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P19174

- PLCG1_HUMAN

UniProt

P19174 - PLCG1_HUMAN

Protein

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

Gene

PLCG1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 189 (01 Oct 2014)
      Sequence version 1 (01 Nov 1990)
      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.1 Publication

    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.

    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. neurotrophin TRKA receptor binding Source: UniProtKB
    3. phosphatidylinositol phospholipase C activity Source: UniProtKB
    4. phospholipase C activity Source: Reactome
    5. protein binding Source: UniProtKB
    6. protein kinase binding Source: BHF-UCL
    7. receptor signaling protein activity Source: UniProtKB

    GO - Biological processi

    1. activation of MAPKK activity Source: Reactome
    2. activation of phospholipase C activity Source: Reactome
    3. axon guidance Source: Reactome
    4. blood coagulation Source: Reactome
    5. calcium-mediated signaling Source: BHF-UCL
    6. cell migration Source: BHF-UCL
    7. cellular response to epidermal growth factor stimulus Source: UniProtKB
    8. cytokine-mediated signaling pathway Source: Reactome
    9. epidermal growth factor receptor signaling pathway Source: BHF-UCL
    10. Fc-epsilon receptor signaling pathway Source: Reactome
    11. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
    12. fibroblast growth factor receptor signaling pathway Source: Reactome
    13. innate immune response Source: Reactome
    14. inositol phosphate metabolic process Source: Reactome
    15. in utero embryonic development Source: Ensembl
    16. leukocyte migration Source: Reactome
    17. neurotrophin TRK receptor signaling pathway Source: Reactome
    18. phospholipid catabolic process Source: InterPro
    19. positive regulation of angiogenesis Source: DFLAT
    20. positive regulation of blood vessel endothelial cell migration Source: DFLAT
    21. positive regulation of epithelial cell migration Source: UniProtKB
    22. positive regulation of release of sequestered calcium ion into cytosol Source: BHF-UCL
    23. signal transduction Source: UniProtKB
    24. small molecule metabolic process Source: Reactome
    25. T cell receptor signaling pathway Source: Reactome
    26. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Transducer

    Keywords - Biological processi

    Host-virus interaction, Lipid degradation, Lipid metabolism

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_111064. DAG and IP3 signaling.
    REACT_115720. PLCG1 events in ERBB2 signaling.
    REACT_115831. ISG15 antiviral mechanism.
    REACT_115852. Signaling by constitutively active EGFR.
    REACT_118700. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
    REACT_12076. Frs2-mediated activation.
    REACT_12079. PLC-gamma1 signalling.
    REACT_121141. Signaling by FGFR1 fusion mutants.
    REACT_121398. Signaling by FGFR mutants.
    REACT_12478. EGFR interacts with phospholipase C-gamma.
    REACT_12519. PECAM1 interactions.
    REACT_12623. Generation of second messenger molecules.
    REACT_147814. DAP12 signaling.
    REACT_150312. Synthesis of IP3 and IP4 in the cytosol.
    REACT_160158. Role of phospholipids in phagocytosis.
    REACT_163701. FCERI mediated MAPK activation.
    REACT_163834. FCERI mediated Ca+2 mobilization.
    REACT_17025. Downstream signal transduction.
    REACT_21310. Phospholipase C-mediated cascade.
    REACT_22228. Role of second messengers in netrin-1 signaling.
    SignaLinkiP19174.

    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
    Synonyms:PLC1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:9065. PLCG1.

