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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 – 3271 By similarity
Active sitei372 – 3721 By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. activation of store-operated calcium channel activity Source: Ensembl
  2. B cell differentiation Source: UniProtKB
  3. B cell receptor signaling pathway Source: UniProtKB
  4. blood coagulation Source: Reactome
  5. calcium-mediated signaling Source: UniProtKB
  6. Fc-epsilon receptor signaling pathway Source: Reactome
  7. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
  8. follicular B cell differentiation Source: Ensembl
  9. innate immune response Source: Reactome
  10. inositol phosphate metabolic process Source: Reactome
  11. inositol trisphosphate biosynthetic process Source: Ensembl
  12. negative regulation of programmed cell death Source: Ensembl
  13. phosphatidylinositol biosynthetic process Source: UniProtKB
  14. phospholipid catabolic process Source: InterPro
  15. platelet activation Source: Reactome
  16. regulation of gene expression Source: Ensembl
  17. release of sequestered calcium ion into cytosol Source: UniProtKB
  18. response to lipopolysaccharide Source: Ensembl
  19. small molecule metabolic process Source: Reactome
  20. T cell receptor signaling pathway Source: UniProtKB
  21. 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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.1 Publication
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 BTK By 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.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP16885.
PaxDbiP16885.
PRIDEiP16885.

PTM databases

PhosphoSiteiP16885.

Expressioni

Gene expression databases

ArrayExpressiP16885.
BgeeiP16885.
CleanExiHS_PLCG2.
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
EGFRP005332EBI-617403,EBI-297353
EPORP192353EBI-617403,EBI-617321
ERBB2P046262EBI-617403,EBI-641062
GAB1Q1348015EBI-617403,EBI-517684
KITP107218EBI-617403,EBI-1379503

Protein-protein interaction databases

BioGridi111352. 21 interactions.
IntActiP16885. 14 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.

Miscellaneous databases

EvolutionaryTraceiP16885.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 131112PHAdd
BLAST
Domaini312 – 456145PI-PLC X-boxAdd
BLAST
Domaini532 – 635104SH2 1Add
BLAST
Domaini646 – 73590SH2 2Add
BLAST
Domaini769 – 82961SH3Add
BLAST
Domaini930 – 1044115PI-PLC Y-boxAdd
BLAST
Domaini1059 – 115294C2Add
BLAST

Sequence similaritiesi

Contains 1 C2 domain.
Contains 1 PH domain.
Contains 2 SH2 domains.
Contains 1 SH3 domain.

Keywords - Domaini

Repeat, SH2 domain, SH3 domain

Phylogenomic databases

eggNOGiNOG268751.
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

MSTTVNVDSL AEYEKSQIKR ALELGTVMTV FSFRKSTPER RTVQVIMETR     50
QVAWSKTADK IEGFLDIMEI KEIRPGKNSK DFERAKAVRQ KEDCCFTILY 100
GTQFVLSTLS LAADSKEDAV NWLSGLKILH QEAMNASTPT IIESWLRKQI 150
YSVDQTRRNS ISLRELKTIL PLINFKVSSA KFLKDKFVEI GAHKDELSFE 200
QFHLFYKKLM FEQQKSILDE FKKDSSVFIL GNTDRPDASA VYLHDFQRFL 250
IHEQQEHWAQ DLNKVRERMT KFIDDTMRET AEPFLFVDEF LTYLFSRENS 300
IWDEKYDAVD MQDMNNPLSH YWISSSHNTY LTGDQLRSES SPEAYIRCLR 350
MGCRCIELDC WDGPDGKPVI YHGWTRTTKI KFDDVVQAIK DHAFVTSSFP 400
VILSIEEHCS VEQQRHMAKA FKEVFGDLLL TKPTEASADQ LPSPSQLREK 450
IIIKHKKLGP RGDVDVNMED KKDEHKQQGE LYMWDSIDQK WTRHYCAIAD 500
AKLSFSDDIE QTMEEEVPQD IPPTELHFGE KWFHKKVEKR TSAEKLLQEY 550
CMETGGKDGT FLVRESETFP NDYTLSFWRS GRVQHCRIRS TMEGGTLKYY 600
LTDNLTFSSI YALIQHYRET HLRCAEFELR LTDPVPNPNP HESKPWYYDS 650
LSRGEAEDML MRIPRDGAFL IRKREGSDSY AITFRARGKV KHCRINRDGR 700
HFVLGTSAYF ESLVELVSYY EKHSLYRKMR LRYPVTPELL ERYNMERDIN 750
SLYDVSRMYV DPSEINPSMP QRTVKALYDY KAKRSDELSF CRGALIHNVS 800
KEPGGWWKGD YGTRIQQYFP SNYVEDISTA DFEELEKQII EDNPLGSLCR 850
GILDLNTYNV VKAPQGKNQK SFVFILEPKQ QGDPPVEFAT DRVEELFEWF 900
QSIREITWKI DTKENNMKYW EKNQSIAIEL SDLVVYCKPT SKTKDNLENP 950
DFREIRSFVE TKADSIIRQK PVDLLKYNQK GLTRVYPKGQ RVDSSNYDPF 1000
RLWLCGSQMV ALNFQTADKY MQMNHALFSL NGRTGYVLQP ESMRTEKYDP 1050
MPPESQRKIL MTLTVKVLGA RHLPKLGRSI ACPFVEVEIC GAEYDNNKFK 1100
TTVVNDNGLS PIWAPTQEKV TFEIYDPNLA FLRFVVYEED MFSDPNFLAH 1150
ATYPIKAVKS GFRSVPLKNG YSEDIELASL LVFCEMRPVL ESEEELYSSC 1200
RQLRRRQEEL NNQLFLYDTH QNLRNANRDA LVKEFSVNEN QLQLYQEKCN 1250
KRLREKRVSN SKFYS 1265
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.

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti606 – 6105TFSSI → RFRRM in CAA32194. 1 Publication
Sequence conflicti606 – 6105TFSSI → RFRRM in AAA60112. 1 Publication
Sequence conflicti606 – 6105TFSSI → RFRRM in AAQ76815. 1 Publication
Sequence conflicti623 – 6231R → P in AAA60112. 1 Publication
Sequence conflicti623 – 6231R → P in CAA32194. 1 Publication
Sequence conflicti623 – 6231R → P in AAQ76815. 1 Publication
Sequence conflicti745 – 7451M → T in AAA60112. 1 Publication
Sequence conflicti745 – 7451M → T in CAA32194. 1 Publication
Sequence conflicti745 – 7451M → T in AAQ76815. 1 Publication
Sequence conflicti880 – 8801Q → E in AAA60112. 1 Publication
Sequence conflicti880 – 8801Q → E in CAA32194. 1 Publication
Sequence conflicti880 – 8801Q → E in AAQ76815. 1 Publication
Sequence conflicti912 – 9121T → S in AAA60112. 1 Publication
Sequence conflicti912 – 9121T → S in CAA32194. 1 Publication
Sequence conflicti912 – 9121T → S in AAQ76815. 1 Publication
Sequence conflicti1095 – 10951D → G in AAA60112. 1 Publication
Sequence conflicti1095 – 10951D → G in CAA32194. 1 Publication
Sequence conflicti1095 – 10951D → G in AAQ76815. 1 Publication

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

EnsembliENST00000359376; ENSP00000352336; 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. 14 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 ENST00000359376 ; ENSP00000352336 ; 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.
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

ArrayExpressi P16885.
Bgeei P16885.
CleanExi HS_PLCG2.
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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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: September 3, 2014
This is version 176 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

Dasty 3

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