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P08487

- PLCG1_BOVIN

UniProt

P08487 - PLCG1_BOVIN

Protein

1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1

Gene

PLCG1

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 160 (01 Oct 2014)
      Sequence version 1 (01 Aug 1988)
      Previous versions | rss
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    Functioni

    Mediates the production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). Plays an important role in the regulation of intracellular signaling cascades. Becomes activated in response to ligand-mediated activation of receptor-type tyrosine kinases, such as PDGFRA, PDGFRB, FGFR1, FGFR2, FGFR3 and FGFR4. Plays a role in actin reorganization and cell migration By similarity.By similarity

    Catalytic activityi

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

    Cofactori

    Calcium.

    Enzyme regulationi

    Activated by phosphorylation on tyrosine residues.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei335 – 3351PROSITE-ProRule annotation
    Active sitei380 – 3801PROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi165 – 17612PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

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

    GO - Biological processi

    1. cellular response to epidermal growth factor stimulus Source: UniProtKB
    2. intracellular signal transduction Source: InterPro
    3. in utero embryonic development Source: AgBase
    4. phospholipid catabolic process Source: InterPro
    5. positive regulation of epithelial cell migration Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Transducer

    Keywords - Biological processi

    Lipid degradation, Lipid metabolism

    Keywords - Ligandi

    Calcium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1 (EC:3.1.4.11)
    Alternative name(s):
    PLC-148
    Phosphoinositide phospholipase C-gamma-1
    Phospholipase C-II
    Short name:
    PLC-II
    Phospholipase C-gamma-1
    Short name:
    PLC-gamma-1
    Gene namesi
    Name:PLCG1
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Unplaced

    Subcellular locationi

    Cell projectionlamellipodium By similarity. Cell projectionruffle By similarity
    Note: Rapidly redistributed to ruffles and lamellipodia structures in response to epidermal growth factor (EGF) treatment.By similarity

    GO - Cellular componenti

    1. COP9 signalosome Source: UniProtKB
    2. lamellipodium Source: UniProtKB
    3. ruffle Source: UniProtKB

    Keywords - Cellular componenti

    Cell projection

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 129112901-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1PRO_0000088497Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei506 – 5061PhosphotyrosineBy similarity
    Modified residuei771 – 7711Phosphotyrosine; by SYK2 Publications
    Modified residuei775 – 7751PhosphotyrosineBy similarity
    Modified residuei783 – 7831Phosphotyrosine; alternate3 Publications
    Modified residuei783 – 7831Phosphotyrosine; by ITK, SYK and TXK; alternateBy similarity
    Modified residuei977 – 9771PhosphotyrosineBy similarity
    Modified residuei1222 – 12221PhosphoserineBy similarity
    Modified residuei1249 – 12491PhosphoserineBy similarity
    Modified residuei1254 – 12541Phosphotyrosine3 Publications

    Post-translational modificationi

    May be dephosphorylated by PTPRJ By similarity. Tyrosine phosphorylated by activated FGFR1, FGFR2, FGFR3 and FGFR4. The receptor-mediated activation of PLCG1 involves its phosphorylation by tyrosine kinases in response to ligation of a variety of growth factor receptors and immune system receptors. For instance, SYK phosphorylates and activates PLCG1 in response to ligation of the B-cell receptor. Tyrosine phosphorylated in response to signaling via activated FLT1, FLT3, PDGFRA, PDGFRB and KIT. Phosphorylated by ITK and TXK on Tyr-783 upon TCR activation in T-cells By similarity.By similarity
    Ubiquitinated by CBLB in activated T-cells.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PRIDEiP08487.

    Interactioni

    Subunit structurei

    Interacts (via SH2 domain) with FGFR1, FGFR2, FGFR3 and FGFR4 (phosphorylated). Interacts (via SH3 domain) with AGAP2. Interacts with LAT (phosphorylated) upon TCR activation. Interacts (via SH3 domain) with the Pro-rich domain of TNK1. Associates with BLNK, VAV1, GRB2 and NCK1 in a B-cell antigen receptor-dependent fashion. Interacts with CBLB in activated T-cells; which inhibits phosphorylation. Interacts with SHB. Interacts (via SH3 domain) with the Arg/Gly-rich-flanked Pro-rich domains of KHDRBS1/SAM68. This interaction is selectively regulated by arginine methylation of KHDRBS1/SAM68. Interacts with INPP5D/SHIP1, THEMIS and CLNK By similarity. Interacts with RALGPS1. Interacts (via SH2 domain) with PDGFRB (tyrosine phosphorylated) By similarity. Interacts (via SH3 domain) with HEV ORF3 protein. Interacts (via the SH2 domains) with VIL1 (phosphorylated at C-terminus tyrosine phosphorylation sites). Interacts with FLT1 (tyrosine-phosphorylated). Interacts with AXL, FLT4 and KIT By similarity. Interacts (via SH2 domain) with RET. Interacts (via SH2 domain) with PDGFRA (tyrosine phosphorylated). Interacts with PIP5K1C By similarity. Interacts with NTRK1 and NTRK2 (phosphorylated upon ligand-binding) By similarity. Interacts with SYK; activates PLCG1 By similarity. Interacts with TESPA1 By similarity. Interacts with GRB2, LAT and THEMIS upon TCR activation in thymocytes By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CBLP226813EBI-8013886,EBI-518228From a different organism.
    LATO43561-24EBI-8013886,EBI-8070286From a different organism.
    LCP2Q130945EBI-8013886,EBI-346946From a different organism.
    PDGFRBP096193EBI-8013886,EBI-641237From a different organism.
    SykP480254EBI-8013886,EBI-300116From a different organism.
    VAV1P154984EBI-8013886,EBI-625518From a different organism.

