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Q9NQ66 (PLCB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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 beta-1

EC=3.1.4.11
Alternative name(s):
PLC-154
Phosphoinositide phospholipase C-beta-1
Phospholipase C-I
Short name=PLC-I
Phospholipase C-beta-1
Short name=PLC-beta-1
Gene names
Name:PLCB1
Synonyms:KIAA0581
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1216 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.

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 DGKQ. Ref.10

Subcellular location

Nucleus membrane By similarity. Cytoplasm By similarity. Note: Colocalizes with the adrenergic receptors, ADREN1A and ADREN1B, at the nuclear membrane of cardiac myocytes By similarity.

Involvement in disease

Epileptic encephalopathy, early infantile, 12 (EIEE12) [MIM:613722]: A form of epilepsy characterized by frequent tonic seizures or spasms beginning in infancy with a specific EEG finding of suppression-burst patterns, characterized by high-voltage bursts alternating with almost flat suppression phases. Patients may progress to West syndrome, which is characterized by tonic spasms with clustering, arrest of psychomotor development, and hypsarrhythmia on EEG.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11

Miscellaneous

The receptor-mediated activation of PLC-beta-1 is mediated by two G-protein alpha subunits, alpha-Q and alpha-11.

Sequence similarities

Contains 1 C2 domain.

Contains 1 PI-PLC X-box domain.

Contains 1 PI-PLC Y-box domain.

Sequence caution

The sequence BAA25507.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAB14641.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processLipid degradation
Lipid metabolism
   Cellular componentCytoplasm
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseEpilepsy
   LigandCalcium
   Molecular functionHydrolase
Transducer
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled acetylcholine receptor signaling pathway

Inferred from sequence or structural similarity. Source: BHF-UCL

G2/M transition of mitotic cell cycle

Inferred from sequence or structural similarity. Source: BHF-UCL

activation of meiosis involved in egg activation

Inferred from sequence or structural similarity. Source: BHF-UCL

cerebral cortex development

Inferred from sequence or structural similarity. Source: BHF-UCL

fat cell differentiation

Inferred from electronic annotation. Source: Ensembl

glutamate receptor signaling pathway

Inferred from sequence or structural similarity. Source: BHF-UCL

inositol phosphate metabolic process

Traceable author statement. Source: Reactome

insulin-like growth factor receptor signaling pathway

Inferred from sequence or structural similarity. Source: BHF-UCL

interleukin-1-mediated signaling pathway

Inferred from direct assay PubMed 8872139. Source: BHF-UCL

interleukin-12-mediated signaling pathway

Inferred from direct assay PubMed 11743656. Source: BHF-UCL

interleukin-15-mediated signaling pathway

Inferred from direct assay PubMed 11743656. Source: BHF-UCL

intracellular signal transduction

Inferred from electronic annotation. Source: InterPro

lipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

memory

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of monocyte extravasation

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: BHF-UCL

phosphatidylinositol metabolic process

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of CD24 biosynthetic process

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of G1/S transition of mitotic cell cycle

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of GTPase activity

Inferred from direct assay PubMed 1322796. Source: GOC

positive regulation of JNK cascade

Inferred from direct assay PubMed 9500449. Source: BHF-UCL

positive regulation of acrosome reaction

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of developmental growth

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of embryonic development

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of interleukin-12 production

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of myoblast differentiation

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of G-protein coupled receptor protein signaling pathway

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of fertilization

Inferred from sequence or structural similarity. Source: BHF-UCL

signal transduction

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

small molecule metabolic process

Traceable author statement. Source: Reactome

synaptic transmission

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay Ref.1. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19199708. Source: UniProt

nuclear chromatin

Inferred from sequence or structural similarity. Source: BHF-UCL

nuclear membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear speck

Inferred from direct assay Ref.10. Source: BHF-UCL

nucleus

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

   Molecular_functionGTPase activator activity

Inferred from direct assay PubMed 1322796. Source: BHF-UCL

calcium ion binding

Inferred from electronic annotation. Source: InterPro

calmodulin binding

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

enzyme binding

Inferred from physical interaction Ref.10. Source: UniProtKB

phosphatidylinositol phospholipase C activity

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

phosphatidylinositol-4,5-bisphosphate binding

Inferred from direct assay Ref.10. Source: BHF-UCL

protein homodimerization activity

Inferred from sequence or structural similarity. Source: BHF-UCL

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 A (identifier: Q9NQ66-1)

