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Q01970 (PLCB3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 141. 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 beta-3

EC=3.1.4.11
Alternative name(s):
Phosphoinositide phospholipase C-beta-3
Phospholipase C-beta-3
Short name=PLC-beta-3
Gene names
Name:PLCB3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1234 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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.

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 SHANK2 By similarity. Interacts with LPAR2. Ref.7

Subcellular location

Membrane; Peripheral membrane protein.

Sequence similarities

Contains 1 C2 domain.

Contains 1 PI-PLC X-box domain.

Contains 1 PI-PLC Y-box domain.

Sequence caution

The sequence AAH32659.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processLipid degradation
Lipid metabolism
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandCalcium
   Molecular functionHydrolase
Transducer
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processinositol phosphate metabolic process

Traceable author statement. Source: Reactome

intracellular signal transduction

Inferred from electronic annotation. Source: InterPro

lipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of systemic arterial blood pressure

Inferred from direct assay PubMed 18468998. Source: MGI

small molecule metabolic process

Traceable author statement. Source: Reactome

synaptic transmission

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay. Source: HPA

protein complex

Inferred from direct assay PubMed 18468998. Source: MGI

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

calmodulin binding

Inferred from physical interaction PubMed 12821674. Source: BHF-UCL

phosphatidylinositol phospholipase C activity

Inferred from electronic annotation. Source: UniProtKB-EC

phospholipase C activity

Traceable author statement Ref.2. Source: ProtInc

signal transducer activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q01970-1)

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: Q01970-2)

The sequence of this isoform differs from the canonical sequence as follows:
     33-99: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.12
Chain2 – 123412331-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3
PRO_0000088491

Regions

Domain318 – 468151PI-PLC X-box
Domain590 – 706117PI-PLC Y-box
Domain713 – 81098C2
Region1231 – 12344Interaction with SHANK2 By similarity

Sites

Active site3321 By similarity
Active site3791 By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.12
Modified residue4741Phosphoserine Ref.11
Modified residue5371Phosphoserine Ref.9 Ref.11
Modified residue11051Phosphoserine Ref.11

Natural variations

Alternative sequence33 – 9967Missing in isoform 2.
VSP_046054
Natural variant4831R → H.
Corresponds to variant rs12146487 [ dbSNP | Ensembl ].
VAR_029229

Experimental info

Sequence conflict8451S → L in CAA78903. Ref.6
Sequence conflict8811G → E in CAA85776. Ref.2
Sequence conflict1089 – 111931REKKE…HKKEA → SWPSWPRSVRSSGRGSPRRS AGACWARCRRG in CAA85776. Ref.2

Secondary structure

........................................................................................................................................ 1234
Helix Strand Turn

Details...

Sequences

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

Last modified October 1, 1996. Version 2.
Checksum: C5106EFBA8037788

FASTA1,234138,799
        10         20         30         40         50         60 
MAGAQPGVHA LQLEPPTVVE TLRRGSKFIK WDEETSSRNL VTLRVDPNGF FLYWTGPNME 

        70         80         90        100        110        120 
VDTLDISSIR DTRTGRYARL PKDPKIREVL GFGGPDARLE EKLMTVVSGP DPVNTVFLNF 

       130        140        150        160        170        180 
MAVQDDTAKV WSEELFKLAM NILAQNASRN TFLRKAYTKL KLQVNQDGRI PVKNILKMFS 

       190        200        210        220        230        240 
ADKKRVETAL ESCGLKFNRS ESIRPDEFSL EIFERFLNKL CLRPDIDKIL LEIGAKGKPY 

       250        260        270        280        290        300 
LTLEQLMDFI NQKQRDPRLN EVLYPPLRPS QARLLIEKYE PNQQFLERDQ MSMEGFSRYL 

       310        320        330        340        350        360 
GGEENGILPL EALDLSTDMT QPLSAYFINS SHNTYLTAGQ LAGTSSVEMY RQALLWGCRC 

       370        380        390        400        410        420 
VELDVWKGRP PEEEPFITHG FTMTTEVPLR DVLEAIAETA FKTSPYPVIL SFENHVDSAK 

       430        440        450        460        470        480 
QQAKMAEYCR SIFGDALLIE PLDKYPLAPG VPLPSPQDLM GRILVKNKKR HRPSAGGPDS 

       490        500        510        520        530        540 
AGRKRPLEQS NSALSESSAA TEPSSPQLGS PSSDSCPGLS NGEEVGLEKP SLEPQKSLGD 

       550        560        570        580        590        600 
EGLNRGPYVL GPADREDEEE DEEEEEQTDP KKPTTDEGTA SSEVNATEEM STLVNYIEPV 

       610        620        630        640        650        660 
KFKSFEAARK RNKCFEMSSF VETKAMEQLT KSPMEFVEYN KQQLSRIYPK GTRVDSSNYM 

       670        680        690        700        710        720 
PQLFWNVGCQ LVALNFQTLD VAMQLNAGVF EYNGRSGYLL KPEFMRRPDK SFDPFTEVIV 

       730        740        750        760        770        780 
DGIVANALRV KVISGQFLSD RKVGIYVEVD MFGLPVDTRR KYRTRTSQGN SFNPVWDEEP 

       790        800        810        820        830        840 
FDFPKVVLPT LASLRIAAFE EGGKFVGHRI LPVSAIRSGY HYVCLRNEAN QPLCLPALLI 

       850        860        870        880        890        900 
YTEASDYIPD DHQDYAEALI NPIKHVSLMD QRARQLAALI GESEAQAGQE TCQDTQSQQL 

       910        920        930        940        950        960 
GSQPSSNPTP SPLDASPRRP PGPTTSPAST SLSSPGQRDD LIASILSEVA PTPLDELRGH 

       970        980        990       1000       1010       1020 
KALVKLRSRQ ERDLRELRKK HQRKAVTLTR RLLDGLAQAQ AEGRCRLRPG ALGGAADVED 

      1030       1040       1050       1060       1070       1080 
TKEGEDEAKR YQEFQNRQVQ SLLELREAQV DAEAQRRLEH LRQALQRLRE VVLDANTTQF 

      1090       1100       1110       1120       1130       1140 
KRLKEMNERE KKELQKILDR KRHNSISEAK MRDKHKKEAE LTEINRRHIT ESVNSIRRLE 

      1150       1160       1170       1180       1190       1200 
EAQKQRHDRL VAGQQQVLQQ LAEEEPKLLA QLAQECQEQR ARLPQEIRRS LLGEMPEGLG 

      1210       1220       1230 
DGPLVACASN GHAPGSSGHL SGADSESQEE NTQL 

« Hide

Isoform 2 [UniParc].

Checksum: 597C35D7C25D4773
Show »

FASTA1,167131,205

References

« Hide 'large scale' references
[1]"Structural organization and expression of the human phosphatidylinositol-specific phospholipase C beta-3 gene."
Mazuruk K., Schoen T.J., Chader G.J., Rodriguez I.R.
Biochem. Biophys. Res. Commun. 212:190-195(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Genomic organization and complete cDNA sequence of the human phosphoinositide-specific phospholipase C beta 3 gene (PLCB3)."
Lagercrantz J., Carson E., Phelan C., Grimmond S., Rosen A., Dare E., Nordenskjoeld M., Hayward N.K., Larsson C., Weber G.
Genomics 26:467-472(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [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 (JUL-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).
Tissue: Uterus.
[6]"Identification, purification and characterization of a novel phosphatidylinositol-specific phospholipase C, a third member of the beta subfamily."
Carozzi A.J., Kriz R.W., Webster C., Parker P.J.
Eur. J. Biochem. 210:521-529(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 184-1234 (ISOFORM 1/2).
[7]"NHERF2 specifically interacts with LPA2 receptor and defines the specificity and efficiency of receptor-mediated phospholipase C-beta3 activation."
Oh Y.-S., Jo N.W., Choi J.W., Kim H.S., Seo S.-W., Kang K.-O., Hwang J.-I., Heo K., Kim S.-H., Kim Y.-H., Kim I.-H., Kim J.H., Banno Y., Ryu S.H., Suh P.-G.
Mol. Cell. Biol. 24:5069-5079(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LPAR2.
[8]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"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-537, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"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].
[11]"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-474; SER-537 AND SER-1105, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U26425 Genomic DNA. Translation: AAA77683.1.
Z37544 expand/collapse EMBL AC list , Z37545, Z37546, Z37547, Z37548, Z37549, Z37550, Z37551, Z37552, Z37553, Z37554, Z37555, Z37556, Z37557, Z37558, Z37559, Z37560, Z37561, Z37562, Z37564, Z37565, Z37566, Z37567, Z37568, Z37569, Z37570, Z37571, Z37572, Z37573, Z37574 Genomic DNA. Translation: CAA85776.1.
AP001453 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW74230.1.
CH471076 Genomic DNA. Translation: EAW74231.1.
BC032659 mRNA. Translation: AAH32659.1. Different initiation.
BC142681 mRNA. Translation: AAI42682.1.
Z16411 mRNA. Translation: CAA78903.1.
PIRI38994.
S27002.
S52099.
RefSeqNP_000923.1. NM_000932.2.
NP_001171812.1. NM_001184883.1.
XP_005274109.1. XM_005274052.2.
UniGeneHs.523761.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3OHMX-ray2.70B10-886[»]
4GNKX-ray4.00B/D10-1234[»]
E934-1192[»]
ProteinModelPortalQ01970.
SMRQ01970. Positions 10-881, 934-1192.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111347. 9 interactions.
DIPDIP-41928N.
MINTMINT-4999151.
STRING9606.ENSP00000279230.

Chemistry

BindingDBQ01970.

PTM databases

PhosphoSiteQ01970.

Polymorphism databases

DMDM1730573.

Proteomic databases

PaxDbQ01970.
PRIDEQ01970.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000279230; ENSP00000279230; ENSG00000149782. [Q01970-1]
ENST00000325234; ENSP00000324660; ENSG00000149782. [Q01970-2]
ENST00000540288; ENSP00000443631; ENSG00000149782. [Q01970-1]
GeneID5331.
KEGGhsa:5331.
UCSCuc009ypg.2. human. [Q01970-1]
uc009yph.2. human.

Organism-specific databases

CTD5331.
GeneCardsGC11P064019.
HGNCHGNC:9056. PLCB3.
HPACAB009257.
HPA039279.
HPA043907.
MIM600230. gene.
neXtProtNX_Q01970.
PharmGKBPA33386.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG149692.
HOGENOMHOG000232046.
HOVERGENHBG053609.
InParanoidQ01970.
KOK05858.
OMAKEMNERE.
OrthoDBEOG7WDN1N.
PhylomeDBQ01970.
TreeFamTF313216.

Enzyme and pathway databases

BRENDA3.1.4.11. 2681.
ReactomeREACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_13685. Neuronal System.

Gene expression databases

BgeeQ01970.
CleanExHS_PLCB3.
GenevestigatorQ01970.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
2.30.29.30. 1 hit.
2.60.40.150. 1 hit.
3.20.20.190. 2 hits.
InterProIPR000008. C2_dom.
IPR011992. EF-hand-dom_pair.
IPR011993. PH_like_dom.
IPR001192. PI-PLC_fam.
IPR016280. PLC-beta.
IPR028390. PLC-beta3.
IPR014815. PLC-beta_C.
IPR009535. PLC-beta_CS.
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.
[Graphical view]
PANTHERPTHR10336. PTHR10336. 1 hit.
PTHR10336:SF11. PTHR10336:SF11. 1 hit.
PfamPF00168. C2. 1 hit.
PF06631. DUF1154. 1 hit.
PF09279. EF-hand_like. 1 hit.
PF00388. PI-PLC-X. 1 hit.
PF00387. PI-PLC-Y. 1 hit.
PF08703. PLC-beta_C. 1 hit.
[Graphical view]
PIRSFPIRSF000956. PLC-beta. 1 hit.
PRINTSPR00390. PHPHLIPASEC.
SMARTSM00239. C2. 1 hit.
SM00148. PLCXc. 1 hit.
SM00149. PLCYc. 1 hit.
[Graphical view]
SUPFAMSSF49562. SSF49562. 1 hit.
SSF51695. SSF51695. 2 hits.
PROSITEPS50004. C2. 1 hit.
PS50007. PIPLC_X_DOMAIN. 1 hit.
PS50008. PIPLC_Y_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiPLCB3.
GenomeRNAi5331.
NextBio20644.
PROQ01970.
SOURCESearch...

Entry information

Entry namePLCB3_HUMAN
AccessionPrimary (citable) accession number: Q01970
Secondary accession number(s): A5PKZ6, G5E960, Q8N1A4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 141 of the entry and version 2 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 11

Human chromosome 11: entries, gene names and cross-references to MIM