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Q62077

- PLCG1_MOUSE

UniProt

Q62077 - PLCG1_MOUSE

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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

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. receptor tyrosine kinase binding Source: UniProtKB
  5. signal transducer activity Source: UniProtKB-KW

GO - Biological processi

  1. calcium-mediated signaling Source: Ensembl
  2. cell migration Source: Ensembl
  3. cellular response to epidermal growth factor stimulus Source: UniProtKB
  4. epidermal growth factor receptor signaling pathway Source: Ensembl
  5. in utero embryonic development Source: MGI
  6. phospholipid catabolic process Source: InterPro
  7. positive regulation of angiogenesis Source: Ensembl
  8. positive regulation of blood vessel endothelial cell migration Source: Ensembl
  9. positive regulation of epithelial cell migration Source: UniProtKB
  10. positive regulation of release of sequestered calcium ion into cytosol Source: Ensembl
  11. T cell receptor signaling pathway Source: MGI
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ62077.
CleanExiMM_PLCG1.
ExpressionAtlasiQ62077. baseline.
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

        10         20         30         40         50
MAGVATPCAN GCGPGAPSEA EVLHLCRSLE VGTVMTLFYS KKSQRPERKT
60 70 80 90 100
FQVKLETRQI TWSRGADKIE GSIDIREIKE IRPGKTSRDF DRYQEDPAFR
110 120 130 140 150
PDQSHCFVIL YGMEFRLKTL SLQATSEDEV NMWIKGLTWL MEDTLQAATP
160 170 180 190 200
LQIERWLRKQ FYSVDRNRED RISAKDLKNM LSQVNYRVPN MRFLRERLTD
210 220 230 240 250
LEQRSGDITY GQFAQLYRSL MYSAQKTMDL PFLETNALRT GERPEHCQVS
260 270 280 290 300
LSEFQQFLLE YQGELWAVDR LQVQEFMLSF LRDPLREIEE PYFFLDELVT
310 320 330 340 350
FLFSKENSVW NSQLDAVCPD TMNNPLSHYW ISSSHNTYLT GDQFSSESSL
360 370 380 390 400
EAYARCLRMG CRCIELDCWD GPDGMPVIYH GHTLTTKIKF SDVLHTIKEH
410 420 430 440 450
AFVASEYPVI LSIEDHCSIA QQRNMAQHFR KVLGDTLLTK PVDIAADGLP
460 470 480 490 500
SPNQLRRKIL IKHKKLAEGS AYEEVPTSVM YSENDISNSI KNGILYLEDP
510 520 530 540 550
VNHEWYPHYF VLTSSKIYYS EETSSDQGNE DEEEPKEASS STELHSSEKW
560 570 580 590 600
FHGKLGAGRD GRHIAERLLT EYCIETGAPD GSFLVRESET FVGDYTLSFW
610 620 630 640 650
RNGKVQHCRI HSRQDAGTPK FFLTDNLVFD SLYDLITHYQ QVPLRCNEFE
660 670 680 690 700
MRLSEPVPQT NAHESKEWYH ASLTRAQAEH MLMRVPRDGA FLVRKRNEPN
710 720 730 740 750
SYAISFRAEG KIKHCRVQQE GQTVMLGNSE FDSLVDLISY YEKHPLYRKM
760 770 780 790 800
KLRYPINEEA LEKIGTAEPD YGALYEGRNP GFYVEANPMP TFKCAVKALF
810 820 830 840 850
DYKAQREDEL TFTKSAIIQN VEKQDGGWWR GDYGGKKQLW FPSNYVEEMI
860 870 880 890 900
NPAVLEPERE HLDENSPLGD LLRGVLDVPA CQIAIRPEGK NNRLFVFSIS
910 920 930 940 950
MPSVAQWSLD VAADSQEELQ DWVKKIREVA QTADARLTEG KMMERRKKIA
960 970 980 990 1000
LELSELVVYC RPVPFDEEKI GTERACYRDM SSFPETKAEK YVNKAKGKKF
1010 1020 1030 1040 1050
LQYNRLQLSR IYPKGQRLDS SNYDPLPMWI CGSQLVALNF QTPDKPMQMN
1060 1070 1080 1090 1100
QALFMAGGHC GYVLQPSTMR DEAFDPFDKS SLRGLEPCVI CIEVLGARHL
1110 1120 1130 1140 1150
PKNGRGIVCP FVEIEVAGAE YDSTKQKTEF VVDNGLNPVW PAKPFHFQIS
1160 1170 1180 1190 1200
NPEFAFLRFV VYEEDMFSDQ NFLAQATFPV KGLKTGYRAV PLKNNYSEDL
1210 1220 1230 1240 1250
ELASLLIKID IFPAKENGDL SPFSGISLRE RASDASSQLF HVRAREGSFE
1260 1270 1280 1290 1300
ARYQQPFEDF RISQEHLADH FDSRERSTSD GPSSATNLIE DPLHDKLWKC

SL
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

Bgeei Q62077.
CleanExi MM_PLCG1.
ExpressionAtlasi Q62077. baseline.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 148 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