    Protein-protein interaction databases

    DIPiDIP-42760N.
    IntActiP08487. 8 interactions.
    MINTiMINT-2837008.
    STRINGi9913.ENSBTAP00000023383.

    Structurei

    Secondary structure

    1
    1291
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi664 – 6663
    Beta strandi667 – 6704
    Beta strandi671 – 6733
    Helixi676 – 6849
    Beta strandi685 – 6884
    Beta strandi691 – 6955
    Beta strandi697 – 7004
    Beta strandi702 – 7087
    Beta strandi711 – 7133
    Beta strandi716 – 7183
    Beta strandi721 – 7255
    Beta strandi727 – 7326
    Helixi735 – 7439
    Beta strandi746 – 7494

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2FCINMR-A663-759[»]
    2PLDNMR-A663-759[»]
    2PLENMR-A663-759[»]
    ProteinModelPortaliP08487.
    SMRiP08487. Positions 489-658, 663-759, 790-933.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP08487.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini27 – 142116PH 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini152 – 18736EF-handPROSITE-ProRule annotationAdd
    BLAST
    Domaini320 – 464145PI-PLC X-boxPROSITE-ProRule annotationAdd
    BLAST
    Domaini489 – 52335PH 2; first partPROSITE-ProRule annotationAdd
    BLAST
    Domaini550 – 657108SH2 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini668 – 75689SH2 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini791 – 85161SH3PROSITE-ProRule annotationAdd
    BLAST
    Domaini895 – 93137PH 2; second partPROSITE-ProRule annotationAdd
    BLAST
    Domaini953 – 1070118PI-PLC Y-boxPROSITE-ProRule annotationAdd
    BLAST
    Domaini1075 – 1177103C2PROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The SH3 domain mediates interaction with CLNK and RALGPS1.By similarity

    Sequence similaritiesi

    Contains 1 C2 domain.PROSITE-ProRule annotation
    Contains 1 EF-hand domain.PROSITE-ProRule annotation
    Contains 2 PH domains.PROSITE-ProRule annotation
    Contains 1 PI-PLC X-box domain.PROSITE-ProRule annotation
    Contains 1 PI-PLC Y-box domain.PROSITE-ProRule annotation
    Contains 2 SH2 domains.PROSITE-ProRule annotation
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, SH2 domain, SH3 domain

    Phylogenomic databases

    eggNOGiNOG268751.
    HOGENOMiHOG000230864.
    HOVERGENiHBG053611.
    InParanoidiP08487.
    KOiK01116.

    Family and domain databases

    Gene3Di2.30.29.30. 3 hits.
    2.60.40.150. 1 hit.
    3.20.20.190. 2 hits.
    3.30.505.10. 2 hits.
    InterProiIPR000008. C2_dom.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR001192. PI-PLC_fam.
    IPR016279. PLC-gamma.
    IPR028380. PLC-gamma1.
    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.
    IPR000980. SH2.
    IPR001452. SH3_domain.
    [Graphical view]
    PANTHERiPTHR10336. PTHR10336. 1 hit.
    PTHR10336:SF52. PTHR10336:SF52. 1 hit.
    PfamiPF00168. C2. 1 hit.
    PF09279. EF-hand_like. 1 hit.
    PF00388. PI-PLC-X. 1 hit.
    PF00387. PI-PLC-Y. 1 hit.
    PF00017. SH2. 2 hits.
    PF00018. SH3_1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000952. PLC-gamma. 1 hit.
    PRINTSiPR00390. PHPHLIPASEC.
    PR00401. SH2DOMAIN.
    PR00452. SH3DOMAIN.
    SMARTiSM00239. C2. 1 hit.
    SM00233. PH. 3 hits.
    SM00148. PLCXc. 1 hit.
    SM00149. PLCYc. 1 hit.
    SM00252. SH2. 2 hits.
    SM00326. SH3. 1 hit.
    [Graphical view]
    SUPFAMiSSF49562. SSF49562. 1 hit.
    SSF50044. SSF50044. 1 hit.
    SSF51695. SSF51695. 2 hits.
    SSF55550. SSF55550. 2 hits.
    PROSITEiPS50004. C2. 1 hit.
    PS00018. EF_HAND_1. 1 hit.
    PS50222. EF_HAND_2. 1 hit.
    PS50003. PH_DOMAIN. 2 hits.
    PS50007. PIPLC_X_DOMAIN. 1 hit.
    PS50008. PIPLC_Y_DOMAIN. 1 hit.
    PS50001. SH2. 2 hits.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P08487-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAGAASPCAN GCGPSAPSDA EVVHLCRSLE VGTVMTLFYS KKSQRPERKT     50
    FQVKLETRQI TWSRGADKIE GAIDIREIKE IRPGKTSRDF DRYQEDPAFR 100
    PDQSHCFVIL YGMEFRLKTL SLQATSEDEV NMWIRGLTWL MEDTLQAATP 150
    LQIERWLRKQ FYSVDRNRED RISAKDLKNM LSQVNYRVPN MRFLRERLTD 200
    LEQRTSDITY GQFAQLYRSL MYSAQKTMDL PFLEASALRA GERPELCRVS 250
    LPEFQQFLLE YQGELWAVDR LQVQEFMLSF LRDPLREIEE PYFFLDEFVT 300
    FLFSKENSIW NSQLDEVCPD TMNNPLSHYW ISSSHNTYLT GDQFSSESSL 350
    EAYARCLRMG CRCIELDCWD GPDGMPVIYH GHTLTTKIKF SDVLHTIKEH 400
    AFVASEYPVI LSIEDHCSIA QQRNMAQYFK KVLGDTLLTK PVDIAADGLP 450
    SPNQLKRKIL IKHKKLAEGS AYEEVPTSVM YSENDISNSI KNGILYLEDP 500
    VNHEWYPHYF VLTSSKIYYS EETSSDQGNE DEEEPKEASG STELHSNEKW 550
    FHGKLGAGRD GRHIAERLLT EYCIETGAPD GSFLVRESET FVGDYTLSFW 600
    RNGKVQHCRI HSRQDAGTPK FFLTDNLVFD SLYDLITHYQ QVPLRCNEFE 650
    MRLSEPVPQT NAHESKEWYH ASLTRAQAEH MLMRVPRDGA FLVRKRNEPN 700
    SYAISFRAEG KIKHCRVQQE GQTVMLGNSE FDSLVDLISY YEKHPLYRKM 750
    KLRYPINEEA LEKIGTAEPD YGALYEGRNP GFYVEANPMP TFKCAVKALF 800
    DYKAQREDEL TFTKSAIIQN VEKQEGGWWR GDYGGKKQLW FPSNYVEEMV 850
    SPAALEPERE HLDENSPLGD LLRGVLDVPA CQIAVRPEGK NNRLFVFSIS 900
    MASVAHWSLD VAADSQEELQ DWVKKIREVA QTADARLTEG KMMERRKKIA 950
    LELSELVVYC RPVPFDEEKI GTERACYRDM SSFPETKAEK YVNKAKGKKF 1000
    LQYNRLQLSR IYPKGQRLDS SNYDPLPMWI CGSQLVALNF QTPDKPMQMN 1050
    QALFLAGGHC GYVLQPSVMR DEAFDPFDKS SLRGLEPCAI CIEVLGARHL 1100
    PKNGRGIVCP FVEIEVAGAE YDSIKQKTEF VVDNGLNPVW PAKPFHFQIS 1150
    NPEFAFLRFV VYEEDMFSDQ NFLAQATFPV KGLKTGYRAV PLKNNYSEGL 1200
    ELASLLVKID VFPAKQENGD LSPFGGASLR ERSCDASGPL FHGRAREGSF 1250
    EARYQQPFED FRISQEHLAD HFDGRDRRTP RRTRVNGDNR L 1291
    Length:1,291
    Mass (Da):148,313
    Last modified:August 1, 1988 - v1
    Checksum:i9F31C7DAA3F8EA77
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00301 mRNA. Translation: CAA68406.1.
    PIRiS00666.
    RefSeqiNP_776850.1. NM_174425.3.
    UniGeneiBt.307.

    Genome annotation databases

    GeneIDi281987.
    KEGGibta:281987.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00301 mRNA. Translation: CAA68406.1 .
    PIRi S00666.
    RefSeqi NP_776850.1. NM_174425.3.
    UniGenei Bt.307.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2FCI NMR - A 663-759 [» ]
    2PLD NMR - A 663-759 [» ]
    2PLE NMR - A 663-759 [» ]
    ProteinModelPortali P08487.
    SMRi P08487. Positions 489-658, 663-759, 790-933.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-42760N.
    IntActi P08487. 8 interactions.
    MINTi MINT-2837008.
    STRINGi 9913.ENSBTAP00000023383.

    Chemistry

    BindingDBi P08487.
    ChEMBLi CHEMBL5566.

    Proteomic databases

    PRIDEi P08487.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 281987.
    KEGGi bta:281987.

    Organism-specific databases

    CTDi 5335.

    Phylogenomic databases

    eggNOGi NOG268751.
    HOGENOMi HOG000230864.
    HOVERGENi HBG053611.
    InParanoidi P08487.
    KOi K01116.

    Miscellaneous databases

    EvolutionaryTracei P08487.
    NextBioi 20805855.

    Family and domain databases

    Gene3Di 2.30.29.30. 3 hits.
    2.60.40.150. 1 hit.
    3.20.20.190. 2 hits.
    3.30.505.10. 2 hits.
    InterProi IPR000008. C2_dom.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR001192. PI-PLC_fam.
    IPR016279. PLC-gamma.
    IPR028380. PLC-gamma1.
    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.
    IPR000980. SH2.
    IPR001452. SH3_domain.
    [Graphical view ]
    PANTHERi PTHR10336. PTHR10336. 1 hit.
    PTHR10336:SF52. PTHR10336:SF52. 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.
    PF00017. SH2. 2 hits.
    PF00018. SH3_1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000952. PLC-gamma. 1 hit.
    PRINTSi PR00390. PHPHLIPASEC.
    PR00401. SH2DOMAIN.
    PR00452. SH3DOMAIN.
    SMARTi SM00239. C2. 1 hit.
    SM00233. PH. 3 hits.
    SM00148. PLCXc. 1 hit.
    SM00149. PLCYc. 1 hit.
    SM00252. SH2. 2 hits.
    SM00326. SH3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49562. SSF49562. 1 hit.
    SSF50044. SSF50044. 1 hit.
    SSF51695. SSF51695. 2 hits.
    SSF55550. SSF55550. 2 hits.
    PROSITEi PS50004. C2. 1 hit.
    PS00018. EF_HAND_1. 1 hit.
    PS50222. EF_HAND_2. 1 hit.
    PS50003. PH_DOMAIN. 2 hits.
    PS50007. PIPLC_X_DOMAIN. 1 hit.
    PS50008. PIPLC_Y_DOMAIN. 1 hit.
    PS50001. SH2. 2 hits.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence similarity of phospholipase C with the non-catalytic region of src."
      Stahl M.L., Ferenz C.R., Kelleher K.L., Kriz R.W., Knopf J.L.
      Nature 332:269-272(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    2. "Tyrosine residues in bovine phospholipase C-gamma phosphorylated by the epidermal growth factor receptor in vitro."
      Kim J.W., Sim S.S., Kim U.H., Nishibe S., Whal M.I., Carpenter G., Rhee S.G.
      J. Biol. Chem. 265:3940-3943(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-771; TYR-783 AND TYR-1254.
    3. "Identification of two epidermal growth factor-sensitive tyrosine phosphorylation sites of phospholipase C-gamma in intact HSC-1 cells."
      Whal M.I., Nishibe S., Kim J.W., Kim H.K., Rhee S.G., Carpenter G.
      J. Biol. Chem. 265:3944-3948(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-771; TYR-783 AND TYR-1254.
    4. "Binding of SH2 domains of phospholipase C gamma 1, GAP, and Src to activated growth factor receptors."
      Anderson D., Koch C.A., Grey L., Ellis C., Moran M.F., Pawson T.
      Science 250:979-982(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PDGFRA.
    5. "PDGF stimulation of inositol phospholipid hydrolysis requires PLC-gamma 1 phosphorylation on tyrosine residues 783 and 1254."
      Kim H.K., Kim J.W., Zilberstein A., Margolis B., Kim J.G., Schlessinger J., Rhee S.G.
      Cell 65:435-441(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-783 AND TYR-1254.
    6. "Direct association between the Ret receptor tyrosine kinase and the Src homology 2-containing adapter protein Grb7."
      Pandey A., Liu X., Dixon J.E., Di Fiore P.P., Dixit V.M.
      J. Biol. Chem. 271:10607-10610(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RET.
    7. "Nuclear magnetic resonance structure of an SH2 domain of phospholipase C-gamma 1 complexed with a high affinity binding peptide."
      Pascal S.M., Singer A.U., Gish G., Yamazaki T., Shoelson S.E., Pawson T., Kay L.E., Forman-Kay J.D.
      Cell 77:461-472(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 663-759.

    Entry informationi

    Entry nameiPLCG1_BOVIN
    AccessioniPrimary (citable) accession number: P08487
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: August 1, 1988
    Last modified: October 1, 2014
    This is version 160 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3