    Subcellular locationi

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

    GO - Cellular componenti

    1. cell projection Source: BHF-UCL
    2. COP9 signalosome Source: UniProtKB
    3. cytoplasm Source: MGI
    4. cytosol Source: UniProtKB
    5. lamellipodium Source: UniProtKB
    6. plasma membrane Source: UniProtKB
    7. ruffle Source: UniProtKB

    Keywords - Cellular componenti

    Cell projection

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33392.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 129012891-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1PRO_0000088498Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei506 – 5061PhosphotyrosineBy similarity
    Modified residuei771 – 7711Phosphotyrosine; by SYK4 Publications
    Modified residuei775 – 7751Phosphotyrosine1 Publication
    Modified residuei783 – 7831Phosphotyrosine; by ITK, SYK and TXK4 Publications
    Modified residuei977 – 9771PhosphotyrosineBy similarity
    Modified residuei1221 – 12211Phosphoserine3 Publications
    Modified residuei1248 – 12481Phosphoserine1 Publication
    Modified residuei1253 – 12531Phosphotyrosine2 Publications

    Post-translational modificationi

    Tyrosine phosphorylated in response to signaling via activated FLT3, KIT and PDGFRA By similarity. Tyrosine phosphorylated by activated FGFR1, FGFR2, FGFR3 and FGFR4. Tyrosine phosphorylated by activated FLT1 and KDR. Tyrosine phosphorylated by activated PDGFRB. 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. May be dephosphorylated by PTPRJ. Phosphorylated by ITK and TXK on Tyr-783 upon TCR activation in T-cells.By similarity15 Publications
    Ubiquitinated by CBLB in activated T-cells.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP19174.
    PaxDbiP19174.
    PRIDEiP19174.

    PTM databases

    PhosphoSiteiP19174.

    Expressioni

    Gene expression databases

    ArrayExpressiP19174.
    BgeeiP19174.
    CleanExiHS_PLCG1.
    GenevestigatoriP19174.

    Organism-specific databases

    HPAiCAB004277.
    HPA036681.
    HPA036682.

    Interactioni

    Subunit structurei

    Interacts with AGAP2 via its SH3 domain. Interacts (via SH2 domain) with RET. Interacts with FLT1 (tyrosine-phosphorylated) By similarity. Interacts (via SH2 domain) with FGFR1, FGFR2, FGFR3 and FGFR4 (phosphorylated). 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 AXL, FLT4 and KIT. Interacts with RALGPS1. Interacts (via SH3 domain) with HEV ORF3 protein. Interacts (via the SH2 domains) with VIL1 (phosphorylated at C-terminus tyrosine phosphorylation sites). Interacts (via SH2 domain) with PDGFRA and PDGFRB (tyrosine phosphorylated). Interacts with PIP5K1C By similarity. Interacts with NTRK1 and NTRK2 (phosphorylated upon ligand-binding). Interacts with SYK; activates PLCG1. Interacts with GRB2, LAT and THEMIS upon TCR activation in thymocytes By similarity. Interacts with TESPA1; the association is increased with prolonged stimulation of the TCR and may facilitate the assembly of the LAT signalosome.By similarity20 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ABL2P426844EBI-79387,EBI-1102694
    AKT1P317499EBI-79387,EBI-296087
    ARP1027522EBI-79387,EBI-608057
    ASAP1Q9ULH13EBI-79387,EBI-346622
    ASAP2O431503EBI-79387,EBI-310968
    CD22P202732EBI-79387,EBI-78277
    DUSP15Q9H1R22EBI-79387,EBI-1752795
    EEF1A2Q71V393EBI-79387,EBI-7645815From a different organism.
    EGFRP005336EBI-79387,EBI-297353
    ERBB2P046265EBI-79387,EBI-641062
    ERBB3P218604EBI-79387,EBI-720706
    FCGR2BP319942EBI-79387,EBI-724784
    FGFR1P113625EBI-79387,EBI-1028277
    FLT1P179482EBI-79387,EBI-1026718
    GAB1Q1348036EBI-79387,EBI-517684
    GRB2P629932EBI-79387,EBI-401755
    HCKP086312EBI-79387,EBI-346340
    INSRP062139EBI-79387,EBI-475899
    KHDRBS1Q076662EBI-79387,EBI-1364
    KITP1072131EBI-79387,EBI-1379503
    LATO435616EBI-79387,EBI-1222766
    LCP2Q130943EBI-79387,EBI-346946
    MAP4K1Q929186EBI-79387,EBI-881
    METP0858110EBI-79387,EBI-1039152
    PDGFRBP096195EBI-79387,EBI-641237
    RAC1P630007EBI-79387,EBI-413628
    RETP079492EBI-79387,EBI-2480756
    RIN3Q8TB243EBI-79387,EBI-1570523
    SCARB2Q141082EBI-79387,EBI-1564650
    SHANK2Q9UPX84EBI-79387,EBI-1570571
    SHANK3Q9BYB02EBI-79387,EBI-1752330
    SNX17Q150362EBI-79387,EBI-1752620
    SOS1Q078893EBI-79387,EBI-297487
    SOS2Q078904EBI-79387,EBI-298181
    SYKP434054EBI-79387,EBI-78302
    VIL1P093275EBI-79387,EBI-746958

    Protein-protein interaction databases

    BioGridi111351. 94 interactions.
    DIPiDIP-100N.
    IntActiP19174. 109 interactions.
    MINTiMINT-102915.
    STRINGi9606.ENSP00000244007.

    Structurei

    Secondary structure

    1
    1290
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi551 – 5544
    Beta strandi556 – 5583
    Helixi561 – 57616
    Beta strandi583 – 5875
    Beta strandi589 – 5913
    Beta strandi595 – 6017
    Beta strandi604 – 61310
    Helixi615 – 6173
    Beta strandi620 – 6245
    Beta strandi627 – 6315
    Helixi632 – 64110
    Beta strandi644 – 6463
    Beta strandi649 – 6513
    Helixi662 – 6654
    Beta strandi669 – 6724
    Helixi675 – 6839
    Beta strandi690 – 6956
    Beta strandi701 – 7088
    Beta strandi711 – 72010
    Beta strandi723 – 7264
    Beta strandi729 – 7324
    Helixi734 – 74310
    Helixi758 – 7636
    Beta strandi792 – 7943
    Beta strandi805 – 8095
    Beta strandi817 – 8204
    Turni825 – 8273
    Beta strandi834 – 8363
    Turni843 – 8453

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1HSQNMR-A790-851[»]
    2HSPNMR-A790-851[»]
    4EY0X-ray2.80A/B/C/D545-790[»]
    4FBNX-ray2.40A545-790[»]
    ProteinModelPortaliP19174.
    SMRiP19174. Positions 73-483, 489-933, 952-1207.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP19174.

    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 By similarity. The SH3 domain also mediates interaction with 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.
    HOVERGENiHBG053611.
    KOiK01116.
    OMAiYRSLMYS.
    OrthoDBiEOG7W419X.
    PhylomeDBiP19174.
    TreeFamiTF313216.

    Family and domain databases

    Gene3Di1.10.238.10. 1 hit.
    2.30.29.30. 3 hits.
    2.60.40.150. 1 hit.
    3.20.20.190. 2 hits.
    3.30.505.10. 2 hits.
    InterProiIPR000008. C2_dom.
    IPR011992. EF-hand-dom_pair.
    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.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P19174-1) [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

