Reviewed, UniProtKB/Swiss-Prot P19174 (PLCG1_HUMAN)

Names and origin

Protein names

Recommended name:
    1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-1
    EC=3.1.4.11
Alternative name(s):
    Phosphoinositide phospholipase C
    Phospholipase C-gamma-1
      Short name=PLC-gamma-1
    PLC-II
    PLC-148

Gene names

Name:	PLCG1
Synonyms:	PLC1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1290 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	PLC-gamma is a major substrate for heparin-binding growth factor 1 (acidic fibroblast growth factor)-activated tyrosine kinase.
Catalytic activity	1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol.
Cofactor	Calcium.
Subunit structure	Interacts with AGAP2 via its SH3 domain By similarity. Interacts with phosphorylated LAT upon TCR activation. Interacts with the Pro-rich domain of TNK1 via its SH3 domain. 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 its 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 and CLNK By similarity. Interacts with RALGPS1. Interacts (via SH3 domain) with HEV ORF3 protein.
Domain	The SH3 domain mediates interaction with CLNK By similarity. The SH3 domain also mediates interaction with RALGPS1.
Post-translational modification	The receptor-mediated activation of PLC-gamma-1 and PLC-gamma-2 involves their phosphorylation by tyrosine kinases in response to ligation of a variety of growth factor receptors and immune system receptors. 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 process	Host-virus interaction Lipid degradation
Coding sequence diversity	Polymorphism
Domain	Repeat SH2 domain SH3 domain
Ligand	Calcium
Molecular function	Hydrolase Transducer
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure
Gene Ontology (GO)
Biological process	interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW intracellular signaling cascade Inferred from electronic annotation. Source: InterPro phospholipid catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytosol Inferred from Experiment. Source: Reactome plasma membrane Inferred from Experiment. Source: Reactome
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoinositide phospholipase C activity Non-traceable author statement. Source: UniProtKB protein binding Ref.6 Inferred from physical interaction. Source: UniProtKB receptor signaling protein activity Ref.17 Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ABL1	P00519	1	EBI-79387,EBI-375543
ABL2	P42684	2	EBI-79387,EBI-1102694
ADNP	Q9H2P0	1	EBI-79387,EBI-1764854
AFF2	P51816	1	EBI-79387,EBI-1754468
AIRE	O43918	1	EBI-79387,EBI-1753081
AKAP2	Q9Y2D5	1	EBI-79387,EBI-1754555
ARHGEF11	O15085	1	EBI-79387,EBI-311099
ASAP1	Q9ULH1	2	EBI-79387,EBI-346622
ASAP2	O43150	2	EBI-79387,EBI-310968
CAST	P20810	1	EBI-79387,EBI-1268770
CD22	P20273	1	EBI-79387,EBI-78277
CHAF1A	Q13111	1	EBI-79387,EBI-1020839
CKAP5	Q14008	1	EBI-79387,EBI-310585
COBRA1	Q8WX92	1	EBI-79387,EBI-347721
CSMD2	Q7Z408	1	EBI-79387,EBI-1957312
DLGAP1	O14490	1	EBI-79387,EBI-1753207
DLGAP3	O95886	1	EBI-79387,EBI-1752541
DLX4	Q92988	1	EBI-79387,EBI-1752755
DTNBP1	Q96EV8	1	EBI-79387,EBI-465804
DUSP15	Q9H1R2	1	EBI-79387,EBI-1752795
EFS	O43281	1	EBI-79387,EBI-718488
EPX	P11678	1	EBI-79387,EBI-1761505
EXTL3	O43909	1	EBI-79387,EBI-1754679
F2RL2	O00254	1	EBI-79387,EBI-1751853
FANCA	O15360	1	EBI-79387,EBI-81570
FCGR2B	P31994	1	EBI-79387,EBI-724784
FCGR2C	P31995	1	EBI-79387,EBI-1396036
FLNA	P21333	1	EBI-79387,EBI-350432
FLNB	O75369	1	EBI-79387,EBI-352089
FLNC	Q14315	1	EBI-79387,EBI-489954
GHR	P10912	1	EBI-79387,EBI-286316
GLTSCR1	Q9NZM4	1	EBI-79387,EBI-1754943
ID4	P47928	1	EBI-79387,EBI-1754719
IL3RA	P26951	1	EBI-79387,EBI-1757512
ISG20L2	Q9H9L3	1	EBI-79387,EBI-751335
JAK2	O60674	1	EBI-79387,EBI-518647
KHDRBS1	Q07666	1	EBI-79387,EBI-1364
LAT	O43561	1	EBI-79387,EBI-1222766
LIG3	P49916	1	EBI-79387,EBI-1753381
MAP4	P27816	1	EBI-79387,EBI-715255
MAP4K1	Q92918	5	EBI-79387,EBI-881
MEPE	Q9NQ76	1	EBI-79387,EBI-1753293
PDIA2	Q13087	1	EBI-79387,EBI-1752525
PHACTR2	O75167	1	EBI-79387,EBI-1754409
PPFIA4	O75335	1	EBI-79387,EBI-947323
RAG1	P15918	1	EBI-79387,EBI-1755109
RGS7	P49802	1	EBI-79387,EBI-1754797
RIN3	Q8TB24	2	EBI-79387,EBI-1570523
RPL13	P26373	1	EBI-79387,EBI-356849
RRAS	P10301	1	EBI-79387,EBI-968703
RYR1	P21817	1	EBI-79387,EBI-1221290
SEC24B	O95487	1	EBI-79387,EBI-81101
SERPINC1	P01008	1	EBI-79387,EBI-1039832
SHANK2	Q9UPX8	2	EBI-79387,EBI-1570571
SHANK3	Q9BYB0	1	EBI-79387,EBI-1752330
SLC23A1	Q9UHI7	1	EBI-79387,EBI-1759386
SNX17	Q15036	1	EBI-79387,EBI-1752620
SNX7	Q9UNH6	1	EBI-79387,EBI-751422
SOS1	Q07889	1	EBI-79387,EBI-297487
SOS2	Q07890	2	EBI-79387,EBI-298181
SPEN	Q96T58	1	EBI-79387,EBI-765739
SUV39H2	Q9H5I1	1	EBI-79387,EBI-723127
TDRD1	Q9BXT4	1	EBI-79387,EBI-1757688
TGOLN2	O43493	1	EBI-79387,EBI-1752146
TRAIP	Q9BWF2	1	EBI-79387,EBI-1756205
ZP2	Q05996	1	EBI-79387,EBI-1755919

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1290

1290

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

PRO_0000088498

Regions

Domain

27 – 142

116

PH 1

Domain

152 – 187

36

EF-hand

Domain

320 – 464

145

PI-PLC X-box

Domain

489 – 523

35

PH 2; first part

Domain

550 – 657

108

SH2 1

Domain

668 – 756

89

SH2 2

Domain

791 – 851

61

SH3

Domain

895 – 931

37

PH 2; second part

Domain

953 – 1070

118

PI-PLC Y-box

Domain

1075 – 1177

103

C2

Calcium binding

165 – 176

12

Potential

Sites

Active site

335

1

By similarity

Active site

380

1

By similarity

Amino acid modifications

Modified residue

379

1

Phosphotyrosine By similarity

Modified residue

481

1

Phosphotyrosine By similarity

Modified residue

506

1

Phosphotyrosine By similarity

Modified residue

771

1

Phosphotyrosine Ref.11 Ref.12

Modified residue

775

1

Phosphotyrosine Ref.11 Ref.10

Modified residue

783

1

Phosphotyrosine Ref.10

Modified residue

977

1

Phosphotyrosine Ref.13

Modified residue

1221

1

Phosphoserine Ref.15

Modified residue

1253

1

Phosphotyrosine Ref.12

Modified residue

1263

1

Phosphoserine Ref.14

Natural variations

Natural variant

209

1

T → N: dbSNP rs2229348. Ref.2

VAR_025213

Natural variant

279

1

S → G: dbSNP rs2228246. Ref.2

VAR_022130

Natural variant

739

1

S → T Ref.2

VAR_025214

Natural variant

813

1

I → T: dbSNP rs753381. Ref.2

VAR_011908

Experimental info

Sequence conflict

1215

1

K → KQ in ABB84466. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

1290

Helix Strand Turn

Details...

Beta strand

792 – 794

3

Beta strand

805 – 809

5

Turn

825 – 827

3

Beta strand

834 – 836

3

Turn

843 – 845

3

Sequences

	Sequence		Length	Mass (Da)
	P19174-1 [UniParc]. Last modified November 1, 1990. Version 1. Checksum: AE05ABE2A18EDDAC	FASTA	1,290	148,532
	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

References

	« Hide 'large scale' referencesShow '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: 2167438] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. 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. , 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: 11780052] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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: 9489702] [Abstract] Cited for: INTERACTION WITH LAT.
[5]	"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: 10488157] [Abstract] Cited for: INTERACTION WITH SHB.
[6]	"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: 10873601] [Abstract] Cited for: INTERACTION WITH TNK1.
[7]	"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: 11518702] [Abstract] Cited for: INTERACTION WITH HEV ORF3 PROTEIN.
[8]	"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: 10747847] [Abstract] Cited for: INTERACTION WITH RALGPS1.
[9]	"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: 15270728] [Abstract] Cited for: INTERACTION WITH BLNK; VAV1; GRB2 AND NCK1.
[10]	"Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules." Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., Lauffenburger D.A., White F.M. Mol. Cell. Proteomics 4:1240-1250(2005) [PubMed: 15951569] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-775 AND TYR-783, MASS SPECTROMETRY. Tissue: Epithelium.
[11]	"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: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-771 AND TYR-775, MASS SPECTROMETRY.
[12]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-771 AND TYR-1253, MASS SPECTROMETRY. Tissue: Epithelium.
[13]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-977, MASS SPECTROMETRY.
[14]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1263, MASS SPECTROMETRY.
[15]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1221, MASS SPECTROMETRY.
[16]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[17]	"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: 7681365] [Abstract] Cited for: STRUCTURE BY NMR OF SH3 DOMAIN.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBLGenBankDDBJ

M34667 mRNA. Translation: AAA36452.1.
DQ297143 Genomic DNA. Translation: ABB84466.1.
AL022394 Genomic DNA. Translation: CAA18537.1.

IPI

IPI00016736.

PIR

A36466.

RefSeq

NP_877963.1.

UniGene

Hs.268177

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1HSQ	NMR	-	A	790-852	[»]
2HSP	NMR	-	A	790-852	[»]

SMR

P19174. Positions 489-553, 663-759, 851-933.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:100N.

IntAct

P19174. 67 interactions.

PTM databases

PhosphoSite

P19174.

Proteomic databases

PRIDE

P19174.

Genome annotation databases

Ensembl

ENSG00000124181. Homo sapiens. [Contig view]

GeneID

5335.

Organism-specific databases

GeneCards

GC20P039199.

H-InvDB

HIX0015819.

HGNC

HGNC:9065. PLCG1.

HPA

CAB004277.

MIM

172420. gene.

PharmGKB

PA33392.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P19174.

Enzyme and pathway databases

BRENDA

3.1.4.11. 247.

Pathway_Interaction_DB

pi3kcipathway. Class I PI3K signaling events.
epha_fwdpathway. EPHA forward signaling.
epopathway. EPO signaling pathway.
fcer1pathway. Fc-epsilon receptor I signaling in mast cells.
fgf_pathway. FGF signaling pathway.
lysophospholipid_pathway. LPA receptor mediated events.
trkrpathway. Neurotrophic factor-mediated Trk receptor signaling.
wnt_calcium_pathway. Noncanonical Wnt signaling pathway.
pdgfrapathway. PDGFR-alpha signaling pathway.
pdgfrbpathway. PDGFR-beta signaling pathway.
s1p_s1p1_pathway. S1P1 pathway.
s1p_s1p4_pathway. S1P4 pathway.
met_pathway. Signaling events activated by Hepatocyte Growth Factor Receptor (c-Met).
vegfr1_2_pathway. Signaling events mediated by VEGFR1 and VEGFR2.
tcrpathway. TCR signaling in naive CD4+ T cells.
cd8tcrpathway. TCR signaling in naive CD8+ T cells.
pi3kplctrkpathway. Trk receptor signaling mediated by PI3K and PLC-gamma.
vegfr1_pathway. VEGFR1 specific signals.

Reactome

REACT_11061. Signalling by NGF.
REACT_604. Hemostasis.
REACT_6900. Signaling in Immune system.
REACT_9417. Signaling by EGFR.

Gene expression databases

ArrayExpress

P19174.

Bgee

P19174.

CleanEx

HS_PLCG1.

GermOnline

ENSG00000124181. Homo sapiens.

Family and domain databases

InterPro

IPR000008. C2_Ca-dep.
IPR018029. C2_membr_targeting.
IPR018247. EF_HAND_1.
IPR018249. EF_HAND_2.
IPR011993. PH_type.
IPR001192. Phospholipase_C_Pinositol-sp_C.
IPR000909. Phospholipase_C_Pinositol-sp_X.
IPR001711. Phospholipase_C_Pinositol-sp_Y.
IPR016279. PLC-gamma.
IPR017946. PLC-like_Pdiesterase_TIM-brl.
IPR001849. Pleckstrin_homology.
IPR000980. SH2.
IPR001452. SH3_domain.
[Graphical view]

Gene3D

G3DSA:2.30.29.30. PH_type. 1 hit.
G3DSA:3.20.20.190. PLC-like_Pdiesterase_TIM-brl. 1 hit.

Pfam

PF00168. C2. 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]

PIRSF

PIRSF000952. PLC-gamma. 1 hit.

PRINTS

PR00390. PHPHLIPASEC.
PR00401. SH2DOMAIN.

ProDom

PD001202. PI_PLC_Y. 2 hits.
PD000093. SH2. 2 hits.
PD000066. SH3. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

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]

PROSITE

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]

ProtoNet

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Other Resources

NextBio

20662.

SOURCE

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Entry information

Entry name

PLCG1_HUMAN

Accession

Primary (citable) accession number: P19174
Secondary accession number(s): Q2V575

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	November 1, 1990
Last modified:	June 16, 2009
This is version 128 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)