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 B (identifier: Q9NQ66-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1142-1216: LQVELEQEYQ...IPGKEFDTPL → GEGSSSFLSETCHEDPSVSPNFTPPNPQALKW

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 121612161-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1
PRO_0000088486

Regions

Domain316 – 467152PI-PLC X-box
Domain540 – 656117PI-PLC Y-box
Domain663 – 76199C2

Sites

Active site3311 By similarity
Active site3781 By similarity

Amino acid modifications

Modified residue8871Phosphoserine; by PKC By similarity

Natural variations

Alternative sequence1142 – 121675LQVEL…FDTPL → GEGSSSFLSETCHEDPSVSP NFTPPNPQALKW in isoform B.
VSP_004718
Natural variant8541E → K.
Corresponds to variant rs2076413 [ dbSNP | Ensembl ].
VAR_050541
Natural variant9071A → P in a breast cancer sample; somatic mutation. Ref.12
VAR_036547

Experimental info

Sequence conflict1 – 3434MAGAQ…KWDDD → MGSLQGIATKILIRILSDAL IRKETDLKS in AAF86613. Ref.2
Sequence conflict1891L → M in AAF86613. Ref.2
Sequence conflict2031P → L in AAF86613. Ref.2
Sequence conflict2161L → F in AAF86613. Ref.2
Sequence conflict2211P → L in AAF86613. Ref.2
Sequence conflict2661L → P in AAF86613. Ref.2
Sequence conflict3091P → T in AAF86613. Ref.2
Sequence conflict3201Q → R in AAF86613. Ref.2
Sequence conflict3521V → A in AAF86613. Ref.2
Sequence conflict3661K → R in AAF86613. Ref.2
Sequence conflict3931E → K in AAF86613. Ref.2
Sequence conflict9831P → S in CAB98143. Ref.1

Sequences

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

Last modified October 1, 2000. Version 1.
Checksum: 6F4263D1A50C6FD1

FASTA1,216138,567
        10         20         30         40         50         60 
MAGAQPGVHA LQLKPVCVSD SLKKGTKFVK WDDDSTIVTP IILRTDPQGF FFYWTDQNKE 

        70         80         90        100        110        120 
TELLDLSLVK DARCGRHAKA PKDPKLRELL DVGNIGRLEQ RMITVVYGPD LVNISHLNLV 

       130        140        150        160        170        180 
AFQEEVAKEW TNEVFSLATN LLAQNMSRDA FLEKAYTKLK LQVTPEGRIP LKNIYRLFSA 

       190        200        210        220        230        240 
DRKRVETALE ACSLPSSRND SIPQEDFTPE VYRVFLNNLC PRPEIDNIFS EFGAKSKPYL 

       250        260        270        280        290        300 
TVDQMMDFIN LKQRDPRLNE ILYPPLKQEQ VQVLIEKYEP NNSLARKGQI SVDGFMRYLS 

       310        320        330        340        350        360 
GEENGVVSPE KLDLNEDMSQ PLSHYFINSS HNTYLTAGQL AGNSSVEMYR QVLLSGCRCV 

       370        380        390        400        410        420 
ELDCWKGRTA EEEPVITHGF TMTTEISFKE VIEAIAECAF KTSPFPILLS FENHVDSPKQ 

       430        440        450        460        470        480 
QAKMAEYCRL IFGDALLMEP LEKYPLESGV PLPSPMDLMY KILVKNKKKS HKSSEGSGKK 

       490        500        510        520        530        540 
KLSEQASNTY SDSSSMFEPS SPGAGEADTE SDDDDDDDDC KKSSMDEGTA GSEAMATEEM 

       550        560        570        580        590        600 
SNLVNYIQPV KFESFEISKK RNKSFEMSSF VETKGLEQLT KSPVEFVEYN KMQLSRIYPK 

       610        620        630        640        650        660 
GTRVDSSNYM PQLFWNAGCQ MVALNFQTMD LAMQINMGMY EYNGKSGYRL KPEFMRRPDK 

       670        680        690        700        710        720 
HFDPFTEGIV DGIVANTLSV KIISGQFLSD KKVGTYVEVD MFGLPVDTRR KAFKTKTSQG 

       730        740        750        760        770        780 
NAVNPVWEEE PIVFKKVVLP TLACLRIAVY EEGGKFIGHR ILPVQAIRPG YHYICLRNER 

       790        800        810        820        830        840 
NQPLTLPAVF VYIEVKDYVP DTYADVIEAL SNPIRYVNLM EQRAKQLAAL TLEDEEEVKK 

       850        860        870        880        890        900 
EADPGETPSE APSEARTTPA ENGVNHTTTL TPKPPSQALH SQPAPGSVKA PAKTEDLIQS 

       910        920        930        940        950        960 
VLTEVEAQTI EELKQQKSFV KLQKKHYKEM KDLVKRHHKK TTDLIKEHTT KYNEIQNDYL 

       970        980        990       1000       1010       1020 
RRRAALEKSA KKDSKKKSEP SSPDHGSSTI EQDLAALDAE MTQKLIDLKD KQQQQLLNLR 

      1030       1040       1050       1060       1070       1080 
QEQYYSEKYQ KREHIKLLIQ KLTDVAEECQ NNQLKKLKEI CEKEKKELKK KMDKKRQEKI 

      1090       1100       1110       1120       1130       1140 
TEAKSKDKSQ MEEEKTEMIR SYIQEVVQYI KRLEEAQSKR QEKLVEKHKE IRQQILDEKP 

      1150       1160       1170       1180       1190       1200 
KLQVELEQEY QDKFKRLPLE ILEFVQEAMK GKISEDSNHG SAPLSLSSDP GKVNHKTPSS 

      1210 
EELGGDIPGK EFDTPL 

« Hide

Isoform B [UniParc].

Checksum: B9DA88251A5769FB
Show »

FASTA1,173133,703

References

« Hide 'large scale' references
[1]"Cloning and characterization of the human phosphoinositide-specific phospholipase C-beta 1 (PLCbeta1)."
Caricasole A., Sala C., Roncarati R., Formenti E., Terstappen G.C.
Biochim. Biophys. Acta 1517:63-72(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
Tissue: Brain.
[2]"Identification and chromosomal localisation by fluorescence in situ hybridisation of human gene of phosphoinositide-specific phospholipase C beta 1."
Peruzzi D., Calabrese G., Faenza I., Manzoli L., Matteucci A., Gianfrancesco F., Billi A.M., Stuppia L., Palka G., Cocco L.
Biochim. Biophys. Acta 1484:175-182(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
Tissue: Brain.
[3]"Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
Tissue: Brain.
[4]"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[5]"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].
[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] (ISOFORMS A AND B).
Tissue: Brain.
[8]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 261-1216 (ISOFORM B).
Tissue: Testis.
[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 417-1062 (ISOFORMS A AND B).
Tissue: Placenta.
[10]"Diacylglycerol kinase-theta is localized in the speckle domains of the nucleus."
Tabellini G., Bortul R., Santi S., Riccio M., Baldini G., Cappellini A., Billi A.M., Berezney R., Ruggeri A., Cocco L., Martelli A.M.
Exp. Cell Res. 287:143-154(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DGKQ.
[11]"Phospholipase C beta 1 deficiency is associated with early-onset epileptic encephalopathy."
Kurian M.A., Meyer E., Vassallo G., Morgan N.V., Prakash N., Pasha S., Hai N.A., Shuib S., Rahman F., Wassmer E., Cross J.H., O'Callaghan F.J., Osborne J.P., Scheffer I.E., Gissen P., Maher E.R.
Brain 133:2964-2970(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN EIEE12.
[12]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] PRO-907.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ278313 mRNA. Translation: CAB98142.1.
AJ278314 mRNA. Translation: CAB98143.1.
AY004175 mRNA. Translation: AAF86613.1.
AB011153 mRNA. Translation: BAA25507.3. Different initiation.
AL031683 expand/collapse EMBL AC list , AL034551, AL049593, AL049632, AL050315, AL050323 Genomic DNA. Translation: CAI43121.1.
AL031683 expand/collapse EMBL AC list , AL034551, AL050315, AL049632, AL050323 Genomic DNA. Translation: CAI43122.1.
AL034551 expand/collapse EMBL AC list , AL031683, AL049593, AL049632, AL050315, AL050323 Genomic DNA. Translation: CAI21973.1.
AL034551 expand/collapse EMBL AC list , AL031683, AL050315, AL049632, AL050323 Genomic DNA. Translation: CAI21974.1.
AL049593 expand/collapse EMBL AC list , AL031683, AL034551, AL049632, AL050315, AL050323 Genomic DNA. Translation: CAI22175.1.
AL049632 expand/collapse EMBL AC list , AL031683, AL034551, AL049593, AL050315, AL050323 Genomic DNA. Translation: CAI43151.1.
AL049632 expand/collapse EMBL AC list , AL031683, AL034551, AL050315, AL050323 Genomic DNA. Translation: CAI43152.1.
AL050315 expand/collapse EMBL AC list , AL031683, AL034551, AL049593, AL049632, AL050323 Genomic DNA. Translation: CAI42238.1.
AL050315 expand/collapse EMBL AC list , AL031683, AL034551, AL049632, AL050323 Genomic DNA. Translation: CAI42239.1.
AL050323 expand/collapse EMBL AC list , AL031683, AL034551, AL049593, AL049632, AL050315 Genomic DNA. Translation: CAI22830.1.
AL050323 expand/collapse EMBL AC list , AL031683, AL034551, AL050315, AL049632 Genomic DNA. Translation: CAI22831.1.
CH471133 Genomic DNA. Translation: EAX10372.1.
CH471133 Genomic DNA. Translation: EAX10373.1.
CH471133 Genomic DNA. Translation: EAX10374.1.
CH471133 Genomic DNA. Translation: EAX10376.1.
BC069420 mRNA. Translation: AAH69420.1.
BC117231 mRNA. Translation: AAI17232.1.
AL137267 mRNA. Translation: CAB70666.1.
AK023689 mRNA. Translation: BAB14641.1. Different initiation.
RefSeqNP_056007.1. NM_015192.3.
NP_877398.1. NM_182734.2.
UniGeneHs.431173.

3D structure databases

ProteinModelPortalQ9NQ66.
SMRQ9NQ66. Positions 11-830, 890-1170.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116841. 9 interactions.
IntActQ9NQ66. 1 interaction.
MINTMINT-5005654.

Chemistry

BindingDBQ9NQ66.
ChEMBLCHEMBL4034.

PTM databases

PhosphoSiteQ9NQ66.

Polymorphism databases

DMDM12643814.

Proteomic databases

PaxDbQ9NQ66.
PRIDEQ9NQ66.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000338037; ENSP00000338185; ENSG00000182621. [Q9NQ66-1]
ENST00000378637; ENSP00000367904; ENSG00000182621. [Q9NQ66-2]
ENST00000378641; ENSP00000367908; ENSG00000182621. [Q9NQ66-2]
GeneID23236.
KEGGhsa:23236.
UCSCuc002wna.4. human. [Q9NQ66-2]
uc002wnb.4. human. [Q9NQ66-1]

Organism-specific databases

CTD23236.
GeneCardsGC20P008061.
HGNCHGNC:15917. PLCB1.
HPACAB004275.
CAB005334.
MIM607120. gene.
613722. phenotype.
neXtProtNX_Q9NQ66.
Orphanet1934. Early infantile epileptic encephalopathy.
293181. Malignant migrating partial seizures of infancy.
PharmGKBPA33384.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG149692.
HOVERGENHBG053609.
InParanoidQ9NQ66.
KOK05858.
OMAMMDFINL.
OrthoDBEOG7WDN1N.
PhylomeDBQ9NQ66.
TreeFamTF313216.

Enzyme and pathway databases

BRENDA3.1.4.11. 2681.
ReactomeREACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_13685. Neuronal System.
SignaLinkQ9NQ66.

Gene expression databases

ArrayExpressQ9NQ66.
BgeeQ9NQ66.
GenevestigatorQ9NQ66.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
2.60.40.150. 1 hit.
3.20.20.190. 2 hits.
InterProIPR000008. C2_dom.
IPR011992. EF-hand-dom_pair.
IPR001192. PI-PLC_fam.
IPR016280. PLC-beta.
IPR028400. PLC-beta1.
IPR014815. PLC-beta_C.
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:SF12. PTHR10336:SF12. 1 hit.
PfamPF00168. C2. 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. 1 hit.
PROSITEPS50004. C2. 1 hit.
PS50007. PIPLC_X_DOMAIN. 1 hit.
PS50008. PIPLC_Y_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPLCB1. human.
GeneWikiPLCB1.
GenomeRNAi23236.
NextBio44882.
PROQ9NQ66.
SOURCESearch...

Entry information

Entry namePLCB1_HUMAN
AccessionPrimary (citable) accession number: Q9NQ66
Secondary accession number(s): D3DW12 expand/collapse secondary AC list , D3DW13, O60325, Q17RQ6, Q5TFF7, Q5TGC9, Q8IV93, Q9BQW2, Q9H4H2, Q9H8H5, Q9NQ65, Q9NQH9, Q9NTH4, Q9UJP6, Q9UM26
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: October 1, 2000
Last modified: April 16, 2014
This is version 147 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

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