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P10686

- PLCG1_RAT

UniProt

P10686 - PLCG1_RAT

Protein

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

Gene

Plcg1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 167 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      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 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.

    Enzyme regulationi

    Activated by phosphorylation on tyrosine residues.By similarity

    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. insulin receptor binding Source: RGD
    3. phosphatidylinositol phospholipase C activity Source: UniProtKB-EC
    4. phosphoprotein binding Source: RGD
    5. protein binding Source: IntAct
    6. signal transducer activity Source: UniProtKB-KW

    GO - Biological processi

    1. calcium ion transport Source: RGD
    2. cellular response to epidermal growth factor stimulus Source: UniProtKB
    3. inositol trisphosphate biosynthetic process Source: RGD
    4. intracellular signal transduction Source: InterPro
    5. phospholipid catabolic process Source: InterPro
    6. positive regulation of epithelial cell migration Source: RGD
    7. protein secretion Source: RGD
    8. regulation of store-operated calcium channel activity Source: RGD
    9. response to gravity Source: RGD
    10. response to hydrogen peroxide Source: RGD
    11. response to morphine Source: RGD
    12. response to organonitrogen compound Source: RGD
    13. signal transduction Source: RGD

    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. 5301.
    ReactomeiREACT_194374. Role of phospholipids in phagocytosis.
    REACT_219269. PLC-gamma1 signalling.
    REACT_220575. DAG and IP3 signaling.

    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
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi3347. 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. COP9 signalosome Source: UniProtKB
    2. cytoplasm Source: RGD
    3. lamellipodium Source: UniProtKB
    4. plasma membrane Source: Reactome
    5. ruffle Source: UniProtKB

    Keywords - Cellular componenti

    Cell projection

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi842 – 8421P → L: Inhibits interaction with AGAP2. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 129012891-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1PRO_0000088500Add
    BLAST

    Amino acid modifications

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

    Post-translational modificationi

    May be dephosphorylated by PTPRJ By similarity. Tyrosine phosphorylated by activated FGFR1, FGFR2, FGFR3 and FGFR4. 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. Tyrosine phosphorylated in response to signaling via activated FLT1, FLT3, KIT and PDGFRB. Phosphorylated by ITK and TXK on Tyr-783 upon TCR activation in T-cells By similarity.By similarity
    Ubiquitinated by CBLB in activated T-cells.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiP10686.
    PRIDEiP10686.

    PTM databases

    PhosphoSiteiP10686.

    Miscellaneous databases

    PMAP-CutDBP10686.

    Expressioni

    Gene expression databases

    GenevestigatoriP10686.

    Interactioni

    Subunit structurei

    Interacts (via SH2 domain) with FGFR1, FGFR2, FGFR3 and FGFR4 (phosphorylated). Interacts (via SH3 domain) with AGAP2. 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 By similarity. Interacts with RALGPS1. Interacts (via the SH2 domains) with VIL1 (phosphorylated at C-terminus tyrosine phosphorylation sites). Interacts (via SH2 domain) with RET By similarity. Interacts with FLT1 (tyrosine-phosphorylated). Interacts with AXL, FLT4 and KIT. Interacts (via SH2 domain) with PDGFRA and PDGFRB (tyrosine phosphorylated) By similarity. Interacts with PIP5K1C By similarity. Interacts with NTRK1 and NTRK2 (phosphorylated upon ligand-binding) By similarity. Interacts with SYK; activates PLCG1 By similarity. Interacts with TESPA1 By similarity. Interacts with GRB2, LAT and THEMIS upon TCR activation in thymocytes By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FGFR1P113624EBI-520788,EBI-1028277From a different organism.
    Fgfr1Q045892EBI-520788,EBI-2480918
    Jak2Q621203EBI-520788,EBI-646604From a different organism.
    PTPN1P180314EBI-520788,EBI-968788From a different organism.
    TRPC3Q135072EBI-520788,EBI-520807From a different organism.

    Protein-protein interaction databases

    BioGridi247766. 1 interaction.
    DIPiDIP-2863N.
    IntActiP10686. 10 interactions.
    MINTiMINT-231720.
    STRINGi10116.ENSRNOP00000022276.

    Structurei

    Secondary structure

    1
    1290
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi491 – 4999
    Turni500 – 5034
    Beta strandi504 – 51310
    Beta strandi516 – 5194
    Beta strandi551 – 5533
    Helixi556 – 5583
    Helixi561 – 57616
    Beta strandi583 – 5875
    Beta strandi589 – 5913
    Beta strandi594 – 6007
    Beta strandi605 – 6139
    Beta strandi616 – 6183
    Beta strandi620 – 6245
    Beta strandi627 – 6315
    Helixi632 – 64110
    Helixi665 – 6684
    Beta strandi669 – 6724
    Helixi675 – 6828
    Beta strandi690 – 6956
    Beta strandi701 – 7088
    Beta strandi711 – 72010
    Beta strandi723 – 7264
    Beta strandi729 – 7335
    Helixi734 – 74310
    Helixi758 – 7625
    Beta strandi796 – 8005
    Beta strandi817 – 8226
    Beta strandi825 – 8339
    Beta strandi836 – 8427
    Helixi843 – 8453
    Beta strandi846 – 8483
    Beta strandi860 – 8623
    Turni864 – 8707
    Beta strandi874 – 8763
    Beta strandi882 – 8865
    Beta strandi890 – 8923
    Beta strandi896 – 9005
    Beta strandi904 – 9063
    Beta strandi909 – 9124
    Helixi916 – 93015

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1Y0MX-ray1.20A791-851[»]
    1YWOX-ray1.81A790-851[»]
    1YWPX-ray1.60A790-851[»]
    2FJLNMR-A489-547[»]
    A851-933[»]
    3GQIX-ray2.50B545-770[»]
    4K44X-ray1.70A/B664-766[»]
    4K45X-ray1.50A664-766[»]
    B770-787[»]
    ProteinModelPortaliP10686.
    SMRiP10686. Positions 320-454, 489-658, 663-759, 795-848, 851-933.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP10686.

    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 CLNK and RALGPS1.By similarity

    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.
    HOGENOMiHOG000230864.
    HOVERGENiHBG053611.
    KOiK01116.
    PhylomeDBiP10686.

    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.

    P10686-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAGVGTPCAN GCGPSAPSEA EVLHLCRSLE VGTVMTLFYS KKSQRPERKT     50
    FQVKLETRQI TWSRGADKIE GSIDIREIKE IRPGKTSRDF DRYQEDPAFR 100
    PDQSHCFVIL YGMEFRLKTL SLQATSEDEV NMWIKGLTWL MEDTLQAATP 150
    LQIERWLRKQ FYSVDRNRED RISAKDLKNM LSQVNYRVPN MRFLRERLTD 200
    FEQRSGDITY GQFAQLYRSL MYSAQKTMDL PFLETNTLRT GERPELCQVS 250
    LSEFQQFLLE YQGELWAVDR LQVQEFMLSF LRDPLREIEE PYFFLDELVT 300
    FLFSKENSVW NSQLDAVCPE TMNNPLSHYW ISSSHNTYLT GDQFSSESSL 350
    EAYARCLRMG CRCIELDCWD GPDGMPVIYH GHTLTTKIKF SDVLHTIKEH 400
    AFVASEYPVI LSIEDHCSIA QQRNMAQHFR KVLGDTLLTK PVDIAADGLP 450
    SPNQLKRKIL IKHKKLAEGS AYEEVPTSVM YSENDISNSI KNGILYLEDP 500
    VNHEWYPHYF VLTSSKIYYS EETSSDQGNE DEEEPKEASG 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
    NPAILEPERE 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 SPFSGTSLRE RASDASSQLF HVRAREGSFE 1250
    ARYQQPFEDF RISQEHLADH FDSRERRAPR RTRVNGDNRL 1290
    Length:1,290
    Mass (Da):148,548
    Last modified:July 1, 1989 - v1
    Checksum:iBB3240C27972CE3B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03806 mRNA. Translation: AAA41921.1.
    L14476 Genomic DNA. No translation available.
    PIRiA31317.
    RefSeqiNP_037319.1. NM_013187.1.
    UniGeneiRn.11243.

    Genome annotation databases

    GeneIDi25738.
    KEGGirno:25738.
    UCSCiRGD:3347. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03806 mRNA. Translation: AAA41921.1 .
    L14476 Genomic DNA. No translation available.
    PIRi A31317.
    RefSeqi NP_037319.1. NM_013187.1.
    UniGenei Rn.11243.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1Y0M X-ray 1.20 A 791-851 [» ]
    1YWO X-ray 1.81 A 790-851 [» ]
    1YWP X-ray 1.60 A 790-851 [» ]
    2FJL NMR - A 489-547 [» ]
    A 851-933 [» ]
    3GQI X-ray 2.50 B 545-770 [» ]
    4K44 X-ray 1.70 A/B 664-766 [» ]
    4K45 X-ray 1.50 A 664-766 [» ]
    B 770-787 [» ]
    ProteinModelPortali P10686.
    SMRi P10686. Positions 320-454, 489-658, 663-759, 795-848, 851-933.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 247766. 1 interaction.
    DIPi DIP-2863N.
    IntActi P10686. 10 interactions.
    MINTi MINT-231720.
    STRINGi 10116.ENSRNOP00000022276.

    Chemistry

    BindingDBi P10686.
    ChEMBLi CHEMBL5188.

    PTM databases

    PhosphoSitei P10686.

    Proteomic databases

    PaxDbi P10686.
    PRIDEi P10686.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 25738.
    KEGGi rno:25738.
    UCSCi RGD:3347. rat.

    Organism-specific databases

    CTDi 5335.
    RGDi 3347. Plcg1.

    Phylogenomic databases

    eggNOGi NOG268751.
    HOGENOMi HOG000230864.
    HOVERGENi HBG053611.
    KOi K01116.
    PhylomeDBi P10686.

    Enzyme and pathway databases

    BRENDAi 3.1.4.11. 5301.
    Reactomei REACT_194374. Role of phospholipids in phagocytosis.
    REACT_219269. PLC-gamma1 signalling.
    REACT_220575. DAG and IP3 signaling.

    Miscellaneous databases

    EvolutionaryTracei P10686.
    NextBioi 607883.
    PMAP-CutDB P10686.
    PROi P10686.

    Gene expression databases

    Genevestigatori P10686.

    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. "Inositol phospholipid-specific phospholipase C: complete cDNA and protein sequences and sequence homology to tyrosine kinase-related oncogene products."
      Suh P.-G., Ryu S.H., Moon K.H., Suh H.W., Rhee S.G.
      Proc. Natl. Acad. Sci. U.S.A. 85:5419-5423(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Promoter region of the rat phospholipase C-gamma 1 gene."
      Lee S.J., Ryu S.H., Suh P.G.
      Biochem. Biophys. Res. Commun. 194:294-300(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
    3. "Signal transduction by fibroblast growth factor receptor-4 (FGFR-4). Comparison with FGFR-1."
      Vainikka S., Joukov V., Wennstrom S., Bergman M., Pelicci P.G., Alitalo K.
      J. Biol. Chem. 269:18320-18326(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FGFR4, PHOSPHORYLATION.
    4. "Phospholipase C gamma 1 is a physiological guanine nucleotide exchange factor for the nuclear GTPase PIKE."
      Ye K., Aghdasi B., Luo H.R., Moriarity J.L., Wu F.Y., Hong J.J., Hurt K.J., Bae S.S., Suh P.-G., Snyder S.H.
      Nature 415:541-544(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AGAP2, MUTAGENESIS OF PRO-842.
    5. "Structural characterization of the split pleckstrin homology domain in phospholipase C-gamma1 and its interaction with TRPC3."
      Wen W., Yan J., Zhang M.
      J. Biol. Chem. 281:12060-12068(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 489-553 AND 663-759.

    Entry informationi

    Entry nameiPLCG1_RAT
    AccessioniPrimary (citable) accession number: P10686
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 167 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3