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Q00722

- PLCB2_HUMAN

UniProt

Q00722 - PLCB2_HUMAN

Protein

1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2

Gene

PLCB2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 2 (25 Nov 2008)
      Previous versions | rss
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    Functioni

    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 activityi

    1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol.

    Cofactori

    Binds 1 calcium ion per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei327 – 3271PROSITE-ProRule annotation
    Metal bindingi328 – 3281Calcium
    Metal bindingi357 – 3571Calcium
    Metal bindingi359 – 3591Calcium
    Active sitei374 – 3741PROSITE-ProRule annotation
    Metal bindingi408 – 4081Calcium

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. phosphatidylinositol phospholipase C activity Source: ProtInc
    3. phospholipase C activity Source: ProtInc
    4. signal transducer activity Source: UniProtKB-KW

    GO - Biological processi

    1. activation of phospholipase C activity Source: ProtInc
    2. inositol phosphate metabolic process Source: Reactome
    3. intracellular signal transduction Source: InterPro
    4. lipid catabolic process Source: UniProtKB-KW
    5. phospholipid metabolic process Source: ProtInc
    6. sensory perception of bitter taste Source: Ensembl
    7. small molecule metabolic process Source: Reactome
    8. synaptic transmission Source: Reactome

    Keywords - Molecular functioni

    Hydrolase, Transducer

    Keywords - Biological processi

    Lipid degradation, Lipid metabolism

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS06408-MONOMER.
    BRENDAi3.1.4.11. 2681.
    ReactomeiREACT_150312. Synthesis of IP3 and IP4 in the cytosol.
    REACT_15426. PLC beta mediated events.
    REACT_172761. Ca2+ pathway.
    REACT_18283. G alpha (q) signalling events.
    REACT_18405. Acetylcholine regulates insulin secretion.
    REACT_19145. G beta:gamma signalling through PLC beta.
    REACT_19193. Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion.
    REACT_21254. Presynaptic function of Kainate receptors.
    SignaLinkiQ00722.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2 (EC:3.1.4.11)
    Alternative name(s):
    Phosphoinositide phospholipase C-beta-2
    Phospholipase C-beta-2
    Short name:
    PLC-beta-2
    Gene namesi
    Name:PLCB2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:9055. PLCB2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi52 – 521Q → A: Strongly reduces interaction with RAC1. 1 Publication

    Organism-specific databases

    PharmGKBiPA33385.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 118511851-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2PRO_0000088489Add
    BLAST

    Proteomic databases

    MaxQBiQ00722.
    PaxDbiQ00722.
    PRIDEiQ00722.

    PTM databases

    PhosphoSiteiQ00722.

    Expressioni

    Gene expression databases

    ArrayExpressiQ00722.
    BgeeiQ00722.
    CleanExiHS_PLCB2.
    GenevestigatoriQ00722.

    Organism-specific databases

    HPAiCAB009443.

    Interactioni

    Subunit structurei

    Interacts with RAC1.

    Protein-protein interaction databases

    BioGridi111346. 12 interactions.
    DIPiDIP-29259N.
    MINTiMINT-1726830.
    STRINGi9606.ENSP00000260402.

    Structurei

    Secondary structure

    1
    1185
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi15 – 195
    Beta strandi21 – 3111
    Beta strandi33 – 408
    Beta strandi46 – 516
    Beta strandi56 – 605
    Helixi61 – 633
    Beta strandi64 – 696
    Helixi70 – 723
    Helixi79 – 846
    Turni85 – 884
    Helixi94 – 963
    Beta strandi98 – 1036
    Beta strandi105 – 1095
    Beta strandi111 – 12111
    Helixi122 – 13413
    Helixi137 – 1404
    Helixi144 – 15714
    Helixi167 – 1737
    Helixi178 – 18710
    Beta strandi193 – 1953
    Helixi200 – 2023
    Helixi207 – 2159
    Helixi219 – 2268
    Helixi238 – 24710
    Helixi269 – 2746
    Helixi288 – 2969
    Helixi305 – 3084
    Helixi318 – 3203
    Beta strandi321 – 3233
    Beta strandi325 – 3284
    Beta strandi331 – 3333
    Beta strandi335 – 3384
    Helixi343 – 3508
    Beta strandi355 – 3617
    Turni365 – 3684
    Helixi384 – 39411
    Turni395 – 3973
    Beta strandi403 – 4097
    Helixi414 – 42815
    Helixi429 – 4313
    Turni451 – 4566
    Beta strandi458 – 4614
    Turni523 – 53311
    Helixi534 – 5374
    Helixi544 – 5474
    Helixi561 – 5677
    Beta strandi572 – 5776
    Helixi578 – 59821
    Beta strandi599 – 6046
    Helixi618 – 6225
    Helixi637 – 6459
    Turni646 – 6483
    Helixi649 – 6513
    Beta strandi653 – 6564
    Helixi659 – 6613
    Beta strandi683 – 69311
    Beta strandi701 – 7088
    Beta strandi724 – 7263
    Beta strandi738 – 7403
    Helixi746 – 7483
    Beta strandi750 – 7578
    Turni758 – 7603
    Beta strandi761 – 7699
    Helixi770 – 7723
    Beta strandi776 – 7838
    Beta strandi789 – 80214

