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1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase epsilon-1 (EC 3.1.4.11) (Pancreas-enriched phospholipase C) (Phosphoinositide phospholipase C-epsilon-1) (Phospholipase C-epsilon-1) (PLC-epsilon-1)

 PLCE1_HUMAN             Reviewed;        2302 AA.
Q9P212; A6NGW0; A6NLA1; A7MBN7; A8K1D7; B9EIJ6; Q1X6H8; Q5VWL4;
Q5VWL5; Q9H9X8; Q9HBX6; Q9HC53; Q9UHV3;
31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
31-OCT-2006, sequence version 3.
20-JUN-2018, entry version 159.
RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase epsilon-1;
EC=3.1.4.11;
AltName: Full=Pancreas-enriched phospholipase C;
AltName: Full=Phosphoinositide phospholipase C-epsilon-1;
AltName: Full=Phospholipase C-epsilon-1;
Short=PLC-epsilon-1;
Name=PLCE1; Synonyms=KIAA1516, PLCE, PPLC;
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 SPECIFICITY, CATALYTIC
ACTIVITY, COFACTOR, INTERACTION WITH HRAS AND RAP1A, SUBCELLULAR
LOCATION, ENZYME REGULATION, AND VARIANTS ILE-1777 AND ARG-1927.
TISSUE=Fetal brain;
PubMed=11022048; DOI=10.1074/jbc.M008324200;
Song C., Hu C.-D., Masago M., Kariya K., Yamawaki-Kataoka Y.,
Shibatohge M., Wu D., Satoh T., Kataoka T.;
"Regulation of a novel human phospholipase C, PLCepsilon, through
membrane targeting by Ras.";
J. Biol. Chem. 276:2752-2757(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY,
SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, ENZYME REGULATION, AND
MUTAGENESIS OF HIS-1452.
TISSUE=Heart;
PubMed=11022047; DOI=10.1074/jbc.M008119200;
Lopez I., Mak E.C., Ding J., Hamm H.E., Lomasney J.W.;
"A novel bifunctional phospholipase C that is regulated by Galpha 12
and stimulates the Ras/mitogen-activated protein kinase pathway.";
J. Biol. Chem. 276:2758-2765(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
ARG-1927.
TISSUE=Brain;
PubMed=10819331; DOI=10.1093/dnares/7.2.143;
Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XVII.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 7:143-150(2000).
[4]
SEQUENCE REVISION.
Ohara O., Nagase T., Kikuno R.;
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[6]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
ARG-1927.
TISSUE=Brain;
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).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 1098-2302 (ISOFORMS 1/2), AND VARIANTS
ILE-1777 AND ARG-1927.
TISSUE=Pancreas;
Kawasaki H., Chen E.J., Springett G.M., Graybiel A.M., Housman D.E.;
"A novel phospholipase C enriched in pancreas.";
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1383 (ISOFORM 2), AND
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1475-2302 (ISOFORMS 1/2).
TISSUE=Brain, and Teratocarcinoma;
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).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 1987-2302 (ISOFORMS 1/2).
TISSUE=Brain;
Buessow K.;
"Sequence of cDNA clone MPMGp800D13530.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[11]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=11395506; DOI=10.1074/jbc.M103530200;
Jin T.-G., Satoh T., Liao Y., Song C., Gao X., Kariya K., Hu C.-D.,
Kataoka T.;
"Role of the CDC25 homology domain of phospholipase Cepsilon in
amplification of Rap1-dependent signaling.";
J. Biol. Chem. 276:30301-30307(2001).
[12]
FUNCTION, AND ENZYME REGULATION.
PubMed=11715024; DOI=10.1038/ncb1101-1020;
Schmidt M., Evellin S., Weernink P.A.O., von Dorp F., Rehmann H.,
Lomasney J.W., Jakobs K.H.;
"A new phospholipase-C-calcium signalling pathway mediated by cyclic
AMP and a Rap GTPase.";
Nat. Cell Biol. 3:1020-1024(2001).
[13]
FUNCTION, AND ENZYME REGULATION.
PubMed=11877431; DOI=10.1074/jbc.M112024200;
Evellin S., Nolte J., Tysack K., vom Dorp F., Thiel M.,
Weernink P.A.O., Jakobs K.H., Webb E.J., Lomasney J.W., Schmidt M.;
"Stimulation of phospholipase C-epsilon by the M3 muscarinic
acetylcholine receptor mediated by cyclic AMP and the GTPase Rap2B.";
J. Biol. Chem. 277:16805-16813(2002).
[14]
INTERACTION WITH RAP1A; RAP2A AND RAP2B.
