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P19174 (PLCG1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 184. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·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):
PLC-148
Phosphoinositide phospholipase C-gamma-1
Phospholipase C-II
Short name=PLC-II
Phospholipase C-gamma-1
Short name=PLC-gamma-1
Gene names
Name:PLCG1
Synonyms:PLC1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1290 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.29

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 with AGAP2 via its SH3 domain. Interacts (via SH2 domain) with RET. Interacts with FLT1 (tyrosine-phosphorylated) By similarity. Interacts (via SH2 domain) with FGFR1, FGFR2, FGFR3 and FGFR4 (phosphorylated). 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 AXL, FLT4 and KIT. Interacts with RALGPS1. Interacts (via SH3 domain) with HEV ORF3 protein. Interacts (via the SH2 domains) with VIL1 (phosphorylated at C-terminus tyrosine phosphorylation sites). Interacts (via SH2 domain) with PDGFRA and PDGFRB (tyrosine phosphorylated). Interacts with PIP5K1C By similarity. Interacts with NTRK1 and NTRK2 (phosphorylated upon ligand-binding). Interacts with SYK; activates PLCG1. Interacts with GRB2, LAT and THEMIS upon TCR activation in thymocytes By similarity. Interacts with TESPA1; the association is increased with prolonged stimulation of the TCR and may facilitate the assembly of the LAT signalosome. Ref.6 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.16 Ref.17 Ref.22 Ref.24 Ref.25 Ref.28 Ref.29 Ref.31 Ref.34 Ref.36 Ref.39 Ref.41

Subcellular location

Cell projectionlamellipodium. Cell projectionruffle. Note: Rapidly redistributed to ruffles and lamellipodia structures in response to epidermal growth factor (EGF) treatment. Ref.19 Ref.29

Domain

The SH3 domain mediates interaction with CLNK By similarity. The SH3 domain also mediates interaction with RALGPS1. Ref.43

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. May be dephosphorylated by PTPRJ. Phosphorylated by ITK and TXK on Tyr-783 upon TCR activation in T-cells. Ref.1 Ref.7 Ref.9 Ref.14 Ref.18 Ref.19 Ref.20 Ref.26 Ref.27 Ref.28 Ref.30 Ref.36 Ref.39

Ubiquitinated by CBLB in activated T-cells By similarity.

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 processHost-virus interaction
Lipid degradation
Lipid metabolism
   Cellular componentCell projection
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
SH2 domain
SH3 domain
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
Transducer
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processFc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

Fc-gamma receptor signaling pathway involved in phagocytosis

Traceable author statement. Source: Reactome

T cell receptor signaling pathway

Traceable author statement. Source: Reactome

activation of MAPKK activity

Traceable author statement. Source: Reactome

activation of phospholipase C activity

Traceable author statement. Source: Reactome

axon guidance

Traceable author statement. Source: Reactome

blood coagulation

Traceable author statement. Source: Reactome

cellular response to epidermal growth factor stimulus

Inferred from direct assay Ref.29. Source: UniProtKB

cytokine-mediated signaling pathway

Traceable author statement. Source: Reactome

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

fibroblast growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

innate immune response

Traceable author statement. Source: Reactome

inositol phosphate metabolic process

Traceable author statement. Source: Reactome

leukocyte migration

Traceable author statement. Source: Reactome

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

phospholipid catabolic process

Inferred from electronic annotation. Source: InterPro

positive regulation of angiogenesis

Inferred from direct assay PubMed 20011604. Source: DFLAT

positive regulation of blood vessel endothelial cell migration

Inferred from direct assay PubMed 20011604. Source: DFLAT

positive regulation of epithelial cell migration

Inferred from mutant phenotype Ref.29. Source: UniProtKB

signal transduction

Non-traceable author statement Ref.43. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentCOP9 signalosome

