asp-3 giving rise to 2 major
isoelectric variants, called CB and CA respectively.
-!- PTM: When myristoylated, Ser-11 is autophosphorylated probably in
conjunction with deamidation of Asn-3.
{ECO:0000269|PubMed:11141074, ECO:0000269|PubMed:8395513}.
-!- PTM: Phosphorylated at Tyr-331 by activated receptor tyrosine
kinases EGFR and PDGFR; this increases catalytic efficienncy.
{ECO:0000269|PubMed:21866565}.
-!- DISRUPTION PHENOTYPE: Frequent early postnatal lethality.
Survivals are runted accompanied with mature sperm exhibiting
defective forward motility. {ECO:0000269|PubMed:11875122}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. cAMP subfamily. {ECO:0000305}.
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EMBL; M19960; AAA39937.1; -; Genomic_DNA.
EMBL; M18240; AAA39937.1; JOINED; Genomic_DNA.
EMBL; M18241; AAA39937.1; JOINED; Genomic_DNA.
EMBL; M19953; AAA39937.1; JOINED; Genomic_DNA.
EMBL; M19954; AAA39937.1; JOINED; Genomic_DNA.
EMBL; M19955; AAA39937.1; JOINED; Genomic_DNA.
EMBL; M19956; AAA39937.1; JOINED; Genomic_DNA.
EMBL; M19957; AAA39937.1; JOINED; Genomic_DNA.
EMBL; M19958; AAA39937.1; JOINED; Genomic_DNA.
EMBL; M19959; AAA39937.1; JOINED; Genomic_DNA.
EMBL; M12303; AAA39936.1; -; mRNA.
EMBL; BC003238; AAH03238.1; -; mRNA.
EMBL; BC054834; AAH54834.1; -; mRNA.
EMBL; AF239743; AAF76425.1; -; mRNA.
CCDS; CCDS22463.1; -. [P05132-1]
CCDS; CCDS85574.1; -. [P05132-2]
PIR; A28619; OKMSCA.
RefSeq; NP_001264827.1; NM_001277898.1. [P05132-2]
RefSeq; NP_032880.1; NM_008854.5. [P05132-1]
UniGene; Mm.19111; -.
PDB; 1APM; X-ray; 2.00 A; E=2-351.
PDB; 1ATP; X-ray; 2.20 A; E=2-351.
PDB; 1BKX; X-ray; 2.60 A; A=2-351.
PDB; 1BX6; X-ray; 2.10 A; A=2-351.
PDB; 1FMO; X-ray; 2.20 A; E=2-351.
PDB; 1J3H; X-ray; 2.90 A; A/B=2-351.
PDB; 1JBP; X-ray; 2.20 A; E=2-351.
PDB; 1JLU; X-ray; 2.25 A; E=2-351.
PDB; 1L3R; X-ray; 2.00 A; E=2-351.
PDB; 1PVK; Model; -; B=16-351.
PDB; 1RDQ; X-ray; 1.26 A; E=2-351.
PDB; 1RE8; X-ray; 2.10 A; A=2-351.
PDB; 1REJ; X-ray; 2.20 A; A=2-351.
PDB; 1REK; X-ray; 2.30 A; A=2-351.
PDB; 1SYK; X-ray; 2.80 A; A/B=2-351.
PDB; 2CPK; X-ray; 2.70 A; E=2-351.
PDB; 2ERZ; X-ray; 2.20 A; E=1-351.
PDB; 2QCS; X-ray; 2.20 A; A=2-351.
PDB; 2QUR; X-ray; 2.50 A; A=2-351.
PDB; 2QVS; X-ray; 2.50 A; E=2-351.
PDB; 3FHI; X-ray; 2.00 A; A=2-351.
PDB; 3FJQ; X-ray; 1.60 A; E=2-351.
PDB; 3IDB; X-ray; 1.62 A; A=2-351.
PDB; 3IDC; X-ray; 2.70 A; A=2-351.
PDB; 3J4Q; EM; 35.00 A; D/E=1-351.
PDB; 3J4R; EM; 35.00 A; D/E=1-351.
PDB; 3O7L; X-ray; 2.80 A; B/D=2-351.
PDB; 3OW3; X-ray; 1.90 A; A=2-351.
PDB; 3PVB; X-ray; 3.30 A; A=7-351.
PDB; 3QAL; X-ray; 1.70 A; E=2-351.
PDB; 3QAM; X-ray; 1.92 A; E=2-351.
PDB; 3TNP; X-ray; 2.30 A; C/F=2-351.
PDB; 3TNQ; X-ray; 3.10 A; B=2-351.
PDB; 3X2U; X-ray; 2.40 A; A=1-351.
PDB; 3X2V; X-ray; 1.77 A; A=1-351.
PDB; 3X2W; X-ray; 1.70 A; A=1-351.
PDB; 4DFX; X-ray; 1.35 A; E=2-351.
PDB; 4DFY; X-ray; 3.00 A; A/E=1-351.
PDB; 4DFZ; X-ray; 2.00 A; E=2-351.
PDB; 4DG0; X-ray; 2.00 A; E=2-351.
PDB; 4DG2; X-ray; 2.00 A; E=2-351.
PDB; 4DG3; X-ray; 1.80 A; E=1-351.
PDB; 4DH1; X-ray; 2.00 A; A=16-351.
PDB; 4DH3; X-ray; 2.20 A; A=2-351.
PDB; 4DH5; X-ray; 2.20 A; A=2-351.
PDB; 4DH7; X-ray; 1.80 A; A=2-351.
PDB; 4DH8; X-ray; 2.30 A; A=2-351.
PDB; 4DIN; X-ray; 3.70 A; A=2-351.
PDB; 4HPT; X-ray; 2.15 A; E=2-351.
PDB; 4HPU; X-ray; 1.55 A; E=2-351.
PDB; 4IAC; X-ray; 2.15 A; A=2-351.
PDB; 4IAD; X-ray; 1.90 A; A=2-351.
PDB; 4IAF; X-ray; 2.20 A; A=2-351.
PDB; 4IAI; X-ray; 1.55 A; A=2-351.
PDB; 4IAK; X-ray; 1.60 A; A=2-351.
PDB; 4IAY; X-ray; 2.00 A; A=2-351.
PDB; 4IAZ; X-ray; 1.85 A; A=2-351.
PDB; 4IB0; X-ray; 1.87 A; A=2-351.
PDB; 4IB1; X-ray; 1.63 A; A=2-351.
PDB; 4IB3; X-ray; 2.20 A; A=2-351.
PDB; 4NTS; X-ray; 2.90 A; A/B=2-351.
PDB; 4NTT; X-ray; 3.50 A; A/B=2-351.
PDB; 4O21; X-ray; 1.95 A; A=16-351.
PDB; 4O22; X-ray; 1.70 A; A=16-351.
PDB; 4WBB; X-ray; 2.80 A; B=2-351.
PDB; 4X6Q; X-ray; 2.52 A; C=2-351.
PDB; 4X6R; X-ray; 2.40 A; A=2-351.
PDB; 4XW4; X-ray; 1.82 A; A=15-351.
PDB; 4XW5; X-ray; 1.95 A; A=15-351.
PDB; 4XW6; X-ray; 1.90 A; A=15-351.
PDB; 5JR7; X-ray; 3.56 A; A/C=2-351.
PDB; 5X3F; X-ray; 3.38 A; B=5-351.
PDBsum; 1APM; -.
PDBsum; 1ATP; -.
PDBsum; 1BKX; -.
PDBsum; 1BX6; -.
PDBsum; 1FMO; -.
PDBsum; 1J3H; -.
PDBsum; 1JBP; -.
PDBsum; 1JLU; -.
PDBsum; 1L3R; -.
PDBsum; 1PVK; -.
PDBsum; 1RDQ; -.
PDBsum; 1RE8; -.
PDBsum; 1REJ; -.
PDBsum; 1REK; -.
PDBsum; 1SYK; -.
PDBsum; 2CPK; -.
PDBsum; 2ERZ; -.
PDBsum; 2QCS; -.
PDBsum; 2QUR; -.
PDBsum; 2QVS; -.
PDBsum; 3FHI; -.
PDBsum; 3FJQ; -.
PDBsum; 3IDB; -.
PDBsum; 3IDC; -.
PDBsum; 3J4Q; -.
PDBsum; 3J4R; -.
PDBsum; 3O7L; -.
PDBsum; 3OW3; -.
PDBsum; 3PVB; -.
PDBsum; 3QAL; -.
PDBsum; 3QAM; -.
PDBsum; 3TNP; -.
PDBsum; 3TNQ; -.
PDBsum; 3X2U; -.
PDBsum; 3X2V; -.
PDBsum; 3X2W; -.
PDBsum; 4DFX; -.
PDBsum; 4DFY; -.
PDBsum; 4DFZ; -.
PDBsum; 4DG0; -.
PDBsum; 4DG2; -.
