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Q8N3E9

- PLCD3_HUMAN

UniProt

Q8N3E9 - PLCD3_HUMAN

Protein

1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-3

Gene

PLCD3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 3 (02 Oct 2007)
      Previous versions | rss
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    Functioni

    Hydrolyzes the phosphatidylinositol 4,5-bisphosphate (PIP2) to generate 2 second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). DAG mediates the activation of protein kinase C (PKC), while IP3 releases Ca2+ from intracellular stores. Essential for trophoblast and placental development. May participate in cytokinesis by hydrolyzing PIP2 at the cleavage furrow.

    Catalytic activityi

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

    Cofactori

    Binds 3 calcium ions per subunit. Two of the calcium ions are bound to the C2 domain Probable.1 Publication

    Enzyme regulationi

    Strongly activated by phosphatidic acid. Inhibited by phosphatidylethanolamine (PtdEtn), phosphatidylcholine (PtdCho), sphingomyelin and phosphatidylserine (PtdSer).2 Publications

    Kineticsi

    1. KM=105.3 µM for PIP21 Publication

    Vmax=28.5 µmol/min/mg enzyme1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei352 – 3521PROSITE-ProRule annotation
    Metal bindingi353 – 3531Calcium 1; catalyticBy similarity
    Metal bindingi382 – 3821Calcium 1; catalyticBy similarity
    Metal bindingi384 – 3841Calcium 1; catalyticBy similarity
    Active sitei397 – 3971PROSITE-ProRule annotation
    Metal bindingi431 – 4311Calcium 1; catalyticBy similarity
    Binding sitei480 – 4801SubstrateBy similarity
    Binding sitei482 – 4821SubstrateBy similarity
    Binding sitei557 – 5571SubstrateBy similarity
    Binding sitei584 – 5841SubstrateBy similarity
    Metal bindingi683 – 6831Calcium 2; via carbonyl oxygenBy similarity
    Metal bindingi685 – 6851Calcium 2By similarity
    Metal bindingi709 – 7091Calcium 2By similarity
    Metal bindingi738 – 7381Calcium 3By similarity
    Metal bindingi739 – 7391Calcium 3; via carbonyl oxygenBy similarity
    Metal bindingi740 – 7401Calcium 3By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi195 – 206121Sequence AnalysisAdd
    BLAST
    Calcium bindingi231 – 242122Sequence AnalysisAdd
    BLAST

    GO - Molecular functioni

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

    GO - Biological processi

    1. angiogenesis Source: Ensembl
    2. inositol phosphate metabolic process Source: Reactome
    3. intracellular signal transduction Source: InterPro
    4. labyrinthine layer blood vessel development Source: Ensembl
    5. lipid catabolic process Source: UniProtKB-KW
    6. regulation of cell proliferation Source: Ensembl
    7. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Hydrolase, Transducer

    Keywords - Biological processi

    Lipid degradation, Lipid metabolism

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_150312. Synthesis of IP3 and IP4 in the cytosol.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-3 (EC:3.1.4.11)
    Alternative name(s):
    Phosphoinositide phospholipase C-delta-3
    Phospholipase C-delta-3
    Short name:
    PLC-delta-3
    Gene namesi
    Name:PLCD3
    Synonyms:KIAA1964
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:9061. PLCD3.

    Subcellular locationi

    Membrane; Peripheral membrane protein. Cytoplasm. Cleavage furrow
    Note: Localizes at the cleavage furrow during cytokinesis.

    GO - Cellular componenti

    1. cleavage furrow Source: UniProtKB-SubCell
    2. cytosol Source: Ensembl
    3. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33389.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 7897891-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-3PRO_0000306821Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei105 – 1051Phosphoserine1 Publication
    Modified residuei496 – 4961PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ8N3E9.
    PaxDbiQ8N3E9.
    PeptideAtlasiQ8N3E9.
    PRIDEiQ8N3E9.