Inferred from direct assay Ref.41. Source: UniProtKB

cytoplasm

Inferred from direct assay PubMed 15702972. Source: MGI

cytosol

Inferred from direct assay PubMed 2550068. Source: UniProtKB

lamellipodium

Inferred from direct assay Ref.29. Source: UniProtKB

plasma membrane

Inferred from direct assay PubMed 2550068. Source: UniProtKB

ruffle

Inferred from direct assay Ref.29. Source: UniProtKB

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

neurotrophin TRKA receptor binding

Inferred from physical interaction Ref.22. Source: UniProtKB

phosphatidylinositol phospholipase C activity

Inferred from direct assay PubMed 2550068. Source: UniProtKB

phospholipase C activity

Traceable author statement. Source: Reactome

receptor signaling protein activity

Non-traceable author statement Ref.43. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P19174-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P19174-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1215-1215: K → KQ
Note: Contains a phosphoserine at position 1222.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.33
Chain2 – 129012891-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1
PRO_0000088498

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 Ref.33
Modified residue5061Phosphotyrosine By similarity
Modified residue7711Phosphotyrosine; by SYK Ref.9 Ref.21 Ref.35 Ref.36
Modified residue7751Phosphotyrosine Ref.35
Modified residue7831Phosphotyrosine; by ITK, SYK and TXK Ref.9 Ref.19 Ref.26 Ref.35
Modified residue9771Phosphotyrosine By similarity
Modified residue12211Phosphoserine Ref.32 Ref.35 Ref.37
Modified residue12481Phosphoserine Ref.7
Modified residue12531Phosphotyrosine Ref.21 Ref.37

Natural variations

Alternative sequence12151K → KQ in isoform 2.
VSP_038692
Natural variant2091T → N. Ref.2
Corresponds to variant rs2229348 [ dbSNP | Ensembl ].
VAR_025213
Natural variant2791S → G. Ref.2
Corresponds to variant rs2228246 [ dbSNP | Ensembl ].
VAR_022130
Natural variant7391S → T. Ref.2
Corresponds to variant rs34203315 [ dbSNP | Ensembl ].
VAR_025214
Natural variant8131I → T. Ref.2 Ref.5
Corresponds to variant rs753381 [ dbSNP | Ensembl ].
VAR_011908

Secondary structure

.......................................................... 1290
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: AE05ABE2A18EDDAC

FASTA1,290148,532
        10         20         30         40         50         60 
MAGAASPCAN GCGPGAPSDA EVLHLCRSLE VGTVMTLFYS KKSQRPERKT FQVKLETRQI 

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

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

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

       250        260        270        280        290        300 
GERPELCRVS LPEFQQFLLD YQGELWAVDR LQVQEFMLSF LRDPLREIEE PYFFLDEFVT 

       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 
QQRNMAQYFK KVLGDTLLTK PVEISADGLP SPNQLKRKIL IKHKKLAEGS AYEEVPTSMM 

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

       550        560        570        580        590        600 
STELHSNEKW 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 TFIKSAIIQN VEKQEGGWWR GDYGGKKQLW 

       850        860        870        880        890        900 
FPSNYVEEMV NPVALEPERE HLDENSPLGD LLRGVLDVPA CQIAIRPEGK NNRLFVFSIS 

       910        920        930        940        950        960 
MASVAHWSLD VAADSQEELQ DWVKKIREVA QTADARLTEG KIMERRKKIA LELSELVVYC 

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

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

      1090       1100       1110       1120       1130       1140 
SLRGLEPCAI SIEVLGARHL PKNGRGIVCP FVEIEVAGAE YDSTKQKTEF VVDNGLNPVW 

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

      1210       1220       1230       1240       1250       1260 
ELASLLIKID IFPAKENGDL SPFSGTSLRE RGSDASGQLF HGRAREGSFE SRYQQPFEDF 

      1270       1280       1290 
RISQEHLADH FDSRERRAPR RTRVNGDNRL 

« Hide

Isoform 2 [UniParc].

