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Q8CIH5

- PLCG2_MOUSE

UniProt

Q8CIH5 - PLCG2_MOUSE

Protein

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

Gene

Plcg2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      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 By similarity.By similarity

    Catalytic activityi

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

    Cofactori

    Calcium.By similarity

    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: MGI
    3. protein binding Source: IntAct
    4. signal transducer activity Source: UniProtKB-KW

    GO - Biological processi

    1. activation of store-operated calcium channel activity Source: MGI
    2. B cell differentiation Source: UniProtKB
    3. B cell receptor signaling pathway Source: UniProtKB
    4. follicular B cell differentiation Source: MGI
    5. inositol trisphosphate biosynthetic process Source: MGI
    6. intracellular signal transduction Source: InterPro
    7. negative regulation of programmed cell death Source: MGI
    8. phosphatidylinositol biosynthetic process Source: UniProtKB
    9. phospholipid catabolic process Source: InterPro
    10. regulation of gene expression Source: MGI
    11. release of sequestered calcium ion into cytosol Source: UniProtKB
    12. response to lipopolysaccharide Source: MGI
    13. T cell receptor signaling pathway Source: MGI

    Keywords - Molecular functioni

    Hydrolase, Transducer

    Keywords - Biological processi

    Lipid degradation, Lipid metabolism

    Keywords - Ligandi

    Calcium

    Enzyme and pathway databases

    ReactomeiREACT_188185. DAP12 signaling.
    REACT_188194. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
    REACT_188202. FCERI mediated Ca+2 mobilization.
    REACT_188530. FCERI mediated MAPK activation.
    REACT_196473. Synthesis of IP3 and IP4 in the cytosol.
    REACT_210240. Role of phospholipids in phagocytosis.
    REACT_220092. GPVI-mediated activation cascade.

    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-gamma-2
    Short name:
    PLC-gamma-2
    Gene namesi
    Name:Plcg2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 8

    Organism-specific databases

    MGIiMGI:97616. Plcg2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. plasma membrane Source: UniProtKB

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 126512651-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2PRO_0000342364Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei753 – 7531Phosphotyrosine; alternate2 Publications
    Modified residuei753 – 7531Phosphotyrosine; by BTK; alternate2 Publications
    Modified residuei759 – 7591Phosphotyrosine; by BTKBy similarity
    Modified residuei1197 – 11971Phosphotyrosine; by BTKBy similarity
    Modified residuei1217 – 12171Phosphotyrosine2 Publications
    Modified residuei1245 – 12451Phosphotyrosine2 Publications

    Post-translational modificationi

    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 similarity. Phosphorylated on tyrosine residues by CSF1R.By similarity2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ8CIH5.
    PaxDbiQ8CIH5.
    PRIDEiQ8CIH5.

    PTM databases

    PhosphoSiteiQ8CIH5.

    Expressioni

    Gene expression databases

    BgeeiQ8CIH5.
    GenevestigatoriQ8CIH5.

    Interactioni

    Subunit structurei

    Interacts (via SH2 domain) with CSF1R (tyrosine phosphorylated).1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EporP147532EBI-617954,EBI-617901
    Fhl2O704333EBI-617954,EBI-299379
    FlnaQ8BTM83EBI-617954,EBI-641991
    Fn1P112766EBI-617954,EBI-641955
    Inpp5dQ9ES523EBI-617954,EBI-300210
    LynP259112EBI-617954,EBI-643537
    Pdcd6ipQ9WU787EBI-617954,EBI-641897
    Trim27Q621584EBI-617954,EBI-642025
    Zbtb7bQ643213EBI-617954,EBI-642868

    Protein-protein interaction databases

    IntActiQ8CIH5. 32 interactions.
    MINTiMINT-1348529.
    STRINGi10090.ENSMUSP00000079991.

    Structurei

    Secondary structure

    1
    1265
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi523 – 5253
    Helixi540 – 55112
    Turni552 – 5554
    Beta strandi561 – 5655
    Beta strandi567 – 5693
    Beta strandi573 – 5797
    Beta strandi582 – 59312
    Beta strandi596 – 6027
    Beta strandi607 – 6093
    Helixi610 – 6167
    Turni617 – 6193
    Helixi625 – 6273
    Beta strandi773 – 7786
    Beta strandi784 – 7863
    Beta strandi795 – 7984
    Beta strandi803 – 8053
    Beta strandi807 – 8115
    Beta strandi814 – 8196
    Helixi821 – 8233
    Beta strandi824 – 8263

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2DX0X-ray2.50A/B516-640[»]
    2EQINMR-A772-827[»]
    ProteinModelPortaliQ8CIH5.
    SMRiQ8CIH5. Positions 159-446, 476-511, 520-829, 844-909, 930-1181.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8CIH5.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 131131PHPROSITE-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
    Domaini1048 – 1152105C2PROSITE-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.
    InParanoidiQ8CIH5.
    KOiK05859.
    OMAiMLMRIPR.
    OrthoDBiEOG7W419X.
    PhylomeDBiQ8CIH5.
    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.
    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.

    Q8CIH5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTTMVNVDTL PEYEKSQIKR ALELGTVMTV FNARKSTPER RTVQMIMETR     50
    QVAWSKTADK IEGFLDIMEI KEIRPGKNSK DFERAKAVRH KAECCFTILY 100
    GTQFVLSTLS LATDSKEDAV KWLSGLKILH QEAMSASTPT MIESWLRKQI 150
    YSVDQTRRNS ISLRELKTIL PLVNFKVSGI KFLKDKLVEI GAQKDELSFE 200
    QFHLFYKKLM FDQQKSILDE FKKDSSVFIL GNTDRPDASA VYLQDFQRFL 250
    LHEQQELWAQ DLNKVRERMT KFIDDTMRET AEPFLFVDEF LTYLFSRENS 300
    IWDEKYDAVD MQDMNNPLSH YWISSSHNTY LTGDQLRSES STEAYIRCLR 350
    AGCRCIELDC WDGPDGKPII YHGWTRTTKI KFDDVVQAIR DHAFVTSSFP 400
    VILSIEEHCS VEQQRHMAKV FKEVLGDMLL TKPTEASADQ LPSPSQLREK 450
    IIIKHKKLGP KGDVDVNVED KKDEHKPQGE LYMWDSIDQK WTRHYCAIAD 500
    AKLSFGDDIE QAVEEEPVQD TPPTELHFGE KWFHKKVESR TSAEKLLQEY 550
    CAETGAKDGT FLVRESETFP NDYTLSFWRS GRVQHCRIRS TMENGVMKYY 600
    LTDNLTFNSI YALIQHYREA HLRCAEFELR LTDPVPNPNP HESKPWYYDS 650
    LSRGEAEDML MRIPRDGAFL IRKREGTNSY AITFRARGKV KHCRINRDGR 700
    HFVLGTSAYF ESLVELVSYY EKHALYRKMR LRYPVTPELL ERYNMERDIN 750
    SLYDVSRMYV DPSEINPSMP QRTVKALYDY KAKRSDELTF CRGALIHNVS 800
    KEPGGWWKGD YGTRIQQYFP SNYVEDISAG DAEEMEKQII EDNPLGSLCK 850
    GILDLNTYNV VKAPQGKNQK AFVFILEPKK QGDPPVEFAT DRVEELFEWF 900
    QSIREITWKM DTKENNMKYW ERNQSIAIEL SDLVVYCKPT SKTKDHLENP 950
    DFREIRSFVE TKADSIVRQK PVDLLRYNQK GLTRVYPKGQ RVDSSNYDPF 1000
    RLWLCGSQMV ALNFQTPDKY MQMNHALFSL NGRTGYVLQP ESMRSEKYDP 1050
    MPLESQRKIL MTLTVKVLGA RHLPKLGRSI ACPFVEVEIC GAEYDSNKFK 1100
    TTVVNDNGLS PVWAPTQEKV TFEIYDPNLA FLRFVVYEED MFSDPNFLAH 1150
    ATYPIKGIKS GFRSVPLKNG YSEDIELASL LVFCEMRPVL ESEEELYSSC 1200
    RQLRRRQEEL NNQLFLYDTH QNLRGANRDA LVKEFNVNEN QLQLYQEKCN 1250
    RRLREKRVSN SRFYS 1265
    Length:1,265
    Mass (Da):147,592
    Last modified:March 1, 2003 - v1
    Checksum:iE4A2A6AD6F05160E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti787 – 7871E → G in BAE24959. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK142173 mRNA. Translation: BAE24959.1.
    AK151039 mRNA. Translation: BAE30056.1.
    BC019654 mRNA. Translation: AAH19654.1.
    BC023877 mRNA. Translation: AAH23877.1.
    CCDSiCCDS22700.1.
    RefSeqiNP_758489.1. NM_172285.1.
    UniGeneiMm.192699.

    Genome annotation databases

    EnsembliENSMUST00000081232; ENSMUSP00000079991; ENSMUSG00000034330.
    GeneIDi234779.
    KEGGimmu:234779.
    UCSCiuc009npc.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK142173 mRNA. Translation: BAE24959.1 .
    AK151039 mRNA. Translation: BAE30056.1 .
    BC019654 mRNA. Translation: AAH19654.1 .
    BC023877 mRNA. Translation: AAH23877.1 .
    CCDSi CCDS22700.1.
    RefSeqi NP_758489.1. NM_172285.1.
    UniGenei Mm.192699.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DX0 X-ray 2.50 A/B 516-640 [» ]
    2EQI NMR - A 772-827 [» ]
    ProteinModelPortali Q8CIH5.
    SMRi Q8CIH5. Positions 159-446, 476-511, 520-829, 844-909, 930-1181.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q8CIH5. 32 interactions.
    MINTi MINT-1348529.
    STRINGi 10090.ENSMUSP00000079991.

    PTM databases

    PhosphoSitei Q8CIH5.

    Proteomic databases

    MaxQBi Q8CIH5.
    PaxDbi Q8CIH5.
    PRIDEi Q8CIH5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000081232 ; ENSMUSP00000079991 ; ENSMUSG00000034330 .
    GeneIDi 234779.
    KEGGi mmu:234779.
    UCSCi uc009npc.1. mouse.

    Organism-specific databases

    CTDi 5336.
    MGIi MGI:97616. Plcg2.

    Phylogenomic databases

    eggNOGi NOG268751.
    GeneTreei ENSGT00730000110782.
    HOGENOMi HOG000230864.
    HOVERGENi HBG053611.
    InParanoidi Q8CIH5.
    KOi K05859.
    OMAi MLMRIPR.
    OrthoDBi EOG7W419X.
    PhylomeDBi Q8CIH5.
    TreeFami TF313216.

    Enzyme and pathway databases

    Reactomei REACT_188185. DAP12 signaling.
    REACT_188194. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
    REACT_188202. FCERI mediated Ca+2 mobilization.
    REACT_188530. FCERI mediated MAPK activation.
    REACT_196473. Synthesis of IP3 and IP4 in the cytosol.
    REACT_210240. Role of phospholipids in phagocytosis.
    REACT_220092. GPVI-mediated activation cascade.

    Miscellaneous databases

    EvolutionaryTracei Q8CIH5.
    NextBioi 382355.
    PROi Q8CIH5.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8CIH5.
    Genevestigatori Q8CIH5.

    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.
    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. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Bone marrow macrophage and Embryonic heart.
    2. "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].
      Strain: Czech II and FVB/N.
      Tissue: Mammary tumor.
    3. "Sequential activation of phoshatidylinositol 3-kinase and phospholipase C-gamma2 by the M-CSF receptor is necessary for differentiation signaling."
      Bourette R.P., Myles G.M., Choi J.L., Rohrschneider L.R.
      EMBO J. 16:5880-5893(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, INTERACTION WITH CSF1R.
    4. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
      Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
      J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-753; TYR-1217 AND TYR-1245, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Mast cell.
    5. "Crystal structure of the N-terminal SH2 domain of mouse phospholipase c-gamma 2."
      RIKEN structural genomics initiative (RSGI)
      Submitted (SEP-2007) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 516-640.

    Entry informationi

    Entry nameiPLCG2_MOUSE
    AccessioniPrimary (citable) accession number: Q8CIH5
    Secondary accession number(s): Q3UBA8, Q3UQT0, Q8VE69
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 2008
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 111 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3