    MAGAASPCAN GCGPGAPSDA EVLHLCRSLE VGTVMTLFYS KKSQRPERKT     50
    FQVKLETRQI TWSRGADKIE GAIDIREIKE IRPGKTSRDF DRYQEDPAFR 100
    PDQSHCFVIL YGMEFRLKTL SLQATSEDEV NMWIKGLTWL MEDTLQAPTP 150
    LQIERWLRKQ FYSVDRNRED RISAKDLKNM LSQVNYRVPN MRFLRERLTD 200
    LEQRSGDITY GQFAQLYRSL MYSAQKTMDL PFLEASTLRA GERPELCRVS 250
    LPEFQQFLLD YQGELWAVDR LQVQEFMLSF LRDPLREIEE PYFFLDEFVT 300
    FLFSKENSVW NSQLDAVCPD TMNNPLSHYW ISSSHNTYLT GDQFSSESSL 350
    EAYARCLRMG CRCIELDCWD GPDGMPVIYH GHTLTTKIKF SDVLHTIKEH 400
    AFVASEYPVI LSIEDHCSIA QQRNMAQYFK KVLGDTLLTK PVEISADGLP 450
    SPNQLKRKIL IKHKKLAEGS AYEEVPTSMM YSENDISNSI KNGILYLEDP 500
    VNHEWYPHYF VLTSSKIYYS EETSSDQGNE DEEEPKEVSS 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 TFIKSAIIQN VEKQEGGWWR GDYGGKKQLW FPSNYVEEMV 850
    NPVALEPERE HLDENSPLGD LLRGVLDVPA CQIAIRPEGK NNRLFVFSIS 900
    MASVAHWSLD VAADSQEELQ DWVKKIREVA QTADARLTEG KIMERRKKIA 950
    LELSELVVYC RPVPFDEEKI GTERACYRDM SSFPETKAEK YVNKAKGKKF 1000
    LQYNRLQLSR IYPKGQRLDS SNYDPLPMWI CGSQLVALNF QTPDKPMQMN 1050
    QALFMTGRHC GYVLQPSTMR DEAFDPFDKS SLRGLEPCAI SIEVLGARHL 1100
    PKNGRGIVCP FVEIEVAGAE YDSTKQKTEF VVDNGLNPVW PAKPFHFQIS 1150
    NPEFAFLRFV VYEEDMFSDQ NFLAQATFPV KGLKTGYRAV PLKNNYSEDL 1200
    ELASLLIKID IFPAKENGDL SPFSGTSLRE RGSDASGQLF HGRAREGSFE 1250
    SRYQQPFEDF RISQEHLADH FDSRERRAPR RTRVNGDNRL 1290
    Length:1,290
    Mass (Da):148,532
    Last modified:November 1, 1990 - v1
    Checksum:iAE05ABE2A18EDDAC
    GO
    Isoform 2 (identifier: P19174-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1215-1215: K → KQ

    Note: Contains a phosphoserine at position 1222.

    Show »
    Length:1,291
    Mass (Da):148,660
    Checksum:iEDDBB8D4E49B2F3E
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti209 – 2091T → N.1 Publication
    Corresponds to variant rs2229348 [ dbSNP | Ensembl ].
    VAR_025213
    Natural varianti279 – 2791S → G.1 Publication
    Corresponds to variant rs2228246 [ dbSNP | Ensembl ].
    VAR_022130
    Natural varianti739 – 7391S → T.1 Publication
    Corresponds to variant rs34203315 [ dbSNP | Ensembl ].
    VAR_025214
    Natural varianti813 – 8131I → T.2 Publications
    Corresponds to variant rs753381 [ dbSNP | Ensembl ].
    VAR_011908

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1215 – 12151K → KQ in isoform 2. 1 PublicationVSP_038692

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M34667 mRNA. Translation: AAA36452.1.
    DQ297143 Genomic DNA. Translation: ABB84466.1.
    AL022394 Genomic DNA. Translation: CAA18537.1.
    CH471077 Genomic DNA. Translation: EAW75991.1.
    CH471077 Genomic DNA. Translation: EAW75992.1.
    BC136466 mRNA. Translation: AAI36467.1.
    BC144136 mRNA. Translation: AAI44137.1.
    CCDSiCCDS13313.1. [P19174-2]
    CCDS13314.1. [P19174-1]
    PIRiA36466.
    RefSeqiNP_002651.2. NM_002660.2. [P19174-2]
    NP_877963.1. NM_182811.1. [P19174-1]
    UniGeneiHs.268177.

    Genome annotation databases

    EnsembliENST00000244007; ENSP00000244007; ENSG00000124181. [P19174-2]
    ENST00000373271; ENSP00000362368; ENSG00000124181. [P19174-1]
    GeneIDi5335.
    KEGGihsa:5335.
    UCSCiuc002xjp.1. human. [P19174-1]

    Polymorphism databases

    DMDMi130225.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M34667 mRNA. Translation: AAA36452.1 .
    DQ297143 Genomic DNA. Translation: ABB84466.1 .
    AL022394 Genomic DNA. Translation: CAA18537.1 .
    CH471077 Genomic DNA. Translation: EAW75991.1 .
    CH471077 Genomic DNA. Translation: EAW75992.1 .
    BC136466 mRNA. Translation: AAI36467.1 .
    BC144136 mRNA. Translation: AAI44137.1 .
    CCDSi CCDS13313.1. [P19174-2 ]
    CCDS13314.1. [P19174-1 ]
    PIRi A36466.
    RefSeqi NP_002651.2. NM_002660.2. [P19174-2 ]
    NP_877963.1. NM_182811.1. [P19174-1 ]
    UniGenei Hs.268177.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1HSQ NMR - A 790-851 [» ]
    2HSP NMR - A 790-851 [» ]
    4EY0 X-ray 2.80 A/B/C/D 545-790 [» ]
    4FBN X-ray 2.40 A 545-790 [» ]
    ProteinModelPortali P19174.
    SMRi P19174. Positions 73-483, 489-933, 952-1207.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111351. 94 interactions.
    DIPi DIP-100N.
    IntActi P19174. 109 interactions.
    MINTi MINT-102915.
    STRINGi 9606.ENSP00000244007.

    Chemistry

    BindingDBi P19174.
    ChEMBLi CHEMBL3964.

    PTM databases

    PhosphoSitei P19174.

    Polymorphism databases

    DMDMi 130225.

    Proteomic databases

    MaxQBi P19174.
    PaxDbi P19174.
    PRIDEi P19174.

    Protocols and materials databases

    DNASUi 5335.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000244007 ; ENSP00000244007 ; ENSG00000124181 . [P19174-2 ]
    ENST00000373271 ; ENSP00000362368 ; ENSG00000124181 . [P19174-1 ]
    GeneIDi 5335.
    KEGGi hsa:5335.
    UCSCi uc002xjp.1. human. [P19174-1 ]

    Organism-specific databases

    CTDi 5335.
    GeneCardsi GC20P039765.
    HGNCi HGNC:9065. PLCG1.
    HPAi CAB004277.
    HPA036681.
    HPA036682.
    MIMi 172420. gene.
    neXtProti NX_P19174.
    PharmGKBi PA33392.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG268751.
    HOVERGENi HBG053611.
    KOi K01116.
    OMAi YRSLMYS.
    OrthoDBi EOG7W419X.
    PhylomeDBi P19174.
    TreeFami TF313216.

    Enzyme and pathway databases

    Reactomei REACT_111064. DAG and IP3 signaling.
    REACT_115720. PLCG1 events in ERBB2 signaling.
    REACT_115831. ISG15 antiviral mechanism.
    REACT_115852. Signaling by constitutively active EGFR.
    REACT_118700. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
    REACT_12076. Frs2-mediated activation.
    REACT_12079. PLC-gamma1 signalling.
    REACT_121141. Signaling by FGFR1 fusion mutants.
    REACT_121398. Signaling by FGFR mutants.
    REACT_12478. EGFR interacts with phospholipase C-gamma.
    REACT_12519. PECAM1 interactions.
    REACT_12623. Generation of second messenger molecules.
    REACT_147814. DAP12 signaling.
    REACT_150312. Synthesis of IP3 and IP4 in the cytosol.
    REACT_160158. Role of phospholipids in phagocytosis.
    REACT_163701. FCERI mediated MAPK activation.
    REACT_163834. FCERI mediated Ca+2 mobilization.
    REACT_17025. Downstream signal transduction.
    REACT_21310. Phospholipase C-mediated cascade.
    REACT_22228. Role of second messengers in netrin-1 signaling.
    SignaLinki P19174.