Checksum: EDDBB8D4E49B2F3E
Show »

FASTA1,291148,660

References

« Hide 'large scale' references
[1]"Characterization and cDNA cloning of phospholipase C-gamma, a major substrate for heparin-binding growth factor 1 (acidic fibroblast growth factor)-activated tyrosine kinase."
Burgess W.H., Dionne C.A., Kaplow J.M., Mudd R., Friesel R., Zilberstein A., Schlessinger J., Jaye M.
Mol. Cell. Biol. 10:4770-4777(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PHOSPHORYLATION.
Tissue: Brain and Vein.
[2]NIEHS SNPs program
Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ASN-209; GLY-279; THR-739 AND THR-813.
[3]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] (ISOFORMS 1 AND 2), VARIANT THR-813.
Tissue: Brain and Testis.
[6]"A tyrosine-phosphorylated carboxy-terminal peptide of the fibroblast growth factor receptor (Flg) is a binding site for the SH2 domain of phospholipase C-gamma 1."
Mohammadi M., Honegger A.M., Rotin D., Fischer R., Bellot F., Li W., Dionne C.A., Jaye M., Rubinstein M., Schlessinger J.
Mol. Cell. Biol. 11:5068-5078(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FGFR1.
[7]"Inhibition of CD3-linked phospholipase C by phorbol ester and by cAMP is associated with decreased phosphotyrosine and increased phosphoserine contents of PLC-gamma 1."
Park D.J., Min H.K., Rhee S.G.
J. Biol. Chem. 267:1496-1501(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-1248.
[8]"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.
[9]"Phospholipase C-gamma1 interacts with conserved phosphotyrosyl residues in the linker region of Syk and is a substrate for Syk."
Law C.L., Chandran K.A., Sidorenko S.P., Clark E.A.
Mol. Cell. Biol. 16:1305-1315(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-771 AND TYR-783 BY SYK, INTERACTION WITH SYK.
[10]"Direct association of Csk homologous kinase (CHK) with the diphosphorylated site Tyr568/570 of the activated c-KIT in megakaryocytes."
Price D.J., Rivnay B., Fu Y., Jiang S., Avraham S., Avraham H.
J. Biol. Chem. 272:5915-5920(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KIT.
[11]"Intracellular signaling of the Ufo/Axl receptor tyrosine kinase is mediated mainly by a multi-substrate docking-site."
Braunger J., Schleithoff L., Schulz A.S., Kessler H., Lammers R., Ullrich A., Bartram C.R., Janssen J.W.
Oncogene 14:2619-2631(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AXL.
[12]"LAT: the ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation."
Zhang W., Sloan-Lancaster J., Kitchen J., Trible R.P., Samelson L.E.
Cell 92:83-92(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LAT.
[13]"Requirement of the Src homology 2 domain protein Shb for T cell receptor-dependent activation of the interleukin-2 gene nuclear factor for activation of T cells element in Jurkat T cells."
Lindholm C.K., Gylfe E., Zhang W., Samelson L.E., Welsh M.
J. Biol. Chem. 274:28050-28057(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SHB.
[14]"Autophosphorylation of KDR in the kinase domain is required for maximal VEGF-stimulated kinase activity and receptor internalization."
Dougher M., Terman B.I.
Oncogene 18:1619-1627(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY KDR.
[15]"Characterization of the tyrosine kinase Tnk1 and its binding with phospholipase C-gamma1."
Felschow D.M., Civin C.I., Hoehn G.T.
Biochem. Biophys. Res. Commun. 273:294-301(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TNK1.
[16]"The ORF3 protein of hepatitis E virus binds to Src homology 3 domains and activates MAPK."
Korkaya H., Jameel S., Gupta D., Tyagi S., Kumar R., Zafrullah M., Mazumdar M., Lal S.K., Xiaofang L., Sehgal D., Das S.R., Sahal D.
J. Biol. Chem. 276:42389-42400(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HEV ORF3 PROTEIN.
[17]"Identification and characterization of a new family of guanine nucleotide exchange factors for the ras-related GTPase Ral."
Rebhun J.F., Chen H., Quilliam L.A.
J. Biol. Chem. 275:13406-13410(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RALGPS1.
[18]"Protein tyrosine phosphatase CD148-mediated inhibition of T-cell receptor signal transduction is associated with reduced LAT and phospholipase Cgamma1 phosphorylation."
Baker J.E., Majeti R., Tangye S.G., Weiss A.
Mol. Cell. Biol. 21:2393-2403(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PROBABLE DEPHOSPHORYLATION BY PTPRJ.
[19]"Membrane raft-dependent regulation of phospholipase Cgamma-1 activation in T lymphocytes."
Veri M.C., DeBell K.E., Seminario M.C., DiBaldassarre A., Reischl I., Rawat R., Graham L., Noviello C., Rellahan B.L., Miscia S., Wange R.L., Bonvini E.
Mol. Cell. Biol. 21:6939-6950(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-783, SUBCELLULAR LOCATION.
[20]"The tyrosine phosphatase CD148 is excluded from the immunologic synapse and down-regulates prolonged T cell signaling."
Lin J., Weiss A.
J. Cell Biol. 162:673-682(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROBABLE DEPHOSPHORYLATION BY PTPRJ.
[21]"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-771 AND TYR-1253, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[22]"TrkA alternative splicing: a regulated tumor-promoting switch in human neuroblastoma."
Tacconelli A., Farina A.R., Cappabianca L., Desantis G., Tessitore A., Vetuschi A., Sferra R., Rucci N., Argenti B., Screpanti I., Gulino A., Mackay A.R.
Cancer Cell 6:347-360(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NTRK1.
[23]"Signal transduction via the stem cell factor receptor/c-Kit."
