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UniProtKB/Swiss-Prot entry P16885


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PLCG2_HUMAN
Primary accession number P16885
Secondary accession numbers Q3ZTS2 Q59H45 Q969T5
Integrated into Swiss-Prot on August 1, 1990
Sequence was last modified on November 25, 2008 (Sequence version 4)
Annotations were last modified on    June 16, 2009 (Entry version 116)
Name and origin of the protein
Protein name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-2
Synonyms EC 3.1.4.11
Phosphoinositide phospholipase C
Phospholipase C-gamma-2
PLC-gamma-2
PLC-IV
Gene name
Name: PLCG2
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Lymphoblast;
DOI=10.1016/0014-5793(88)80979-7; PubMed=2849563 [NCBI, ExPASy, EBI, Israel, Japan]
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].
DOI=10.1186/1471-2164-7-48; PubMed=16533400 [NCBI, ExPASy, EBI, Israel, Japan]
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].
DOI=10.1038/nature03187; PubMed=15616553 [NCBI, ExPASy, EBI, Israel, Japan]
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 MRNA], AND VARIANTS ARG-244 AND TYR-883.
TISSUE=Lymph;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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]
PHOSPHORYLATION AT TYR-753 AND TYR-759.
DOI=10.1124/mol.62.3.672; PubMed=12181444 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1245, AND MASS SPECTROMETRY.
TISSUE=T-cell;
DOI=10.1021/ac035352d; PubMed=15144186 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-733, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
[9]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M37238; AAA60112.1; ALT_FRAME; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X14034; CAA32194.1; ALT_FRAME; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB208914; BAD92151.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY364256; AAQ76815.1; ALT_FRAME; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC092142; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
AC098966; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
AC099524; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
BC007565; AAH07565.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC011772; AAH11772.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC014561; AAH14561.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC018646; AAH18646.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00329185; -.
PIR S02004; S02004.
RefSeq NP_002652.2; -.
UniGene Hs.413111
3D structure databases
PDB
2K2J; NMR; -; A=471-913.[ExPASy / RCSB / EBI]
2W2W; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I/J/K/L=471-913.[ExPASy / RCSB / EBI]
2W2X; X-ray; 2.30 A; C=471-913, D=471-913.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 2K2J; -.
2W2W; -.
2W2X; -.
ModBase P16885.
Protein-protein interaction databases
IntAct P16885; 3.
PTM databases
PhosphoSite P16885; -.
Enzyme and pathway databases
BRENDA 3.1.4.11; 247.
Pathway_Interaction_DB bcr_5pathway; BCR signaling pathway.
pi3kcipathway; Class I PI3K signaling events.
epopathway; EPO signaling pathway.
Reactome REACT_604; Hemostasis.
Organism-specific databases
GeneCards GC16P080370; -.
H-InvDB HIX0013277; -.
HGNC HGNC:9066; PLCG2.
GenAtlas PLCG2.
HPA CAB004280; -.
MIM 600220; gene. [NCBI / EBI]
PharmGKB PA33393; -.
Gene expression databases
ArrayExpress P16885; -.
Bgee P16885; -.
CleanEx HS_PLCG2; -.
GermOnline ENSG00000197943; Homo sapiens.
Ontologies
GO
GO:0005886; Cellular component: plasma membrane (inferred from experiment from Reactome).
GO:0005509; Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004435; Molecular function: phosphoinositide phospholipase C activity (inferred from electronic annotation from EC).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0004871; Molecular function: signal transducer activity (inferred from electronic annotation from UniProtKB-KW).
GO:0007242; Biological process: intracellular signaling cascade (inferred from electronic annotation from InterPro).
GO:0009395; Biological process: phospholipid catabolic process (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR000008; C2_Ca-dep.
IPR018029; C2_membr_targeting.
IPR011993; PH_type.
IPR001192; Phospholipase_C_Pinositol-sp_C.
IPR000909; Phospholipase_C_Pinositol-sp_X.
IPR001711; Phospholipase_C_Pinositol-sp_Y.
IPR016279; PLC-gamma.
IPR017946; PLC-like_Pdiesterase_TIM-brl.
IPR001849; Pleckstrin_homology.
IPR000980; SH2.
IPR001452; SH3_domain.
Graphical view of domain structure.
Gene3D G3DSA:2.30.29.30; PH_type; 1.
G3DSA:3.20.20.190; PLC-like_Pdiesterase_TIM-brl; 1.
Pfam PF00168; C2; 1.
PF00169; PH; 1.
PF00388; PI-PLC-X; 1.
PF00387; PI-PLC-Y; 1.
PF00017; SH2; 2.
PF00018; SH3_1; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000952; PLC-gamma; 1.
PRINTS PR00390; PHPHLIPASEC.
PR00401; SH2DOMAIN.
ProDom PD001202; PI_PLC_Y; 2.
PD000093; SH2; 2.
PD000066; SH3; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00239; C2; 1.
SM00233; PH; 2.
SM00148; PLCXc; 1.
SM00149; PLCYc; 1.
SM00252; SH2; 2.
SM00326; SH3; 1.
SMART graphical view of domain structure.
PROSITE PS50004; C2; 1.
PS50003; PH_DOMAIN; 1.
PS50007; PIPLC_X_DOMAIN; 1.
PS50008; PIPLC_Y_DOMAIN; 1.
PS50001; SH2; 2.
PS50002; SH3; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE P16885; -.
Genome annotation databases
Ensembl ENSG00000197943; Homo sapiens. [Contig view]
GeneID 5336; -.
KEGG hsa:5336; -.
Phylogenomic databases
HOGENOM P16885; -.
HOVERGEN P16885; -.
OMA P16885; YPKGQRV.
Other
NextBio 20668; -.
SOURCE PLCG2; Homo sapiens.
ProtoNet P16885.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Calcium; Hydrolase; Lipid degradation; Phosphoprotein; Polymorphism; Repeat; SH2 domain; SH3 domain; Transducer.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
CHAIN   1   1265  1265     1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-2. PRO_0000088501
DOMAIN   20    131  112     PH. 
DOMAIN   312    456  145     PI-PLC X-box. 
DOMAIN   532    635  104     SH2 1. 
DOMAIN   646    735  90     SH2 2. 
DOMAIN   769    829  61     SH3. 
DOMAIN   930   1044  115     PI-PLC Y-box. 
DOMAIN   1059   1152  94     C2. 
ACT_SITE   327    327        By similarity. 
ACT_SITE   372    372        By similarity. 
MOD_RES   733    733        Phosphotyrosine. 
MOD_RES   753    753        Phosphotyrosine. 
MOD_RES   759    759        Phosphotyrosine. 
MOD_RES   1245   1245        Phosphotyrosine. 
VARIANT   244    244  1     H -> R (in dbSNP:rs11548656 [NCBI]). VAR_031560 
VARIANT   268    268  1     R -> W (in dbSNP:rs17537869 [NCBI]). VAR_031561 
VARIANT   541    541  1     T -> A (in dbSNP:rs11548657 [NCBI]). VAR_047427 [3D]
VARIANT   883    883  1     D -> Y (in dbSNP:rs17856213 [NCBI]). VAR_047428 
CONFLICT   606    610        TFSSI -> RFRRM (in Ref. 1; CAA32194/AAA60112 and 3; AAQ76815). 
CONFLICT   623    623        R -> P (in Ref. 1; AAA60112/CAA32194 and 3; AAQ76815). 
CONFLICT   745    745        M -> T (in Ref. 1; AAA60112/CAA32194 and 3; AAQ76815). 
CONFLICT   880    880        Q -> E (in Ref. 1; AAA60112/CAA32194 and 3; AAQ76815). 
CONFLICT   912    912        T -> S (in Ref. 1; AAA60112/CAA32194 and 3; AAQ76815). 
CONFLICT   1095   1095        D -> G (in Ref. 1; AAA60112/CAA32194 and 3; AAQ76815). 
Sequence information
Length: 1265 AA [This is the length of the unprocessed precursor] Molecular weight: 147870 Da [This is the MW of the unprocessed precursor] CRC64: 1D56BCBF51D7A0D3 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSTTVNVDSL AEYEKSQIKR ALELGTVMTV FSFRKSTPER RTVQVIMETR QVAWSKTADK 

