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P16885

- PLCG2_HUMAN

UniProt

P16885 - PLCG2_HUMAN

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Protein

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

Gene

PLCG2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 activityi

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

Cofactori

Calcium.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei327 – 3271PROSITE-ProRule annotation
Active sitei372 – 3721PROSITE-ProRule annotation

GO - Molecular functioni

  1. phosphatidylinositol phospholipase C activity Source: UniProtKB
  2. phospholipase C activity Source: Reactome
  3. signal transducer activity Source: UniProtKB-KW

GO - Biological processi

  1. B cell differentiation Source: UniProtKB
  2. B cell receptor signaling pathway Source: UniProtKB
  3. blood coagulation Source: Reactome
  4. calcium-mediated signaling Source: UniProtKB
  5. Fc-epsilon receptor signaling pathway Source: Reactome
  6. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
  7. innate immune response Source: Reactome
  8. inositol phosphate metabolic process Source: Reactome
  9. phosphatidylinositol biosynthetic process Source: UniProtKB
  10. phospholipid catabolic process Source: InterPro
  11. platelet activation Source: Reactome
  12. release of sequestered calcium ion into cytosol Source: UniProtKB
  13. small molecule metabolic process Source: Reactome
  14. T cell receptor signaling pathway Source: UniProtKB
  15. Wnt signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transducer

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium

Enzyme and pathway databases

BioCyciMetaCyc:HS06773-MONOMER.
BRENDAi3.1.4.11. 2681.
ReactomeiREACT_118700. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_147814. DAP12 signaling.
REACT_150312. Synthesis of IP3 and IP4 in the cytosol.
REACT_160158. Role of phospholipids in phagocytosis.
REACT_163701. FCERI mediated MAPK activation.
REACT_163834. FCERI mediated Ca+2 mobilization.
REACT_1695. GPVI-mediated activation cascade.
REACT_6894. Toll Like Receptor 4 (TLR4) Cascade.
SignaLinkiP16885.

Names & Taxonomyi

Protein namesi
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 namesi
Name:PLCG2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:9066. PLCG2.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: UniProt
  3. plasma membrane Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti707 – 7071S → Y in APLAID; results in increased epidermal growth factor-stimulated production of intracellular IP3 and increased intracellular calcium release; is a hypermorphic mutation. 1 Publication
VAR_069211

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi614468. phenotype.
614878. phenotype.
Orphaneti324530. Autoinflammation and PLCG2-associated antibody deficiency and immune dysregulation.
300359. PLCG2-associated antibody deficiency and immune dysregulation.
PharmGKBiPA33393.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 126512651-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2PRO_0000088501Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei753 – 7531Phosphotyrosine; by BTK3 Publications
Modified residuei759 – 7591Phosphotyrosine; by BTK3 Publications
Modified residuei1197 – 11971Phosphotyrosine; by BTKBy similarity
Modified residuei1217 – 12171Phosphotyrosine1 Publication
Modified residuei1245 – 12451Phosphotyrosine1 Publication

Post-translational modificationi

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.By similarity4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP16885.
PaxDbiP16885.
PRIDEiP16885.

PTM databases

PhosphoSiteiP16885.

Expressioni

Gene expression databases

BgeeiP16885.
CleanExiHS_PLCG2.
ExpressionAtlasiP16885. baseline and differential.
GenevestigatoriP16885.

Organism-specific databases

HPAiCAB004280.
HPA020099.
HPA020100.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
ARP102756EBI-617403,EBI-608057
EGFRP005335EBI-617403,EBI-297353
EPORP192353EBI-617403,EBI-617321
ERBB2P046263EBI-617403,EBI-641062
GAB1Q1348015EBI-617403,EBI-517684
KITP107218EBI-617403,EBI-1379503
PIK3R1P279862EBI-617403,EBI-79464

Protein-protein interaction databases

BioGridi111352. 21 interactions.
IntActiP16885. 15 interactions.
MINTiMINT-1199011.
STRINGi9606.ENSP00000352336.

Structurei

Secondary structure

1
1265
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi478 – 4858
Turni486 – 4894
Beta strandi490 – 49910
Beta strandi502 – 5054
Helixi509 – 5146
Beta strandi850 – 8545
Helixi855 – 8573
Beta strandi858 – 8625
Beta strandi867 – 8693
Beta strandi870 – 88213
Beta strandi886 – 8927
Helixi893 – 90715

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP16885.
SMRiP16885. Positions 65-458, 476-514, 520-913, 930-1181.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16885.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 131112PHPROSITE-ProRule annotationAdd
BLAST
Domaini312 – 456145PI-PLC X-boxPROSITE-ProRule annotationAdd
BLAST
Domaini532 – 635104SH2 1PROSITE-ProRule annotationAdd
BLAST
Domaini646 – 73590SH2 2PROSITE-ProRule annotationAdd
BLAST
Domaini769 – 82961SH3PROSITE-ProRule annotationAdd
BLAST
Domaini930 – 1044115PI-PLC Y-boxPROSITE-ProRule annotationAdd
BLAST
Domaini1059 – 115294C2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 C2 domain.PROSITE-ProRule annotation
Contains 1 PH domain.PROSITE-ProRule annotation
Contains 1 PI-PLC X-box domain.PROSITE-ProRule annotation
Contains 1 PI-PLC Y-box domain.PROSITE-ProRule annotation
Contains 2 SH2 domains.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, SH2 domain, SH3 domain

Phylogenomic databases

eggNOGiNOG268751.
GeneTreeiENSGT00730000110782.
HOGENOMiHOG000230864.
HOVERGENiHBG053611.
InParanoidiP16885.
KOiK05859.
OMAiMLMRIPR.
OrthoDBiEOG7W419X.
PhylomeDBiP16885.
TreeFamiTF313216.

Family and domain databases

Gene3Di2.30.29.30. 3 hits.
2.60.40.150. 1 hit.
3.20.20.190. 2 hits.
3.30.505.10. 2 hits.
InterProiIPR000008. C2_dom.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR001192. PI-PLC_fam.
IPR016279. PLC-gamma.
IPR028381. PLC-gamma2.
IPR017946. PLC-like_Pdiesterase_TIM-brl.
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]
PANTHERiPTHR10336. PTHR10336. 1 hit.
PTHR10336:SF25. PTHR10336:SF25. 1 hit.
PfamiPF00168. 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]
PIRSFiPIRSF000952. PLC-gamma. 1 hit.
PRINTSiPR00390. PHPHLIPASEC.
PR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
SMARTiSM00239. 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]
SUPFAMiSSF49562. SSF49562. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF51695. SSF51695. 2 hits.
SSF55550. SSF55550. 2 hits.
PROSITEiPS50004. 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]

Sequencei

Sequence statusi: Complete.

P16885-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSTTVNVDSL AEYEKSQIKR ALELGTVMTV FSFRKSTPER RTVQVIMETR
60 70 80 90 100
QVAWSKTADK IEGFLDIMEI KEIRPGKNSK DFERAKAVRQ KEDCCFTILY
110 120 130 140 150
GTQFVLSTLS LAADSKEDAV NWLSGLKILH QEAMNASTPT IIESWLRKQI
160 170 180 190 200
YSVDQTRRNS ISLRELKTIL PLINFKVSSA KFLKDKFVEI GAHKDELSFE
210 220 230 240 250
QFHLFYKKLM FEQQKSILDE FKKDSSVFIL GNTDRPDASA VYLHDFQRFL
260 270 280 290 300
IHEQQEHWAQ DLNKVRERMT KFIDDTMRET AEPFLFVDEF LTYLFSRENS
310 320 330 340 350
IWDEKYDAVD MQDMNNPLSH YWISSSHNTY LTGDQLRSES SPEAYIRCLR
360 370 380 390 400
MGCRCIELDC WDGPDGKPVI YHGWTRTTKI KFDDVVQAIK DHAFVTSSFP
410 420 430 440 450
VILSIEEHCS VEQQRHMAKA FKEVFGDLLL TKPTEASADQ LPSPSQLREK
460 470 480 490 500
IIIKHKKLGP RGDVDVNMED KKDEHKQQGE LYMWDSIDQK WTRHYCAIAD
510 520 530 540 550
AKLSFSDDIE QTMEEEVPQD IPPTELHFGE KWFHKKVEKR TSAEKLLQEY
560 570 580 590 600
CMETGGKDGT FLVRESETFP NDYTLSFWRS GRVQHCRIRS TMEGGTLKYY
610 620 630 640 650
LTDNLTFSSI YALIQHYRET HLRCAEFELR LTDPVPNPNP HESKPWYYDS
660 670 680 690 700
LSRGEAEDML MRIPRDGAFL IRKREGSDSY AITFRARGKV KHCRINRDGR
710 720 730 740 750
HFVLGTSAYF ESLVELVSYY EKHSLYRKMR LRYPVTPELL ERYNMERDIN
760 770 780 790 800
SLYDVSRMYV DPSEINPSMP QRTVKALYDY KAKRSDELSF CRGALIHNVS
810 820 830 840 850
KEPGGWWKGD YGTRIQQYFP SNYVEDISTA DFEELEKQII EDNPLGSLCR
860 870 880 890 900
GILDLNTYNV VKAPQGKNQK SFVFILEPKQ QGDPPVEFAT DRVEELFEWF
910 920 930 940 950
QSIREITWKI DTKENNMKYW EKNQSIAIEL SDLVVYCKPT SKTKDNLENP
960 970 980 990 1000
DFREIRSFVE TKADSIIRQK PVDLLKYNQK GLTRVYPKGQ RVDSSNYDPF
1010 1020 1030 1040 1050
RLWLCGSQMV ALNFQTADKY MQMNHALFSL NGRTGYVLQP ESMRTEKYDP
1060 1070 1080 1090 1100
MPPESQRKIL MTLTVKVLGA RHLPKLGRSI ACPFVEVEIC GAEYDNNKFK
1110 1120 1130 1140 1150
TTVVNDNGLS PIWAPTQEKV TFEIYDPNLA FLRFVVYEED MFSDPNFLAH
1160 1170 1180 1190 1200
ATYPIKAVKS GFRSVPLKNG YSEDIELASL LVFCEMRPVL ESEEELYSSC
1210 1220 1230 1240 1250
RQLRRRQEEL NNQLFLYDTH QNLRNANRDA LVKEFSVNEN QLQLYQEKCN
1260
KRLREKRVSN SKFYS
Length:1,265
Mass (Da):147,870
Last modified:November 25, 2008 - v4
Checksum:i1D56BCBF51D7A0D3
GO

Sequence cautioni

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 CAA32194.1 differs from that shown. Reason: Frameshift at position 1242.
The sequence BAD92151.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti606 – 6105TFSSI → RFRRM in CAA32194. (PubMed:2849563)Curated
Sequence conflicti606 – 6105TFSSI → RFRRM in AAA60112. (PubMed:2849563)Curated
Sequence conflicti606 – 6105TFSSI → RFRRM in AAQ76815. (PubMed:16533400)Curated
Sequence conflicti623 – 6231R → P in AAA60112. (PubMed:2849563)Curated
Sequence conflicti623 – 6231R → P in CAA32194. (PubMed:2849563)Curated
Sequence conflicti623 – 6231R → P in AAQ76815. (PubMed:16533400)Curated
Sequence conflicti745 – 7451M → T in AAA60112. (PubMed:2849563)Curated
Sequence conflicti745 – 7451M → T in CAA32194. (PubMed:2849563)Curated
Sequence conflicti745 – 7451M → T in AAQ76815. (PubMed:16533400)Curated
Sequence conflicti880 – 8801Q → E in AAA60112. (PubMed:2849563)Curated
Sequence conflicti880 – 8801Q → E in CAA32194. (PubMed:2849563)Curated
Sequence conflicti880 – 8801Q → E in AAQ76815. (PubMed:16533400)Curated
Sequence conflicti912 – 9121T → S in AAA60112. (PubMed:2849563)Curated
Sequence conflicti912 – 9121T → S in CAA32194. (PubMed:2849563)Curated
Sequence conflicti912 – 9121T → S in AAQ76815. (PubMed:16533400)Curated
Sequence conflicti1095 – 10951D → G in AAA60112. (PubMed:2849563)Curated
Sequence conflicti1095 – 10951D → G in CAA32194. (PubMed:2849563)Curated
Sequence conflicti1095 – 10951D → G in AAQ76815. (PubMed:16533400)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti244 – 2441H → R.1 Publication
Corresponds to variant rs11548656 [ dbSNP | Ensembl ].
VAR_031560
Natural varianti268 – 2681R → W.
Corresponds to variant rs17537869 [ dbSNP | Ensembl ].
VAR_031561
Natural varianti541 – 5411T → A.
Corresponds to variant rs11548657 [ dbSNP | Ensembl ].
VAR_047427
Natural varianti707 – 7071S → Y in APLAID; results in increased epidermal growth factor-stimulated production of intracellular IP3 and increased intracellular calcium release; is a hypermorphic mutation. 1 Publication
VAR_069211
Natural varianti883 – 8831D → Y.1 Publication
Corresponds to variant rs17856213 [ dbSNP | Ensembl ].
VAR_047428

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS42204.1.
PIRiS02004.
RefSeqiNP_002652.2. NM_002661.4.
UniGeneiHs.372303.
Hs.413111.
Hs.586906.
Hs.710001.

Genome annotation databases

EnsembliENST00000564138; ENSP00000482457; ENSG00000197943.
GeneIDi5336.
KEGGihsa:5336.
UCSCiuc002fgt.3. human.

Polymorphism databases

DMDMi215274231.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS42204.1.
PIRi S02004.
RefSeqi NP_002652.2. NM_002661.4.
UniGenei Hs.372303.
Hs.413111.
Hs.586906.
Hs.710001.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P16885.
SMRi P16885. Positions 65-458, 476-514, 520-913, 930-1181.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111352. 21 interactions.
IntActi P16885. 15 interactions.
MINTi MINT-1199011.
STRINGi 9606.ENSP00000352336.

Chemistry

BindingDBi P16885.
ChEMBLi CHEMBL4100.

PTM databases

PhosphoSitei P16885.

Polymorphism databases

DMDMi 215274231.

Proteomic databases

MaxQBi P16885.
PaxDbi P16885.
PRIDEi P16885.

Protocols and materials databases

DNASUi 5336.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000564138 ; ENSP00000482457 ; ENSG00000197943 .
GeneIDi 5336.
KEGGi hsa:5336.
UCSCi uc002fgt.3. human.

Organism-specific databases

CTDi 5336.
GeneCardsi GC16P081773.
HGNCi HGNC:9066. PLCG2.
HPAi CAB004280.
HPA020099.
HPA020100.
MIMi 600220. gene.
614468. phenotype.
614878. phenotype.
neXtProti NX_P16885.
Orphaneti 324530. Autoinflammation and PLCG2-associated antibody deficiency and immune dysregulation.
300359. PLCG2-associated antibody deficiency and immune dysregulation.
PharmGKBi PA33393.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG268751.
GeneTreei ENSGT00730000110782.
HOGENOMi HOG000230864.
HOVERGENi HBG053611.
InParanoidi P16885.
KOi K05859.
OMAi MLMRIPR.
OrthoDBi EOG7W419X.
PhylomeDBi P16885.
TreeFami TF313216.

Enzyme and pathway databases

BioCyci MetaCyc:HS06773-MONOMER.
BRENDAi 3.1.4.11. 2681.
Reactomei REACT_118700. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_147814. DAP12 signaling.
REACT_150312. Synthesis of IP3 and IP4 in the cytosol.
REACT_160158. Role of phospholipids in phagocytosis.
REACT_163701. FCERI mediated MAPK activation.
REACT_163834. FCERI mediated Ca+2 mobilization.
REACT_1695. GPVI-mediated activation cascade.
REACT_6894. Toll Like Receptor 4 (TLR4) Cascade.
SignaLinki P16885.

Miscellaneous databases

EvolutionaryTracei P16885.
GeneWikii PLCG2.
GenomeRNAii 5336.
NextBioi 20668.
PROi P16885.
SOURCEi Search...

Gene expression databases

Bgeei P16885.
CleanExi HS_PLCG2.
ExpressionAtlasi P16885. baseline and differential.
Genevestigatori P16885.

Family and domain databases

Gene3Di 2.30.29.30. 3 hits.
2.60.40.150. 1 hit.
3.20.20.190. 2 hits.
3.30.505.10. 2 hits.
InterProi IPR000008. C2_dom.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR001192. PI-PLC_fam.
IPR016279. PLC-gamma.
IPR028381. PLC-gamma2.
IPR017946. PLC-like_Pdiesterase_TIM-brl.
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 ]
PANTHERi PTHR10336. PTHR10336. 1 hit.
PTHR10336:SF25. PTHR10336:SF25. 1 hit.
Pfami PF00168. 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 ]
PIRSFi PIRSF000952. PLC-gamma. 1 hit.
PRINTSi PR00390. PHPHLIPASEC.
PR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
SMARTi 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 ]
SUPFAMi SSF49562. SSF49562. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF51695. SSF51695. 2 hits.
SSF55550. SSF55550. 2 hits.
PROSITEi 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 ]
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Publicationsi

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  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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. 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.

Entry informationi

Entry nameiPLCG2_HUMAN
AccessioniPrimary (citable) accession number: P16885
Secondary accession number(s): D3DUL3
, Q3ZTS2, Q59H45, Q969T5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: November 25, 2008
Last modified: October 29, 2014
This is version 178 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

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