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Q9P212 (PLCE1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 125. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase epsilon-1

EC=3.1.4.11
Alternative name(s):
Pancreas-enriched phospholipase C
Phosphoinositide phospholipase C-epsilon-1
Phospholipase C-epsilon-1
Short name=PLC-epsilon-1
Gene names
Name:PLCE1
Synonyms:KIAA1516, PLCE, PPLC
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2302 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. PLCE1 is a bifunctional enzyme which also regulates small GTPases of the Ras superfamily through its Ras guanine-exchange factor (RasGEF) activity. As an effector of heterotrimeric and small G-protein, it may play a role in cell survival, cell growth, actin organization and T-cell activation. Ref.2 Ref.11 Ref.12 Ref.13 Ref.15 Ref.19 Ref.21

Catalytic activity

1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol. Ref.1 Ref.2

Cofactor

Calcium. Ref.1

Enzyme regulation

Activated by the heterotrimeric G-protein subunits GNA12, GNA13 and GNB1-GNG2. Activated by HRAS, RAP1A, RHOA, RHOB, RHOC, RRAS and RRAS2. Activated by the G(s)-coupled GPCRs ADRB2, PTGER1 and CHRM3 through cyclic-AMP formation and RAP2B activation. Inhibited by G(i)-coupled GPCRs. Ref.1 Ref.2 Ref.12 Ref.13 Ref.16 Ref.19

Subunit structure

Interacts with RHOA By similarity. Interacts with IQGAP1, HRAS, RAP1A, RAP2A, RAP2B and RRAS. Ref.1 Ref.14 Ref.19 Ref.21

Subcellular location

Cytoplasmcytosol. Cell membrane. Golgi apparatus membrane. Note: Recruited to plasma membrane by activated HRAS and RAP2. Recruited to perinuclear membrane by activated RAP1A. Isoform 1 and isoform 2 associates with Golgi membranes. Ref.1 Ref.2 Ref.11 Ref.18

Tissue specificity

Widely expressed. Isoform 1 is broadly expressed and only absent in peripheral blood leukocytes. Isoform 2 is specifically expressed in placenta, lung and spleen. Ref.1 Ref.2 Ref.18

Induction

Overexpressed during heart failure. Ref.1 Ref.2 Ref.12 Ref.13 Ref.16 Ref.17 Ref.19

Domain

The Ras-associating domain 1 is degenerated and may not bind HRAS. The Ras-associating domain 2 mediates interaction with GTP-bound HRAS, RAP1A, RAP2A and RAP2B and recruitment of HRAS to the cell membrane.

The Ras-GEF domain has a GEF activity towards HRAS and RAP1A. Mediates activation of the mitogen-activated protein kinase pathway.

Involvement in disease

Nephrotic syndrome 3 (NPHS3) [MIM:610725]: A form of nephrotic syndrome, a renal disease clinically characterized by severe proteinuria, resulting in complications such as hypoalbuminemia, hyperlipidemia and edema. Kidney biopsies show non-specific histologic changes such as focal segmental glomerulosclerosis and diffuse mesangial proliferation. Some affected individuals have an inherited steroid-resistant form and progress to end-stage renal failure. Most patients with NPHS3 show diffuse mesangial sclerosis on renal biopsy, which is a pathologic entity characterized by mesangial matrix expansion with no mesangial hypercellularity, hypertrophy of the podocytes, vacuolized podocytes, thickened basement membranes, and diminished patency of the capillary lumen.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.21

Sequence similarities

Contains 1 C2 domain.

Contains 1 PI-PLC X-box domain.

Contains 1 PI-PLC Y-box domain.

Contains 2 Ras-associating domains.

Contains 1 Ras-GEF domain.

Sequence caution

The sequence AAF22005.1 differs from that shown. Reason: Frameshift at position 1131.

The sequence AAG17145.2 differs from that shown. Reason: Frameshift at position 2296.

The sequence BAA96040.2 differs from that shown. Reason: Erroneous initiation.

The sequence BAB14090.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAH70739.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAH73288.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAH73757.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI16674.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processLipid degradation
Lipid metabolism
   Cellular componentCell membrane
Cytoplasm
Golgi apparatus
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainRepeat
   Molecular functionGuanine-nucleotide releasing factor
Hydrolase
Transducer
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRas protein signal transduction

Traceable author statement Ref.1. Source: UniProtKB

activation of MAPK activity

Inferred from direct assay Ref.2. Source: UniProtKB

calcium-mediated signaling

Non-traceable author statement Ref.1. Source: UniProtKB

cell proliferation

Non-traceable author statement Ref.1. Source: UniProtKB

cytoskeleton organization

Non-traceable author statement Ref.2. Source: UniProtKB

diacylglycerol biosynthetic process

Traceable author statement Ref.2. Source: UniProtKB

epidermal growth factor receptor signaling pathway

Non-traceable author statement Ref.1. Source: UniProtKB

glomerulus development

Inferred from mutant phenotype Ref.21. Source: HGNC

heart development

Traceable author statement Ref.2. Source: UniProtKB

inositol phosphate metabolic process

Traceable author statement. Source: Reactome

inositol phosphate-mediated signaling

Traceable author statement Ref.2. Source: UniProtKB

lipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

phospholipase C-activating G-protein coupled receptor signaling pathway

Inferred from direct assay Ref.2. Source: UniProtKB

phospholipid metabolic process

Inferred by curator Ref.1. Source: UniProtKB

positive regulation of cytosolic calcium ion concentration

Traceable author statement Ref.2. Source: UniProtKB

protein kinase C-activating G-protein coupled receptor signaling pathway

Non-traceable author statement Ref.1. Source: UniProtKB

regulation of G-protein coupled receptor protein signaling pathway

Inferred from direct assay Ref.2. Source: UniProtKB

regulation of GTPase activity

Traceable author statement Ref.2. Source: GOC

regulation of Ras protein signal transduction

Inferred from direct assay Ref.2. Source: UniProtKB

regulation of cell growth

Traceable author statement Ref.2. Source: UniProtKB

regulation of protein kinase activity

Inferred from direct assay Ref.2. Source: UniProtKB

regulation of smooth muscle contraction

Traceable author statement Ref.2. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentGolgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Inferred from direct assay Ref.1. Source: UniProtKB

plasma membrane

Inferred from direct assay Ref.1. Source: UniProtKB

   Molecular_functionRas GTPase binding

Traceable author statement Ref.1. Source: UniProtKB

calcium ion binding

Inferred from electronic annotation. Source: InterPro

enzyme binding

Inferred from physical interaction Ref.1. Source: UniProtKB

guanyl-nucleotide exchange factor activity

Traceable author statement Ref.2. Source: UniProtKB

phosphatidylinositol phospholipase C activity

Inferred from direct assay Ref.2Ref.1. Source: UniProtKB

phospholipase C activity

Inferred from direct assay Ref.2. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.1. Source: UniProtKB

receptor signaling protein activity

Traceable author statement Ref.1. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9P212-1)

Also known as: PLCepsilon1a;

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: Q9P212-2)

Also known as: PLCepsilon1b;

The sequence of this isoform differs from the canonical sequence as follows:
     1-308: Missing.
     309-402: DVEEDAFKSK...QRLSEAQWYP → MVSEGSAAGR...CGCWRLKEDQ

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 230223021-phosphatidylinositol 4,5-bisphosphate phosphodiesterase epsilon-1
PRO_0000256238

Regions

Domain531 – 790260Ras-GEF
Domain1392 – 1540149PI-PLC X-box
Domain1730 – 1846117PI-PLC Y-box
Domain1856 – 1956101C2
Domain2012 – 2114103Ras-associating 1
Domain2135 – 2238104Ras-associating 2
Region1686 – 176479Required for activation by RHOA, RHOB, GNA12, GNA13 and G-beta gamma By similarity