    Miscellaneous databases

    ChiTaRSi PLCG1. human.
    EvolutionaryTracei P19174.
    GeneWikii PLCG1.
    GenomeRNAii 5335.
    NextBioi 20662.
    PROi P19174.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P19174.
    Bgeei P19174.
    CleanExi HS_PLCG1.
    Genevestigatori P19174.

    Family and domain databases

    Gene3Di 1.10.238.10. 1 hit.
    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.
    IPR011992. EF-hand-dom_pair.
    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.
    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. "Characterization and cDNA cloning of phospholipase C-gamma, a major substrate for heparin-binding growth factor 1 (acidic fibroblast growth factor)-activated tyrosine kinase."
      Burgess W.H., Dionne C.A., Kaplow J.M., Mudd R., Friesel R., Zilberstein A., Schlessinger J., Jaye M.
      Mol. Cell. Biol. 10:4770-4777(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PHOSPHORYLATION.
      Tissue: Brain and Vein.
    2. NIEHS SNPs program
      Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ASN-209; GLY-279; THR-739 AND THR-813.
    3. "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.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORMS 1 AND 2), VARIANT THR-813.
      Tissue: Brain and Testis.
    6. "A tyrosine-phosphorylated carboxy-terminal peptide of the fibroblast growth factor receptor (Flg) is a binding site for the SH2 domain of phospholipase C-gamma 1."
      Mohammadi M., Honegger A.M., Rotin D., Fischer R., Bellot F., Li W., Dionne C.A., Jaye M., Rubinstein M., Schlessinger J.
      Mol. Cell. Biol. 11:5068-5078(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FGFR1.
    7. "Inhibition of CD3-linked phospholipase C by phorbol ester and by cAMP is associated with decreased phosphotyrosine and increased phosphoserine contents of PLC-gamma 1."
      Park D.J., Min H.K., Rhee S.G.
      J. Biol. Chem. 267:1496-1501(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-1248.
    8. "Signal transduction by fibroblast growth factor receptor-4 (FGFR-4). Comparison with FGFR-1."
      Vainikka S., Joukov V., Wennstrom S., Bergman M., Pelicci P.G., Alitalo K.
      J. Biol. Chem. 269:18320-18326(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FGFR4.
    9. "Phospholipase C-gamma1 interacts with conserved phosphotyrosyl residues in the linker region of Syk and is a substrate for Syk."
      Law C.L., Chandran K.A., Sidorenko S.P., Clark E.A.
      Mol. Cell. Biol. 16:1305-1315(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-771 AND TYR-783 BY SYK, INTERACTION WITH SYK.
    10. "Direct association of Csk homologous kinase (CHK) with the diphosphorylated site Tyr568/570 of the activated c-KIT in megakaryocytes."
      Price D.J., Rivnay B., Fu Y., Jiang S., Avraham S., Avraham H.
      J. Biol. Chem. 272:5915-5920(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KIT.
    11. "Intracellular signaling of the Ufo/Axl receptor tyrosine kinase is mediated mainly by a multi-substrate docking-site."
      Braunger J., Schleithoff L., Schulz A.S., Kessler H., Lammers R., Ullrich A., Bartram C.R., Janssen J.W.
      Oncogene 14:2619-2631(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AXL.
    12. "LAT: the ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation."
      Zhang W., Sloan-Lancaster J., Kitchen J., Trible R.P., Samelson L.E.
      Cell 92:83-92(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LAT.
    13. "Requirement of the Src homology 2 domain protein Shb for T cell receptor-dependent activation of the interleukin-2 gene nuclear factor for activation of T cells element in Jurkat T cells."
      Lindholm C.K., Gylfe E., Zhang W., Samelson L.E., Welsh M.
      J. Biol. Chem. 274:28050-28057(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SHB.
    14. "Autophosphorylation of KDR in the kinase domain is required for maximal VEGF-stimulated kinase activity and receptor internalization."
      Dougher M., Terman B.I.