    Expressioni

    Tissue specificityi

    Present in corneal epithelial cells (at protein level).1 Publication

    Inductioni

    Down-regulated by Ca2+ and cAMP.1 Publication

    Gene expression databases

    ArrayExpressiQ8N3E9.
    BgeeiQ8N3E9.
    CleanExiHS_PLCD3.
    GenevestigatoriQ8N3E9.

    Organism-specific databases

    HPAiHPA025711.
    HPA053665.

    Interactioni

    Protein-protein interaction databases

    BioGridi125222. 2 interactions.
    IntActiQ8N3E9. 1 interaction.
    MINTiMINT-1193970.
    STRINGi9606.ENSP00000313731.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8N3E9.
    SMRiQ8N3E9. Positions 55-787.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini63 – 172110PHAdd
    BLAST
    Domaini182 – 21736EF-hand 1Add
    BLAST
    Domaini218 – 25336EF-hand 2Add
    BLAST
    Domaini250 – 28536EF-hand 3Add
    BLAST
    Domaini337 – 482146PI-PLC X-boxPROSITE-ProRule annotationAdd
    BLAST
    Domaini528 – 644117PI-PLC Y-boxPROSITE-ProRule annotationAdd
    BLAST
    Domaini647 – 752106C2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni73 – 10129Substrate bindingBy similarityAdd
    BLAST

    Domaini

    The C2 domain is a Ca2+-dependent membrane-targeting module.
    The PH domain mediates interaction with the surface membrane by binding to PIP2.

    Sequence similaritiesi

    Contains 1 C2 domain.PROSITE-ProRule annotation
    Contains 3 EF-hand domains.Curated
    Contains 1 PH domain.Curated
    Contains 1 PI-PLC X-box domain.PROSITE-ProRule annotation
    Contains 1 PI-PLC Y-box domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG149692.
    HOGENOMiHOG000006871.
    HOVERGENiHBG053610.
    InParanoidiQ8N3E9.
    KOiK05857.
    OrthoDBiEOG7V49XT.
    PhylomeDBiQ8N3E9.
    TreeFamiTF313216.

    Family and domain databases

    Gene3Di1.10.238.10. 2 hits.
    2.30.29.30. 1 hit.
    2.60.40.150. 1 hit.
    3.20.20.190. 2 hits.
    InterProiIPR000008. C2_dom.
    IPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR001192. PI-PLC_fam.
    IPR028406. PLC-delta3.
    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:SF33. PTHR10336:SF33. 1 hit.
    PfamiPF00168. C2. 1 hit.
    PF09279. EF-hand_like. 1 hit.
    PF00388. PI-PLC-X. 1 hit.
    PF00387. PI-PLC-Y. 1 hit.
    [Graphical view]
    PRINTSiPR00390. PHPHLIPASEC.
    SMARTiSM00239. C2. 1 hit.
    SM00233. PH. 1 hit.
    SM00148. PLCXc. 1 hit.
    SM00149. PLCYc. 1 hit.
    [Graphical view]
    SUPFAMiSSF49562. SSF49562. 1 hit.
    SSF51695. SSF51695. 1 hit.
    PROSITEiPS50004. C2. 1 hit.
    PS00018. EF_HAND_1. 1 hit.
    PS50007. PIPLC_X_DOMAIN. 1 hit.
    PS50008. PIPLC_Y_DOMAIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8N3E9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLCGRWRRCR RPPEEPPVAA QVAAQVAAPV ALPSPPTPSD GGTKRPGLRA    50
    LKKMGLTEDE DVRAMLRGSR LRKIRSRTWH KERLYRLQED GLSVWFQRRI 100
    PRAPSQHIFF VQHIEAVREG HQSEGLRRFG GAFAPARCLT IAFKGRRKNL 150
    DLAAPTAEEA QRWVRGLTKL RARLDAMSQR ERLDHWIHSY LHRADSNQDS 200
    KMSFKEIKSL LRMVNVDMND MYAYLLFKEC DHSNNDRLEG AEIEEFLRRL 250
    LKRPELEEIF HQYSGEDRVL SAPELLEFLE DQGEEGATLA RAQQLIQTYE 300
    LNETAKQHEL MTLDGFMMYL LSPEGAALDN THTCVFQDMN QPLAHYFISS 350
    SHNTYLTDSQ IGGPSSTEAY VRAFAQGCRC VELDCWEGPG GEPVIYHGHT 400
    LTSKILFRDV VQAVRDHAFT LSPYPVILSL ENHCGLEQQA AMARHLCTIL 450
    GDMLVTQALD SPNPEELPSP EQLKGRVLVK GKKLPAARSE DGRALSDREE 500
    EEEDDEEEEE EVEAAAQRRL AKQISPELSA LAVYCHATRL RTLHPAPNAP 550
    QPCQVSSLSE RKAKKLIREA GNSFVRHNAR QLTRVYPLGL RMNSANYSPQ 600
    EMWNSGCQLV ALNFQTPGYE MDLNAGRFLV NGQCGYVLKP ACLRQPDSTF 650
    DPEYPGPPRT TLSIQVLTAQ QLPKLNAEKP HSIVDPLVRI EIHGVPADCA 700
    RQETDYVLNN GFNPRWGQTL QFQLRAPELA LVRFVVEDYD ATSPNDFVGQ 750
    FTLPLSSLKQ GYRHIHLLSK DGASLSPATL FIQIRIQRS 789
    Length:789
    Mass (Da):89,258
    Last modified:October 2, 2007 - v3
    Checksum:iC6901404D2C9D070
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti207 – 2071I → T in CAD39054. (PubMed:17974005)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti652 – 6521P → L.
    Corresponds to variant rs734921 [ dbSNP | Ensembl ].
    VAR_035316

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK074240 mRNA. Translation: BAB85029.1.
    BC010668 mRNA. Translation: AAH10668.2.
    BC072384 mRNA. Translation: AAH72384.1.
    AL834392 mRNA. Translation: CAD39054.2.
    AB075844 mRNA. Translation: BAB85550.1.
    RefSeqiNP_588614.1. NM_133373.4.
    UniGeneiHs.380094.

    Genome annotation databases

    EnsembliENST00000322765; ENSP00000313731; ENSG00000161714.
    GeneIDi113026.
    KEGGihsa:113026.
    UCSCiuc002iib.3. human.

    Polymorphism databases

    DMDMi158706388.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK074240 mRNA. Translation: BAB85029.1 .
    BC010668 mRNA. Translation: AAH10668.2 .
    BC072384 mRNA. Translation: AAH72384.1 .
    AL834392 mRNA. Translation: CAD39054.2 .
    AB075844 mRNA. Translation: BAB85550.1 .
    RefSeqi NP_588614.1. NM_133373.4.
    UniGenei Hs.380094.

    3D structure databases

    ProteinModelPortali Q8N3E9.
    SMRi Q8N3E9. Positions 55-787.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 125222. 2 interactions.
    IntActi Q8N3E9. 1 interaction.
    MINTi MINT-1193970.
    STRINGi 9606.ENSP00000313731.

    Chemistry

    DrugBanki DB00144. Phosphatidylserine.

    Polymorphism databases

    DMDMi 158706388.

    Proteomic databases

    MaxQBi Q8N3E9.
    PaxDbi Q8N3E9.
    PeptideAtlasi Q8N3E9.
    PRIDEi Q8N3E9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000322765 ; ENSP00000313731 ; ENSG00000161714 .
    GeneIDi 113026.
    KEGGi hsa:113026.
    UCSCi uc002iib.3. human.

    Organism-specific databases

    CTDi 113026.
    GeneCardsi GC17M043197.
    HGNCi HGNC:9061. PLCD3.
    HPAi HPA025711.
    HPA053665.
    MIMi 608795. gene.
    neXtProti NX_Q8N3E9.
    PharmGKBi PA33389.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG149692.
    HOGENOMi HOG000006871.
    HOVERGENi HBG053610.
    InParanoidi Q8N3E9.
    KOi K05857.
    OrthoDBi EOG7V49XT.
    PhylomeDBi Q8N3E9.
    TreeFami TF313216.

    Enzyme and pathway databases

    Reactomei REACT_150312. Synthesis of IP3 and IP4 in the cytosol.

    Miscellaneous databases

    ChiTaRSi PLCD3. human.
    GeneWikii PLCD3.
    GenomeRNAii 113026.
    NextBioi 78735.
    PROi Q8N3E9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8N3E9.
    Bgeei Q8N3E9.
    CleanExi HS_PLCD3.
    Genevestigatori Q8N3E9.

    Family and domain databases

    Gene3Di 1.10.238.10. 2 hits.
    2.30.29.30. 1 hit.
    2.60.40.150. 1 hit.
    3.20.20.190. 2 hits.
    InterProi IPR000008. C2_dom.
    IPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR001192. PI-PLC_fam.
    IPR028406. PLC-delta3.
    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:SF33. PTHR10336:SF33. 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.
    [Graphical view ]
    PRINTSi PR00390. PHPHLIPASEC.
    SMARTi SM00239. C2. 1 hit.
    SM00233. PH. 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.
    PS00018. EF_HAND_1. 1 hit.
    PS50007. PIPLC_X_DOMAIN. 1 hit.
    PS50008. PIPLC_Y_DOMAIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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].
    2. "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].
      Tissue: Colon and Pancreas.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 13-789.
      Tissue: Amygdala.
    4. "Prediction of the coding sequences of unidentified human genes. XXII. The complete sequences of 50 new cDNA clones which code for large proteins."
      Nagase T., Kikuno R., Ohara O.
      DNA Res. 8:319-327(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 33-789.
      Tissue: Brain.
    5. "Expression, purification and kinetic properties of human recombinant phospholipase C delta 3."
      Pawelczyk T., Matecki A.
      Acta Biochim. Pol. 44:221-229(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PURIFICATION.
    6. "Phospholipase C isoforms delta 1 and delta 3 from human fibroblasts. High-yield expression in Escherichia coli, simple purification, and properties."
      Ghosh S., Pawelczyk T., Lowenstein J.M.
      Protein Expr. Purif. 9:262-278(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PURIFICATION.
    7. "Localization of phospholipase C delta3 in the cell and regulation of its activity by phospholipids and calcium."
      Pawelczyk T., Matecki A.
      Eur. J. Biochem. 257:169-177(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, COFACTOR, ENZYME REGULATION.
    8. "Assignment of the human PLC delta3 gene (PLCD3) to human chromosome band 17q21 by fluorescence in situ hybridization."
      Kim H., Suh P.-G., Ryu S.H., Park S.H.
      Cytogenet. Cell Genet. 87:209-210(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION.
    9. "Phospholipase C-delta3 binds with high specificity to phosphatidylinositol 4,5-bisphosphate and phosphatidic acid in bilayer membranes."
      Pawelczyk T., Matecki A.
      Eur. J. Biochem. 262:291-298(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, DOMAIN PH.
    10. Cited for: INDUCTION.
    11. "Membrane targeting of C2 domains of phospholipase C-delta isoforms."
      Ananthanarayanan B., Das S., Rhee S.-G., Murray D., Cho W.
      J. Biol. Chem. 277:3568-3575(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN C2.
    12. "Expression of phospholipases A2 and C in human corneal epithelial cells."
      Landreville S., Coulombe S., Carrier P., Gelb M.H., Guerin S.L., Salesse C.
      Invest. Ophthalmol. Vis. Sci. 45:3997-4003(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    13. "Phospholipase C isoforms are localized at the cleavage furrow during cytokinesis."
      Naito Y., Okada M., Yagisawa H.
      J. Biochem. 140:785-791(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.

    Entry informationi

    Entry nameiPLCD3_HUMAN
    AccessioniPrimary (citable) accession number: Q8N3E9
    Secondary accession number(s): Q8TEC1, Q8TF37, Q96FL6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 2, 2007
    Last sequence update: October 2, 2007
    Last modified: October 1, 2014
    This is version 122 of the entry and version 3 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

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3