PDBsum; 4DG3; -.
PDBsum; 4DH1; -.
PDBsum; 4DH3; -.
PDBsum; 4DH5; -.
PDBsum; 4DH7; -.
PDBsum; 4DH8; -.
PDBsum; 4DIN; -.
PDBsum; 4HPT; -.
PDBsum; 4HPU; -.
PDBsum; 4IAC; -.
PDBsum; 4IAD; -.
PDBsum; 4IAF; -.
PDBsum; 4IAI; -.
PDBsum; 4IAK; -.
PDBsum; 4IAY; -.
PDBsum; 4IAZ; -.
PDBsum; 4IB0; -.
PDBsum; 4IB1; -.
PDBsum; 4IB3; -.
PDBsum; 4NTS; -.
PDBsum; 4NTT; -.
PDBsum; 4O21; -.
PDBsum; 4O22; -.
PDBsum; 4WBB; -.
PDBsum; 4X6Q; -.
PDBsum; 4X6R; -.
PDBsum; 4XW4; -.
PDBsum; 4XW5; -.
PDBsum; 4XW6; -.
PDBsum; 5JR7; -.
PDBsum; 5X3F; -.
ProteinModelPortal; P05132; -.
SMR; P05132; -.
BioGrid; 202192; 21.
CORUM; P05132; -.
DIP; DIP-6086N; -.
ELM; P05132; -.
IntAct; P05132; 18.
MINT; MINT-4051347; -.
STRING; 10090.ENSMUSP00000005606; -.
BindingDB; P05132; -.
iPTMnet; P05132; -.
PhosphoSitePlus; P05132; -.
EPD; P05132; -.
MaxQB; P05132; -.
PaxDb; P05132; -.
PeptideAtlas; P05132; -.
PRIDE; P05132; -.
Ensembl; ENSMUST00000005606; ENSMUSP00000005606; ENSMUSG00000005469. [P05132-1]
Ensembl; ENSMUST00000211558; ENSMUSP00000147256; ENSMUSG00000005469. [P05132-2]
GeneID; 18747; -.
KEGG; mmu:18747; -.
UCSC; uc009mll.3; mouse. [P05132-1]
UCSC; uc009mlm.2; mouse. [P05132-2]
CTD; 5566; -.
MGI; MGI:97592; Prkaca.
eggNOG; KOG0616; Eukaryota.
eggNOG; ENOG410XPQQ; LUCA.
GeneTree; ENSGT00810000125385; -.
HOGENOM; HOG000233033; -.
HOVERGEN; HBG108317; -.
InParanoid; P05132; -.
KO; K04345; -.
OMA; GQHFAMK; -.
OrthoDB; EOG091G10O8; -.
PhylomeDB; P05132; -.
TreeFam; TF313399; -.
BRENDA; 2.7.11.11; 3474.
Reactome; R-MMU-163358; PKA-mediated phosphorylation of key metabolic factors.
Reactome; R-MMU-163560; Triglyceride catabolism.
Reactome; R-MMU-163615; PKA activation.
Reactome; R-MMU-164378; PKA activation in glucagon signalling.
Reactome; R-MMU-180024; DARPP-32 events.
Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
Reactome; R-MMU-380259; Loss of Nlp from mitotic centrosomes.
Reactome; R-MMU-380270; Recruitment of mitotic centrosome proteins and complexes.
Reactome; R-MMU-380320; Recruitment of NuMA to mitotic centrosomes.
Reactome; R-MMU-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
Reactome; R-MMU-392517; Rap1 signalling.
Reactome; R-MMU-422356; Regulation of insulin secretion.
Reactome; R-MMU-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
Reactome; R-MMU-512988; Interleukin-3, 5 and GM-CSF signaling.
Reactome; R-MMU-5578775; Ion homeostasis.
Reactome; R-MMU-5610783; Degradation of GLI2 by the proteasome.
Reactome; R-MMU-5610785; GLI3 is processed to GLI3R by the proteasome.
Reactome; R-MMU-5610787; Hedgehog 'off' state.
Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
Reactome; R-MMU-5621575; CD209 (DC-SIGN) signaling.
Reactome; R-MMU-5687128; MAPK6/MAPK4 signaling.
Reactome; R-MMU-8854518; AURKA Activation by TPX2.
Reactome; R-MMU-8963896; HDL assembly.
Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production.
ChiTaRS; Prkaca; mouse.
EvolutionaryTrace; P05132; -.
PRO; PR:P05132; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000005469; -.
CleanEx; MM_PRKACA; -.