PubMed=12444546; DOI=10.1038/sj.onc.1206003;
Song C., Satoh T., Edamatsu H., Wu D., Tadano M., Gao X., Kataoka T.;
"Differential roles of Ras and Rap1 in growth factor-dependent
activation of phospholipase C epsilon.";
Oncogene 21:8105-8113(2002).
[15]
FUNCTION.
PubMed=12721365; DOI=10.1073/pnas.1031494100;
Czyzyk J., Brogdon J.L., Badou A., Henegariu O., Preston Hurlburt P.,
Flavell R., Bottomly K.;
"Activation of CD4 T cells by Raf-independent effectors of Ras.";
Proc. Natl. Acad. Sci. U.S.A. 100:6003-6008(2003).
[16]
ENZYME REGULATION.
PubMed=15157671; DOI=10.1016/j.cellsig.2004.01.009;
vom Dorp F., Sari A.Y., Sanders H., Keiper M., Oude Weernink P.A.,
Jakobs K.H., Schmidt M.;
"Inhibition of phospholipase C-epsilon by Gi-coupled receptors.";
Cell. Signal. 16:921-928(2004).
[17]
INDUCTION.
PubMed=16293787; DOI=10.1161/01.RES.0000196578.15385.bb;
Wang H., Oestreich E.A., Maekawa N., Bullard T.A., Vikstrom K.L.,
Dirksen R.T., Kelley G.G., Blaxall B.C., Smrcka A.V.;
"Phospholipase C epsilon modulates beta-adrenergic receptor-dependent
cardiac contraction and inhibits cardiac hypertrophy.";
Circ. Res. 97:1305-1313(2005).
[18]
TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=15558028; DOI=10.1038/sj.onc.1208168;
Sorli S.C., Bunney T.D., Sugden P.H., Paterson H.F., Katan M.;
"Signaling properties and expression in normal and tumor tissues of
two phospholipase C epsilon splice variants.";
Oncogene 24:90-100(2005).
[19]
FUNCTION, INTERACTION WITH RRAS, AND ENZYME REGULATION.
PubMed=16537651; DOI=10.1242/jcs.02835;
Ada-Nguema A.S., Xenias H., Sheetz M.P., Keely P.J.;
"The small GTPase R-Ras regulates organization of actin and drives
membrane protrusions through the activity of PLCepsilon.";
J. Cell Sci. 119:1307-1319(2006).
[20]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2131-2246 OF MUTANT LEU-2176
IN COMPLEX WITH HRAS, STRUCTURE BY NMR OF 2006-2114 AND 2131-2246, AND
MUTAGENESIS OF GLN-2140; GLN-2148; ARG-2150; LYS-2171 AND TYR-2174.
PubMed=16483931; DOI=10.1016/j.molcel.2006.01.008;
Bunney T.D., Harris R., Gandarillas N.L., Josephs M.B., Roe S.M.,
Sorli S.C., Paterson H.F., Rodrigues-Lima F., Esposito D.,
Ponting C.P., Gierschik P., Pearl L.H., Driscoll P.C., Katan M.;
"Structural and mechanistic insights into ras association domains of
phospholipase C epsilon.";
Mol. Cell 21:495-507(2006).
[21]
VARIANT NPHS3 LEU-1484, FUNCTION, AND INTERACTION WITH IQGAP1.
PubMed=17086182; DOI=10.1038/ng1918;
Hinkes B., Wiggins R.C., Gbadegesin R., Vlangos C.N., Seelow D.,
Nuernberg G., Garg P., Verma R., Chaib H., Hoskins B.E., Ashraf S.,
Becker C., Hennies H.C., Goyal M., Wharram B.L., Schachter A.D.,
Mudumana S., Drummond I., Kerjaschki D., Waldherr R., Dietrich A.,
Ozaltin F., Bakkaloglu A., Cleper R., Basel-Vanagaite L., Pohl M.,
Griebel M., Tsygin A.N., Soylu A., Mueller D., Sorli C.S.,
Bunney T.D., Katan M., Liu J., Attanasio M., O'toole J.F.,
Hasselbacher K., Mucha B., Otto E.A., Airik R., Kispert A.,
Kelley G.G., Smrcka A.V., Gudermann T., Holzman L.B., Nuernberg P.,
Hildebrandt F.;
"Positional cloning uncovers mutations in PLCE1 responsible for a
nephrotic syndrome variant that may be reversible.";
Nat. Genet. 38:1397-1405(2006).
-!- FUNCTION: The production of the second messenger molecules
diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is
mediated by activated phosphatidylinositol-specific phospholipase
C enzymes. PLCE1 is a bifunctional enzyme which also regulates
small GTPases of the Ras superfamily through its Ras guanine-
exchange factor (RasGEF) activity. As an effector of
heterotrimeric and small G-protein, it may play a role in cell
survival, cell growth, actin organization and T-cell activation.
