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P16885

- PLCG2_HUMAN

UniProt

P16885 - PLCG2_HUMAN

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
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    • History
      Entry version 177 (01 Oct 2014)
      Sequence version 4 (25 Nov 2008)
      Previous versions | rss
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    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. 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

    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

    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

    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
    EGFRP005333EBI-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.
    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.

    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

    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. 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 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

    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 1, 2014
    This is version 177 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