Genevisible; P05132; MM.
GO; GO:0001669; C:acrosomal vesicle; IDA:UniProtKB.
GO; GO:0005952; C:cAMP-dependent protein kinase complex; IMP:CAFA.
GO; GO:0005813; C:centrosome; ISO:MGI.
GO; GO:0097546; C:ciliary base; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0043197; C:dendritic spine; IDA:SynGO.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0045171; C:intercellular bridge; ISO:MGI.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0031594; C:neuromuscular junction; IDA:MGI.
GO; GO:0016607; C:nuclear speck; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0031588; C:nucleotide-activated protein kinase complex; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0044853; C:plasma membrane raft; ISO:MGI.
GO; GO:0036126; C:sperm flagellum; IDA:UniProtKB.
GO; GO:0097225; C:sperm midpiece; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IDA:CAFA.
GO; GO:0004691; F:cAMP-dependent protein kinase activity; IDA:UniProtKB.
GO; GO:0000287; F:magnesium ion binding; IDA:CAFA.
GO; GO:0030145; F:manganese ion binding; IMP:CAFA.
GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
GO; GO:0034237; F:protein kinase A regulatory subunit binding; IPI:CAFA.
GO; GO:0004672; F:protein kinase activity; IDA:MGI.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:CAFA.
GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; ISO:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0071333; P:cellular response to glucose stimulus; ISO:MGI.
GO; GO:0034605; P:cellular response to heat; ISS:UniProtKB.
GO; GO:0071374; P:cellular response to parathyroid hormone stimulus; IMP:MGI.
GO; GO:0035556; P:intracellular signal transduction; TAS:Reactome.
GO; GO:0001707; P:mesoderm formation; IGI:MGI.
GO; GO:0050804; P:modulation of chemical synaptic transmission; IMP:MGI.
GO; GO:0006397; P:mRNA processing; ISO:MGI.
GO; GO:1901621; P:negative regulation of smoothened signaling pathway involved in dorsal/ventral neural tube patterning; IGI:MGI.
GO; GO:0001843; P:neural tube closure; IGI:MGI.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:CAFA.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:MGI.
GO; GO:0071158; P:positive regulation of cell cycle arrest; IDA:UniProtKB.
GO; GO:0046827; P:positive regulation of protein export from nucleus; IMP:MGI.
GO; GO:0046777; P:protein autophosphorylation; IDA:MGI.
GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
GO; GO:2000810; P:regulation of bicellular tight junction assembly; ISO:MGI.
GO; GO:0045667; P:regulation of osteoblast differentiation; ISO:MGI.
GO; GO:0061136; P:regulation of proteasomal protein catabolic process; ISO:MGI.
GO; GO:0070613; P:regulation of protein processing; IGI:MGI.
GO; GO:0048240; P:sperm capacitation; IDA:UniProtKB.
GO; GO:0019433; P:triglyceride catabolic process; TAS:Reactome.
InterPro; IPR000961; AGC-kinase_C.
InterPro; IPR011009; Kinase-like_dom.
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; Cytoplasm;
Cytoplasmic vesicle; Flagellum; Kinase; Lipoprotein; Membrane;
Mitochondrion; Myristate; Nucleotide-binding; Nucleus; Phosphoprotein;
Reference proteome; Serine/threonine-protein kinase; Transferase.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:11141074}.
CHAIN 2 351 cAMP-dependent protein kinase catalytic
subunit alpha.
/FTId=PRO_0000086053.
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.
NP_BIND 169 172 ATP.
ACT_SITE 167 167 Proton acceptor.
BINDING 73 73 ATP.
MOD_RES 3 3 Deamidated asparagine; partial.
{ECO:0000269|PubMed:11141074}.
MOD_RES 11 11 Phosphoserine; by autocatalysis.
{ECO:0000269|PubMed:11141074,
ECO:0000269|PubMed:8395513}.
MOD_RES 49 49 Phosphothreonine.
{ECO:0000250|UniProtKB:P17612}.
MOD_RES 140 140 Phosphoserine.
{ECO:0000269|PubMed:22323819,
ECO:0000305|PubMed:8395513}.
MOD_RES 196 196 Phosphothreonine.
{ECO:0000250|UniProtKB:P17612}.
MOD_RES 198 198 Phosphothreonine; by PDPK1.
{ECO:0000269|PubMed:22323819,
ECO:0000269|PubMed:8395513,
ECO:0000269|PubMed:9707564}.
MOD_RES 202 202 Phosphothreonine.
{ECO:0000250|UniProtKB:P17612}.
MOD_RES 331 331 Phosphotyrosine.
{ECO:0000269|PubMed:21866565}.
MOD_RES 339 339 Phosphoserine.
{ECO:0000305|PubMed:8395513}.
LIPID 2 2 N-myristoyl glycine.
{ECO:0000269|PubMed:11141074}.
VAR_SEQ 1 15 MGNAAAAKKGSEQES -> MASSSND (in isoform
2). {ECO:0000303|PubMed:10982398}.
/FTId=VSP_004760.
MUTAGEN 198 198 T->D: No phosphorylation by PDPK1.
MUTAGEN 286 286 K->P: Impaired inhibition by the R-
subunit. {ECO:0000269|PubMed:19122195}.
MUTAGEN 328 328 F->A: Reduced catalytic activity and
impaired inhibition by the R-subunit.
{ECO:0000269|PubMed:19122195}.
CONFLICT 33 33 T -> D (in Ref. 2; AAA39936).
{ECO:0000305}.
CONFLICT 287 287 N -> D (in Ref. 2; AAA39936).
{ECO:0000305}.
HELIX 3 7 {ECO:0000244|PDB:4DFX}.
TURN 9 12 {ECO:0000244|PDB:4DFX}.
HELIX 16 32 {ECO:0000244|PDB:1RDQ}.
HELIX 41 43 {ECO:0000244|PDB:1RDQ}.
STRAND 44 52 {ECO:0000244|PDB:1RDQ}.
STRAND 57 63 {ECO:0000244|PDB:1RDQ}.
TURN 64 66 {ECO:0000244|PDB:1RDQ}.
STRAND 69 76 {ECO:0000244|PDB:1RDQ}.
HELIX 77 82 {ECO:0000244|PDB:1RDQ}.
HELIX 86 96 {ECO:0000244|PDB:1RDQ}.
STRAND 107 112 {ECO:0000244|PDB:1RDQ}.
STRAND 114 122 {ECO:0000244|PDB:1RDQ}.
HELIX 129 136 {ECO:0000244|PDB:1RDQ}.
HELIX 141 160 {ECO:0000244|PDB:1RDQ}.
STRAND 162 164 {ECO:0000244|PDB:1BKX}.
HELIX 170 172 {ECO:0000244|PDB:1RDQ}.
STRAND 173 175 {ECO:0000244|PDB:1RDQ}.
STRAND 181 183 {ECO:0000244|PDB:1RDQ}.
HELIX 186 188 {ECO:0000244|PDB:1RE8}.
HELIX 203 205 {ECO:0000244|PDB:1RDQ}.
HELIX 208 211 {ECO:0000244|PDB:1RDQ}.
HELIX 219 234 {ECO:0000244|PDB:1RDQ}.
HELIX 244 253 {ECO:0000244|PDB:1RDQ}.
HELIX 264 273 {ECO:0000244|PDB:1RDQ}.
TURN 278 280 {ECO:0000244|PDB:1RDQ}.
TURN 282 284 {ECO:0000244|PDB:4XW6}.
TURN 286 289 {ECO:0000244|PDB:1RDQ}.
HELIX 290 293 {ECO:0000244|PDB:1RDQ}.
HELIX 296 298 {ECO:0000244|PDB:1RDQ}.
HELIX 303 307 {ECO:0000244|PDB:1RDQ}.
STRAND 321 326 {ECO:0000244|PDB:1REK}.
TURN 345 350 {ECO:0000244|PDB:1RDQ}.
SEQUENCE 351 AA; 40571 MW; 02F85D66EB21A1FA CRC64;
MGNAAAAKKG SEQESVKEFL AKAKEDFLKK WETPSQNTAQ LDQFDRIKTL GTGSFGRVML
VKHKESGNHY AMKILDKQKV VKLKQIEHTL NEKRILQAVN FPFLVKLEFS FKDNSNLYMV
MEYVAGGEMF SHLRRIGRFS EPHARFYAAQ IVLTFEYLHS LDLIYRDLKP ENLLIDQQGY
IQVTDFGFAK RVKGRTWTLC GTPEYLAPEI ILSKGYNKAV DWWALGVLIY EMAAGYPPFF
ADQPIQIYEK IVSGKVRFPS HFSSDLKDLL RNLLQVDLTK RFGNLKNGVN DIKNHKWFAT
TDWIAIYQRK VEAPFIPKFK GPGDTSNFDD YEEEEIRVSI NEKCGKEFTE F


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