      Oncogene 18:1619-1627(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY KDR.
    15. "Characterization of the tyrosine kinase Tnk1 and its binding with phospholipase C-gamma1."
      Felschow D.M., Civin C.I., Hoehn G.T.
      Biochem. Biophys. Res. Commun. 273:294-301(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TNK1.
    16. "The ORF3 protein of hepatitis E virus binds to Src homology 3 domains and activates MAPK."
      Korkaya H., Jameel S., Gupta D., Tyagi S., Kumar R., Zafrullah M., Mazumdar M., Lal S.K., Xiaofang L., Sehgal D., Das S.R., Sahal D.
      J. Biol. Chem. 276:42389-42400(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HEV ORF3 PROTEIN.
    17. "Identification and characterization of a new family of guanine nucleotide exchange factors for the ras-related GTPase Ral."
      Rebhun J.F., Chen H., Quilliam L.A.
      J. Biol. Chem. 275:13406-13410(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RALGPS1.
    18. "Protein tyrosine phosphatase CD148-mediated inhibition of T-cell receptor signal transduction is associated with reduced LAT and phospholipase Cgamma1 phosphorylation."
      Baker J.E., Majeti R., Tangye S.G., Weiss A.
      Mol. Cell. Biol. 21:2393-2403(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROBABLE DEPHOSPHORYLATION BY PTPRJ.
    19. Cited for: PHOSPHORYLATION AT TYR-783, SUBCELLULAR LOCATION.
    20. "The tyrosine phosphatase CD148 is excluded from the immunologic synapse and down-regulates prolonged T cell signaling."
      Lin J., Weiss A.
      J. Cell Biol. 162:673-682(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROBABLE DEPHOSPHORYLATION BY PTPRJ.
    21. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
      Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
      Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-771 AND TYR-1253, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    22. Cited for: INTERACTION WITH NTRK1.
    23. "Signal transduction via the stem cell factor receptor/c-Kit."
      Ronnstrand L.
      Cell. Mol. Life Sci. 61:2535-2548(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON INTERACTION WITH KIT AND ROLE IN KIT SIGNALING.
    24. "Deficiency of BLNK hampers PLC-gamma2 phosphorylation and Ca2+ influx induced by the pre-B-cell receptor in human pre-B cells."
      Taguchi T., Kiyokawa N., Takenouch H., Matsui J., Tang W.-R., Nakajima H., Suzuki K., Shiozawa Y., Saito M., Katagiri Y.U., Takahashi T., Karasuyama H., Matsuo Y., Okita H., Fujimoto J.
      Immunology 112:575-582(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BLNK; VAV1; GRB2 AND NCK1.
    25. "Activation of vascular endothelial growth factor receptor-3 and its downstream signaling promote cell survival under oxidative stress."
      Wang J.F., Zhang X., Groopman J.E.
      J. Biol. Chem. 279:27088-27097(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FLT4.
    26. "Vascular endothelial growth factor (VEGF)-D and VEGF-A differentially regulate KDR-mediated signaling and biological function in vascular endothelial cells."
      Jia H., Bagherzadeh A., Bicknell R., Duchen M.R., Liu D., Zachary I.
      J. Biol. Chem. 279:36148-36157(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-783 IN RESPONSE TO KDR ACTIVATION.
    27. "Early phosphorylation kinetics of proteins involved in proximal TCR-mediated signaling pathways."
      Houtman J.C., Houghtling R.A., Barda-Saad M., Toda Y., Samelson L.E.
      J. Immunol. 175:2449-2458(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY ITK.
    28. "Intracellular retention, degradation, and signaling of glycosylation-deficient FGFR2 and craniosynostosis syndrome-associated FGFR2C278F."
      Hatch N.E., Hudson M., Seto M.L., Cunningham M.L., Bothwell M.
      J. Biol. Chem. 281:27292-27305(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FGFR2, PHOSPHORYLATION.
    29. "Obligatory role for phospholipase C-gamma(1) in villin-induced epithelial cell migration."
      Wang Y., Tomar A., George S.P., Khurana S.
      Am. J. Physiol. 292:C1775-C1786(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH VIL1, SUBCELLULAR LOCATION.
    30. "Sustained phosphorylation of mutated FGFR3 is a crucial feature of genetic dwarfism and induces apoptosis in the ATDC5 chondrogenic cell line via PLCgamma-activated STAT1."
      Harada D., Yamanaka Y., Ueda K., Nishimura R., Morishima T., Seino Y., Tanaka H.
      Bone 41:273-281(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY FGFR3.
    31. "Binding of Cbl to a phospholipase Cgamma1-docking site on platelet-derived growth factor receptor beta provides a dual mechanism of negative regulation."
      Reddi A.L., Ying G., Duan L., Chen G., Dimri M., Douillard P., Druker B.J., Naramura M., Band V., Band H.
      J. Biol. Chem. 282:29336-29347(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PDGFRB.
    32. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1221, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1222 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    33. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    34. "A novel interaction between fibroblast growth factor receptor 3 and the p85 subunit of phosphoinositide 3-kinase: activation-dependent regulation of ERK by p85 in multiple myeloma cells."
      Salazar L., Kashiwada T., Krejci P., Muchowski P., Donoghue D., Wilcox W.R., Thompson L.M.
      Hum. Mol. Genet. 18:1951-1961(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FGFR3.
    35. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-771; TYR-775; TYR-783 AND SER-1221, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1222 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    36. "Mutation of tyrosine residue 857 in the PDGF beta-receptor affects cell proliferation but not migration."
      Wardega P., Heldin C.H., Lennartsson J.
      Cell. Signal. 22:1363-1368(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PDGFRB, PHOSPHORYLATION AT TYR-771.
    37. "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-1221 AND TYR-1253, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    38. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    39. "Nedd4-1 binds and ubiquitylates activated FGFR1 to control its endocytosis and function."
      Persaud A., Alberts P., Hayes M., Guettler S., Clarke I., Sicheri F., Dirks P., Ciruna B., Rotin D.
      EMBO J. 30:3259-3273(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FGFR1, PHOSPHORYLATION BY FGFR1.
    40. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1222 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    41. "Tespa1 is involved in late thymocyte development through the regulation of TCR-mediated signaling."
      Wang D., Zheng M., Lei L., Ji J., Yao Y., Qiu Y., Ma L., Lou J., Ouyang C., Zhang X., He Y., Chi J., Wang L., Kuang Y., Wang J., Cao X., Lu L.
      Nat. Immunol. 13:560-568(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TESPA1.
      Tissue: Thymocyte.
    42. "Cellular signaling by fibroblast growth factor receptors."
      Eswarakumar V.P., Lax I., Schlessinger J.
      Cytokine Growth Factor Rev. 16:139-149(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON ROLE IN FGF-ACTIVATED SIGNALING PATHWAYS.
    43. "Solution structure of the SH3 domain of phospholipase C-gamma."
      Kohda D., Hatanaka H., Odaka M., Mandiyan V., Ullrich A., Schlessinger J., Inagaki F.
      Cell 72:953-960(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF SH3 DOMAIN.

    Entry informationi

    Entry nameiPLCG1_HUMAN
    AccessioniPrimary (citable) accession number: P19174
    Secondary accession number(s): B7ZLY7
    , B9EGH4, E1P5W4, Q2V575
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: November 1, 1990
    Last modified: October 1, 2014
    This is version 189 of the entry and version 1 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 20
      Human chromosome 20: 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