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2FJUX-ray2.20B1-803[»]
    2ZKMX-ray1.62X1-799[»]
    ProteinModelPortaliQ00722.
    SMRiQ00722. Positions 11-803, 883-1151.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ00722.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini312 – 463152PI-PLC X-boxPROSITE-ProRule annotationAdd
    BLAST
    Domaini546 – 662117PI-PLC Y-boxPROSITE-ProRule annotationAdd
    BLAST
    Domaini669 – 76799C2PROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili988 – 1147160Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi500 – 54546Glu-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 C2 domain.PROSITE-ProRule annotation
    Contains 1 PI-PLC X-box domain.PROSITE-ProRule annotation
    Contains 1 PI-PLC Y-box domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG149692.
    HOGENOMiHOG000232046.
    HOVERGENiHBG053609.
    InParanoidiQ00722.
    KOiK05858.
    OMAiFIKWDDE.
    OrthoDBiEOG7WDN1N.
    PhylomeDBiQ00722.
    TreeFamiTF313216.

    Family and domain databases

    Gene3Di1.10.238.10. 1 hit.
    2.60.40.150. 1 hit.
    3.20.20.190. 2 hits.
    InterProiIPR000008. C2_dom.
    IPR011992. EF-hand-dom_pair.
    IPR001192. PI-PLC_fam.
    IPR016280. PLC-beta.
    IPR028403. PLC-beta2.
    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]
    PANTHERiPTHR10336. PTHR10336. 1 hit.
    PTHR10336:SF10. PTHR10336:SF10. 1 hit.
    PfamiPF00168. 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]
    PIRSFiPIRSF000956. PLC-beta. 1 hit.
    PRINTSiPR00390. PHPHLIPASEC.
    SMARTiSM00239. C2. 1 hit.
    SM00148. PLCXc. 1 hit.
    SM00149. PLCYc. 1 hit.
    [Graphical view]
    SUPFAMiSSF49562. SSF49562. 1 hit.
    SSF51695. SSF51695. 1 hit.
    PROSITEiPS50004. C2. 1 hit.
    PS50007. PIPLC_X_DOMAIN. 1 hit.
    PS50008. PIPLC_Y_DOMAIN. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q00722-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MSLLNPVLLP PKVKAYLSQG ERFIKWDDET TVASPVILRV DPKGYYLYWT     50
    YQSKEMEFLD ITSIRDTRFG KFAKMPKSQK LRDVFNMDFP DNSFLLKTLT 100
    VVSGPDMVDL TFHNFVSYKE NVGKAWAEDV LALVKHPLTA NASRSTFLDK 150
    ILVKLKMQLN SEGKIPVKNF FQMFPADRKR VEAALSACHL PKGKNDAINP 200
    EDFPEPVYKS FLMSLCPRPE IDEIFTSYHA KAKPYMTKEH LTKFINQKQR 250
    DSRLNSLLFP PARPDQVQGL IDKYEPSGIN AQRGQLSPEG MVWFLCGPEN 300
    SVLAQDKLLL HHDMTQPLNH YFINSSHNTY LTAGQFSGLS SAEMYRQVLL 350
    SGCRCVELDC WKGKPPDEEP IITHGFTMTT DIFFKEAIEA IAESAFKTSP 400
    YPIILSFENH VDSPRQQAKM AEYCRTIFGD MLLTEPLEKF PLKPGVPLPS 450
    PEDLRGKILI KNKKNQFSGP TSSSKDTGGE AEGSSPPSAP AGEGTVWAGE 500
    EGTELEEEEV EEEEEEESGN LDEEEIKKMQ SDEGTAGLEV TAYEEMSSLV 550
    NYIQPTKFVS FEFSAQKNRS YVISSFTELK AYDLLSKASV QFVDYNKRQM 600
    SRIYPKGTRM DSSNYMPQMF WNAGCQMVAL NFQTMDLPMQ QNMAVFEFNG 650
    QSGYLLKHEF MRRPDKQFNP FSVDRIDVVV ATTLSITVIS GQFLSERSVR 700
    TYVEVELFGL PGDPKRRYRT KLSPSTNSIN PVWKEEPFVF EKILMPELAS 750
    LRVAVMEEGN KFLGHRIIPI NALNSGYHHL CLHSESNMPL TMPALFIFLE 800
    MKDYIPGAWA DLTVALANPI KFFSAHDTKS VKLKEAMGGL PEKPFPLASP 850
    VASQVNGALA PTSNGSPAAR AGAREEAMKE AAEPRTASLE ELRELKGVVK 900
    LQRRHEKELR ELERRGARRW EELLQRGAAQ LAELGPPGVG GVGACKLGPG 950
    KGSRKKRSLP REESAGAAPG EGPEGVDGRV RELKDRLELE LLRQGEEQYE 1000
    CVLKRKEQHV AEQISKMMEL AREKQAAELK ALKETSENDT KEMKKKLETK 1050
    RLERIQGMTK VTTDKMAQER LKREINNSHI QEVVQVIKQM TENLERHQEK 1100
    LEEKQAACLE QIREMEKQFQ KEALAEYEAR MKGLEAEVKE SVRACLRTCF 1150
    PSEAKDKPER ACECPPELCE QDPLIAKADA QESRL 1185
    Length:1,185
    Mass (Da):134,024
    Last modified:November 25, 2008 - v2
    Checksum:iA0397309D943672A
    GO
    Isoform 2 (identifier: Q00722-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         492-495: Missing.

    Show »
    Length:1,181
    Mass (Da):133,680
    Checksum:i7A6889F204D17FA4
    GO
    Isoform 3 (identifier: Q00722-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         868-882: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,170
    Mass (Da):132,511
    Checksum:iBC9DC96247E5762D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti119 – 1191K → R in BAF84346. (PubMed:14702039)Curated
    Sequence conflicti1060 – 10601K → R in BAF84346. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti324 – 3241N → I.
    Corresponds to variant rs45628633 [ dbSNP | Ensembl ].
    VAR_047509
    Natural varianti598 – 5981R → H.
    Corresponds to variant rs8025153 [ dbSNP | Ensembl ].
    VAR_047510
    Natural varianti664 – 6641P → L.
    Corresponds to variant rs9972332 [ dbSNP | Ensembl ].
    VAR_047511
    Natural varianti712 – 7121G → R.
    Corresponds to variant rs28395835 [ dbSNP | Ensembl ].
    VAR_047512
    Natural varianti1095 – 10951E → G.1 Publication
    Corresponds to variant rs936212 [ dbSNP | Ensembl ].
    VAR_047513

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei492 – 4954Missing in isoform 2. 1 PublicationVSP_035770
    Alternative sequencei868 – 88215Missing in isoform 3. 1 PublicationVSP_054490Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M95678 mRNA. Translation: AAA36453.1.
    AK291657 mRNA. Translation: BAF84346.1.
    AC020658 Genomic DNA. No translation available.
    BC136467 mRNA. Translation: AAI36468.1.
    CCDSiCCDS42020.1. [Q00722-1]
    CCDS61591.1. [Q00722-3]
    CCDS61592.1. [Q00722-2]
    PIRiA43346.
    RefSeqiNP_001271226.1. NM_001284297.1. [Q00722-2]
    NP_001271227.1. NM_001284298.1. [Q00722-3]
    NP_004564.2. NM_004573.2. [Q00722-1]
    UniGeneiHs.355888.

    Genome annotation databases

    EnsembliENST00000260402; ENSP00000260402; ENSG00000137841. [Q00722-1]
    ENST00000456256; ENSP00000411991; ENSG00000137841. [Q00722-3]
    ENST00000557821; ENSP00000453975; ENSG00000137841. [Q00722-2]
    GeneIDi5330.
    KEGGihsa:5330.
    UCSCiuc001zld.3. human. [Q00722-1]
    uc010bbo.3. human. [Q00722-2]

    Polymorphism databases

    DMDMi215273902.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M95678 mRNA. Translation: AAA36453.1 .
    AK291657 mRNA. Translation: BAF84346.1 .
    AC020658 Genomic DNA. No translation available.
    BC136467 mRNA. Translation: AAI36468.1 .
    CCDSi CCDS42020.1. [Q00722-1 ]
    CCDS61591.1. [Q00722-3 ]
    CCDS61592.1. [Q00722-2 ]
    PIRi A43346.
    RefSeqi NP_001271226.1. NM_001284297.1. [Q00722-2 ]
    NP_001271227.1. NM_001284298.1. [Q00722-3 ]
    NP_004564.2. NM_004573.2. [Q00722-1 ]
    UniGenei Hs.355888.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2FJU X-ray 2.20 B 1-803 [» ]
    2ZKM X-ray 1.62 X 1-799 [» ]
    ProteinModelPortali Q00722.
    SMRi Q00722. Positions 11-803, 883-1151.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111346. 12 interactions.
    DIPi DIP-29259N.
    MINTi MINT-1726830.
    STRINGi 9606.ENSP00000260402.

    PTM databases

    PhosphoSitei Q00722.

    Polymorphism databases

    DMDMi 215273902.

    Proteomic databases

    MaxQBi Q00722.
    PaxDbi Q00722.
    PRIDEi Q00722.

    Protocols and materials databases

    DNASUi 5330.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000260402 ; ENSP00000260402 ; ENSG00000137841 . [Q00722-1 ]
    ENST00000456256 ; ENSP00000411991 ; ENSG00000137841 . [Q00722-3 ]
    ENST00000557821 ; ENSP00000453975 ; ENSG00000137841 . [Q00722-2 ]
    GeneIDi 5330.
    KEGGi hsa:5330.
    UCSCi uc001zld.3. human. [Q00722-1 ]
    uc010bbo.3. human. [Q00722-2 ]

    Organism-specific databases

    CTDi 5330.
    GeneCardsi GC15M040580.
    H-InvDB HIX0012125.
    HGNCi HGNC:9055. PLCB2.
    HPAi CAB009443.
    MIMi 604114. gene.
    neXtProti NX_Q00722.
    PharmGKBi PA33385.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG149692.
    HOGENOMi HOG000232046.
    HOVERGENi HBG053609.
    InParanoidi Q00722.
    KOi K05858.
    OMAi FIKWDDE.
    OrthoDBi EOG7WDN1N.
    PhylomeDBi Q00722.
    TreeFami TF313216.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS06408-MONOMER.
    BRENDAi 3.1.4.11. 2681.
    Reactomei REACT_150312. Synthesis of IP3 and IP4 in the cytosol.
    REACT_15426. PLC beta mediated events.
    REACT_172761. Ca2+ pathway.
    REACT_18283. G alpha (q) signalling events.
    REACT_18405. Acetylcholine regulates insulin secretion.
    REACT_19145. G beta:gamma signalling through PLC beta.
    REACT_19193. Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion.
    REACT_21254. Presynaptic function of Kainate receptors.
    SignaLinki Q00722.

    Miscellaneous databases

    ChiTaRSi PLCB2. human.
    EvolutionaryTracei Q00722.
    GeneWikii PLCB2.
    GenomeRNAii 5330.
    NextBioi 20640.
    PROi Q00722.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q00722.
    Bgeei Q00722.
    CleanExi HS_PLCB2.
    Genevestigatori Q00722.

    Family and domain databases

    Gene3Di 1.10.238.10. 1 hit.
    2.60.40.150. 1 hit.
    3.20.20.190. 2 hits.
    InterProi IPR000008. C2_dom.
    IPR011992. EF-hand-dom_pair.
    IPR001192. PI-PLC_fam.
    IPR016280. PLC-beta.
    IPR028403. PLC-beta2.
    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 ]
    PANTHERi PTHR10336. PTHR10336. 1 hit.
    PTHR10336:SF10. PTHR10336:SF10. 1 hit.
    Pfami PF00168. 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 ]
    PIRSFi PIRSF000956. PLC-beta. 1 hit.
    PRINTSi PR00390. PHPHLIPASEC.
    SMARTi SM00239. C2. 1 hit.
    SM00148. PLCXc. 1 hit.
    SM00149. PLCYc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49562. SSF49562. 1 hit.
    SSF51695. SSF51695. 1 hit.
    PROSITEi PS50004. C2. 1 hit.
    PS50007. PIPLC_X_DOMAIN. 1 hit.
    PS50008. PIPLC_Y_DOMAIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, sequencing, expression, and Gq-independent activation of phospholipase C-beta 2."
      Park D., Jhon D.-Y., Kriz R., Knopf J., Rhee S.G.
      J. Biol. Chem. 267:16048-16055(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    2. "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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT GLY-1095.
      Tissue: Placenta.
    3. "Analysis of the DNA sequence and duplication history of human chromosome 15."
      Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
      , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
      Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Testis.
    5. "Crystal structure of Rac1 bound to its effector phospholipase C-beta2."
      Jezyk M.R., Snyder J.T., Gershberg S., Worthylake D.K., Harden T.K., Sondek J.
      Nat. Struct. Mol. Biol. 13:1135-1140(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-803 (ISOFORM 2) IN COMPLEX WITH RAC1, MUTAGENESIS OF GLN-52.

    Entry informationi

    Entry nameiPLCB2_HUMAN
    AccessioniPrimary (citable) accession number: Q00722
    Secondary accession number(s): A8K6J2, B9EGH5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: November 25, 2008
    Last modified: October 1, 2014
    This is version 146 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Miscellaneous

    The receptor-mediated activation of PLC-beta-2 is most effectively mediated by one G-protein alpha subunit, alpha-16.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 15
      Human chromosome 15: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3