Q9NQ66 (PLCB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

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	1216 AA.
Sequence status	Complete.
Protein existence	Evidence 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
Involvement in disease	Defects in PLCB1 are the cause of epileptic encephalopathy early infantile type 12 (EIEE12) [MIM:613722]. EIEE12 is 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. Ref.13
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 process	Lipid degradation
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Epilepsy
Ligand	Calcium
Molecular function	Hydrolase Transducer
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	CD24 biosynthetic process Inferred from sequence or structural similarity. Source: BHF-UCL G-protein coupled acetylcholine receptor signaling pathway Inferred from sequence or structural similarity. Source: BHF-UCL G1 phase 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 glutamate signaling pathway Inferred from sequence or structural similarity. Source: BHF-UCL 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. Source: BHF-UCL interleukin-12-mediated signaling pathway Inferred from direct assay. Source: BHF-UCL interleukin-15-mediated signaling pathway Inferred from direct assay. 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-dependent Inferred from sequence or structural similarity. Source: BHF-UCL phosphatidylinositol metabolic process Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of JNK cascade Inferred from direct assay. 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-dependent 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 synaptic transmission Traceable author statement. Source: Reactome
Cellular component	cytosol Traceable author statement. Source: Reactome nuclear chromatin Inferred from sequence or structural similarity. Source: BHF-UCL nuclear speck Inferred from direct assay Ref.10. Source: BHF-UCL
Molecular function	GTPase activator activity Inferred from direct assay. Source: BHF-UCL calmodulin binding Inferred from physical interaction. 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1216	1216	1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-1		PRO_0000088486
Regions
	Domain	316 – 467	152	PI-PLC X-box
	Domain	540 – 656	117	PI-PLC Y-box
	Domain	663 – 761	99	C2
Sites
	Active site	331	1	By similarity
	Active site	378	1	By similarity
Amino acid modifications
	Modified residue	333	1	Phosphothreonine By similarity
	Modified residue	334	1	Phosphotyrosine By similarity
	Modified residue	336	1	Phosphothreonine By similarity
	Modified residue	569	1	Phosphoserine Ref.12
	Modified residue	573	1	Phosphothreonine Ref.12
	Modified residue	887	1	Phosphoserine; by PKC By similarity
	Modified residue	972	1	N6-acetyllysine Ref.11
	Modified residue	976	1	N6-acetyllysine Ref.11
Natural variations
	Alternative sequence	1142 – 1216	75	LQVEL…FDTPL → GEGSSSFLSETCHEDPSVSP NFTPPNPQALKW in isoform B.		VSP_004718
	Natural variant	854	1	E → K. Corresponds to variant rs2076413 [ dbSNP | Ensembl ].		VAR_050541
	Natural variant	907	1	A → P in a breast cancer sample; somatic mutation. Ref.14		VAR_036547
Experimental info
	Sequence conflict	1 – 34	34	MAGAQ…KWDDD → MGSLQGIATKILIRILSDAL IRKETDLKS in AAF86613. Ref.2
	Sequence conflict	189	1	L → M in AAF86613. Ref.2
	Sequence conflict	203	1	P → L in AAF86613. Ref.2
	Sequence conflict	216	1	L → F in AAF86613. Ref.2
	Sequence conflict	221	1	P → L in AAF86613. Ref.2
	Sequence conflict	266	1	L → P in AAF86613. Ref.2
	Sequence conflict	309	1	P → T in AAF86613. Ref.2
	Sequence conflict	320	1	Q → R in AAF86613. Ref.2
	Sequence conflict	352	1	V → A in AAF86613. Ref.2
	Sequence conflict	366	1	K → R in AAF86613. Ref.2
	Sequence conflict	393	1	E → K in AAF86613. Ref.2
	Sequence conflict	983	1	P → S in CAB98143. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform A [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 6F4263D1A50C6FD1	FASTA	1,216	138,567
	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
	Isoform B [UniParc]. Checksum: B9DA88251A5769FB	FASTA	1,173	133,703
	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 KGEGSSSFLS ETCHEDPSVS PNFTPPNPQA LKW

References

	« Hide 'large scale' referencesShow '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: 11118617] [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: 10760467] [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: 9628581] [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: 12168954] [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. , 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].
[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. , 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: 15489334] [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: 17974005] [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. , 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: 14702039] [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: 12799190] [Abstract] Cited for: INTERACTION WITH DGKQ.
[11]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-972 AND LYS-976, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569 AND THR-573, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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: 20833646] [Abstract] Cited for: INVOLVEMENT IN EIEE12.
[14]	"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. , 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: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] PRO-907.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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 , AL034551, AL049593, AL049632, AL050315, AL050323 Genomic DNA. Translation: CAI43121.1. AL031683 , AL034551, AL050315, AL049632, AL050323 Genomic DNA. Translation: CAI43122.1. AL034551 , AL031683, AL049593, AL049632, AL050315, AL050323 Genomic DNA. Translation: CAI21973.1. AL034551 , AL031683, AL050315, AL049632, AL050323 Genomic DNA. Translation: CAI21974.1. AL049593 , AL031683, AL034551, AL049632, AL050315, AL050323 Genomic DNA. Translation: CAI22175.1. AL049632 , AL031683, AL034551, AL049593, AL050315, AL050323 Genomic DNA. Translation: CAI43151.1. AL049632 , AL031683, AL034551, AL050315, AL050323 Genomic DNA. Translation: CAI43152.1. AL050315 , AL031683, AL034551, AL049593, AL049632, AL050323 Genomic DNA. Translation: CAI42238.1. AL050315 , AL031683, AL034551, AL049632, AL050323 Genomic DNA. Translation: CAI42239.1. AL050323 , AL031683, AL034551, AL049593, AL049632, AL050315 Genomic DNA. Translation: CAI22830.1. AL050323 , 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.
IPI	IPI00219563. IPI00395561.
RefSeq	NP_056007.1. NM_015192.2. NP_877398.1. NM_182734.1.
UniGene	Hs.431173.
3D structure databases
ProteinModelPortal	Q9NQ66.
SMR	Q9NQ66. Positions 12-833.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9NQ66. 1 interaction.
STRING	Q9NQ66.
PTM databases
PhosphoSite	Q9NQ66.
Polymorphism databases
DMDM	12643814.
Proteomic databases
PRIDE	Q9NQ66.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000338037; ENSP00000338185; ENSG00000182621.
GeneID	23236.
KEGG	hsa:23236.
UCSC	uc002wna.1. human. uc002wnb.1. human.
Organism-specific databases
CTD	23236.
GeneCards	GC20P008061.
H-InvDB	HIX0015634.
HGNC	HGNC:15917. PLCB1.
HPA	CAB004275. CAB005334.
MIM	607120. gene. 613722. phenotype.
neXtProt	NX_Q9NQ66.
Orphanet	1934. Early infantile epileptic encephalopathy.
PharmGKB	PA33384.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG05575.
GeneTree	ENSGT00600000084213.
HOVERGEN	HBG053609.
InParanoid	Q9NQ66.
OMA	YEYNGKS.
PhylomeDB	Q9NQ66.
Enzyme and pathway databases
BRENDA	3.1.4.11. 2681.
Pathway_Interaction_DB	endothelinpathway. Endothelins. er_nongenomic_pathway. Plasma membrane estrogen receptor signaling.
Reactome	REACT_111102. Signal Transduction. REACT_111217. Metabolism. REACT_13685. Neuronal System.
Gene expression databases
ArrayExpress	Q9NQ66.
Bgee	Q9NQ66.
Genevestigator	Q9NQ66.
Family and domain databases
InterPro	IPR000008. C2_Ca-dep. IPR008973. C2_Ca/lipid-bd_dom_CaLB. IPR018029. C2_membr_targeting. IPR011992. EF-hand-like_dom. IPR001192. Pinositol_PLipase_C. IPR016280. PLC-beta. 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]
Gene3D	G3DSA:1.10.238.10. EF-Hand_type. 1 hit. G3DSA:3.20.20.190. PLC-like_Pdiesterase_TIM-brl. 2 hits.
KO	K05858.
Pfam	PF00168. C2. 1 hit. PF06631. DUF1154. 1 hit. PF09279. efhand_like. 1 hit. PF00388. PI-PLC-X. 1 hit. PF00387. PI-PLC-Y. 1 hit. PF08703. PLC-beta_C. 1 hit. [Graphical view]
PIRSF	PIRSF000956. PLC-beta. 1 hit.
PRINTS	PR00390. PHPHLIPASEC.
SMART	SM00239. C2. 1 hit. SM00148. PLCXc. 1 hit. SM00149. PLCYc. 1 hit. [Graphical view]
SUPFAM	SSF49562. C2_CaLB. 1 hit. SSF51695. PLC-like_Pdiesterase_TIM-brl. 1 hit.
PROSITE	PS50004. C2. 1 hit. PS50007. PIPLC_X_DOMAIN. 1 hit. PS50008. PIPLC_Y_DOMAIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	44882.
SOURCE	Search...

Entry information

Entry name

PLCB1_HUMAN

Accession

Primary (citable) accession number: Q9NQ66
Secondary accession number(s): D3DW12 , 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:	January 25, 2012
This is version 123 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.