Ronnstrand L.
Cell. Mol. Life Sci. 61:2535-2548(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON INTERACTION WITH KIT AND ROLE IN KIT SIGNALING.
[24]"Deficiency of BLNK hampers PLC-gamma2 phosphorylation and Ca2+ influx induced by the pre-B-cell receptor in human pre-B cells."
Taguchi T., Kiyokawa N., Takenouch H., Matsui J., Tang W.-R., Nakajima H., Suzuki K., Shiozawa Y., Saito M., Katagiri Y.U., Takahashi T., Karasuyama H., Matsuo Y., Okita H., Fujimoto J.
Immunology 112:575-582(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BLNK; VAV1; GRB2 AND NCK1.
[25]"Activation of vascular endothelial growth factor receptor-3 and its downstream signaling promote cell survival under oxidative stress."
Wang J.F., Zhang X., Groopman J.E.
J. Biol. Chem. 279:27088-27097(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FLT4.
[26]"Vascular endothelial growth factor (VEGF)-D and VEGF-A differentially regulate KDR-mediated signaling and biological function in vascular endothelial cells."
Jia H., Bagherzadeh A., Bicknell R., Duchen M.R., Liu D., Zachary I.
J. Biol. Chem. 279:36148-36157(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-783 IN RESPONSE TO KDR ACTIVATION.
[27]"Early phosphorylation kinetics of proteins involved in proximal TCR-mediated signaling pathways."
Houtman J.C., Houghtling R.A., Barda-Saad M., Toda Y., Samelson L.E.
J. Immunol. 175:2449-2458(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY ITK.
[28]"Intracellular retention, degradation, and signaling of glycosylation-deficient FGFR2 and craniosynostosis syndrome-associated FGFR2C278F."
Hatch N.E., Hudson M., Seto M.L., Cunningham M.L., Bothwell M.
J. Biol. Chem. 281:27292-27305(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FGFR2, PHOSPHORYLATION.
[29]"Obligatory role for phospholipase C-gamma(1) in villin-induced epithelial cell migration."
Wang Y., Tomar A., George S.P., Khurana S.
Am. J. Physiol. 292:C1775-C1786(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH VIL1, SUBCELLULAR LOCATION.
[30]"Sustained phosphorylation of mutated FGFR3 is a crucial feature of genetic dwarfism and induces apoptosis in the ATDC5 chondrogenic cell line via PLCgamma-activated STAT1."
Harada D., Yamanaka Y., Ueda K., Nishimura R., Morishima T., Seino Y., Tanaka H.
Bone 41:273-281(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY FGFR3.
[31]"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.
[32]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1221, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1222 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[33]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[34]"A novel interaction between fibroblast growth factor receptor 3 and the p85 subunit of phosphoinositide 3-kinase: activation-dependent regulation of ERK by p85 in multiple myeloma cells."
Salazar L., Kashiwada T., Krejci P., Muchowski P., Donoghue D., Wilcox W.R., Thompson L.M.
Hum. Mol. Genet. 18:1951-1961(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FGFR3.
[35]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-771; TYR-775; TYR-783 AND SER-1221, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1222 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[36]"Mutation of tyrosine residue 857 in the PDGF beta-receptor affects cell proliferation but not migration."
Wardega P., Heldin C.H., Lennartsson J.
Cell. Signal. 22:1363-1368(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PDGFRB, PHOSPHORYLATION AT TYR-771.
[37]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1221 AND TYR-1253, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[38]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[39]"Nedd4-1 binds and ubiquitylates activated FGFR1 to control its endocytosis and function."
Persaud A., Alberts P., Hayes M., Guettler S., Clarke I., Sicheri F., Dirks P., Ciruna B., Rotin D.
EMBO J. 30:3259-3273(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FGFR1, PHOSPHORYLATION BY FGFR1.
[40]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1222 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[41]"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 TESPA1.
Tissue: Thymocyte.
[42]"Cellular signaling by fibroblast growth factor receptors."
Eswarakumar V.P., Lax I., Schlessinger J.
Cytokine Growth Factor Rev. 16:139-149(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON ROLE IN FGF-ACTIVATED SIGNALING PATHWAYS.
[43]"Solution structure of the SH3 domain of phospholipase C-gamma."
Kohda D., Hatanaka H., Odaka M., Mandiyan V., Ullrich A., Schlessinger J., Inagaki F.
Cell 72:953-960(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF SH3 DOMAIN.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M34667 mRNA. Translation: AAA36452.1.
DQ297143 Genomic DNA. Translation: ABB84466.1.
AL022394 Genomic DNA. Translation: CAA18537.1.
CH471077 Genomic DNA. Translation: EAW75991.1.
CH471077 Genomic DNA. Translation: EAW75992.1.
BC136466 mRNA. Translation: AAI36467.1.
BC144136 mRNA. Translation: AAI44137.1.
PIRA36466.
RefSeqNP_002651.2. NM_002660.2.
NP_877963.1. NM_182811.1.
UniGeneHs.268177.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HSQNMR-A790-852[»]
2HSPNMR-A790-852[»]
4EY0X-ray2.80A/B/C/D545-790[»]
4FBNX-ray2.40A545-790[»]
ProteinModelPortalP19174.
SMRP19174. Positions 73-483, 489-933, 952-1207.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111351. 94 interactions.
DIPDIP-100N.
IntActP19174. 103 interactions.
MINTMINT-102915.
STRING9606.ENSP00000244007.

