Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2 (EC 3.1.4.11) (Phosphoinositide phospholipase C-gamma-2) (Phospholipase C-IV) (PLC-IV) (Phospholipase C-gamma-2) (PLC-gamma-2)

 PLCG2_HUMAN             Reviewed;        1265 AA.
P16885; D3DUL3; Q3ZTS2; Q59H45; Q969T5;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
25-NOV-2008, sequence version 4.
28-MAR-2018, entry version 211.
RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2;
EC=3.1.4.11;
AltName: Full=Phosphoinositide phospholipase C-gamma-2;
AltName: Full=Phospholipase C-IV;
Short=PLC-IV;
AltName: Full=Phospholipase C-gamma-2;
Short=PLC-gamma-2;
Name=PLCG2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Lymphoblast;
PubMed=2849563; DOI=10.1016/0014-5793(88)80979-7;
Ohta S., Matsui A., Nazawa Y., Kagawa Y.;
"Complete cDNA encoding a putative phospholipase C from transformed
human lymphocytes.";
FEBS Lett. 242:31-35(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Spleen;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=16533400; DOI=10.1186/1471-2164-7-48;
Kemmer D., Podowski R.M., Arenillas D., Lim J., Hodges E., Roth P.,
Sonnhammer E.L.L., Hoeoeg C., Wasserman W.W.;
"NovelFam3000 -- uncharacterized human protein domains conserved
across model organisms.";
BMC Genomics 7:48-48(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[5]
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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ARG-244 AND
TYR-883.
TISSUE=Lymph;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PHOSPHORYLATION AT TYR-753 AND TYR-759.
PubMed=11606584; DOI=10.1074/jbc.M107577200;
Rodriguez R., Matsuda M., Perisic O., Bravo J., Paul A., Jones N.P.,
Light Y., Swann K., Williams R.L., Katan M.;
"Tyrosine residues in phospholipase Cgamma 2 essential for the enzyme
function in B-cell signaling.";
J. Biol. Chem. 276:47982-47992(2001).
[8]
PHOSPHORYLATION AT TYR-753 AND TYR-759.
PubMed=12181444; DOI=10.1124/mol.62.3.672;
Ozdener F., Dangelmaier C., Ashby B., Kunapuli S.P., Daniel J.L.;
"Activation of phospholipase Cgamma2 by tyrosine phosphorylation.";
Mol. Pharmacol. 62:672-679(2002).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1245, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=15144186; DOI=10.1021/ac035352d;
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
Peters E.C.;
"Robust phosphoproteomic profiling of tyrosine phosphorylation sites
from human T cells using immobilized metal affinity chromatography and
tandem mass spectrometry.";
Anal. Chem. 76:2763-2772(2004).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-753; TYR-759 AND
TYR-1217, 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).
[11]
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).
[12]
INVOLVEMENT IN FCAS3.
PubMed=22236196; DOI=10.1056/NEJMoa1102140;
Ombrello M.J., Remmers E.F., Sun G., Freeman A.F., Datta S.,
Torabi-Parizi P., Subramanian N., Bunney T.D., Baxendale R.W.,
Martins M.S., Romberg N., Komarow H., Aksentijevich I., Kim H.S.,
Ho J., Cruse G., Jung M.Y., Gilfillan A.M., Metcalfe D.D., Nelson C.,
O'Brien M., Wisch L., Stone K., Douek D.C., Gandhi C., Wanderer A.A.,
Lee H., Nelson S.F., Shianna K.V., Cirulli E.T., Goldstein D.B.,
Long E.O., Moir S., Meffre E., Holland S.M., Kastner D.L., Katan M.,
Hoffman H.M., Milner J.D.;
"Cold urticaria, immunodeficiency, and autoimmunity related to PLCG2
deletions.";
N. Engl. J. Med. 366:330-338(2012).
[13]
VARIANT APLAID TYR-707.
PubMed=23000145; DOI=10.1016/j.ajhg.2012.08.006;
Zhou Q., Lee G.S., Brady J., Datta S., Katan M., Sheikh A.,
Martins M.S., Bunney T.D., Santich B.H., Moir S., Kuhns D.B.,
Long Priel D.A., Ombrello A., Stone D., Ombrello M.J., Khan J.,
Milner J.D., Kastner D.L., Aksentijevich I.;
"A hypermorphic missense mutation in PLCG2, encoding phospholipase
Cgamma2, causes a dominantly inherited autoinflammatory disease with
immunodeficiency.";
Am. J. Hum. Genet. 91:713-720(2012).
[14]
VARIANTS TRP-665 AND PHE-845.
PubMed=24869598; DOI=10.1056/NEJMoa1400029;
Woyach J.A., Furman R.R., Liu T.M., Ozer H.G., Zapatka M.,
Ruppert A.S., Xue L., Li D.H., Steggerda S.M., Versele M., Dave S.S.,
Zhang J., Yilmaz A.S., Jaglowski S.M., Blum K.A., Lozanski A.,
Lozanski G., James D.F., Barrientos J.C., Lichter P., Stilgenbauer S.,
Buggy J.J., Chang B.Y., Johnson A.J., Byrd J.C.;
"Resistance mechanisms for the Bruton's tyrosine kinase inhibitor
ibrutinib.";
N. Engl. J. Med. 370:2286-2294(2014).
-!- 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. It is a crucial enzyme in transmembrane signaling.
-!- CATALYTIC ACTIVITY: 1-phosphatidyl-1D-myo-inositol 4,5-
bisphosphate + H(2)O = 1D-myo-inositol 1,4,5-trisphosphate +
diacylglycerol.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
-!- SUBUNIT: Interacts (via SH2 domain) with CSF1R (tyrosine
phosphorylated). {ECO:0000250}.
-!- INTERACTION:
P10275:AR; NbExp=6; IntAct=EBI-617403, EBI-608057;
P00533:EGFR; NbExp=5; IntAct=EBI-617403, EBI-297353;
P19235:EPOR; NbExp=3; IntAct=EBI-617403, EBI-617321;
P04626:ERBB2; NbExp=3; IntAct=EBI-617403, EBI-641062;
O95073-2:FSBP; NbExp=2; IntAct=EBI-617403, EBI-10696047;
Q13480:GAB1; NbExp=15; IntAct=EBI-617403, EBI-517684;
P10721:KIT; NbExp=8; IntAct=EBI-617403, EBI-1379503;
P27986:PIK3R1; NbExp=2; IntAct=EBI-617403, EBI-79464;
O43242:PSMD3; NbExp=2; IntAct=EBI-617403, EBI-357622;
O14796:SH2D1B; NbExp=2; IntAct=EBI-617403, EBI-3923013;
-!- PTM: Phosphorylated on tyrosine residues by CSF1R (By similarity).
Phosphorylated on tyrosine residues by BTK and SYK; upon ligand-
induced activation of a variety of growth factor receptors and
immune system receptors. Phosphorylation leads to increased
phospholipase activity. {ECO:0000250, ECO:0000269|PubMed:11606584,
ECO:0000269|PubMed:12181444}.
-!- DISEASE: Familial cold autoinflammatory syndrome 3 (FCAS3)
[MIM:614468]: An autosomal dominant immune disorder characterized
by the development of cutaneous urticaria, erythema, and pruritis
in response to cold exposure. Affected individuals have variable
additional immunologic defects, including antibody deficiency,
decreased numbers of B-cells, defective B-cells, increased
susceptibility to infection, and increased risk of autoimmune
disorders. {ECO:0000269|PubMed:22236196}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- DISEASE: Autoinflammation, antibody deficiency, and immune
dysregulation PLCG2-associated (APLAID) [MIM:614878]: An autosomal
dominant systemic disorder characterized by recurrent blistering
skin lesions with a dense inflammatory infiltrate and variable
involvement of other tissues, including joints, the eye, and the
gastrointestinal tract. Affected individuals have a mild humoral
immune deficiency associated with recurrent sinopulmonary
infections, but no evidence of circulating autoantibodies.
{ECO:0000269|PubMed:23000145}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SEQUENCE CAUTION:
Sequence=AAA60112.1; Type=Frameshift; Positions=1242; Evidence={ECO:0000305};
Sequence=AAQ76815.1; Type=Frameshift; Positions=1242; Evidence={ECO:0000305};
Sequence=BAD92151.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=CAA32194.1; Type=Frameshift; Positions=1242; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M37238; AAA60112.1; ALT_FRAME; mRNA.
EMBL; X14034; CAA32194.1; ALT_FRAME; mRNA.
EMBL; AB208914; BAD92151.1; ALT_INIT; mRNA.
EMBL; AY364256; AAQ76815.1; ALT_FRAME; mRNA.
EMBL; AC092142; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC098966; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC099524; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471114; EAW95524.1; -; Genomic_DNA.
EMBL; CH471114; EAW95525.1; -; Genomic_DNA.
EMBL; BC007565; AAH07565.1; -; mRNA.
EMBL; BC011772; AAH11772.1; -; mRNA.
EMBL; BC014561; AAH14561.1; -; mRNA.
EMBL; BC018646; AAH18646.1; -; mRNA.
CCDS; CCDS42204.1; -.
PIR; S02004; S02004.
RefSeq; NP_002652.2; NM_002661.4.
UniGene; Hs.372303; -.
UniGene; Hs.413111; -.
UniGene; Hs.586906; -.
PDB; 2K2J; NMR; -; A=471-514, A=841-913.
PDB; 2W2W; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I/J/K/L=471-514, A/B/C/D/E/F/G/H/I/J/K/L=841-913.
PDB; 2W2X; X-ray; 2.30 A; C/D=471-514, C/D=841-913.
PDBsum; 2K2J; -.
PDBsum; 2W2W; -.
PDBsum; 2W2X; -.
ProteinModelPortal; P16885; -.
SMR; P16885; -.
BioGrid; 111352; 44.
CORUM; P16885; -.
IntAct; P16885; 37.
MINT; P16885; -.
STRING; 9606.ENSP00000352336; -.
BindingDB; P16885; -.
ChEMBL; CHEMBL4100; -.
GuidetoPHARMACOLOGY; 1408; -.
SwissLipids; SLP:000000647; -.
iPTMnet; P16885; -.
PhosphoSitePlus; P16885; -.
BioMuta; PLCG2; -.
DMDM; 215274231; -.
EPD; P16885; -.
MaxQB; P16885; -.
PaxDb; P16885; -.
PeptideAtlas; P16885; -.
PRIDE; P16885; -.
DNASU; 5336; -.
Ensembl; ENST00000564138; ENSP00000482457; ENSG00000197943.
GeneID; 5336; -.
KEGG; hsa:5336; -.
UCSC; uc002fgt.4; human.
CTD; 5336; -.
DisGeNET; 5336; -.
EuPathDB; HostDB:ENSG00000197943.9; -.
GeneCards; PLCG2; -.
HGNC; HGNC:9066; PLCG2.
HPA; CAB004280; -.
HPA; HPA020099; -.
HPA; HPA020100; -.
MalaCards; PLCG2; -.
MIM; 600220; gene.
MIM; 614468; phenotype.
MIM; 614878; phenotype.
neXtProt; NX_P16885; -.
OpenTargets; ENSG00000197943; -.
Orphanet; 324530; Autoinflammation-PLCG2-associated antibody deficiency-immune dysregulation.
Orphanet; 300359; PLCG2-associated antibody deficiency and immune dysregulation.
PharmGKB; PA33393; -.
eggNOG; KOG1264; Eukaryota.
eggNOG; ENOG410XPXE; LUCA.
GeneTree; ENSGT00730000110782; -.
HOGENOM; HOG000230864; -.
HOVERGEN; HBG053611; -.
InParanoid; P16885; -.
KO; K05859; -.
OMA; MLMRIPR; -.
OrthoDB; EOG091G07R3; -.
PhylomeDB; P16885; -.
TreeFam; TF313216; -.
BioCyc; MetaCyc:HS06773-MONOMER; -.
BRENDA; 3.1.4.11; 2681.
Reactome; R-HSA-114604; GPVI-mediated activation cascade.
Reactome; R-HSA-166016; Toll Like Receptor 4 (TLR4) Cascade.
Reactome; R-HSA-1855204; Synthesis of IP3 and IP4 in the cytosol.
Reactome; R-HSA-2029485; Role of phospholipids in phagocytosis.
Reactome; R-HSA-2424491; DAP12 signaling.
Reactome; R-HSA-2871796; FCERI mediated MAPK activation.
Reactome; R-HSA-2871809; FCERI mediated Ca+2 mobilization.
Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-HSA-5621480; Dectin-2 family.
Reactome; R-HSA-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
SignaLink; P16885; -.
SIGNOR; P16885; -.
EvolutionaryTrace; P16885; -.
GeneWiki; PLCG2; -.
GenomeRNAi; 5336; -.
PRO; PR:P16885; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000197943; -.
CleanEx; HS_PLCG2; -.