{ECO:0000269|PubMed:11022047, ECO:0000269|PubMed:11395506,
ECO:0000269|PubMed:11715024, ECO:0000269|PubMed:11877431,
ECO:0000269|PubMed:12721365, ECO:0000269|PubMed:16537651,
ECO:0000269|PubMed:17086182}.
-!- CATALYTIC ACTIVITY: 1-phosphatidyl-1D-myo-inositol 4,5-
bisphosphate + H(2)O = 1D-myo-inositol 1,4,5-trisphosphate +
diacylglycerol. {ECO:0000269|PubMed:11022047,
ECO:0000269|PubMed:11022048}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000269|PubMed:11022048};
-!- ENZYME REGULATION: Activated by the heterotrimeric G-protein
subunits GNA12, GNA13 and GNB1-GNG2. Activated by HRAS, RAP1A,
RHOA, RHOB, RHOC, RRAS and RRAS2. Activated by the G(s)-coupled
GPCRs ADRB2, PTGER1 and CHRM3 through cyclic-AMP formation and
RAP2B activation. Inhibited by G(i)-coupled GPCRs.
{ECO:0000269|PubMed:11022047, ECO:0000269|PubMed:11022048,
ECO:0000269|PubMed:11715024, ECO:0000269|PubMed:11877431,
ECO:0000269|PubMed:15157671, ECO:0000269|PubMed:16537651}.
-!- SUBUNIT: Interacts with RHOA (By similarity). Interacts with
IQGAP1, HRAS, RAP1A, RAP2A, RAP2B and RRAS. {ECO:0000250,
ECO:0000269|PubMed:11022048, ECO:0000269|PubMed:12444546,
ECO:0000269|PubMed:16483931, ECO:0000269|PubMed:16537651,
ECO:0000269|PubMed:17086182}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell membrane. Golgi
apparatus membrane. Note=Recruited to plasma membrane by activated
HRAS and RAP2. Recruited to perinuclear membrane by activated
RAP1A. Isoform 1 and isoform 2 associates with Golgi membranes.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=PLCepsilon1a;
IsoId=Q9P212-1; Sequence=Displayed;
Name=2; Synonyms=PLCepsilon1b;
IsoId=Q9P212-2; Sequence=VSP_021335, VSP_021336;
Note=Ref.2 (AAG28341) sequence is in conflict in position:
69:L->P. {ECO:0000305};
-!- TISSUE SPECIFICITY: Widely expressed. Isoform 1 is broadly
expressed and only absent in peripheral blood leukocytes. Isoform
2 is specifically expressed in placenta, lung and spleen.
{ECO:0000269|PubMed:11022047, ECO:0000269|PubMed:11022048,
ECO:0000269|PubMed:15558028}.
-!- INDUCTION: Overexpressed during heart failure.
{ECO:0000269|PubMed:16293787}.
-!- DOMAIN: The Ras-associating domain 1 is degenerated and may not
bind HRAS. The Ras-associating domain 2 mediates interaction with
GTP-bound HRAS, RAP1A, RAP2A and RAP2B and recruitment of HRAS to
the cell membrane.
-!- DOMAIN: The Ras-GEF domain has a GEF activity towards HRAS and
RAP1A. Mediates activation of the mitogen-activated protein kinase
pathway.
-!- DISEASE: Nephrotic syndrome 3 (NPHS3) [MIM:610725]: A form of
nephrotic syndrome, a renal disease clinically characterized by
severe proteinuria, resulting in complications such as
hypoalbuminemia, hyperlipidemia and edema. Kidney biopsies show
non-specific histologic changes such as focal segmental
glomerulosclerosis and diffuse mesangial proliferation. Some
affected individuals have an inherited steroid-resistant form and
progress to end-stage renal failure. Most patients with NPHS3 show
diffuse mesangial sclerosis on renal biopsy, which is a pathologic
entity characterized by mesangial matrix expansion with no
mesangial hypercellularity, hypertrophy of the podocytes,
vacuolized podocytes, thickened basement membranes, and diminished
patency of the capillary lumen. {ECO:0000269|PubMed:17086182}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SEQUENCE CAUTION:
Sequence=AAF22005.1; Type=Frameshift; Positions=1131; Evidence={ECO:0000305};
Sequence=AAG17145.2; Type=Frameshift; Positions=2296; Evidence={ECO:0000305};
Sequence=BAA96040.2; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAB14090.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=CAH70739.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAH73288.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAH73757.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAI16674.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; AF190642; AAG17145.2; ALT_FRAME; mRNA.
EMBL; AF170071; AAG28341.1; -; mRNA.
EMBL; AB040949; BAA96040.2; ALT_INIT; mRNA.