Sites

Active site14071 By similarity
Active site14521 By similarity

Natural variations

Alternative sequence1 – 308308Missing in isoform 2.
VSP_021335
Alternative sequence309 – 40294DVEED…AQWYP → MVSEGSAAGRDFAGMEEVRQ LHVRFCKGIKIWHQAWFLCS LLGREPQEREAGCQLWLCTL SAVLKVGWLFPLSEVPNFTL LKDGCGCWRLKEDQ in isoform 2.
VSP_021336
Natural variant4691S → T.
Corresponds to variant rs17508082 [ dbSNP | Ensembl ].
VAR_031843
Natural variant5481R → L.
Corresponds to variant rs17417407 [ dbSNP | Ensembl ].
VAR_031844
Natural variant14841S → L in NPHS3; gives rise to focal segmental glomerulosclerosis rather than diffuse mesangial sclerosis. Ref.21
VAR_029883
Natural variant15751R → P.
Corresponds to variant rs2274224 [ dbSNP | Ensembl ].
VAR_031845
Natural variant17771T → I. Ref.1 Ref.8
Corresponds to variant rs3765524 [ dbSNP | Ensembl ].
VAR_031846
Natural variant19271H → R. Ref.1 Ref.3 Ref.7 Ref.8
Corresponds to variant rs2274223 [ dbSNP | Ensembl ].
VAR_031847

Experimental info

Mutagenesis14521H → L: Loss of the phospholipase C enzymatic activity. Still activates HRAS and the MAP kinase pathway. Ref.2
Mutagenesis21401Q → E: Increases 2.8-fold the affinity for HRAS. Ref.20
Mutagenesis21481Q → E: Decreases 17.5-fold the affinity for HRAS. Ref.20
Mutagenesis21481Q → K: Increases 1.4-fold the affinity for HRAS. Ref.20
Mutagenesis21501R → L: Abolishes interaction with HRAS. Ref.20
Mutagenesis21711K → L: No effect on HRAS-binding. Ref.20
Mutagenesis21741Y → L: Reduces HRAS-binding. Ref.20
Sequence conflict5021G → S in AAG28341. Ref.2
Sequence conflict7031V → F in AAG28341. Ref.2
Sequence conflict11331E → K in AAG28341. Ref.2
Sequence conflict1229 – 12302SR → QA in AAF22005. Ref.8
Sequence conflict14561L → P in AAG17145. Ref.1
Sequence conflict15711N → D in BAB14090. Ref.9
Sequence conflict15751R → Q in AAG28341. Ref.2
Sequence conflict16721C → R in AAG17145. Ref.1
Sequence conflict17051P → L in BAB14090. Ref.9
Sequence conflict21251D → G in BAB14090. Ref.9
Isoform 2:
Sequence conflict691L → P in AAG28341. Ref.2

Secondary structure

............................................ 2302
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (PLCepsilon1a) [UniParc].

Last modified October 31, 2006. Version 3.
Checksum: 71DDE446277077A3

FASTA2,302258,715
        10         20         30         40         50         60 
MTSEEMTASV LIPVTQRKVV SAQSAADESS EKVSDINISK AHTVRRSGET SHTISQLNKL 

        70         80         90        100        110        120 
KEEPSGSNLP KILSIAREKI VSDENSNEKC WEKIMPDSAK NLNINCNNIL RNHQHGLPQR 

       130        140        150        160        170        180 
QFYEMYNSVA EEDLCLETGI PSPLERKVFP GIQLELDRPS MGISPLGNQS VIIETGRAHP 

       190        200        210        220        230        240 
DSRRAVFHFH YEVDRRMSDT FCTLSENLIL DDCGNCVPLP GGEEKQKKNY VAYTCKLMEL 

       250        260        270        280        290        300 
AKNCDNKNEQ LQCDHCDTLN DKYFCFEGSC EKVDMVYSGD SFCRKDFTDS QAAKTFLSHF 

