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P16885 (PLCG2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 175. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2

EC=3.1.4.11
Alternative name(s):
Phosphoinositide phospholipase C-gamma-2
Phospholipase C-IV
Short name=PLC-IV
Phospholipase C-gamma-2
Short name=PLC-gamma-2
Gene names
Name:PLCG2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1265 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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 + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol.

Cofactor

Calcium.

Subunit structure

Interacts (via SH2 domain) with CSF1R (tyrosine phosphorylated) By similarity.

Post-translational modification

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. Ref.7 Ref.8

Involvement in 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.13

Sequence similarities

Contains 1 C2 domain.

Contains 1 PH domain.

Contains 1 PI-PLC X-box domain.

Contains 1 PI-PLC Y-box domain.

Contains 2 SH2 domains.

Contains 1 SH3 domain.

Sequence caution

The sequence AAA60112.1 differs from that shown. Reason: Frameshift at position 1242.

The sequence AAQ76815.1 differs from that shown. Reason: Frameshift at position 1242.

The sequence BAD92151.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence CAA32194.1 differs from that shown. Reason: Frameshift at position 1242.

Ontologies

Keywords
   Biological processLipid degradation
Lipid metabolism
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   DomainRepeat
SH2 domain
SH3 domain
   LigandCalcium
   Molecular functionHydrolase
Transducer
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processB cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

B cell receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

Fc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

Fc-gamma receptor signaling pathway involved in phagocytosis

Traceable author statement. Source: Reactome

T cell receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

Wnt signaling pathway

Traceable author statement PubMed 18784435. Source: UniProtKB

activation of store-operated calcium channel activity

Inferred from electronic annotation. Source: Ensembl

blood coagulation

Traceable author statement. Source: Reactome

calcium-mediated signaling

Non-traceable author statement PubMed 11043765. Source: UniProtKB

follicular B cell differentiation

Inferred from electronic annotation. Source: Ensembl

innate immune response

Traceable author statement. Source: Reactome

inositol phosphate metabolic process

Traceable author statement. Source: Reactome

inositol trisphosphate biosynthetic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of programmed cell death

Inferred from electronic annotation. Source: Ensembl

phosphatidylinositol biosynthetic process

Inferred from direct assay Ref.7Ref.8. Source: UniProtKB

phospholipid catabolic process

Inferred from electronic annotation. Source: InterPro

platelet activation

Traceable author statement. Source: Reactome

regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

release of sequestered calcium ion into cytosol

Inferred from direct assay Ref.7. Source: UniProtKB

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

plasma membrane

Inferred from direct assay Ref.7. Source: UniProtKB

   Molecular_functionphosphatidylinositol phospholipase C activity

Inferred from direct assay Ref.7Ref.8. Source: UniProtKB

phospholipase C activity

Traceable author statement. Source: Reactome

protein binding

Inferred from physical interaction PubMed 15644415PubMed 16273093PubMed 24728074. Source: IntAct

signal transducer activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 126512651-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2
PRO_0000088501

Regions

Domain20 – 131112PH
Domain312 – 456145PI-PLC X-box
Domain532 – 635104SH2 1
Domain646 – 73590SH2 2
Domain769 – 82961SH3
Domain930 – 1044115PI-PLC Y-box
Domain1059 – 115294C2

Sites

Active site3271 By similarity
Active site3721 By similarity

Amino acid modifications

Modified residue7531Phosphotyrosine; by BTK Ref.7 Ref.8 Ref.10
Modified residue7591Phosphotyrosine; by BTK Ref.7 Ref.8 Ref.10
Modified residue11971Phosphotyrosine; by BTK By similarity
Modified residue12171Phosphotyrosine Ref.10
Modified residue12451Phosphotyrosine Ref.9

Natural variations

Natural variant2441H → R. Ref.6
Corresponds to variant rs11548656 [ dbSNP | Ensembl ].
VAR_031560
Natural variant2681R → W.
Corresponds to variant rs17537869 [ dbSNP | Ensembl ].
VAR_031561
Natural variant5411T → A.
Corresponds to variant rs11548657 [ dbSNP | Ensembl ].
VAR_047427
Natural variant7071S → Y in APLAID; results in increased epidermal growth factor-stimulated production of intracellular IP3 and increased intracellular calcium release; is a hypermorphic mutation. Ref.13
VAR_069211
Natural variant8831D → Y. Ref.6
Corresponds to variant rs17856213 [ dbSNP | Ensembl ].
VAR_047428

Experimental info

Sequence conflict606 – 6105TFSSI → RFRRM in CAA32194. Ref.1
Sequence conflict606 – 6105TFSSI → RFRRM in AAA60112. Ref.1
Sequence conflict606 – 6105TFSSI → RFRRM in AAQ76815. Ref.3
Sequence conflict6231R → P in AAA60112. Ref.1
Sequence conflict6231R → P in CAA32194. Ref.1
Sequence conflict6231R → P in AAQ76815. Ref.3
Sequence conflict7451M → T in AAA60112. Ref.1
Sequence conflict7451M → T in CAA32194. Ref.1
Sequence conflict7451M → T in AAQ76815. Ref.3
Sequence conflict8801Q → E in AAA60112. Ref.1
Sequence conflict8801Q → E in CAA32194. Ref.1
Sequence conflict8801Q → E in AAQ76815. Ref.3
Sequence conflict9121T → S in AAA60112. Ref.1
Sequence conflict9121T → S in CAA32194. Ref.1
Sequence conflict9121T → S in AAQ76815. Ref.3
Sequence conflict10951D → G in AAA60112. Ref.1
Sequence conflict10951D → G in CAA32194. Ref.1
Sequence conflict10951D → G in AAQ76815. Ref.3

Secondary structure

................... 1265
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P16885 [UniParc].

Last modified November 25, 2008. Version 4.
Checksum: 1D56BCBF51D7A0D3

FASTA1,265147,870
        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 

« Hide

References

« Hide 'large scale' references
[1]"Complete cDNA encoding a putative phospholipase C from transformed human lymphocytes."
Ohta S., Matsui A., Nazawa Y., Kagawa Y.
FEBS Lett. 242:31-35(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Lymphoblast.
[2]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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Spleen.
[3]"NovelFam3000 -- uncharacterized human protein domains conserved across model organisms."
Kemmer D., Podowski R.M., Arenillas D., Lim J., Hodges E., Roth P., Sonnhammer E.L.L., Hoeoeg C., Wasserman W.W.
BMC Genomics 7:48-48(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"The sequence and analysis of duplication-rich human chromosome 16."
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. expand/collapse author list , 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.
Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS ARG-244 AND TYR-883.
Tissue: Lymph.
[7]"Tyrosine residues in phospholipase Cgamma 2 essential for the enzyme function in B-cell signaling."
Rodriguez R., Matsuda M., Perisic O., Bravo J., Paul A., Jones N.P., Light Y., Swann K., Williams R.L., Katan M.
J. Biol. Chem. 276:47982-47992(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-753 AND TYR-759.
[8]"Activation of phospholipase Cgamma2 by tyrosine phosphorylation."
Ozdener F., Dangelmaier C., Ashby B., Kunapuli S.P., Daniel J.L.
Mol. Pharmacol. 62:672-679(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-753 AND TYR-759.
[9]"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1245, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[10]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-753; TYR-759 AND TYR-1217, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Cold urticaria, immunodeficiency, and autoimmunity related to PLCG2 deletions."
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. expand/collapse author list , 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.
N. Engl. J. Med. 366:330-338(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN FCAS3.
[13]"A hypermorphic missense mutation in PLCG2, encoding phospholipase Cgamma2, causes a dominantly inherited autoinflammatory disease with immunodeficiency."
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.
Am. J. Hum. Genet. 91:713-720(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT APLAID TYR-707.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M37238 mRNA. Translation: AAA60112.1. Frameshift.
X14034 mRNA. Translation: CAA32194.1. Frameshift.
AB208914 mRNA. Translation: BAD92151.1. Different initiation.
AY364256 mRNA. Translation: AAQ76815.1. Frameshift.
AC092142 Genomic DNA. No translation available.
AC098966 Genomic DNA. No translation available.
AC099524 Genomic DNA. No translation available.
CH471114 Genomic DNA. Translation: EAW95524.1.
CH471114 Genomic DNA. Translation: EAW95525.1.
BC007565 mRNA. Translation: AAH07565.1.
BC011772 mRNA. Translation: AAH11772.1.
BC014561 mRNA. Translation: AAH14561.1.
BC018646 mRNA. Translation: AAH18646.1.
CCDSCCDS42204.1.
PIRS02004.
RefSeqNP_002652.2. NM_002661.4.
UniGeneHs.372303.
Hs.413111.
Hs.586906.
Hs.710001.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2K2JNMR-A471-913[»]
2W2WX-ray3.30A/B/C/D/E/F/G/H/I/J/K/L471-913[»]
2W2XX-ray2.30C/D471-913[»]
ProteinModelPortalP16885.
SMRP16885. Positions 65-458, 476-514, 520-913, 930-1181.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111352. 21 interactions.
IntActP16885. 14 interactions.
MINTMINT-1199011.
STRING9606.ENSP00000352336.