EMBL; AL139118; CAH70739.1; ALT_SEQ; Genomic_DNA.
EMBL; AL139124; CAH70739.1; JOINED; Genomic_DNA.
EMBL; AL365510; CAH70739.1; JOINED; Genomic_DNA.
EMBL; AL389885; CAH70739.1; JOINED; Genomic_DNA.
EMBL; AL139118; CAH70740.1; -; Genomic_DNA.
EMBL; AL139124; CAH70740.1; JOINED; Genomic_DNA.
EMBL; AL365510; CAH70740.1; JOINED; Genomic_DNA.
EMBL; AL389885; CAH70740.1; JOINED; Genomic_DNA.
EMBL; AL389885; CAH73288.1; ALT_SEQ; Genomic_DNA.
EMBL; AL139118; CAH73288.1; JOINED; Genomic_DNA.
EMBL; AL139124; CAH73288.1; JOINED; Genomic_DNA.
EMBL; AL365510; CAH73288.1; JOINED; Genomic_DNA.
EMBL; AL389885; CAH73289.1; -; Genomic_DNA.
EMBL; AL139118; CAH73289.1; JOINED; Genomic_DNA.
EMBL; AL139124; CAH73289.1; JOINED; Genomic_DNA.
EMBL; AL365510; CAH73289.1; JOINED; Genomic_DNA.
EMBL; AL365510; CAH73757.1; ALT_SEQ; Genomic_DNA.
EMBL; AL139118; CAH73757.1; JOINED; Genomic_DNA.
EMBL; AL139124; CAH73757.1; JOINED; Genomic_DNA.
EMBL; AL389885; CAH73757.1; JOINED; Genomic_DNA.
EMBL; AL365510; CAH73758.1; -; Genomic_DNA.
EMBL; AL139118; CAH73758.1; JOINED; Genomic_DNA.
EMBL; AL139124; CAH73758.1; JOINED; Genomic_DNA.
EMBL; AL389885; CAH73758.1; JOINED; Genomic_DNA.
EMBL; AL139124; CAI16674.1; ALT_SEQ; Genomic_DNA.
EMBL; AL139118; CAI16674.1; JOINED; Genomic_DNA.
EMBL; AL365510; CAI16674.1; JOINED; Genomic_DNA.
EMBL; AL389885; CAI16674.1; JOINED; Genomic_DNA.
EMBL; AL139124; CAI16675.1; -; Genomic_DNA.
EMBL; AL139118; CAI16675.1; JOINED; Genomic_DNA.
EMBL; AL365510; CAI16675.1; JOINED; Genomic_DNA.
EMBL; AL389885; CAI16675.1; JOINED; Genomic_DNA.
EMBL; CH471066; EAW50042.1; -; Genomic_DNA.
EMBL; CH471066; EAW50043.1; -; Genomic_DNA.
EMBL; BC140705; AAI40706.1; -; mRNA.
EMBL; BC151854; AAI51855.1; -; mRNA.
EMBL; AF117948; AAF22005.1; ALT_FRAME; mRNA.
EMBL; AK022543; BAB14090.1; ALT_INIT; mRNA.
EMBL; AK289852; BAF82541.1; -; mRNA.
EMBL; AY995135; AAY45890.1; -; mRNA.
CCDS; CCDS41552.1; -. [Q9P212-1]
CCDS; CCDS53555.1; -. [Q9P212-2]
RefSeq; NP_001159451.1; NM_001165979.2. [Q9P212-2]
RefSeq; NP_001275918.1; NM_001288989.1.
RefSeq; NP_057425.3; NM_016341.3. [Q9P212-1]
UniGene; Hs.655033; -.
PDB; 2BYE; NMR; -; A=2006-2114.
PDB; 2BYF; NMR; -; A=2131-2246.
PDB; 2C5L; X-ray; 1.90 A; C/D=2131-2246.
PDBsum; 2BYE; -.
PDBsum; 2BYF; -.
PDBsum; 2C5L; -.
ProteinModelPortal; Q9P212; -.
SMR; Q9P212; -.
BioGrid; 119370; 5.
IntAct; Q9P212; 3.
STRING; 9606.ENSP00000260766; -.
SwissLipids; SLP:000000663; -.
iPTMnet; Q9P212; -.
PhosphoSitePlus; Q9P212; -.
BioMuta; PLCE1; -.
DMDM; 118595723; -.
PaxDb; Q9P212; -.
PeptideAtlas; Q9P212; -.
PRIDE; Q9P212; -.
ProteomicsDB; 83705; -.
ProteomicsDB; 83706; -. [Q9P212-2]
Ensembl; ENST00000371375; ENSP00000360426; ENSG00000138193. [Q9P212-2]
Ensembl; ENST00000371380; ENSP00000360431; ENSG00000138193. [Q9P212-1]
Ensembl; ENST00000371385; ENSP00000360438; ENSG00000138193. [Q9P212-2]
GeneID; 51196; -.
KEGG; hsa:51196; -.
UCSC; uc001kjk.4; human. [Q9P212-1]
CTD; 51196; -.
DisGeNET; 51196; -.
EuPathDB; HostDB:ENSG00000138193.14; -.
GeneCards; PLCE1; -.
H-InvDB; HIX0009051; -.
H-InvDB; HIX0035415; -.
HGNC; HGNC:17175; PLCE1.
HPA; HPA015597; -.
HPA; HPA015598; -.
MalaCards; PLCE1; -.
MIM; 608414; gene.
MIM; 610725; phenotype.
neXtProt; NX_Q9P212; -.
OpenTargets; ENSG00000138193; -.
Orphanet; 93217; Familial idiopathic steroid-resistant nephrotic syndrome with diffuse mesangial sclerosis.
Orphanet; 93213; Familial idiopathic steroid-resistant nephrotic syndrome with focal segmental hyalinosis.
PharmGKB; PA33391; -.
eggNOG; KOG0169; Eukaryota.
eggNOG; ENOG410XPSW; LUCA.
GeneTree; ENSGT00730000110782; -.
HOVERGEN; HBG059220; -.
InParanoid; Q9P212; -.
KO; K05860; -.
OMA; CCWNMGN; -.
OrthoDB; EOG091G03PC; -.
PhylomeDB; Q9P212; -.
TreeFam; TF314432; -.
BioCyc; MetaCyc:HS06473-MONOMER; -.
BRENDA; 3.1.4.11; 2681.
Reactome; R-HSA-1855204; Synthesis of IP3 and IP4 in the cytosol.
SIGNOR; Q9P212; -.
ChiTaRS; PLCE1; human.
EvolutionaryTrace; Q9P212; -.
GeneWiki; PLCE1; -.
GenomeRNAi; 51196; -.
PRO; PR:Q9P212; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000138193; -.
Genevisible; Q9P212; HS.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; TAS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IDA:UniProtKB.
GO; GO:0004629; F:phospholipase C activity; IDA:UniProtKB.
GO; GO:0017016; F:Ras GTPase binding; IDA:UniProtKB.
GO; GO:0000187; P:activation of MAPK activity; IDA:UniProtKB.
GO; GO:0019722; P:calcium-mediated signaling; TAS:UniProtKB.
GO; GO:0008283; P:cell proliferation; NAS:UniProtKB.
GO; GO:0007010; P:cytoskeleton organization; NAS:UniProtKB.
GO; GO:0006651; P:diacylglycerol biosynthetic process; TAS:UniProtKB.
GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; NAS:UniProtKB.
GO; GO:0032835; P:glomerulus development; IMP:HGNC.
GO; GO:0007507; P:heart development; TAS:UniProtKB.
GO; GO:0043647; P:inositol phosphate metabolic process; TAS:Reactome.
GO; GO:0048016; P:inositol phosphate-mediated signaling; TAS:UniProtKB.
GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
GO; GO:0007200; P:phospholipase C-activating G-protein coupled receptor signaling pathway; IDA:UniProtKB.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; TAS:UniProtKB.
GO; GO:0007265; P:Ras protein signal transduction; IDA:UniProtKB.
GO; GO:0001558; P:regulation of cell growth; TAS:UniProtKB.
GO; GO:0008277; P:regulation of G-protein coupled receptor protein signaling pathway; IDA:UniProtKB.
GO; GO:0045859; P:regulation of protein kinase activity; IDA:UniProtKB.
GO; GO:0046578; P:regulation of Ras protein signal transduction; IDA:UniProtKB.
GO; GO:0006940; P:regulation of smooth muscle contraction; TAS:UniProtKB.
Gene3D; 2.60.40.150; -; 1.
Gene3D; 3.20.20.190; -; 2.
InterPro; IPR000008; C2_dom.
InterPro; IPR035892; C2_domain_sf.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR001192; PI-PLC_fam.
InterPro; IPR028398; PLC-epsilon1.
InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
InterPro; IPR015359; PLC_EF-hand-like.
InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
InterPro; IPR000159; RA_dom.
InterPro; IPR023578; Ras_GEF_dom_sf.
InterPro; IPR001895; RASGEF_cat_dom.
InterPro; IPR029071; Ubiquitin-like_domsf.
PANTHER; PTHR10336; PTHR10336; 1.
PANTHER; PTHR10336:SF6; PTHR10336:SF6; 1.
Pfam; PF00168; C2; 1.
Pfam; PF09279; EF-hand_like; 1.
Pfam; PF00388; PI-PLC-X; 1.
Pfam; PF00387; PI-PLC-Y; 1.
Pfam; PF00788; RA; 1.
Pfam; PF00617; RasGEF; 1.
PRINTS; PR00390; PHPHLIPASEC.
SMART; SM00239; C2; 1.
SMART; SM00148; PLCXc; 1.
SMART; SM00149; PLCYc; 1.
SMART; SM00314; RA; 1.
SMART; SM00147; RasGEF; 1.
SUPFAM; SSF47473; SSF47473; 2.
SUPFAM; SSF48366; SSF48366; 3.
SUPFAM; SSF51695; SSF51695; 3.
SUPFAM; SSF54236; SSF54236; 2.
PROSITE; PS50004; C2; 1.
PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PROSITE; PS50200; RA; 1.
PROSITE; PS50009; RASGEF_CAT; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Calcium; Cell membrane;
Complete proteome; Cytoplasm; Disease mutation; Golgi apparatus;
Guanine-nucleotide releasing factor; Hydrolase; Lipid degradation;
Lipid metabolism; Membrane; Metal-binding; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; Transducer.
CHAIN 1 2302 1-phosphatidylinositol 4,5-bisphosphate
phosphodiesterase epsilon-1.
/FTId=PRO_0000256238.
DOMAIN 531 790 Ras-GEF. {ECO:0000255|PROSITE-
ProRule:PRU00168}.
DOMAIN 1392 1540 PI-PLC X-box. {ECO:0000255|PROSITE-
ProRule:PRU00270}.
DOMAIN 1730 1846 PI-PLC Y-box. {ECO:0000255|PROSITE-
ProRule:PRU00271}.
DOMAIN 1856 1956 C2. {ECO:0000255|PROSITE-
ProRule:PRU00041}.
DOMAIN 2012 2114 Ras-associating 1. {ECO:0000255|PROSITE-
ProRule:PRU00166}.
DOMAIN 2135 2238 Ras-associating 2. {ECO:0000255|PROSITE-
ProRule:PRU00166}.
REGION 1686 1764 Required for activation by RHOA, RHOB,
GNA12, GNA13 and G-beta gamma.
{ECO:0000250}.
ACT_SITE 1407 1407 {ECO:0000255|PROSITE-ProRule:PRU00270}.
ACT_SITE 1452 1452 {ECO:0000255|PROSITE-ProRule:PRU00270}.
MOD_RES 1096 1096 Phosphoserine.
{ECO:0000250|UniProtKB:Q8K4S1}.
VAR_SEQ 1 308 Missing (in isoform 2).
{ECO:0000303|PubMed:11022047,
ECO:0000303|PubMed:14702039}.
/FTId=VSP_021335.
VAR_SEQ 309 402 DVEEDAFKSKKERSTLLVRRFCKNDREVKKSVYTGTRAIVR
TLPSGHIGLTAWSYIDQKRNGPLLPCGRVMEPPSTVEIRQD
GSQRLSEAQWYP -> MVSEGSAAGRDFAGMEEVRQLHVRF
CKGIKIWHQAWFLCSLLGREPQEREAGCQLWLCTLSAVLKV
GWLFPLSEVPNFTLLKDGCGCWRLKEDQ (in isoform
2). {ECO:0000303|PubMed:11022047,
ECO:0000303|PubMed:14702039}.
/FTId=VSP_021336.
VARIANT 469 469 S -> T (in dbSNP:rs17508082).
/FTId=VAR_031843.
VARIANT 548 548 R -> L (in dbSNP:rs17417407).
/FTId=VAR_031844.
VARIANT 1484 1484 S -> L (in NPHS3; gives rise to focal
segmental glomerulosclerosis rather than
diffuse mesangial sclerosis;
dbSNP:rs121912605).
{ECO:0000269|PubMed:17086182}.
/FTId=VAR_029883.
VARIANT 1575 1575 R -> P (in dbSNP:rs2274224).
/FTId=VAR_031845.
VARIANT 1777 1777 T -> I (in dbSNP:rs3765524).
{ECO:0000269|PubMed:11022048,
ECO:0000269|Ref.8}.
/FTId=VAR_031846.
VARIANT 1927 1927 H -> R (in dbSNP:rs2274223).
{ECO:0000269|PubMed:10819331,
ECO:0000269|PubMed:11022048,
ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.8}.
/FTId=VAR_031847.
MUTAGEN 1452 1452 H->L: Loss of the phospholipase C
enzymatic activity. Still activates HRAS
and the MAP kinase pathway.
{ECO:0000269|PubMed:11022047}.