       310        320        330        340        350        360 
EDFPDNCDDV EEDAFKSKKE RSTLLVRRFC KNDREVKKSV YTGTRAIVRT LPSGHIGLTA 

       370        380        390        400        410        420 
WSYIDQKRNG PLLPCGRVME PPSTVEIRQD GSQRLSEAQW YPIYNAVRRE ETENTVGSLL 

       430        440        450        460        470        480 
HFLTKLPASE TAHGRISVGP CLKQCVRDTV CEYRATLQRT SISQYITGSL LEATTSLGAR 

       490        500        510        520        530        540 
SGLLSTFGGS TGRMMLKERQ PGPSVANSNA LPSSSAGISK ELIDLQPLIQ FPEEVASILM 

       550        560        570        580        590        600 
EQEQTIYRRV LPVDYLCFLT RDLGTPECQS SLPCLKASIS ASILTTQNGE HNALEDLVMR 

       610        620        630        640        650        660 
FNEVSSWVTW LILTAGSMEE KREVFSYLVH VAKCCWNMGN YNAVMEFLAG LRSRKVLKMW 

       670        680        690        700        710        720 
QFMDQSDIET MRSLKDAMAQ HESSCEYRKV VTRALHIPGC KVVPFCGVFL KELCEVLDGA 

       730        740        750        760        770        780 
SGLMKLCPRY NSQEETLEFV ADYSGQDNFL QRVGQNGLKN SEKESTVNSI FQVIRSCNRS 

       790        800        810        820        830        840 
LETDEEDSPS EGNSSRKSSL KDKSRWQFII GDLLDSDNDI FEQSKEYDSH GSEDSQKAFD 

       850        860        870        880        890        900 
HGTELIPWYV LSIQADVHQF LLQGATVIHY DQDTHLSARC FLQLQPDNST LTWVKPTTAS 

       910        920        930        940        950        960 
PASSKAKLGV LNNTAEPGKF PLLGNAGLSS LTEGVLDLFA VKAVYMGHPG IDIHTVCVQN 

       970        980        990       1000       1010       1020 
KLGSMFLSET GVTLLYGLQT TDNRLLHFVA PKHTAKMLFS GLLELTRAVR KMRKFPDQRQ 

      1030       1040       1050       1060       1070       1080 
QWLRKQYVSL YQEDGRYEGP TLAHAVELFG GRRWSARNPS PGTSAKNAEK PNMQRNNTLG 

      1090       1100       1110       1120       1130       1140 
ISTTKKKKKI LMRGESGEVT DDEMATRKAK MHKECRSRSG SDPQDINEQE ESEVNAIANP 

      1150       1160       1170       1180       1190       1200 
PNPLPSRRAH SLTTAGSPNL AAGTSSPIRP VSSPVLSSSN KSPSSAWSSS SWHGRIKGGM 

      1210       1220       1230       1240       1250       1260 
KGFQSFMVSD SNMSFVEFVE LFKSFSVRSR KDLKDLFDVY AVPCNRSGSE SAPLYTNLTI 

      1270       1280       1290       1300       1310       1320 
DENTSDLQPD LDLLTRNVSD LGLFIKSKQQ LSDNQRQISD AIAAASIVTN GTGIESTSLG 

      1330       1340       1350       1360       1370       1380 
IFGVGILQLN DFLVNCQGEH CTYDEILSII QKFEPSISMC HQGLMSFEGF ARFLMDKENF 

      1390       1400       1410       1420       1430       1440 
ASKNDESQEN IKELQLPLSY YYIESSHNTY LTGHQLKGES SVELYSQVLL QGCRSVELDC 

      1450       1460       1470       1480       1490       1500 
WDGDDGMPII YHGHTLTTKI PFKEVVEAID RSAFINSDLP IIISIENHCS LPQQRKMAEI 

      1510       1520       1530       1540       1550       1560 
FKTVFGEKLV TKFLFETDFS DDPMLPSPDQ LRKKVLLKNK KLKAHQTPVD ILKQKAHQLA 

      1570       1580       1590       1600       1610       1620 
SMQVQAYNGG NANPRPANNE EEEDEEDEYD YDYESLSDDN ILEDRPENKS CNDKLQFEYN 

      1630       1640       1650       1660       1670       1680 
EEIPKRIKKA DNSACNKGKV YDMELGEEFY LDQNKKESRQ IAPELSDLVI YCQAVKFPGL 

      1690       1700       1710       1720       1730       1740 
STLNASGSSR GKERKSRKSI FGNNPGRMSP GETASFNKTS GKSSCEGIRQ TWEESSSPLN 

      1750       1760       1770       1780       1790       1800 
PTTSLSAIIR TPKCYHISSL NENAAKRLCR RYSQKLTQHT ACQLLRTYPA ATRIDSSNPN 

      1810       1820       1830       1840       1850       1860 
PLMFWLHGIQ LVALNYQTDD LPLHLNAAMF EANGGCGYVL KPPVLWDKNC PMYQKFSPLE 

      1870       1880       1890       1900       1910       1920 
RDLDSMDPAV YSLTIVSGQN VCPSNSMGSP CIEVDVLGMP LDSCHFRTKP IHRNTLNPMW 

      1930       1940       1950       1960       1970       1980 
NEQFLFHVHF EDLVFLRFAV VENNSSAVTA QRIIPLKALK RGYRHLQLRN LHNEVLEISS 

      1990       2000       2010       2020       2030       2040 
LFINSRRMEE NSSGNTMSAS SMFNTEERKC LQTHRVTVHG VPGPEPFTVF TINGGTKAKQ 

      2050       2060       2070       2080       2090       2100 
LLQQILTNEQ DIKPVTTDYF LMEEKYFISK EKNECRKQPF QRAIGPEEEI MQILSSWFPE 

      2110       2120       2130       2140       2150       2160 
EGYMGRIVLK TQQENLEEKN IVQDDKEVIL SSEEESFFVQ VHDVSPEQPR TVIKAPRVST 

      2170       2180       2190       2200       2210       2220 
AQDVIQQTLC KAKYSYSILS NPNPSDYVLL EEVVKDTTNK KTTTPKSSQR VLLDQECVFQ 

      2230       2240       2250       2260       2270       2280 
AQSKWKGAGK FILKLKEQVQ ASREDKKKGI SFASELKKLT KSTKQPRGLT SPSQLLTSES 

      2290       2300 
IQTKEEKPVG GLSSSDTMDY RQ 

« Hide

Isoform 2 (PLCepsilon1b) [UniParc].

Checksum: 069358CFA0D7A1CD
Show »

FASTA1,994223,872

References

« Hide 'large scale' references
[1]"Regulation of a novel human phospholipase C, PLCepsilon, through membrane targeting by Ras."
Song C., Hu C.-D., Masago M., Kariya K., Yamawaki-Kataoka Y., Shibatohge M., Wu D., Satoh T., Kataoka T.
J. Biol. Chem. 276:2752-2757(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, CATALYTIC ACTIVITY, COFACTOR, INTERACTION WITH HRAS AND RAP1A, SUBCELLULAR LOCATION, ENZYME REGULATION, VARIANTS ILE-1777 AND ARG-1927.
Tissue: Fetal brain.
[2]"A novel bifunctional phospholipase C that is regulated by Galpha 12 and stimulates the Ras/mitogen-activated protein kinase pathway."
Lopez I., Mak E.C., Ding J., Hamm H.E., Lomasney J.W.
J. Biol. Chem. 276:2758-2765(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, ENZYME REGULATION, MUTAGENESIS OF HIS-1452.
Tissue: Heart.
[3]"Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
DNA Res. 7:143-150(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ARG-1927.
Tissue: Brain.
[4]Ohara O., Nagase T., Kikuno R.
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[5]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]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].
[7]"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] (ISOFORM 1), VARIANT ARG-1927.
Tissue: Brain.
[8]"A novel phospholipase C enriched in pancreas."
Kawasaki H., Chen E.J., Springett G.M., Graybiel A.M., Housman D.E.
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1098-2302 (ISOFORMS 1/2), VARIANTS ILE-1777 AND ARG-1927.
Tissue: Pancreas.
[9]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1383 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1475-2302 (ISOFORMS 1/2).
Tissue: Brain and Teratocarcinoma.
[10]"Sequence of cDNA clone MPMGp800D13530."
Buessow K.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1987-2302 (ISOFORMS 1/2).
Tissue: Brain.
[11]"Role of the CDC25 homology domain of phospholipase Cepsilon in amplification of Rap1-dependent signaling."
Jin T.-G., Satoh T., Liao Y., Song C., Gao X., Kariya K., Hu C.-D., Kataoka T.
J. Biol. Chem. 276:30301-30307(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[12]"A new phospholipase-C-calcium signalling pathway mediated by cyclic AMP and a Rap GTPase."
Schmidt M., Evellin S., Weernink P.A.O., von Dorp F., Rehmann H., Lomasney J.W., Jakobs K.H.
Nat. Cell Biol. 3:1020-1024(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION.
[13]"Stimulation of phospholipase C-epsilon by the M3 muscarinic acetylcholine receptor mediated by cyclic AMP and the GTPase Rap2B."
Evellin S., Nolte J., Tysack K., vom Dorp F., Thiel M., Weernink P.A.O., Jakobs K.H., Webb E.J., Lomasney J.W., Schmidt M.
J. Biol. Chem. 277:16805-16813(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION.
[14]"Differential roles of Ras and Rap1 in growth factor-dependent activation of phospholipase C epsilon."
Song C., Satoh T., Edamatsu H., Wu D., Tadano M., Gao X., Kataoka T.
Oncogene 21:8105-8113(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAP1A; RAP2A AND RAP2B.
[15]"Activation of CD4 T cells by Raf-independent effectors of Ras."
Czyzyk J., Brogdon J.L., Badou A., Henegariu O., Preston Hurlburt P., Flavell R., Bottomly K.
Proc. Natl. Acad. Sci. U.S.A. 100:6003-6008(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[16]"Inhibition of phospholipase C-epsilon by Gi-coupled receptors."
vom Dorp F., Sari A.Y., Sanders H., Keiper M., Oude Weernink P.A., Jakobs K.H., Schmidt M.
Cell. Signal. 16:921-928(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION.
[17]"Phospholipase C epsilon modulates beta-adrenergic receptor-dependent cardiac contraction and inhibits cardiac hypertrophy."
Wang H., Oestreich E.A., Maekawa N., Bullard T.A., Vikstrom K.L., Dirksen R.T., Kelley G.G., Blaxall B.C., Smrcka A.V.
Circ. Res. 97:1305-1313(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[18]"Signaling properties and expression in normal and tumor tissues of two phospholipase C epsilon splice variants."
Sorli S.C., Bunney T.D., Sugden P.H., Paterson H.F., Katan M.
Oncogene 24:90-100(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[19]"The small GTPase R-Ras regulates organization of actin and drives membrane protrusions through the activity of PLCepsilon."
Ada-Nguema A.S., Xenias H., Sheetz M.P., Keely P.J.
J. Cell Sci. 119:1307-1319(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RRAS, ENZYME REGULATION.
[20]"Structural and mechanistic insights into ras association domains of phospholipase C epsilon."
Bunney T.D., Harris R., Gandarillas N.L., Josephs M.B., Roe S.M., Sorli S.C., Paterson H.F., Rodrigues-Lima F., Esposito D., Ponting C.P., Gierschik P., Pearl L.H., Driscoll P.C., Katan M.
Mol. Cell 21:495-507(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2131-2246 OF MUTANT LEU-2176 IN COMPLEX WITH HRAS, STRUCTURE BY NMR OF 2006-2114 AND 2131-2246, MUTAGENESIS OF GLN-2140; GLN-2148; ARG-2150; LYS-2171 AND TYR-2174.
[21]"Positional cloning uncovers mutations in PLCE1 responsible for a nephrotic syndrome variant that may be reversible."
Hinkes B., Wiggins R.C., Gbadegesin R., Vlangos C.N., Seelow D., Nuernberg G., Garg P., Verma R., Chaib H., Hoskins B.E., Ashraf S., Becker C., Hennies H.C., Goyal M., Wharram B.L., Schachter A.D., Mudumana S., Drummond I. expand/collapse author list , Kerjaschki D., Waldherr R., Dietrich A., Ozaltin F., Bakkaloglu A., Cleper R., Basel-Vanagaite L., Pohl M., Griebel M., Tsygin A.N., Soylu A., Mueller D., Sorli C.S., Bunney T.D., Katan M., Liu J., Attanasio M., O'toole J.F., Hasselbacher K., Mucha B., Otto E.A., Airik R., Kispert A., Kelley G.G., Smrcka A.V., Gudermann T., Holzman L.B., Nuernberg P., Hildebrandt F.
Nat. Genet. 38:1397-1405(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT NPHS3 LEU-1484, FUNCTION, INTERACTION WITH IQGAP1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF190642 mRNA. Translation: AAG17145.2. Frameshift.
AF170071 mRNA. Translation: AAG28341.1.
AB040949 mRNA. Translation: BAA96040.2. Different initiation.
AL139118 expand/collapse EMBL AC list , AL139124, AL365510, AL389885 Genomic DNA. Translation: CAH70739.1. Sequence problems.
AL139118 expand/collapse EMBL AC list , AL139124, AL365510, AL389885 Genomic DNA. Translation: CAH70740.1.
AL389885 expand/collapse EMBL AC list , AL139118, AL139124, AL365510 Genomic DNA. Translation: CAH73288.1. Sequence problems.
AL389885 expand/collapse EMBL AC list , AL139118, AL139124, AL365510 Genomic DNA. Translation: CAH73289.1.
AL365510 expand/collapse EMBL AC list , AL139118, AL139124, AL389885 Genomic DNA. Translation: CAH73757.1. Sequence problems.
AL365510 expand/collapse EMBL AC list , AL139118, AL139124, AL389885 Genomic DNA. Translation: CAH73758.1.
AL139124 expand/collapse EMBL AC list , AL139118, AL365510, AL389885 Genomic DNA. Translation: CAI16674.1. Sequence problems.
AL139124 expand/collapse EMBL AC list , AL139118, AL365510, AL389885 Genomic DNA. Translation: CAI16675.1.
CH471066 Genomic DNA. Translation: EAW50042.1.
CH471066 Genomic DNA. Translation: EAW50043.1.
BC140705 mRNA. Translation: AAI40706.1.
BC151854 mRNA. Translation: AAI51855.1.
AF117948 mRNA. Translation: AAF22005.1. Frameshift.
AK022543 mRNA. Translation: BAB14090.1. Different initiation.
AK289852 mRNA. Translation: BAF82541.1.
AY995135 mRNA. Translation: AAY45890.1.
CCDSCCDS41552.1. [Q9P212-1]
CCDS53555.1. [Q9P212-2]
RefSeqNP_001159451.1. NM_001165979.2. [Q9P212-2]
NP_001275918.1. NM_001288989.1.
NP_057425.3. NM_016341.3. [Q9P212-1]
UniGeneHs.655033.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2BYENMR-A2006-2114[»]
2BYFNMR-A2131-2246[»]
2C5LX-ray1.90C/D2131-2246[»]
ProteinModelPortalQ9P212.
SMRQ9P212. Positions 600-742, 1362-1542, 1663-1983, 2006-2114, 2131-2246.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119370. 5 interactions.
IntActQ9P212. 3 interactions.
MINTMINT-1420367.

PTM databases

PhosphoSiteQ9P212.

Polymorphism databases

DMDM118595723.

Proteomic databases

MaxQBQ9P212.
PaxDbQ9P212.
PRIDEQ9P212.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000260766; ENSP00000260766; ENSG00000138193. [Q9P212-1]
ENST00000371375; ENSP00000360426; ENSG00000138193. [Q9P212-2]
ENST00000371380; ENSP00000360431; ENSG00000138193. [Q9P212-1]
ENST00000371385; ENSP00000360438; ENSG00000138193. [Q9P212-2]
GeneID51196.
KEGGhsa:51196.
UCSCuc001kjk.3. human. [Q9P212-1]
uc001kjm.3. human. [Q9P212-2]

Organism-specific databases

CTD51196.
GeneCardsGC10P095753.
H-InvDBHIX0009051.
HIX0035415.
HGNCHGNC:17175. PLCE1.
HPAHPA015597.
HPA015598.
MIM608414. gene.
610725. phenotype.
neXtProtNX_Q9P212.
Orphanet93217. Familial idiopathic steroid-resistant nephrotic syndrome with diffuse mesangial sclerosis.
93213. Familial idiopathic steroid-resistant nephrotic syndrome with focal segmental hyalinosis.
PharmGKBPA33391.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG149692.
HOVERGENHBG059220.
InParanoidQ9P212.
KOK05860.
OMAVAKCCWN.
OrthoDBEOG7SN8CX.
PhylomeDBQ9P212.
TreeFamTF314432.

Enzyme and pathway databases

BioCycMetaCyc:HS06473-MONOMER.
ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressQ9P212.
BgeeQ9P212.
GenevestigatorQ9P212.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
1.10.840.10. 2 hits.
2.60.40.150. 1 hit.
3.20.20.190. 3 hits.
InterProIPR000008. C2_dom.
IPR011992. EF-hand-dom_pair.
IPR001192. PI-PLC_fam.
IPR028398. PLC-epsilon1.
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.
IPR000159. Ras-assoc.
IPR023578. Ras_GEF_dom.
IPR001895. RasGRF_CDC25.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PANTHERPTHR10336. PTHR10336. 1 hit.
PTHR10336:SF6. PTHR10336:SF6. 1 hit.
PfamPF00168. C2. 1 hit.
PF09279. EF-hand_like. 1 hit.
PF00388. PI-PLC-X. 1 hit.
PF00387. PI-PLC-Y. 1 hit.
PF00788. RA. 1 hit.
PF00617. RasGEF. 1 hit.
[Graphical view]
PRINTSPR00390. PHPHLIPASEC.
SMARTSM00239. C2. 1 hit.
SM00148. PLCXc. 1 hit.
SM00149. PLCYc. 1 hit.
SM00314. RA. 1 hit.
SM00147. RasGEF. 1 hit.
[Graphical view]
SUPFAMSSF48366. SSF48366. 3 hits.
SSF49562. SSF49562. 1 hit.
SSF51695. SSF51695. 3 hits.
SSF54236. SSF54236. 2 hits.
PROSITEPS50004. C2. 1 hit.
PS50007. PIPLC_X_DOMAIN. 1 hit.
PS50008. PIPLC_Y_DOMAIN. 1 hit.
PS50200. RA. 1 hit.
PS50009. RASGEF_CAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPLCE1. human.
EvolutionaryTraceQ9P212.
GeneWikiPLCE1.
GenomeRNAi51196.
NextBio54210.
PROQ9P212.
SOURCESearch...

Entry information

Entry namePLCE1_HUMAN
AccessionPrimary (citable) accession number: Q9P212
Secondary accession number(s): A6NGW0 expand/collapse secondary AC list , A6NLA1, A7MBN7, A8K1D7, B9EIJ6, Q1X6H8, Q5VWL4, Q5VWL5, Q9H9X8, Q9HBX6, Q9HC53, Q9UHV3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: October 31, 2006
Last modified: July 9, 2014
This is version 125 of the entry and version 3 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 10

Human chromosome 10: entries, gene names and cross-references to MIM