ExpressionAtlas; P16885; baseline and differential.
Genevisible; P16885; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IDA:UniProtKB.
GO; GO:0004629; F:phospholipase C activity; TAS:Reactome.
GO; GO:0001784; F:phosphotyrosine residue binding; IPI:CAFA.
GO; GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW.
GO; GO:0032237; P:activation of store-operated calcium channel activity; IEA:Ensembl.
GO; GO:0030183; P:B cell differentiation; ISS:UniProtKB.
GO; GO:0050853; P:B cell receptor signaling pathway; ISS:UniProtKB.
GO; GO:0019722; P:calcium-mediated signaling; NAS:UniProtKB.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
GO; GO:0002316; P:follicular B cell differentiation; IEA:Ensembl.
GO; GO:0043647; P:inositol phosphate metabolic process; TAS:Reactome.
GO; GO:0032959; P:inositol trisphosphate biosynthetic process; IEA:Ensembl.
GO; GO:0043069; P:negative regulation of programmed cell death; IEA:Ensembl.
GO; GO:0006661; P:phosphatidylinositol biosynthetic process; IDA:UniProtKB.
GO; GO:0009395; P:phospholipid catabolic process; IEA:InterPro.
GO; GO:0030168; P:platelet activation; TAS:Reactome.
GO; GO:0002092; P:positive regulation of receptor internalization; IEA:Ensembl.
GO; GO:0032481; P:positive regulation of type I interferon production; IEA:Ensembl.
GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl.
GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IDA:UniProtKB.
GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
GO; GO:0050852; P:T cell receptor signaling pathway; ISS:UniProtKB.
GO; GO:0016055; P:Wnt signaling pathway; TAS:UniProtKB.
CDD; cd09932; SH2_C-SH2_PLC_gamma_like; 1.
CDD; cd10341; SH2_N-SH2_PLC_gamma_like; 1.
CDD; cd11969; SH3_PLCgamma2; 1.
Gene3D; 2.30.29.30; -; 2.
Gene3D; 2.60.40.150; -; 1.
Gene3D; 3.20.20.190; -; 2.
Gene3D; 3.30.505.10; -; 2.
InterPro; IPR000008; C2_dom.
InterPro; IPR035892; C2_domain_sf.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
InterPro; IPR001192; PI-PLC_fam.
InterPro; IPR016279; PLC-gamma.
InterPro; IPR028381; PLC-gamma2.
InterPro; IPR035023; PLC-gamma_C-SH2.
InterPro; IPR035024; PLC-gamma_N-SH2.
InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
InterPro; IPR035723; PLCgamma2_SH3.
InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
PANTHER; PTHR10336; PTHR10336; 1.
PANTHER; PTHR10336:SF25; PTHR10336:SF25; 1.
Pfam; PF00168; C2; 1.
Pfam; PF00388; PI-PLC-X; 1.
Pfam; PF00387; PI-PLC-Y; 1.
Pfam; PF00017; SH2; 2.
Pfam; PF00018; SH3_1; 1.
PIRSF; PIRSF000952; PLC-gamma; 1.
PRINTS; PR00390; PHPHLIPASEC.
PRINTS; PR00401; SH2DOMAIN.
PRINTS; PR00452; SH3DOMAIN.
SMART; SM00239; C2; 1.
SMART; SM00233; PH; 2.
SMART; SM00148; PLCXc; 1.
SMART; SM00149; PLCYc; 1.
SMART; SM00252; SH2; 2.
SMART; SM00326; SH3; 1.
SUPFAM; SSF47473; SSF47473; 1.
SUPFAM; SSF50044; SSF50044; 1.
SUPFAM; SSF51695; SSF51695; 2.
SUPFAM; SSF55550; SSF55550; 2.
PROSITE; PS50004; C2; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PROSITE; PS50001; SH2; 2.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
3D-structure; Calcium; Complete proteome; Disease mutation; Hydrolase;
Lipid degradation; Lipid metabolism; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; SH2 domain; SH3 domain; Transducer.
CHAIN 1 1265 1-phosphatidylinositol 4,5-bisphosphate
phosphodiesterase gamma-2.
/FTId=PRO_0000088501.
DOMAIN 20 131 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 312 456 PI-PLC X-box. {ECO:0000255|PROSITE-
ProRule:PRU00270}.
DOMAIN 532 635 SH2 1. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 646 735 SH2 2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 769 829 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 930 1044 PI-PLC Y-box. {ECO:0000255|PROSITE-
ProRule:PRU00271}.
DOMAIN 1059 1152 C2. {ECO:0000255|PROSITE-
ProRule:PRU00041}.
ACT_SITE 327 327 {ECO:0000255|PROSITE-ProRule:PRU00270}.
ACT_SITE 372 372 {ECO:0000255|PROSITE-ProRule:PRU00270}.
MOD_RES 753 753 Phosphotyrosine; by BTK.
{ECO:0000244|PubMed:19690332,
ECO:0000269|PubMed:11606584,
ECO:0000269|PubMed:12181444}.
MOD_RES 759 759 Phosphotyrosine; by BTK.
{ECO:0000244|PubMed:19690332,
ECO:0000269|PubMed:11606584,
ECO:0000269|PubMed:12181444}.
MOD_RES 1197 1197 Phosphotyrosine; by BTK.
{ECO:0000250|UniProtKB:P24135}.
MOD_RES 1217 1217 Phosphotyrosine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 1245 1245 Phosphotyrosine.
{ECO:0000244|PubMed:15144186}.
VARIANT 244 244 H -> R (in dbSNP:rs11548656).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_031560.
VARIANT 268 268 R -> W (in dbSNP:rs1143687).
/FTId=VAR_031561.
VARIANT 541 541 T -> A (in dbSNP:rs11548657).
/FTId=VAR_047427.
VARIANT 665 665 R -> W (found in patients with chronic
lymphocytic leukemia; associated with BTK
mutation S-481; unknown pathological
significance; results in resistance to
ibrutinib therapy).
{ECO:0000269|PubMed:24869598}.
/FTId=VAR_074310.
VARIANT 707 707 S -> Y (in APLAID; results in increased
epidermal growth factor-stimulated
production of intracellular IP3 and
increased intracellular calcium release;
is a hypermorphic mutation;
dbSNP:rs397514562).
{ECO:0000269|PubMed:23000145}.
/FTId=VAR_069211.
VARIANT 845 845 L -> F (found in patients with chronic
lymphocytic leukemia; associated with BTK
mutation S-481; unknown pathological
significance; results in resistance to
ibrutinib therapy).
{ECO:0000269|PubMed:24869598}.
/FTId=VAR_074311.
VARIANT 883 883 D -> Y (in dbSNP:rs17856213).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_047428.
CONFLICT 606 610 TFSSI -> RFRRM (in Ref. 1; CAA32194/
AAA60112 and 3; AAQ76815). {ECO:0000305}.
CONFLICT 623 623 R -> P (in Ref. 1; AAA60112/CAA32194 and
3; AAQ76815). {ECO:0000305}.
CONFLICT 745 745 M -> T (in Ref. 1; AAA60112/CAA32194 and
3; AAQ76815). {ECO:0000305}.
CONFLICT 880 880 Q -> E (in Ref. 1; AAA60112/CAA32194 and
3; AAQ76815). {ECO:0000305}.
CONFLICT 912 912 T -> S (in Ref. 1; AAA60112/CAA32194 and
3; AAQ76815). {ECO:0000305}.
CONFLICT 1095 1095 D -> G (in Ref. 1; AAA60112/CAA32194 and
3; AAQ76815). {ECO:0000305}.
TURN 815 817 {ECO:0000244|PDB:2W2X}.
STRAND 818 825 {ECO:0000244|PDB:2W2X}.
STRAND 828 831 {ECO:0000244|PDB:2W2X}.
HELIX 835 840 {ECO:0000244|PDB:2W2X}.
STRAND 850 854 {ECO:0000244|PDB:2W2X}.
HELIX 855 857 {ECO:0000244|PDB:2W2X}.
STRAND 858 862 {ECO:0000244|PDB:2W2X}.
STRAND 867 869 {ECO:0000244|PDB:2K2J}.
STRAND 870 882 {ECO:0000244|PDB:2W2X}.
STRAND 886 892 {ECO:0000244|PDB:2W2X}.
HELIX 893 907 {ECO:0000244|PDB:2W2X}.
SEQUENCE 1265 AA; 147870 MW; 1D56BCBF51D7A0D3 CRC64;
MSTTVNVDSL AEYEKSQIKR ALELGTVMTV FSFRKSTPER RTVQVIMETR QVAWSKTADK
IEGFLDIMEI KEIRPGKNSK DFERAKAVRQ KEDCCFTILY GTQFVLSTLS LAADSKEDAV
NWLSGLKILH QEAMNASTPT IIESWLRKQI YSVDQTRRNS ISLRELKTIL PLINFKVSSA
KFLKDKFVEI GAHKDELSFE QFHLFYKKLM FEQQKSILDE FKKDSSVFIL GNTDRPDASA
VYLHDFQRFL IHEQQEHWAQ DLNKVRERMT KFIDDTMRET AEPFLFVDEF LTYLFSRENS
IWDEKYDAVD MQDMNNPLSH YWISSSHNTY LTGDQLRSES SPEAYIRCLR MGCRCIELDC
WDGPDGKPVI YHGWTRTTKI KFDDVVQAIK DHAFVTSSFP VILSIEEHCS VEQQRHMAKA
FKEVFGDLLL TKPTEASADQ LPSPSQLREK IIIKHKKLGP RGDVDVNMED KKDEHKQQGE
LYMWDSIDQK WTRHYCAIAD AKLSFSDDIE QTMEEEVPQD IPPTELHFGE KWFHKKVEKR
TSAEKLLQEY CMETGGKDGT FLVRESETFP NDYTLSFWRS GRVQHCRIRS TMEGGTLKYY
LTDNLTFSSI YALIQHYRET HLRCAEFELR LTDPVPNPNP HESKPWYYDS LSRGEAEDML
MRIPRDGAFL IRKREGSDSY AITFRARGKV KHCRINRDGR HFVLGTSAYF ESLVELVSYY
EKHSLYRKMR LRYPVTPELL ERYNMERDIN SLYDVSRMYV DPSEINPSMP QRTVKALYDY
KAKRSDELSF CRGALIHNVS KEPGGWWKGD YGTRIQQYFP SNYVEDISTA DFEELEKQII
EDNPLGSLCR GILDLNTYNV VKAPQGKNQK SFVFILEPKQ QGDPPVEFAT DRVEELFEWF
QSIREITWKI DTKENNMKYW EKNQSIAIEL SDLVVYCKPT SKTKDNLENP DFREIRSFVE
TKADSIIRQK PVDLLKYNQK GLTRVYPKGQ RVDSSNYDPF RLWLCGSQMV ALNFQTADKY
MQMNHALFSL NGRTGYVLQP ESMRTEKYDP MPPESQRKIL MTLTVKVLGA RHLPKLGRSI
ACPFVEVEIC GAEYDNNKFK TTVVNDNGLS PIWAPTQEKV TFEIYDPNLA FLRFVVYEED
MFSDPNFLAH ATYPIKAVKS GFRSVPLKNG YSEDIELASL LVFCEMRPVL ESEEELYSSC
RQLRRRQEEL NNQLFLYDTH QNLRNANRDA LVKEFSVNEN QLQLYQEKCN KRLREKRVSN
SKFYS


Related products :

Catalog number Product name Quantity
E0269b ELISA 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-1,Bos taurus,Bovine,Phosphoinositide phospholipase C-gamma-1,Phospholipase C-gamma-1,Phospholipase C-II,PLC-148,PLCG1,PLC-gamma-1, 96T
U0269b CLIA 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-1,Bos taurus,Bovine,Phosphoinositide phospholipase C-gamma-1,Phospholipase C-gamma-1,Phospholipase C-II,PLC-148,PLCG1,PLC-gamma-1,P 96T
EIAAB31457 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-2,Homo sapiens,Human,Phosphoinositide phospholipase C-gamma-2,Phospholipase C-gamma-2,Phospholipase C-IV,PLCG2,PLC-gamma-2,PLC-IV
EIAAB31456 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-2,Phosphoinositide phospholipase C-gamma-2,Phospholipase C-gamma-2,Phospholipase C-IV,Plcg2,PLC-gamma-2,PLC-IV,Rat,Rattus norvegicus
U0269h CLIA 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-1,Homo sapiens,Human,Phosphoinositide phospholipase C-gamma-1,Phospholipase C-gamma-1,Phospholipase C-II,PLC1,PLC-148,PLCG1,PLC-gam 96T
E0269h ELISA kit 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-1,Homo sapiens,Human,Phosphoinositide phospholipase C-gamma-1,Phospholipase C-gamma-1,Phospholipase C-II,PLC1,PLC-148,PLCG1,P 96T
E0269h ELISA 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-1,Homo sapiens,Human,Phosphoinositide phospholipase C-gamma-1,Phospholipase C-gamma-1,Phospholipase C-II,PLC1,PLC-148,PLCG1,PLC-ga 96T
E0269b ELISA kit 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-1,Bos taurus,Bovine,Phosphoinositide phospholipase C-gamma-1,Phospholipase C-gamma-1,Phospholipase C-II,PLC-148,PLCG1,PLC-gam 96T
E0269m ELISA 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-1,Mouse,Mus musculus,Phosphoinositide phospholipase C-gamma-1,Phospholipase C-gamma-1,Plcg1,Plcg-1,PLC-gamma-1 96T
E0269m ELISA kit 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-1,Mouse,Mus musculus,Phosphoinositide phospholipase C-gamma-1,Phospholipase C-gamma-1,Plcg1,Plcg-1,PLC-gamma-1 96T
U0269m CLIA 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-1,Mouse,Mus musculus,Phosphoinositide phospholipase C-gamma-1,Phospholipase C-gamma-1,Plcg1,Plcg-1,PLC-gamma-1 96T
U0269r CLIA 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-1,Phosphoinositide phospholipase C-gamma-1,Phospholipase C-gamma-1,Plcg1,PLC-gamma-1,Rat,Rattus norvegicus 96T
E0269r ELISA kit 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-1,Phosphoinositide phospholipase C-gamma-1,Phospholipase C-gamma-1,Plcg1,PLC-gamma-1,Rat,Rattus norvegicus 96T
E0269r ELISA 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-1,Phosphoinositide phospholipase C-gamma-1,Phospholipase C-gamma-1,Plcg1,PLC-gamma-1,Rat,Rattus norvegicus 96T
EIAAB31458 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-2,Mouse,Mus musculus,Phosphoinositide phospholipase C-gamma-2,Phospholipase C-gamma-2,Plcg2,PLC-gamma-2
EIAAB31461 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase eta-2,Mouse,Mus musculus,Phosphoinositide phospholipase C-eta-2,Phosphoinositide phospholipase C-like 4,Phospholipase C-eta-2,Phospholipase C-
EIAAB31462 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase eta-2,Homo sapiens,Human,KIAA0450,Phosphoinositide phospholipase C-eta-2,Phosphoinositide phospholipase C-like 4,Phospholipase C-eta-2,Phospho
18-785-210378 PLC-gamma1 (Phospho-Tyr783) - EC 3.1.4.11; Phosphoinositide phospholipase C; PLC-gamma-1; Phospholipase C-gamma-1; PLC-II; PLC-148 Polyclonal 0.1 mg
18-785-210378 PLC-gamma1 (Phospho-Tyr783) - EC 3.1.4.11; Phosphoinositide phospholipase C; PLC-gamma-1; Phospholipase C-gamma-1; PLC-II; PLC-148 Polyclonal 0.05 mg
18-785-210380 PLC-gamma2 (Phospho-Tyr753) - EC 3.1.4.11; Phosphoinositide phospholipase C; PLC-gamma-2; Phospholipase C-gamma-2; PLC-IV Polyclonal 0.05 mg
18-785-210380 PLC-gamma2 (Phospho-Tyr753) - EC 3.1.4.11; Phosphoinositide phospholipase C; PLC-gamma-2; Phospholipase C-gamma-2; PLC-IV Polyclonal 0.1 mg
EIAAB31460 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase eta-1,Kiaa1069,Mouse,Mus musculus,Phosphoinositide phospholipase C-eta-1,Phospholipase C-eta-1,Phospholipase C-like protein 3,PLC-eta-1,Plch1,
EIAAB31459 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase eta-1,Homo sapiens,Human,KIAA1069,Phosphoinositide phospholipase C-eta-1,Phospholipase C-eta-1,Phospholipase C-like protein 3,PLC-eta-1,PLCH1,
EIAAB31576 Calcium-independent phospholipase A2-gamma,Intracellular membrane-associated calcium-independent phospholipase A2 gamma,Ipla22,Ipla2g,iPLA2-gamma,Mouse,Mus musculus,Patatin-like phospholipase domain-c
18-785-210381 PLC-gamma2 (Ab-753) - EC 3.1.4.11; Phosphoinositide phospholipase C; PLC-gamma-2; Phospholipase C-gamma-2; PLC-IV Polyclonal 0.05 mg


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur