Reviewed,
UniProtKB/Swiss-Prot Q9NQ66 (PLCB1_HUMAN)
Last modified
February 9, 2010.
Version 103.
History...
Clusters with 100%,
90%,
50% identity |
Documents (5) |
Third-party data |
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Names and origin
| Protein names | Recommended name: 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-1 EC=3.1.4.11 Alternative name(s): Phosphoinositide phospholipase C-beta-1 Phospholipase C-beta-1 Short name=PLC-beta-1 Phospholipase C-I Short name=PLC-I PLC-154 | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) [Complete proteome] | ||||
| 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 |
| 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 Polymorphism |
| Ligand | Calcium |
| Molecular function | Hydrolase Transducer |
| PTM | Acetylation Phosphoprotein |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | intracellular signaling cascade Inferred from electronic annotation. Source: InterPro lipid catabolic processInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytosol Ref.1 Inferred from Experiment. Source: Reactome nucleus Ref.2Non-traceable author statement. Source: UniProtKB |
| Molecular function | calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW enzyme binding Ref.10Inferred from physical interaction. Source: UniProtKB phosphoinositide phospholipase C activity Ref.1Non-traceable author statement. Source: UniProtKB signal transducer activityInferred 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: dbSNP rs2076413. | VAR_050541 | |||||
| Natural variant | 907 | 1 | A → P in a breast cancer sample; somatic mutation. Ref.13 | VAR_036547 | |||||
Experimental info | |||||||||
| Sequence conflict | 1 – 34 | 34 | MAGAQ…KWDDD → MGSLQGIATKILIRILSDAL IRKETDLKS Ref.2 | ||||||
| Sequence conflict | 189 | 1 | L → M Ref.2 | ||||||
| Sequence conflict | 203 | 1 | P → L Ref.2 | ||||||
| Sequence conflict | 216 | 1 | L → F Ref.2 | ||||||
| Sequence conflict | 221 | 1 | P → L Ref.2 | ||||||
| Sequence conflict | 266 | 1 | L → P Ref.2 | ||||||
| Sequence conflict | 309 | 1 | P → T Ref.2 | ||||||
| Sequence conflict | 320 | 1 | Q → R Ref.2 | ||||||
| Sequence conflict | 352 | 1 | V → A Ref.2 | ||||||
| Sequence conflict | 366 | 1 | K → R Ref.2 | ||||||
| Sequence conflict | 393 | 1 | E → K Ref.2 | ||||||
| Sequence conflict | 983 | 1 | P → S in CAB98143. Ref.1 | ||||||
Sequences
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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: 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. 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. 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. 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: Epithelium. |
| [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: Epithelium. |
| [13] | "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. Velculescu V.E.Science 314:268-274(2006) [PubMed: 16959974] [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 AL050323 Genomic DNA. Translation: CAI43121.1. AL031683 AL050323 Genomic DNA. Translation: CAI43122.1. AL034551 AL050323 Genomic DNA. Translation: CAI21973.1. AL034551 AL050323 Genomic DNA. Translation: CAI21974.1. AL049593 AL050323 Genomic DNA. Translation: CAI22175.1. AL049632 AL050323 Genomic DNA. Translation: CAI43151.1. AL049632 AL050323 Genomic DNA. Translation: CAI43152.1. AL050315 AL050323 Genomic DNA. Translation: CAI42238.1. AL050315 AL050323 Genomic DNA. Translation: CAI42239.1. AL050323 AL050315 Genomic DNA. Translation: CAI22830.1. AL050323 AL049632 Genomic DNA. Translation: CAI22831.1. CH471133 Genomic DNA. Translation: EAX10374.1. 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. NP_877398.1. |
| UniGene | Hs.431173 |
3D structure databases | |
| SMR | Q9NQ66. Positions 18-797, 900-1171. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q9NQ66. |
PTM databases | |
| PhosphoSite | Q9NQ66. |
Proteomic databases | |
| PRIDE | Q9NQ66. |
Genome annotation databases | |
| Ensembl | ENST00000338037; ENSP00000338185; ENSG00000182621; Homo sapiens. [Genome view] |
| 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. |
| PharmGKB | PA33384. |
| HUGE | Search... |
| GenAtlas | Search... |
Phylogenomic databases | |
| eggNOG | prNOG05575. |
| HOVERGEN | Q9NQ66. |
| InParanoid | Q9NQ66. |
| OMA | YEYNGKS. |
| PhylomeDB | Q9NQ66. |
Enzyme and pathway databases | |
| BRENDA | 3.1.4.11. 247. |
| Pathway_Interaction_DB | endothelinpathway. Endothelins. er_nongenomic_pathway. Plasma membrane estrogen receptor signaling. |
| Reactome | REACT_14797. Signaling by GPCR. REACT_15295. Opioid Signalling. REACT_15380. Diabetes pathways. |
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. IPR015359. Phospholipase_C_EF-hand-like. IPR001192. Phospholipase_C_Pinositol-sp_C. IPR001711. Phospholipase_C_Pinositol-sp_Y. IPR016280. PLC-beta. IPR017946. PLC-like_Pdiesterase_TIM-brl. IPR000909. PLipase_C_PInositol-sp_X_dom. [Graphical view] |
| Gene3D | G3DSA:1.10.238.10. EF-Hand_type. 1 hit. G3DSA:3.20.20.190. PLC-like_Pdiesterase_TIM-brl. 1 hit. |
| Pfam | PF09279. efhand_like. 1 hit. PF00388. PI-PLC-X. 1 hit. PF00387. PI-PLC-Y. 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] |
| PROSITE | PS50004. C2. 1 hit. PS50007. PIPLC_X_DOMAIN. 1 hit. PS50008. PIPLC_Y_DOMAIN. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 44882. |
| SOURCE | Search... |
Entry information
| Entry name | PLCB1_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q9NQ66 Secondary accession number(s): O60325 Q9UM26 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
| 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. | ||||||||
Relevant documents
| Human chromosome 20 Human chromosome 20: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with


