P16885 (PLCG2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1265 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Lipid degradation Lipid metabolism
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	Repeat SH2 domain SH3 domain
Ligand	Calcium
Molecular function	Hydrolase Transducer
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	B cell differentiation Inferred from sequence or structural similarity. Source: UniProtKB B cell receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB 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 receptor signaling pathway Traceable author statement PubMed 18784435. Source: UniProtKB activation of store-operated calcium channel activity Inferred from electronic annotation. Source: Compara calcium-mediated signaling Non-traceable author statement PubMed 11043765. Source: UniProtKB follicular B cell differentiation Inferred from electronic annotation. Source: Compara 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: Compara negative regulation of programmed cell death Inferred from electronic annotation. Source: Compara 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: Compara release of sequestered calcium ion into cytosol Inferred from direct assay Ref.7. Source: UniProtKB response to lipopolysaccharide Inferred from electronic annotation. Source: Compara
Cellular_component	cytosol Traceable author statement. Source: Reactome plasma membrane Inferred from direct assay Ref.7. Source: UniProtKB
Molecular_function	phosphatidylinositol phospholipase C activity Inferred from direct assay Ref.7Ref.8. Source: UniProtKB phospholipid binding Inferred from electronic annotation. Source: InterPro signal transducer activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EPOR	P19235	3	EBI-617403,EBI-617321

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1265

1265

1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2

PRO_0000088501

Regions

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

Sites

Active site

327

1

By similarity

Active site

372

1

By similarity

Amino acid modifications

Modified residue

753

1

Phosphotyrosine; by BTK Ref.7 Ref.8 Ref.10

Modified residue

759

1

Phosphotyrosine; by BTK Ref.7 Ref.8 Ref.10

Modified residue

1197

1

Phosphotyrosine; by BTK By similarity

Modified residue

1217

1

Phosphotyrosine Ref.10

Modified residue

1245

1

Phosphotyrosine Ref.9

Natural variations

Natural variant

244

1

H → R. Ref.6
Corresponds to variant rs11548656 [ dbSNP | Ensembl ].

VAR_031560

Natural variant

268

1

R → W.
Corresponds to variant rs17537869 [ dbSNP | Ensembl ].

VAR_031561

Natural variant

541

1

T → A.
Corresponds to variant rs11548657 [ dbSNP | Ensembl ].

VAR_047427

Natural variant

707

1

S → 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 variant

883

1

D → Y. Ref.6
Corresponds to variant rs17856213 [ dbSNP | Ensembl ].

VAR_047428

Experimental info

Sequence conflict

606 – 610

5

TFSSI → RFRRM in CAA32194. Ref.1

Sequence conflict

606 – 610

5

TFSSI → RFRRM in AAA60112. Ref.1

Sequence conflict

606 – 610

5

TFSSI → RFRRM in AAQ76815. Ref.3

Sequence conflict

623

1

R → P in AAA60112. Ref.1

Sequence conflict

623

1

R → P in CAA32194. Ref.1

Sequence conflict

623

1

R → P in AAQ76815. Ref.3

Sequence conflict

745

1

M → T in AAA60112. Ref.1

Sequence conflict

745

1

M → T in CAA32194. Ref.1

Sequence conflict

745

1

M → T in AAQ76815. Ref.3

Sequence conflict

880

1

Q → E in AAA60112. Ref.1

Sequence conflict

880

1

Q → E in CAA32194. Ref.1

Sequence conflict

880

1

Q → E in AAQ76815. Ref.3

Sequence conflict

912

1

T → S in AAA60112. Ref.1

Sequence conflict

912

1

T → S in CAA32194. Ref.1

Sequence conflict

912

1

T → S in AAQ76815. Ref.3

Sequence conflict

1095

1

D → G in AAA60112. Ref.1

Sequence conflict

1095

1

D → G in CAA32194. Ref.1

Sequence conflict

1095

1

D → G in AAQ76815. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

1265

Helix Strand Turn

Details...

Beta strand

478 – 485

8

Turn

486 – 489

4

Beta strand

490 – 499

10

Beta strand

502 – 505

4

Helix

511 – 514

4

Beta strand

850 – 854

5

Helix

855 – 857

3

Beta strand

858 – 862

5

Beta strand

867 – 869

3

Beta strand

870 – 878

9

Beta strand

880 – 882

3

Beta strand

886 – 891

6

Helix

894 – 907

14

Sequences

	Sequence		Length	Mass (Da)
	P16885 [UniParc]. Last modified November 25, 2008. Version 4. Checksum: 1D56BCBF51D7A0D3	FASTA	1,265	147,870
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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. , 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.

IPI

IPI00329185.

PIR

S02004.

RefSeq

NP_002652.2. NM_002661.3.

UniGene

Hs.413111.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2K2J	NMR	-	A	471-913	[»]
2W2W	X-ray	3.30	A/B/C/D/E/F/G/H/I/J/K/L	471-913	[»]
2W2X	X-ray	2.30	C/D	471-913	[»]

ProteinModelPortal

P16885.

ModBase

Search...

Protein-protein interaction databases

IntAct

P16885. 4 interactions.

MINT

MINT-1199011.

STRING

9606.ENSP00000352336.

PTM databases

PhosphoSite

P16885.

Polymorphism databases

DMDM

215274231.

Proteomic databases

PaxDb

P16885.

PRIDE

P16885.

Protocols and materials databases

DNASU

5336.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000359376; ENSP00000352336; ENSG00000197943.

GeneID

5336.

KEGG

hsa:5336.

UCSC

uc002fgt.3. human.

Organism-specific databases

CTD

5336.

GeneCards

GC16P081773.

HGNC

HGNC:9066. PLCG2.

HPA

CAB004280.
HPA020099.
HPA020100.

MIM

600220. gene.
614468. phenotype.
614878. phenotype.

neXtProt

NX_P16885.

Orphanet

324530. Autoinflammation and PLCG2-associated antibody deficiency and immune dysregulation.
300359. PLCG2-associated antibody deficiency and immune dysregulation.

PharmGKB

PA33393.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG268751.

HOGENOM

HOG000230864.

HOVERGEN

HBG053611.

InParanoid

P16885.

KO

K05859.

OMA

MLMRIPR.

OrthoDB

EOG4VDPXP.

PhylomeDB

P16885.

Enzyme and pathway databases

BioCyc

MetaCyc:HS06773-MONOMER.

BRENDA

3.1.4.11. 2681.

Pathway_Interaction_DB

bcr_5pathway. BCR signaling pathway.
pi3kcipathway. Class I PI3K signaling events.
epopathway. EPO signaling pathway.

Reactome

REACT_111217. Metabolism.
REACT_2080. PLC-mediated hydrolysis of PIP2.
REACT_604. Hemostasis.
REACT_6900. Immune System.

SignaLink

P16885.

Gene expression databases

ArrayExpress

P16885.

Bgee

P16885.

CleanEx

HS_PLCG2.

Genevestigator

P16885.

GermOnline

ENSG00000197943. Homo sapiens.

Family and domain databases

Gene3D

2.30.29.30. 3 hits.
3.20.20.190. 2 hits.
3.30.505.10. 2 hits.

InterPro

IPR000008. C2_Ca-dep.
IPR008973. C2_Ca/lipid-bd_dom_CaLB.
IPR018029. C2_membr_targeting.
IPR011993. PH_like_dom.
IPR001192. Pinositol_PLipase_C.
IPR016279. PLC-gamma.
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]

PANTHER

PTHR10336. PTHR10336. 1 hit.

Pfam

PF00168. C2. 1 hit.
PF09279. efhand_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]

PIRSF

PIRSF000952. PLC-gamma. 1 hit.

PRINTS

PR00390. PHPHLIPASEC.
PR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.

SMART

SM00239. 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]

SUPFAM

SSF49562. C2_CaLB. 1 hit.
SSF51695. PLC-like_Pdiesterase_TIM-brl. 1 hit.
SSF50044. SH3. 1 hit.

PROSITE

PS50004. 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]

ProtoNet

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BindingDB

P16885.

ChEMBL

CHEMBL4100.

EvolutionaryTrace

P16885.

GenomeRNAi

5336.

NextBio

20668.

SOURCE

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Entry information

Entry name

PLCG2_HUMAN

Accession

Primary (citable) accession number: P16885
Secondary accession number(s): D3DUL3 , Q3ZTS2, Q59H45, Q969T5

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	November 25, 2008
Last modified:	May 29, 2013
This is version 162 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.