Chemistry

BindingDBP19174.
ChEMBLCHEMBL3964.

PTM databases

PhosphoSiteP19174.

Polymorphism databases

DMDM130225.

Proteomic databases

PaxDbP19174.
PRIDEP19174.

Protocols and materials databases

DNASU5335.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000244007; ENSP00000244007; ENSG00000124181. [P19174-2]
ENST00000373271; ENSP00000362368; ENSG00000124181. [P19174-1]
ENST00000373272; ENSP00000362369; ENSG00000124181. [P19174-2]
GeneID5335.
KEGGhsa:5335.
UCSCuc002xjp.1. human. [P19174-1]

Organism-specific databases

CTD5335.
GeneCardsGC20P039765.
HGNCHGNC:9065. PLCG1.
HPACAB004277.
HPA036681.
HPA036682.
MIM172420. gene.
neXtProtNX_P19174.
PharmGKBPA33392.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG268751.
HOVERGENHBG053611.
KOK01116.
OMAYRSLMYS.
OrthoDBEOG7W419X.
PhylomeDBP19174.
TreeFamTF313216.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_116125. Disease.
REACT_604. Hemostasis.
REACT_6900. Immune System.
SignaLinkP19174.

Gene expression databases

ArrayExpressP19174.
BgeeP19174.
CleanExHS_PLCG1.
GenevestigatorP19174.

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.
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.
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

ChiTaRSPLCG1. human.
EvolutionaryTraceP19174.
GeneWikiPLCG1.
GenomeRNAi5335.
NextBio20662.
PROP19174.
SOURCESearch...

Entry information

Entry namePLCG1_HUMAN
AccessionPrimary (citable) accession number: P19174
Secondary accession number(s): B7ZLY7 expand/collapse secondary AC list , B9EGH4, E1P5W4, Q2V575
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: April 16, 2014
This is version 184 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM