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Q62077 (PLCG1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Plcg1
Synonyms:Plcg-1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1302 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.11

Catalytic activity

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

Cofactor

Calcium.

Enzyme regulation

Activated by phosphorylation on tyrosine residues.

Subunit structure

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. Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.12 Ref.13 Ref.15 Ref.16 Ref.19 Ref.20

Subcellular location

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.

Domain

The SH3 domain mediates interaction with RALGPS1 By similarity. The SH3 domain also mediates interaction with CLNK. Ref.9

Post-translational modification

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. Ref.3 Ref.6 Ref.11 Ref.12 Ref.21

Ubiquitinated by CBLB in activated T-cells. Ref.11

Sequence similarities

Contains 1 C2 domain.

Contains 1 EF-hand domain.

Contains 2 PH domains.

Contains 1 PI-PLC X-box domain.

Contains 1 PI-PLC Y-box domain.

Contains 2 SH2 domains.

Contains 1 SH3 domain.

Ontologies

Keywords
   Biological processLipid degradation
Lipid metabolism
   Cellular componentCell projection
   DomainRepeat
SH2 domain
SH3 domain
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
Transducer
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processT cell receptor signaling pathway

Inferred from direct assay PubMed 15728238. Source: MGI

cellular response to epidermal growth factor stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

in utero embryonic development

Inferred from mutant phenotype PubMed 11744703. Source: MGI

intracellular signal transduction

Inferred from electronic annotation. Source: InterPro

phospholipid catabolic process

Inferred from electronic annotation. Source: InterPro

positive regulation of angiogenesis

Inferred from electronic annotation. Source: Ensembl

positive regulation of blood vessel endothelial cell migration

Inferred from electronic annotation. Source: Ensembl

positive regulation of epithelial cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentCOP9 signalosome

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from sequence orthology PubMed 15702972. Source: MGI

cytosol

Traceable author statement. Source: Reactome

lamellipodium

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from electronic annotation. Source: Ensembl

ruffle

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

glutamate receptor binding

Inferred from physical interaction PubMed 16710293. Source: MGI

phosphatidylinositol phospholipase C activity

Inferred from electronic annotation. Source: UniProtKB-EC

receptor tyrosine kinase binding

Inferred from physical interaction Ref.10. Source: UniProtKB

signal transducer activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 130213011-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1
PRO_0000088499

Regions

Domain27 – 142116PH 1
Domain152 – 18736EF-hand
Domain320 – 464145PI-PLC X-box
Domain489 – 52335PH 2; first part
Domain550 – 657108SH2 1
Domain668 – 75689SH2 2
Domain791 – 85161SH3
Domain895 – 93137PH 2; second part
Domain953 – 1070118PI-PLC Y-box
Domain1075 – 1177103C2
Calcium binding165 – 17612 Potential

Sites

Active site3351 By similarity
Active site3801 By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue5061Phosphotyrosine Ref.18
Modified residue7711Phosphotyrosine; by SYK Ref.14 Ref.17
Modified residue7751Phosphotyrosine Ref.17
Modified residue7831Phosphotyrosine; by ITK, SYK and TXK By similarity
Modified residue9771Phosphotyrosine Ref.18
Modified residue12211Phosphoserine By similarity
Modified residue12481Phosphoserine By similarity
Modified residue12531Phosphotyrosine By similarity

Experimental info

Sequence conflict9661D → A in CAA64639. Ref.2
Sequence conflict9841P → R in CAA64639. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q62077 [UniParc].

Last modified January 24, 2006. Version 2.
Checksum: 5D123C508D425EB2

FASTA1,302149,668
        10         20         30         40         50         60 
MAGVATPCAN GCGPGAPSEA EVLHLCRSLE VGTVMTLFYS KKSQRPERKT FQVKLETRQI 

        70         80         90        100        110        120 
TWSRGADKIE GSIDIREIKE IRPGKTSRDF DRYQEDPAFR PDQSHCFVIL YGMEFRLKTL 

       130        140        150        160        170        180 
SLQATSEDEV NMWIKGLTWL MEDTLQAATP LQIERWLRKQ FYSVDRNRED RISAKDLKNM 

       190        200        210        220        230        240 
LSQVNYRVPN MRFLRERLTD LEQRSGDITY GQFAQLYRSL MYSAQKTMDL PFLETNALRT 

       250        260        270        280        290        300 
GERPEHCQVS LSEFQQFLLE YQGELWAVDR LQVQEFMLSF LRDPLREIEE PYFFLDELVT 

       310        320        330        340        350        360 
FLFSKENSVW NSQLDAVCPD TMNNPLSHYW ISSSHNTYLT GDQFSSESSL EAYARCLRMG 

       370        380        390        400        410        420 
CRCIELDCWD GPDGMPVIYH GHTLTTKIKF SDVLHTIKEH AFVASEYPVI LSIEDHCSIA 

       430        440        450        460        470        480 
QQRNMAQHFR KVLGDTLLTK PVDIAADGLP SPNQLRRKIL IKHKKLAEGS AYEEVPTSVM 

       490        500        510        520        530        540 
YSENDISNSI KNGILYLEDP VNHEWYPHYF VLTSSKIYYS EETSSDQGNE DEEEPKEASS 

       550        560        570        580        590        600 
STELHSSEKW FHGKLGAGRD GRHIAERLLT EYCIETGAPD GSFLVRESET FVGDYTLSFW 

       610        620        630        640        650        660 
RNGKVQHCRI HSRQDAGTPK FFLTDNLVFD SLYDLITHYQ QVPLRCNEFE MRLSEPVPQT 

       670        680        690        700        710        720 
NAHESKEWYH ASLTRAQAEH MLMRVPRDGA FLVRKRNEPN SYAISFRAEG KIKHCRVQQE 

       730        740        750        760        770        780 
GQTVMLGNSE FDSLVDLISY YEKHPLYRKM KLRYPINEEA LEKIGTAEPD YGALYEGRNP 

       790        800        810        820        830        840 
GFYVEANPMP TFKCAVKALF DYKAQREDEL TFTKSAIIQN VEKQDGGWWR GDYGGKKQLW 

       850        860        870        880        890        900 
FPSNYVEEMI NPAVLEPERE HLDENSPLGD LLRGVLDVPA CQIAIRPEGK NNRLFVFSIS 

       910        920        930        940        950        960 
MPSVAQWSLD VAADSQEELQ DWVKKIREVA QTADARLTEG KMMERRKKIA LELSELVVYC 

       970        980        990       1000       1010       1020 
RPVPFDEEKI GTERACYRDM SSFPETKAEK YVNKAKGKKF LQYNRLQLSR IYPKGQRLDS 

      1030       1040       1050       1060       1070       1080 
SNYDPLPMWI CGSQLVALNF QTPDKPMQMN QALFMAGGHC GYVLQPSTMR DEAFDPFDKS 

      1090       1100       1110       1120       1130       1140 
SLRGLEPCVI CIEVLGARHL PKNGRGIVCP FVEIEVAGAE YDSTKQKTEF VVDNGLNPVW 

      1150       1160       1170       1180       1190       1200 
PAKPFHFQIS NPEFAFLRFV VYEEDMFSDQ NFLAQATFPV KGLKTGYRAV PLKNNYSEDL 

      1210       1220       1230       1240       1250       1260 
ELASLLIKID IFPAKENGDL SPFSGISLRE RASDASSQLF HVRAREGSFE ARYQQPFEDF 

      1270       1280       1290       1300 
RISQEHLADH FDSRERSTSD GPSSATNLIE DPLHDKLWKC SL 

« Hide

References

« Hide 'large scale' references
[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]"Negative regulation of lymphocyte activation and autoimmunity by the molecular adaptor Cbl-b."
Bachmaier K., Krawczyk C., Kozieradzki I., Kong Y.-Y., Sasaki T., Oliveira-dos-Santos A., Mariathasan S., Bouchard D., Wakeham A., Itie A., Le J., Ohashi P.S., Sarosi I., Nishina H., Lipkowitz S., Penninger J.M.
Nature 403:211-216(2000) [PubMed] [Europe PMC] [Abstract]
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]"Essential role of the E3 ubiquitin ligase Cbl-b in T cell anergy induction."
Jeon M.-S., Atfield A., Venuprasad K., Krawczyk C., Sarao R., Elly C., Yang C., Arya S., Bachmaier K., Su L., Bouchard D., Jones R., Gronski M., Ohashi P., Wada T., Bloom D., Fathman C.G., Liu Y.-C., Penninger J.M.
Immunity 21:167-177(2004) [PubMed] [Europe PMC] [Abstract]
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]"Protein-tyrosine phosphatase DEP-1 controls receptor tyrosine kinase FLT3 signaling."
Arora D., Stopp S., Bohmer S.A., Schons J., Godfrey R., Masson K., Razumovskaya E., Ronnstrand L., Tanzer S., Bauer R., Bohmer F.D., Muller J.P.
J. Biol. Chem. 286:10918-10929(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION IN RESPONSE TO FLT3 SIGNALING.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC065091 mRNA. Translation: AAH65091.1.
X95346 mRNA. Translation: CAA64639.1.
RefSeqNP_067255.2. NM_021280.3.
UniGeneMm.44463.

3D structure databases

ProteinModelPortalQ62077.
SMRQ62077. Positions 73-483, 489-933, 952-1207.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202238. 11 interactions.
DIPDIP-29284N.
IntActQ62077. 19 interactions.
MINTMINT-124146.

PTM databases

PhosphoSiteQ62077.

Proteomic databases

PaxDbQ62077.
PRIDEQ62077.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000103115; ENSMUSP00000099404; ENSMUSG00000016933.
GeneID18803.
KEGGmmu:18803.
UCSCuc008nra.1. mouse.

Organism-specific databases

CTD5335.
MGIMGI:97615. Plcg1.

Phylogenomic databases

eggNOGNOG268751.
GeneTreeENSGT00730000110782.
HOGENOMHOG000230864.
HOVERGENHBG053611.
InParanoidQ62077.
KOK01116.
OMAYRSLMYS.
OrthoDBEOG7W419X.
PhylomeDBQ62077.
TreeFamTF313216.

Enzyme and pathway databases

BRENDA3.1.4.11. 3474.

Gene expression databases

ArrayExpressQ62077.
BgeeQ62077.
CleanExMM_PLCG1.
GenevestigatorQ62077.

Family and domain databases

Gene3D1.10.238.10. 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.
InterProIPR000008. C2_dom.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR011993. PH_like_dom.
IPR001192. PI-PLC_fam.
IPR016279. PLC-gamma.
IPR028380. PLC-gamma1.
IPR017946. PLC-like_Pdiesterase_TIM-brl.
IPR001849. Pleckstrin_homology.
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]
PANTHERPTHR10336. PTHR10336. 1 hit.
PTHR10336:SF52. PTHR10336:SF52. 1 hit.
PfamPF00168. 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]
PIRSFPIRSF000952. PLC-gamma. 1 hit.
PRINTSPR00390. PHPHLIPASEC.
PR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
SMARTSM00239. 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]
SUPFAMSSF49562. SSF49562. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF51695. SSF51695. 2 hits.
SSF55550. SSF55550. 2 hits.
PROSITEPS50004. 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]
ProtoNetSearch...

Other

NextBio295106.
PROQ62077.
SOURCESearch...

Entry information

Entry namePLCG1_MOUSE
AccessionPrimary (citable) accession number: Q62077
Secondary accession number(s): Q6P1G1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 24, 2006
Last modified: April 16, 2014
This is version 142 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot