Q9Z1B3 (PLCB1_MOUSE) 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-beta-1
Short name=PLC-beta-1

Gene names

Name:	Plcb1
Synonyms:	Plcb

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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 By similarity.
Catalytic activity	1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol.
Cofactor	Calcium By similarity.
Subunit structure	Interacts with DGKQ By similarity.
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.

Ontologies

Keywords
Biological process	Lipid degradation
Coding sequence diversity	Alternative splicing
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 direct assay. Source: BHF-UCL G-protein coupled acetylcholine receptor signaling pathway Inferred from mutant phenotype. Source: BHF-UCL G1 phase Inferred from direct assay. Source: BHF-UCL G2/M transition of mitotic cell cycle Inferred from direct assay. Source: BHF-UCL activation of meiosis involved in egg activation Inferred from direct assay. Source: BHF-UCL cell adhesion Inferred by curator. Source: BHF-UCL cerebral cortex development Inferred from mutant phenotype. Source: BHF-UCL erythrocyte differentiation Traceable author statement. Source: BHF-UCL fat cell differentiation Inferred from direct assay. Source: BHF-UCL glutamate signaling pathway Inferred from mutant phenotype. Source: BHF-UCL insulin receptor signaling pathway Traceable author statement. Source: BHF-UCL insulin-like growth factor receptor signaling pathway Inferred from direct assay. Source: BHF-UCL interleukin-12-mediated signaling pathway Inferred from sequence or structural similarity. Source: BHF-UCL interleukin-15-mediated signaling pathway Inferred from sequence or structural similarity. Source: BHF-UCL intracellular signal transduction Inferred from electronic annotation. Source: InterPro lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW mRNA processing Traceable author statement. Source: BHF-UCL macrophage differentiation Non-traceable author statement. Source: BHF-UCL memory Inferred from mutant phenotype. Source: BHF-UCL negative regulation of monocyte extravasation Inferred from direct assay. Source: BHF-UCL negative regulation of transcription, DNA-dependent Inferred from direct assay. Source: BHF-UCL oocyte maturation Non-traceable author statement. Source: BHF-UCL phosphatidylinositol metabolic process Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of JNK cascade Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of acrosome reaction Inferred from mutant phenotype. Source: BHF-UCL positive regulation of developmental growth Inferred from mutant phenotype. Source: BHF-UCL positive regulation of embryonic development Inferred from mutant phenotype. Source: BHF-UCL positive regulation of interleukin-12 production Inferred from mutant phenotype. Source: BHF-UCL positive regulation of myoblast differentiation Inferred from direct assay. Source: BHF-UCL positive regulation of sodium:hydrogen antiporter activity Non-traceable author statement. Source: BHF-UCL positive regulation of transcription, DNA-dependent Inferred from direct assay. Source: BHF-UCL regulation of G-protein coupled receptor protein signaling pathway Inferred from mutant phenotype. Source: BHF-UCL regulation of fertilization Inferred from mutant phenotype. Source: BHF-UCL
Cellular component	nuclear chromatin Inferred from direct assay. Source: BHF-UCL nuclear speck Inferred from direct assay. Source: BHF-UCL plasma membrane Traceable author statement. Source: Reactome
Molecular function	calmodulin binding Inferred from sequence or structural similarity. Source: BHF-UCL enzyme binding Inferred from sequence or structural similarity. Source: BHF-UCL lamin binding Inferred from physical interaction. Source: BHF-UCL phosphatidylinositol phospholipase C activity Inferred from direct assay. Source: BHF-UCL phosphatidylinositol-4,5-bisphosphate binding Inferred from sequence or structural similarity. 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 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform A (identifier: Q9Z1B3-1)

Also known as: C-beta-1a;

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: Q9Z1B3-2)

Also known as: C-beta-1b;

The sequence of this isoform differs from the canonical sequence as follows:
     1142-1216: LQTELEQEYQ...NPGREFDTPL → GEGPSSVLSEGCHEDPSVPPNFTPPNPQALKW

Isoform C (identifier: Q9Z1B3-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1199-1216: Missing.

Note: No experimental confirmation available.

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_0000088487
Regions
	Domain	316 – 467	152	PI-PLC X-box
	Domain	540 – 656	117	PI-PLC Y-box
	Domain	663 – 761	99	C2
	Compositional bias	914 – 1088	175	Lys-rich
Sites
	Active site	331	1	By similarity
	Active site	378	1	By similarity
Amino acid modifications
	Modified residue	333	1	Phosphothreonine Ref.7
	Modified residue	334	1	Phosphotyrosine Ref.7
	Modified residue	336	1	Phosphothreonine Ref.7
	Modified residue	569	1	Phosphoserine By similarity
	Modified residue	573	1	Phosphothreonine By similarity
	Modified residue	887	1	Phosphoserine; by PKC By similarity
	Modified residue	972	1	N6-acetyllysine By similarity
	Modified residue	976	1	N6-acetyllysine By similarity
	Modified residue	1197	1	Phosphoserine Ref.8
Natural variations
	Alternative sequence	1142 – 1216	75	LQTEL…FDTPL → GEGPSSVLSEGCHEDPSVPP NFTPPNPQALKW in isoform B.		VSP_008917
	Alternative sequence	1199 – 1216	18	Missing in isoform C.		VSP_008918
Experimental info
	Sequence conflict	28	1	F → L in AAD00571. Ref.1
	Sequence conflict	28	1	F → L in AAD00572. Ref.1
	Sequence conflict	28	1	F → L in AAD00573. Ref.1
	Sequence conflict	41	1	I → T in AAD00571. Ref.1
	Sequence conflict	41	1	I → T in AAD00572. Ref.1
	Sequence conflict	41	1	I → T in AAD00573. Ref.1
	Sequence conflict	67	1	S → T in AAD01749. Ref.5
	Sequence conflict	79	1	K → E in AAD00571. Ref.1
	Sequence conflict	79	1	K → E in AAD00572. Ref.1
	Sequence conflict	79	1	K → E in AAD00573. Ref.1
	Sequence conflict	112	1	V → A in AAD00571. Ref.1
	Sequence conflict	112	1	V → A in AAD00572. Ref.1
	Sequence conflict	112	1	V → A in AAD00573. Ref.1
	Sequence conflict	561	1	R → I in CAA64637. Ref.6
	Sequence conflict	613	1	L → I in CAA64637. Ref.6
	Sequence conflict	622	1	V → M in AAD00571. Ref.1
	Sequence conflict	622	1	V → M in AAD00572. Ref.1
	Sequence conflict	622	1	V → M in AAD00573. Ref.1
	Sequence conflict	714	1	K → T in AAD00571. Ref.1
	Sequence conflict	714	1	K → T in AAD00572. Ref.1
	Sequence conflict	714	1	K → T in AAD00573. Ref.1
	Sequence conflict	795	1	V → D in AAD00571. Ref.1
	Sequence conflict	795	1	V → D in AAD00572. Ref.1
	Sequence conflict	795	1	V → D in AAD00573. Ref.1
	Sequence conflict	923	1	Q → H in AAD00571. Ref.1
	Sequence conflict	923	1	Q → H in AAD00572. Ref.1
	Sequence conflict	923	1	Q → H in AAD00573. Ref.1
	Sequence conflict	957	1	N → I in AAD00571. Ref.1
	Sequence conflict	957	1	N → I in AAD00572. Ref.1
	Sequence conflict	957	1	N → I in AAD00573. Ref.1
	Sequence conflict	1084	1	K → T in AAD00571. Ref.1
	Sequence conflict	1084	1	K → T in AAD00572. Ref.1
	Sequence conflict	1084	1	K → T in AAD00573. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform A (C-beta-1a) [UniParc]. Last modified July 27, 2011. Version 2. Checksum: CC751D49895A47D0	FASTA	1,216	138,396
	10 20 30 40 50 60 MAGAQPGVHA LQLKPVCVSD SLKKGTKFVK WDDDSTIVTP IILRTDPQGF FFYWTDQNKE 70 80 90 100 110 120 TELLDLSLVK DARCGKHAKA PKDPKLRELL DVGNIGHLEQ RMITVVYGPD LVNISHLNLV 130 140 150 160 170 180 AFQEEVAKEW TNEVFSLATN LLAQNMSRDA FLEKAYTKLK LQVTPEGRIP LKNIYRLFSA 190 200 210 220 230 240 DRKRVETALE ACSLPSSRND SIPQEDFTPD VYRVFLNNLC PRPEIDNIFS EFGAKSKPYL 250 260 270 280 290 300 TVDQMMDFIN LKQRDPRLNE ILYPPLKQEQ VQVLIEKYEP NSSLAKKGQM 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 SDSSSVFEPS SPGAGEADTE SDDDDDDDDC KKSSMDEGTA GSEAMATEEM 550 560 570 580 590 600 SNLVNYIQPV KFESFEISKK RNKSFEMSSF VETKGLEQLT KSPVEFVEYN KMQLSRIYPK 610 620 630 640 650 660 GTRVDSSNYM PQLFWNAGCQ MVALNFQTVD LAMQINMGMY EYNGKSGYRL KPEFMRRPDK 670 680 690 700 710 720 HFDPFTEGIV DGIVANTLSV KIISGQFLSD KKVGTYVEVD MFGLPVDTRR KAFKTKTSQG 730 740 750 760 770 780 NAVNPVWEEE PIVFKKVVLP SLACLRIAAY EEGGKFIGHR ILPVQAIRPG YHYICLRNER 790 800 810 820 830 840 NQPLTLPAVF VYIEVKDYVP DTYADVIEAL SNPIRYVNLM EQRAKQLAAL TLEDEEEVKK 850 860 870 880 890 900 EADPGETSSE APSETRTTPA ENGVNHTASL APKPPSQAPH SQPAPGSVKA PAKTEDLIQS 910 920 930 940 950 960 VLTEVEAQTI EELKQQKSFV KLQKKHYKEM KDLVKRHHKK TTELIKEHTT KYNEIQNDYL 970 980 990 1000 1010 1020 RRRAALEKSA KKDSKKKSEP SSPDHGSSAI 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 QEKLVEKHNE IRQQILDEKP 1150 1160 1170 1180 1190 1200 KLQTELEQEY QDKFKRLPLE ILEFVQEAMK GKISEDSNHG SAPPSLASDA AKVNLKSPSS 1210 EEIERENPGR EFDTPL
	Isoform B (C-beta-1b) [UniParc]. Checksum: 5AA8EEB1FCED1D93	FASTA	1,173	133,327
	10 20 30 40 50 60 MAGAQPGVHA LQLKPVCVSD SLKKGTKFVK WDDDSTIVTP IILRTDPQGF FFYWTDQNKE 70 80 90 100 110 120 TELLDLSLVK DARCGKHAKA PKDPKLRELL DVGNIGHLEQ RMITVVYGPD LVNISHLNLV 130 140 150 160 170 180 AFQEEVAKEW TNEVFSLATN LLAQNMSRDA FLEKAYTKLK LQVTPEGRIP LKNIYRLFSA 190 200 210 220 230 240 DRKRVETALE ACSLPSSRND SIPQEDFTPD VYRVFLNNLC PRPEIDNIFS EFGAKSKPYL 250 260 270 280 290 300 TVDQMMDFIN LKQRDPRLNE ILYPPLKQEQ VQVLIEKYEP NSSLAKKGQM 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 SDSSSVFEPS SPGAGEADTE SDDDDDDDDC KKSSMDEGTA GSEAMATEEM 550 560 570 580 590 600 SNLVNYIQPV KFESFEISKK RNKSFEMSSF VETKGLEQLT KSPVEFVEYN KMQLSRIYPK 610 620 630 640 650 660 GTRVDSSNYM PQLFWNAGCQ MVALNFQTVD LAMQINMGMY EYNGKSGYRL KPEFMRRPDK 670 680 690 700 710 720 HFDPFTEGIV DGIVANTLSV KIISGQFLSD KKVGTYVEVD MFGLPVDTRR KAFKTKTSQG 730 740 750 760 770 780 NAVNPVWEEE PIVFKKVVLP SLACLRIAAY EEGGKFIGHR ILPVQAIRPG YHYICLRNER 790 800 810 820 830 840 NQPLTLPAVF VYIEVKDYVP DTYADVIEAL SNPIRYVNLM EQRAKQLAAL TLEDEEEVKK 850 860 870 880 890 900 EADPGETSSE APSETRTTPA ENGVNHTASL APKPPSQAPH SQPAPGSVKA PAKTEDLIQS 910 920 930 940 950 960 VLTEVEAQTI EELKQQKSFV KLQKKHYKEM KDLVKRHHKK TTELIKEHTT KYNEIQNDYL 970 980 990 1000 1010 1020 RRRAALEKSA KKDSKKKSEP SSPDHGSSAI 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 QEKLVEKHNE IRQQILDEKP 1150 1160 1170 KGEGPSSVLS EGCHEDPSVP PNFTPPNPQA LKW
	Isoform C [UniParc]. Checksum: E95E5F34E58C48CA	FASTA	1,198	136,309
	10 20 30 40 50 60 MAGAQPGVHA LQLKPVCVSD SLKKGTKFVK WDDDSTIVTP IILRTDPQGF FFYWTDQNKE 70 80 90 100 110 120 TELLDLSLVK DARCGKHAKA PKDPKLRELL DVGNIGHLEQ RMITVVYGPD LVNISHLNLV 130 140 150 160 170 180 AFQEEVAKEW TNEVFSLATN LLAQNMSRDA FLEKAYTKLK LQVTPEGRIP LKNIYRLFSA 190 200 210 220 230 240 DRKRVETALE ACSLPSSRND SIPQEDFTPD VYRVFLNNLC PRPEIDNIFS EFGAKSKPYL 250 260 270 280 290 300 TVDQMMDFIN LKQRDPRLNE ILYPPLKQEQ VQVLIEKYEP NSSLAKKGQM 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 SDSSSVFEPS SPGAGEADTE SDDDDDDDDC KKSSMDEGTA GSEAMATEEM 550 560 570 580 590 600 SNLVNYIQPV KFESFEISKK RNKSFEMSSF VETKGLEQLT KSPVEFVEYN KMQLSRIYPK 610 620 630 640 650 660 GTRVDSSNYM PQLFWNAGCQ MVALNFQTVD LAMQINMGMY EYNGKSGYRL KPEFMRRPDK 670 680 690 700 710 720 HFDPFTEGIV DGIVANTLSV KIISGQFLSD KKVGTYVEVD MFGLPVDTRR KAFKTKTSQG 730 740 750 760 770 780 NAVNPVWEEE PIVFKKVVLP SLACLRIAAY EEGGKFIGHR ILPVQAIRPG YHYICLRNER 790 800 810 820 830 840 NQPLTLPAVF VYIEVKDYVP DTYADVIEAL SNPIRYVNLM EQRAKQLAAL TLEDEEEVKK 850 860 870 880 890 900 EADPGETSSE APSETRTTPA ENGVNHTASL APKPPSQAPH SQPAPGSVKA PAKTEDLIQS 910 920 930 940 950 960 VLTEVEAQTI EELKQQKSFV KLQKKHYKEM KDLVKRHHKK TTELIKEHTT KYNEIQNDYL 970 980 990 1000 1010 1020 RRRAALEKSA KKDSKKKSEP SSPDHGSSAI 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 QEKLVEKHNE IRQQILDEKP 1150 1160 1170 1180 1190 KLQTELEQEY QDKFKRLPLE ILEFVQEAMK GKISEDSNHG SAPPSLASDA AKVNLKSP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of PI-specific phospholipase C's from 3T3 cells. Expression and membrane targeting of a novel phospholipase C-beta-1 isoform." Bai J., Wu K., Marks D.L., Machamer C., Pagano R.E. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B). Strain: Swiss.
[2]	"High-throughput sequence identification of gene coding variants within alcohol-related QTLs." Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J., Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M. Mamm. Genome 12:657-663(2001) [PubMed: 11471062] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C). Strain: ILS and ISS.
[3]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6.
[4]	"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] (ISOFORM A). Strain: C57BL/6. Tissue: Brain.
[5]	"Patterns of expression for the mRNA corresponding to the four isoforms of phospholipase Cbeta in mouse brain." Watanabe M., Nakamura M., Sato K., Kano M., Simon M.I., Inoue Y. Eur. J. Neurosci. 10:2016-2025(1998) [PubMed: 9753089] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 29-145. Strain: C57BL/6.
[6]	"Phospholipase C in mouse oocytes: characterization of beta and gamma isoforms and their possible involvement in sperm-induced Ca2+ spiking." Dupont G., McGuinness O.M., Johnson M.H., Berridge M.J., Borgese F. Biochem. J. 316:583-591(1996) [PubMed: 8687404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 428-615. Tissue: Oocyte.
[7]	"Proteomic analysis of in vivo phosphorylated synaptic proteins." Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I., Blackstock W.P., Choudhary J.S., Grant S.G. J. Biol. Chem. 280:5972-5982(2005) [PubMed: 15572359] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-333; TYR-334 AND THR-336, MASS SPECTROMETRY. Tissue: Forebrain.
[8]	"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed: 17114649] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1197, MASS SPECTROMETRY. Tissue: Brain cortex.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U85712 mRNA. Translation: AAD00571.1. U85713 mRNA. Translation: AAD00572.1. U85714 mRNA. Translation: AAD00573.1. AF498249 mRNA. Translation: AAM22966.1. AF498250 mRNA. Translation: AAM22967.1. AL928635 , AL840635, AL928956, AL935278 Genomic DNA. Translation: CAM23602.1. AL840635 , AL928635, AL928956, AL935278 Genomic DNA. Translation: CAM23766.1. AL928956 , AL840635, AL928635, AL935278 Genomic DNA. Translation: CAM26804.1. AL935278 , AL840635, AL928635, AL928956 Genomic DNA. Translation: CAM27130.1. BC058710 mRNA. Translation: AAH58710.1. AF022801 mRNA. Translation: AAD01749.1. X95344 mRNA. Translation: CAA64637.1.
IPI	IPI00130045. IPI00323250. IPI00468121.
PIR	S68256.
RefSeq	NP_001139302.1. NM_001145830.1. NP_062651.2. NM_019677.2.
UniGene	Mm.330607.
3D structure databases
ProteinModelPortal	Q9Z1B3.
SMR	Q9Z1B3. Positions 12-833.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9Z1B3. 3 interactions.
STRING	Q9Z1B3.
PTM databases
PhosphoSite	Q9Z1B3.
Proteomic databases
PRIDE	Q9Z1B3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000070724; ENSMUSP00000064844; ENSMUSG00000051177. ENSMUST00000110116; ENSMUSP00000105743; ENSMUSG00000051177.
GeneID	18795.
KEGG	mmu:18795.
Organism-specific databases
CTD	23236.
MGI	MGI:97613. Plcb1.
Phylogenomic databases
GeneTree	ENSGT00600000084213.
HOGENOM	HBG315986.
HOVERGEN	HBG053609.
InParanoid	Q9Z1B3.
OrthoDB	EOG40S0DW.
PhylomeDB	Q9Z1B3.
Enzyme and pathway databases
BRENDA	3.1.4.11. 3474.
Reactome	REACT_112621. Metabolism.
Gene expression databases
ArrayExpress	Q9Z1B3.
Bgee	Q9Z1B3.
CleanEx	MM_PLCB1.
Genevestigator	Q9Z1B3.
GermOnline	ENSMUSG00000051177. Mus musculus.
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	295080.
SOURCE	Search...

Entry information

Entry name

PLCB1_MOUSE

Accession

Primary (citable) accession number: Q9Z1B3
Secondary accession number(s): Q62075 , Q6PDH1, Q8K5A5, Q8K5A6, Q9Z0E5, Q9Z2T5

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 14, 2003
Last sequence update:	July 27, 2011
Last modified:	January 25, 2012
This is version 102 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program