        70         80         90        100        110        120 
IEGFLDIMEI KEIRPGKNSK DFERAKAVRQ KEDCCFTILY GTQFVLSTLS LAADSKEDAV 

       130        140        150        160        170        180 
NWLSGLKILH QEAMNASTPT IIESWLRKQI YSVDQTRRNS ISLRELKTIL PLINFKVSSA 

       190        200        210        220        230        240 
KFLKDKFVEI GAHKDELSFE QFHLFYKKLM FEQQKSILDE FKKDSSVFIL GNTDRPDASA 

       250        260        270        280        290        300 
VYLHDFQRFL IHEQQEHWAQ DLNKVRERMT KFIDDTMRET AEPFLFVDEF LTYLFSRENS 

       310        320        330        340        350        360 
IWDEKYDAVD MQDMNNPLSH YWISSSHNTY LTGDQLRSES SPEAYIRCLR MGCRCIELDC 

       370        380        390        400        410        420 
WDGPDGKPVI YHGWTRTTKI KFDDVVQAIK DHAFVTSSFP VILSIEEHCS VEQQRHMAKA 

       430        440        450        460        470        480 
FKEVFGDLLL TKPTEASADQ LPSPSQLREK IIIKHKKLGP RGDVDVNMED KKDEHKQQGE 

       490        500        510        520        530        540 
LYMWDSIDQK WTRHYCAIAD AKLSFSDDIE QTMEEEVPQD IPPTELHFGE KWFHKKVEKR 

       550        560        570        580        590        600 
TSAEKLLQEY CMETGGKDGT FLVRESETFP NDYTLSFWRS GRVQHCRIRS TMEGGTLKYY 

       610        620        630        640        650        660 
LTDNLTFSSI YALIQHYRET HLRCAEFELR LTDPVPNPNP HESKPWYYDS LSRGEAEDML 

       670        680        690        700        710        720 
MRIPRDGAFL IRKREGSDSY AITFRARGKV KHCRINRDGR HFVLGTSAYF ESLVELVSYY 

       730        740        750        760        770        780 
EKHSLYRKMR LRYPVTPELL ERYNMERDIN SLYDVSRMYV DPSEINPSMP QRTVKALYDY 

       790        800        810        820        830        840 
KAKRSDELSF CRGALIHNVS KEPGGWWKGD YGTRIQQYFP SNYVEDISTA DFEELEKQII 

       850        860        870        880        890        900 
EDNPLGSLCR GILDLNTYNV VKAPQGKNQK SFVFILEPKQ QGDPPVEFAT DRVEELFEWF 

       910        920        930        940        950        960 
QSIREITWKI DTKENNMKYW EKNQSIAIEL SDLVVYCKPT SKTKDNLENP DFREIRSFVE 

       970        980        990       1000       1010       1020 
TKADSIIRQK PVDLLKYNQK GLTRVYPKGQ RVDSSNYDPF RLWLCGSQMV ALNFQTADKY 

      1030       1040       1050       1060       1070       1080 
MQMNHALFSL NGRTGYVLQP ESMRTEKYDP MPPESQRKIL MTLTVKVLGA RHLPKLGRSI 

      1090       1100       1110       1120       1130       1140 
ACPFVEVEIC GAEYDNNKFK TTVVNDNGLS PIWAPTQEKV TFEIYDPNLA FLRFVVYEED 

      1150       1160       1170       1180       1190       1200 
MFSDPNFLAH ATYPIKAVKS GFRSVPLKNG YSEDIELASL LVFCEMRPVL ESEEELYSSC 

      1210       1220       1230       1240       1250       1260 
RQLRRRQEEL NNQLFLYDTH QNLRNANRDA LVKEFSVNEN QLQLYQEKCN KRLREKRVSN 


SKFYS 

P16885 in FASTA format

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