MUTAGEN 2140 2140 Q->E: Increases 2.8-fold the affinity for
HRAS. {ECO:0000269|PubMed:16483931}.
MUTAGEN 2148 2148 Q->E: Decreases 17.5-fold the affinity
for HRAS. {ECO:0000269|PubMed:16483931}.
MUTAGEN 2148 2148 Q->K: Increases 1.4-fold the affinity for
HRAS. {ECO:0000269|PubMed:16483931}.
MUTAGEN 2150 2150 R->L: Abolishes interaction with HRAS.
{ECO:0000269|PubMed:16483931}.
MUTAGEN 2171 2171 K->L: No effect on HRAS-binding.
{ECO:0000269|PubMed:16483931}.
MUTAGEN 2174 2174 Y->L: Reduces HRAS-binding.
{ECO:0000269|PubMed:16483931}.
CONFLICT 502 502 G -> S (in Ref. 2; AAG28341).
{ECO:0000305}.
CONFLICT 703 703 V -> F (in Ref. 2; AAG28341).
{ECO:0000305}.
CONFLICT 1133 1133 E -> K (in Ref. 2; AAG28341).
{ECO:0000305}.
CONFLICT 1229 1230 SR -> QA (in Ref. 8; AAF22005).
{ECO:0000305}.
CONFLICT 1456 1456 L -> P (in Ref. 1; AAG17145).
{ECO:0000305}.
CONFLICT 1571 1571 N -> D (in Ref. 9; BAB14090).
{ECO:0000305}.
CONFLICT 1575 1575 R -> Q (in Ref. 2; AAG28341).
{ECO:0000305}.
CONFLICT 1672 1672 C -> R (in Ref. 1; AAG17145).
{ECO:0000305}.
CONFLICT 1705 1705 P -> L (in Ref. 9; BAB14090).
{ECO:0000305}.
CONFLICT 2125 2125 D -> G (in Ref. 9; BAB14090).
{ECO:0000305}.
STRAND 2015 2020 {ECO:0000244|PDB:2BYE}.
STRAND 2022 2031 {ECO:0000244|PDB:2BYE}.
HELIX 2038 2046 {ECO:0000244|PDB:2BYE}.
STRAND 2049 2052 {ECO:0000244|PDB:2BYE}.
STRAND 2058 2064 {ECO:0000244|PDB:2BYE}.
STRAND 2069 2072 {ECO:0000244|PDB:2BYE}.
STRAND 2081 2084 {ECO:0000244|PDB:2BYE}.
STRAND 2086 2088 {ECO:0000244|PDB:2BYE}.
HELIX 2090 2096 {ECO:0000244|PDB:2BYE}.
TURN 2099 2103 {ECO:0000244|PDB:2BYE}.
STRAND 2107 2112 {ECO:0000244|PDB:2BYE}.
STRAND 2136 2143 {ECO:0000244|PDB:2C5L}.
STRAND 2150 2156 {ECO:0000244|PDB:2C5L}.
HELIX 2161 2171 {ECO:0000244|PDB:2C5L}.
TURN 2172 2174 {ECO:0000244|PDB:2C5L}.
HELIX 2176 2180 {ECO:0000244|PDB:2C5L}.
HELIX 2184 2186 {ECO:0000244|PDB:2C5L}.
STRAND 2187 2194 {ECO:0000244|PDB:2C5L}.
STRAND 2198 2204 {ECO:0000244|PDB:2BYF}.
STRAND 2207 2211 {ECO:0000244|PDB:2C5L}.
HELIX 2218 2223 {ECO:0000244|PDB:2C5L}.
STRAND 2229 2235 {ECO:0000244|PDB:2C5L}.
TURN 2236 2238 {ECO:0000244|PDB:2C5L}.
SEQUENCE 2302 AA; 258715 MW; 71DDE446277077A3 CRC64;
MTSEEMTASV LIPVTQRKVV SAQSAADESS EKVSDINISK AHTVRRSGET SHTISQLNKL
KEEPSGSNLP KILSIAREKI VSDENSNEKC WEKIMPDSAK NLNINCNNIL RNHQHGLPQR
QFYEMYNSVA EEDLCLETGI PSPLERKVFP GIQLELDRPS MGISPLGNQS VIIETGRAHP
DSRRAVFHFH YEVDRRMSDT FCTLSENLIL DDCGNCVPLP GGEEKQKKNY VAYTCKLMEL
AKNCDNKNEQ LQCDHCDTLN DKYFCFEGSC EKVDMVYSGD SFCRKDFTDS QAAKTFLSHF
EDFPDNCDDV EEDAFKSKKE RSTLLVRRFC KNDREVKKSV YTGTRAIVRT LPSGHIGLTA
WSYIDQKRNG PLLPCGRVME PPSTVEIRQD GSQRLSEAQW YPIYNAVRRE ETENTVGSLL
HFLTKLPASE TAHGRISVGP CLKQCVRDTV CEYRATLQRT SISQYITGSL LEATTSLGAR
SGLLSTFGGS TGRMMLKERQ PGPSVANSNA LPSSSAGISK ELIDLQPLIQ FPEEVASILM
EQEQTIYRRV LPVDYLCFLT RDLGTPECQS SLPCLKASIS ASILTTQNGE HNALEDLVMR
FNEVSSWVTW LILTAGSMEE KREVFSYLVH VAKCCWNMGN YNAVMEFLAG LRSRKVLKMW
QFMDQSDIET MRSLKDAMAQ HESSCEYRKV VTRALHIPGC KVVPFCGVFL KELCEVLDGA
SGLMKLCPRY NSQEETLEFV ADYSGQDNFL QRVGQNGLKN SEKESTVNSI FQVIRSCNRS
LETDEEDSPS EGNSSRKSSL KDKSRWQFII GDLLDSDNDI FEQSKEYDSH GSEDSQKAFD
HGTELIPWYV LSIQADVHQF LLQGATVIHY DQDTHLSARC FLQLQPDNST LTWVKPTTAS
PASSKAKLGV LNNTAEPGKF PLLGNAGLSS LTEGVLDLFA VKAVYMGHPG IDIHTVCVQN
KLGSMFLSET GVTLLYGLQT TDNRLLHFVA PKHTAKMLFS GLLELTRAVR KMRKFPDQRQ
QWLRKQYVSL YQEDGRYEGP TLAHAVELFG GRRWSARNPS PGTSAKNAEK PNMQRNNTLG
ISTTKKKKKI LMRGESGEVT DDEMATRKAK MHKECRSRSG SDPQDINEQE ESEVNAIANP
PNPLPSRRAH SLTTAGSPNL AAGTSSPIRP VSSPVLSSSN KSPSSAWSSS SWHGRIKGGM
KGFQSFMVSD SNMSFVEFVE LFKSFSVRSR KDLKDLFDVY AVPCNRSGSE SAPLYTNLTI
DENTSDLQPD LDLLTRNVSD LGLFIKSKQQ LSDNQRQISD AIAAASIVTN GTGIESTSLG
IFGVGILQLN DFLVNCQGEH CTYDEILSII QKFEPSISMC HQGLMSFEGF ARFLMDKENF
ASKNDESQEN IKELQLPLSY YYIESSHNTY LTGHQLKGES SVELYSQVLL QGCRSVELDC
WDGDDGMPII YHGHTLTTKI PFKEVVEAID RSAFINSDLP IIISIENHCS LPQQRKMAEI
FKTVFGEKLV TKFLFETDFS DDPMLPSPDQ LRKKVLLKNK KLKAHQTPVD ILKQKAHQLA
SMQVQAYNGG NANPRPANNE EEEDEEDEYD YDYESLSDDN ILEDRPENKS CNDKLQFEYN
EEIPKRIKKA DNSACNKGKV YDMELGEEFY LDQNKKESRQ IAPELSDLVI YCQAVKFPGL
STLNASGSSR GKERKSRKSI FGNNPGRMSP GETASFNKTS GKSSCEGIRQ TWEESSSPLN
PTTSLSAIIR TPKCYHISSL NENAAKRLCR RYSQKLTQHT ACQLLRTYPA ATRIDSSNPN
PLMFWLHGIQ LVALNYQTDD LPLHLNAAMF EANGGCGYVL KPPVLWDKNC PMYQKFSPLE
RDLDSMDPAV YSLTIVSGQN VCPSNSMGSP CIEVDVLGMP LDSCHFRTKP IHRNTLNPMW
NEQFLFHVHF EDLVFLRFAV VENNSSAVTA QRIIPLKALK RGYRHLQLRN LHNEVLEISS
LFINSRRMEE NSSGNTMSAS SMFNTEERKC LQTHRVTVHG VPGPEPFTVF TINGGTKAKQ
LLQQILTNEQ DIKPVTTDYF LMEEKYFISK EKNECRKQPF QRAIGPEEEI MQILSSWFPE
EGYMGRIVLK TQQENLEEKN IVQDDKEVIL SSEEESFFVQ VHDVSPEQPR TVIKAPRVST
AQDVIQQTLC KAKYSYSILS NPNPSDYVLL EEVVKDTTNK KTTTPKSSQR VLLDQECVFQ
AQSKWKGAGK FILKLKEQVQ ASREDKKKGI SFASELKKLT KSTKQPRGLT SPSQLLTSES
IQTKEEKPVG GLSSSDTMDY RQ


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