Chemistry

BindingDBP16885.
ChEMBLCHEMBL4100.

PTM databases

PhosphoSiteP16885.

Polymorphism databases

DMDM215274231.

Proteomic databases

MaxQBP16885.
PaxDbP16885.
PRIDEP16885.

Protocols and materials databases

DNASU5336.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000359376; ENSP00000352336; ENSG00000197943.
GeneID5336.
KEGGhsa:5336.
UCSCuc002fgt.3. human.

Organism-specific databases

CTD5336.
GeneCardsGC16P081773.
HGNCHGNC:9066. PLCG2.
HPACAB004280.
HPA020099.
HPA020100.
MIM600220. gene.
614468. phenotype.
614878. phenotype.
neXtProtNX_P16885.
Orphanet324530. Autoinflammation and PLCG2-associated antibody deficiency and immune dysregulation.
300359. PLCG2-associated antibody deficiency and immune dysregulation.
PharmGKBPA33393.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG268751.
HOGENOMHOG000230864.
HOVERGENHBG053611.
InParanoidP16885.
KOK05859.
OMAMLMRIPR.
OrthoDBEOG7W419X.
PhylomeDBP16885.
TreeFamTF313216.

Enzyme and pathway databases

BioCycMetaCyc:HS06773-MONOMER.
BRENDA3.1.4.11. 2681.
ReactomeREACT_111217. Metabolism.
REACT_2080. PLC-mediated hydrolysis of PIP2.
REACT_604. Hemostasis.
REACT_6900. Immune System.
SignaLinkP16885.

Gene expression databases

ArrayExpressP16885.
BgeeP16885.
CleanExHS_PLCG2.
GenevestigatorP16885.

Family and domain databases

Gene3D2.30.29.30. 3 hits.
2.60.40.150. 1 hit.
3.20.20.190. 2 hits.
3.30.505.10. 2 hits.
InterProIPR000008. C2_dom.
IPR011993. PH_like_dom.
IPR001192. PI-PLC_fam.
IPR016279. PLC-gamma.
IPR028381. PLC-gamma2.
IPR017946. PLC-like_Pdiesterase_TIM-brl.
IPR001849. Pleckstrin_homology.
IPR015359. PLipase_C_EF-hand-like.
IPR000909. PLipase_C_PInositol-sp_X_dom.
IPR001711. PLipase_C_Pinositol-sp_Y.
IPR000980. SH2.
IPR001452. SH3_domain.
[Graphical view]
PANTHERPTHR10336. PTHR10336. 1 hit.
PTHR10336:SF25. PTHR10336:SF25. 1 hit.
PfamPF00168. C2. 1 hit.
PF09279. EF-hand_like. 1 hit.
PF00388. PI-PLC-X. 1 hit.
PF00387. PI-PLC-Y. 1 hit.
PF00017. SH2. 2 hits.
PF00018. SH3_1. 1 hit.
[Graphical view]
PIRSFPIRSF000952. PLC-gamma. 1 hit.
PRINTSPR00390. PHPHLIPASEC.
PR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
SMARTSM00239. C2. 1 hit.
SM00233. PH. 2 hits.
SM00148. PLCXc. 1 hit.
SM00149. PLCYc. 1 hit.
SM00252. SH2. 2 hits.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF49562. SSF49562. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF51695. SSF51695. 2 hits.
SSF55550. SSF55550. 2 hits.
PROSITEPS50004. C2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS50007. PIPLC_X_DOMAIN. 1 hit.
PS50008. PIPLC_Y_DOMAIN. 1 hit.
PS50001. SH2. 2 hits.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP16885.
GeneWikiPLCG2.
GenomeRNAi5336.
NextBio20668.
PROP16885.
SOURCESearch...

Entry information

Entry namePLCG2_HUMAN
AccessionPrimary (citable) accession number: P16885
Secondary accession number(s): D3DUL3 expand/collapse secondary AC list , Q3ZTS2, Q59H45, Q969T5
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: November 25, 2008
Last modified: July 9, 2014
This is version 175 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM