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Q62077

- PLCG1_MOUSE

UniProt

Q62077 - PLCG1_MOUSE

Protein

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

Gene

Plcg1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 2 (24 Jan 2006)
      Previous versions | rss
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    Functioni

    Mediates the production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). Plays an important role in the regulation of intracellular signaling cascades. Becomes activated in response to ligand-mediated activation of receptor-type tyrosine kinases, such as PDGFRA, PDGFRB, FGFR1, FGFR2, FGFR3 and FGFR4. Plays a role in actin reorganization and cell migration.1 Publication

    Catalytic activityi

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

    Cofactori

    Calcium.

    Enzyme regulationi

    Activated by phosphorylation on tyrosine residues.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei335 – 3351PROSITE-ProRule annotation
    Active sitei380 – 3801PROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi165 – 17612PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. glutamate receptor binding Source: MGI
    3. phosphatidylinositol phospholipase C activity Source: UniProtKB-EC
    4. protein binding Source: UniProtKB
    5. receptor tyrosine kinase binding Source: UniProtKB
    6. signal transducer activity Source: UniProtKB-KW

    GO - Biological processi

    1. cellular response to epidermal growth factor stimulus Source: UniProtKB
    2. intracellular signal transduction Source: InterPro
    3. in utero embryonic development Source: MGI
    4. phospholipid catabolic process Source: InterPro
    5. positive regulation of angiogenesis Source: Ensembl
    6. positive regulation of blood vessel endothelial cell migration Source: Ensembl
    7. positive regulation of epithelial cell migration Source: UniProtKB
    8. T cell receptor signaling pathway Source: MGI

    Keywords - Molecular functioni

    Hydrolase, Transducer

    Keywords - Biological processi

    Lipid degradation, Lipid metabolism

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    BRENDAi3.1.4.11. 3474.
    ReactomeiREACT_188185. DAP12 signaling.
    REACT_188190. PLCG1 events in ERBB2 signaling.
    REACT_188194. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
    REACT_188202. FCERI mediated Ca+2 mobilization.
    REACT_188269. DAG and IP3 signaling.
    REACT_188530. FCERI mediated MAPK activation.
    REACT_196455. Signaling by FGFR mutants.
    REACT_196460. Signaling by FGFR1 fusion mutants.
    REACT_196473. Synthesis of IP3 and IP4 in the cytosol.
    REACT_198533. ISG15 antiviral mechanism.
    REACT_199123. Signaling by constitutively active EGFR.
    REACT_210240. Role of phospholipids in phagocytosis.
    REACT_225768. Generation of second messenger molecules.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1 (EC:3.1.4.11)
    Alternative name(s):
    Phosphoinositide phospholipase C-gamma-1
    Phospholipase C-gamma-1
    Short name:
    PLC-gamma-1
    Gene namesi
    Name:Plcg1
    Synonyms:Plcg-1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:97615. Plcg1.

    Subcellular locationi

    Cell projectionlamellipodium By similarity. Cell projectionruffle By similarity
    Note: Rapidly redistributed to ruffles and lamellipodia structures in response to epidermal growth factor (EGF) treatment.By similarity

    GO - Cellular componenti

    1. cell-cell junction Source: MGI
    2. COP9 signalosome Source: Ensembl
    3. cytoplasm Source: MGI
    4. cytosol Source: Reactome
    5. lamellipodium Source: UniProtKB
    6. plasma membrane Source: Ensembl
    7. ruffle Source: UniProtKB

    Keywords - Cellular componenti

    Cell projection

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 130213011-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1PRO_0000088499Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei506 – 5061Phosphotyrosine1 Publication
    Modified residuei771 – 7711Phosphotyrosine; by SYK2 Publications
    Modified residuei775 – 7751Phosphotyrosine1 Publication
    Modified residuei783 – 7831Phosphotyrosine; by ITK, SYK and TXKBy similarity
    Modified residuei977 – 9771Phosphotyrosine1 Publication
    Modified residuei1221 – 12211PhosphoserineBy similarity
    Modified residuei1248 – 12481PhosphoserineBy similarity
    Modified residuei1253 – 12531PhosphotyrosineBy similarity

    Post-translational modificationi

    Tyrosine phosphorylated in response to signaling via activated FLT3, KIT and PDGFRA By similarity. Tyrosine phosphorylated by activated FGFR1, FGFR2, FGFR3 and FGFR4. Tyrosine phosphorylated by activated FLT1 and KDR. Tyrosine phosphorylated by activated PDGFRB. The receptor-mediated activation of PLCG1 involves its phosphorylation by tyrosine kinases in response to ligation of a variety of growth factor receptors and immune system receptors. For instance, SYK phosphorylates and activates PLCG1 in response to ligation of the B-cell receptor. Phosphorylated by ITK and TXK on Tyr-783 upon TCR activation in T-cells. May be dephosphorylated by PTPRJ By similarity.By similarity
    Ubiquitinated by CBLB in activated T-cells.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ62077.
    PaxDbiQ62077.
    PRIDEiQ62077.

    PTM databases

    PhosphoSiteiQ62077.

    Expressioni

    Gene expression databases

    ArrayExpressiQ62077.
    BgeeiQ62077.
    CleanExiMM_PLCG1.
    GenevestigatoriQ62077.

    Interactioni

    Subunit structurei

    Interacts (via SH2 domain) with FGFR1, FGFR2, FGFR3 and FGFR4 (phosphorylated). Interacts with RALGPS1. Interacts (via SH2 domains) with VIL1 (phosphorylated at C-terminus tyrosine phosphorylation sites). Interacts (via SH2 domain) with RET By similarity. Interacts with AGAP2 via its SH3 domain. Interacts with LAT (phosphorylated) upon TCR activation. Interacts (via SH3 domain) with the Pro-rich domain of TNK1. Associates with BLNK, VAV1, GRB2 and NCK1 in a B-cell antigen receptor-dependent fashion. Interacts with CBLB in activated T-cells; which inhibits phosphorylation. Interacts with SHB. Interacts (via SH3 domain) with the Arg/Gly-rich-flanked Pro-rich domains of KHDRBS1/SAM68. This interaction is selectively regulated by arginine methylation of KHDRBS1/SAM68. Interacts with INPP5D/SHIP1, THEMIS and CLNK. Interacts with FLT4 and KIT. Interacts with AXL By similarity. Interacts with SYK; activates PLCG1 By similarity. Interacts with FLT1 (tyrosine-phosphorylated). Interacts (via SH2 domain) with PDGFRA and PDGFRB (tyrosine phosphorylated). Interacts with PIP5K1C. Interacts with NTRK1 and NTRK2 (phosphorylated upon ligand-binding). Interacts with TESPA1 By similarity. Interacts with GRB2, LAT and THEMIS upon TCR activation in thymocytes; the association is weaker in the absence of TESPA1.By similarity14 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EporP147534EBI-300133,EBI-617901
    Grb2Q606312EBI-300133,EBI-1688
    LatO549572EBI-300133,EBI-6390034
    LeprP483562EBI-300133,EBI-2257257

    Protein-protein interaction databases

    BioGridi202238. 11 interactions.
    DIPiDIP-29284N.
    IntActiQ62077. 19 interactions.
    MINTiMINT-124146.

    Structurei

    3D structure databases

    ProteinModelPortaliQ62077.
    SMRiQ62077. Positions 73-483, 489-848, 851-933, 952-1207.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini27 – 142116PH 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini152 – 18736EF-handPROSITE-ProRule annotationAdd
    BLAST
    Domaini320 – 464145PI-PLC X-boxPROSITE-ProRule annotationAdd
    BLAST
    Domaini489 – 52335PH 2; first partPROSITE-ProRule annotationAdd
    BLAST
    Domaini550 – 657108SH2 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini668 – 75689SH2 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini791 – 85161SH3PROSITE-ProRule annotationAdd
    BLAST
    Domaini895 – 93137PH 2; second partPROSITE-ProRule annotationAdd
    BLAST
    Domaini953 – 1070118PI-PLC Y-boxPROSITE-ProRule annotationAdd
    BLAST
    Domaini1075 – 1177103C2PROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The SH3 domain mediates interaction with RALGPS1 By similarity. The SH3 domain also mediates interaction with CLNK.By similarity1 Publication

    Sequence similaritiesi

    Contains 1 C2 domain.PROSITE-ProRule annotation
    Contains 1 EF-hand domain.PROSITE-ProRule annotation
    Contains 2 PH domains.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.
    InParanoidiQ62077.
    KOiK01116.
    OMAiYRSLMYS.
    OrthoDBiEOG7W419X.
    PhylomeDBiQ62077.
    TreeFamiTF313216.

    Family and domain databases

    Gene3Di1.10.238.10. 1 hit.
    2.30.29.30. 3 hits.
    2.60.40.150. 1 hit.
    3.20.20.190. 2 hits.
    3.30.505.10. 2 hits.
    InterProiIPR000008. C2_dom.
    IPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR001192. PI-PLC_fam.
    IPR016279. PLC-gamma.
    IPR028380. PLC-gamma1.
    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:SF52. PTHR10336:SF52. 1 hit.
    PfamiPF00168. C2. 1 hit.
    PF09279. EF-hand_like. 1 hit.
    PF00169. PH. 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. 3 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.
    PS00018. EF_HAND_1. 1 hit.
    PS50222. EF_HAND_2. 1 hit.
    PS50003. PH_DOMAIN. 2 hits.
    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q62077-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAGVATPCAN GCGPGAPSEA EVLHLCRSLE VGTVMTLFYS KKSQRPERKT     50
    FQVKLETRQI TWSRGADKIE GSIDIREIKE IRPGKTSRDF DRYQEDPAFR 100
    PDQSHCFVIL YGMEFRLKTL SLQATSEDEV NMWIKGLTWL MEDTLQAATP 150
    LQIERWLRKQ FYSVDRNRED RISAKDLKNM LSQVNYRVPN MRFLRERLTD 200
    LEQRSGDITY GQFAQLYRSL MYSAQKTMDL PFLETNALRT GERPEHCQVS 250
    LSEFQQFLLE YQGELWAVDR LQVQEFMLSF LRDPLREIEE PYFFLDELVT 300
    FLFSKENSVW NSQLDAVCPD TMNNPLSHYW ISSSHNTYLT GDQFSSESSL 350
    EAYARCLRMG CRCIELDCWD GPDGMPVIYH GHTLTTKIKF SDVLHTIKEH 400
    AFVASEYPVI LSIEDHCSIA QQRNMAQHFR KVLGDTLLTK PVDIAADGLP 450
    SPNQLRRKIL IKHKKLAEGS AYEEVPTSVM YSENDISNSI KNGILYLEDP 500
    VNHEWYPHYF VLTSSKIYYS EETSSDQGNE DEEEPKEASS STELHSSEKW 550
    FHGKLGAGRD GRHIAERLLT EYCIETGAPD GSFLVRESET FVGDYTLSFW 600
    RNGKVQHCRI HSRQDAGTPK FFLTDNLVFD SLYDLITHYQ QVPLRCNEFE 650
    MRLSEPVPQT NAHESKEWYH ASLTRAQAEH MLMRVPRDGA FLVRKRNEPN 700
    SYAISFRAEG KIKHCRVQQE GQTVMLGNSE FDSLVDLISY YEKHPLYRKM 750
    KLRYPINEEA LEKIGTAEPD YGALYEGRNP GFYVEANPMP TFKCAVKALF 800
    DYKAQREDEL TFTKSAIIQN VEKQDGGWWR GDYGGKKQLW FPSNYVEEMI 850
    NPAVLEPERE HLDENSPLGD LLRGVLDVPA CQIAIRPEGK NNRLFVFSIS 900
    MPSVAQWSLD VAADSQEELQ DWVKKIREVA QTADARLTEG KMMERRKKIA 950
    LELSELVVYC RPVPFDEEKI GTERACYRDM SSFPETKAEK YVNKAKGKKF 1000
    LQYNRLQLSR IYPKGQRLDS SNYDPLPMWI CGSQLVALNF QTPDKPMQMN 1050
    QALFMAGGHC GYVLQPSTMR DEAFDPFDKS SLRGLEPCVI CIEVLGARHL 1100
    PKNGRGIVCP FVEIEVAGAE YDSTKQKTEF VVDNGLNPVW PAKPFHFQIS 1150
    NPEFAFLRFV VYEEDMFSDQ NFLAQATFPV KGLKTGYRAV PLKNNYSEDL 1200
    ELASLLIKID IFPAKENGDL SPFSGISLRE RASDASSQLF HVRAREGSFE 1250
    ARYQQPFEDF RISQEHLADH FDSRERSTSD GPSSATNLIE DPLHDKLWKC 1300
    SL 1302
    Length:1,302
    Mass (Da):149,668
    Last modified:January 24, 2006 - v2
    Checksum:i5D123C508D425EB2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti966 – 9661D → A in CAA64639. (PubMed:8687404)Curated
    Sequence conflicti984 – 9841P → R in CAA64639. (PubMed:8687404)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC065091 mRNA. Translation: AAH65091.1.
    X95346 mRNA. Translation: CAA64639.1.
    CCDSiCCDS16996.1.
    RefSeqiNP_067255.2. NM_021280.3.
    UniGeneiMm.44463.

    Genome annotation databases

    EnsembliENSMUST00000103115; ENSMUSP00000099404; ENSMUSG00000016933.
    GeneIDi18803.
    KEGGimmu:18803.
    UCSCiuc008nra.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC065091 mRNA. Translation: AAH65091.1 .
    X95346 mRNA. Translation: CAA64639.1 .
    CCDSi CCDS16996.1.
    RefSeqi NP_067255.2. NM_021280.3.
    UniGenei Mm.44463.

    3D structure databases

    ProteinModelPortali Q62077.
    SMRi Q62077. Positions 73-483, 489-848, 851-933, 952-1207.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202238. 11 interactions.
    DIPi DIP-29284N.
    IntActi Q62077. 19 interactions.
    MINTi MINT-124146.

    PTM databases

    PhosphoSitei Q62077.

    Proteomic databases

    MaxQBi Q62077.
    PaxDbi Q62077.
    PRIDEi Q62077.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000103115 ; ENSMUSP00000099404 ; ENSMUSG00000016933 .
    GeneIDi 18803.
    KEGGi mmu:18803.
    UCSCi uc008nra.1. mouse.

    Organism-specific databases

    CTDi 5335.
    MGIi MGI:97615. Plcg1.

    Phylogenomic databases

    eggNOGi NOG268751.
    GeneTreei ENSGT00730000110782.
    HOGENOMi HOG000230864.
    HOVERGENi HBG053611.
    InParanoidi Q62077.
    KOi K01116.
    OMAi YRSLMYS.
    OrthoDBi EOG7W419X.
    PhylomeDBi Q62077.
    TreeFami TF313216.

    Enzyme and pathway databases

    BRENDAi 3.1.4.11. 3474.
    Reactomei REACT_188185. DAP12 signaling.
    REACT_188190. PLCG1 events in ERBB2 signaling.
    REACT_188194. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
    REACT_188202. FCERI mediated Ca+2 mobilization.
    REACT_188269. DAG and IP3 signaling.
    REACT_188530. FCERI mediated MAPK activation.
    REACT_196455. Signaling by FGFR mutants.
    REACT_196460. Signaling by FGFR1 fusion mutants.
    REACT_196473. Synthesis of IP3 and IP4 in the cytosol.
    REACT_198533. ISG15 antiviral mechanism.
    REACT_199123. Signaling by constitutively active EGFR.
    REACT_210240. Role of phospholipids in phagocytosis.
    REACT_225768. Generation of second messenger molecules.

    Miscellaneous databases

    NextBioi 295106.
    PROi Q62077.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q62077.
    Bgeei Q62077.
    CleanExi MM_PLCG1.
    Genevestigatori Q62077.

    Family and domain databases

    Gene3Di 1.10.238.10. 1 hit.
    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.
    IPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR001192. PI-PLC_fam.
    IPR016279. PLC-gamma.
    IPR028380. PLC-gamma1.
    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:SF52. PTHR10336:SF52. 1 hit.
    Pfami PF00168. C2. 1 hit.
    PF09279. EF-hand_like. 1 hit.
    PF00169. PH. 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. 3 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.
    PS00018. EF_HAND_1. 1 hit.
    PS50222. EF_HAND_2. 1 hit.
    PS50003. PH_DOMAIN. 2 hits.
    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 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: C57BL/6.
      Tissue: Brain.
    2. "Phospholipase C in mouse oocytes: characterization of beta and gamma isoforms and their possible involvement in sperm-induced Ca2+ spiking."
      Dupont G., McGuinness O.M., Johnson M.H., Berridge M.J., Borgese F.
      Biochem. J. 316:583-591(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 846-1052.
      Tissue: Oocyte.
    3. "Signal transduction by normal isoforms and W mutant variants of the Kit receptor tyrosine kinase."
      Reith A.D., Ellis C., Lyman S.D., Anderson D.M., Williams D.E., Bernstein A., Pawson T.
      EMBO J. 10:2451-2459(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KIT, PHOSPHORYLATION.
    4. "Tyrosine mutations within the alpha platelet-derived growth factor receptor kinase insert domain abrogate receptor-associated phosphatidylinositol-3 kinase activity without affecting mitogenic or chemotactic signal transduction."
      Yu J.C., Heidaran M.A., Pierce J.H., Gutkind J.S., Lombardi D., Ruggiero M., Aaronson S.A.
      Mol. Cell. Biol. 11:3780-3785(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PDGFRA, ACTIVATION BY PDGFRA.
    5. "Phosphorylation of tyrosine 720 in the platelet-derived growth factor alpha receptor is required for binding of Grb2 and SHP-2 but not for activation of Ras or cell proliferation."
      Bazenet C.E., Gelderloos J.A., Kazlauskas A.
      Mol. Cell. Biol. 16:6926-6936(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PDGFRA.
    6. "The phosphorylated 1169-tyrosine containing region of flt-1 kinase (VEGFR-1) is a major binding site for PLCgamma."
      Sawano A., Takahashi T., Yamaguchi S., Shibuya M.
      Biochem. Biophys. Res. Commun. 238:487-491(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, INTERACTION WITH FLT1.
    7. "Arginine methylation inhibits the binding of proline-rich ligands to Src homology 3, but not WW, domains."
      Bedford M.T., Frankel A., Yaffe M.B., Clarke S., Leder P., Richard S.
      J. Biol. Chem. 275:16030-16036(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KHDRBS1.
    8. Cited for: INTERACTION WITH CBLB.
    9. "MIST functions through distinct domains in immunoreceptor signaling in the presence and absence of LAT."
      Goitsuka R., Tatsuno A., Ishiai M., Kurosaki T., Kitamura D.
      J. Biol. Chem. 276:36043-36050(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CLNK, DOMAIN.
    10. "Mechanism of TrkB-mediated hippocampal long-term potentiation."
      Minichiello L., Calella A.M., Medina D.L., Bonhoeffer T., Klein R., Korte M.
      Neuron 36:121-137(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NTRK2.
    11. Cited for: PHOSPHORYLATION, UBIQUITINATION, FUNCTION.
    12. "Tyrosine 769 of the keratinocyte growth factor receptor is required for receptor signaling but not endocytosis."
      Ceridono M., Belleudi F., Ceccarelli S., Torrisi M.R.
      Biochem. Biophys. Res. Commun. 327:523-532(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FGFR2, PHOSPHORYLATION.
    13. "Inositol 5'-phosphatase, SHIP1 interacts with phospholipase C-gamma1 and modulates EGF-induced PLC activity."
      Song M., Kim M.J., Ha S., Park J.B., Ryu S.H., Suh P.-G.
      Exp. Mol. Med. 37:161-168(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH INPP5D.
    14. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-771, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Binding of Cbl to a phospholipase Cgamma1-docking site on platelet-derived growth factor receptor beta provides a dual mechanism of negative regulation."
      Reddi A.L., Ying G., Duan L., Chen G., Dimri M., Douillard P., Druker B.J., Naramura M., Band V., Band H.
      J. Biol. Chem. 282:29336-29347(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PDGFRB.
    16. "Type I gamma phosphatidylinositol phosphate kinase is required for EGF-stimulated directional cell migration."
      Sun Y., Ling K., Wagoner M.P., Anderson R.A.
      J. Cell Biol. 178:297-308(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PIP5K1C.
    17. "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-771 AND TYR-775, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Mast cell.
    18. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
      Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
      J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-506 AND TYR-977, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    19. "Themis controls thymocyte selection through regulation of T cell antigen receptor-mediated signaling."
      Fu G., Vallee S., Rybakin V., McGuire M.V., Ampudia J., Brockmeyer C., Salek M., Fallen P.R., Hoerter J.A.H., Munshi A., Huang Y.H., Hu J., Fox H.S., Sauer K., Acuto O., Gascoigne N.R.J.
      Nat. Immunol. 10:848-856(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH THEMIS.
    20. "Tespa1 is involved in late thymocyte development through the regulation of TCR-mediated signaling."
      Wang D., Zheng M., Lei L., Ji J., Yao Y., Qiu Y., Ma L., Lou J., Ouyang C., Zhang X., He Y., Chi J., Wang L., Kuang Y., Wang J., Cao X., Lu L.
      Nat. Immunol. 13:560-568(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GRB2; LAT AND THEMIS.
      Tissue: Thymocyte.
    21. Cited for: PHOSPHORYLATION IN RESPONSE TO FLT3 SIGNALING.

    Entry informationi

    Entry nameiPLCG1_MOUSE
    AccessioniPrimary (citable) accession number: Q62077
    Secondary accession number(s): Q6P1G1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: January 24, 2006
    Last modified: October 1, 2014
    This is version 147 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3